Publication for RAG1 and RAG2

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
hsa	RAG1	recombination activating 1	5896			[link]
hsa	RAG2	recombination activating 2	5897

Pubmed ID	Priority	Text
19647518	0.98	RAG1 and RAG2 (ii, iii).
	0.97	RAG1, RAG2 and HMGB1 were identified to be protein components of both digested and non-digested SEC bands (Figure 2B, i-iii).
	0.97	RAG1 to RAG2.
	0.97	RAG1 and RAG2.
	0.97	RAG1, RAG2, and the DNA in the SEC.
	0.96	RAG1 and RAG2 are positioned at opposing ends of the complex, and the DNA chains beyond the RSS nonamer emerge from the same face of the complex, near to the RAG1 N-termini.
	0.96	RAG1, RAG2 and HMGB1 (Figure 2D).
	0.96	RAG1:RAG2:HMGB1 ratios were run to assess the stoichiometry of the protein components of the SEC (Figure 2D).
	0.96	RAG1-RAG2 heterodimers bound to the pair of RSS DNAs.
	0.96	RAG1 and RAG2 by a 25 aa flexible tether and are expected to be mobile.
	0.96	RAG2 is at the "drag" end (the wide end), of the anchor and their MBPs form the "arms" and the MBP attached to RAG1 at the "shank" end and form the "tails" (Figure 4),
	0.96	RAG1 end and opposite the RAG2 end.
	0.96	RAG2:RAG1 and HMGB1:RAG1 were calculated for each fraction (open circle) and compared to the stoichiometry standards (X).
	0.95	RAG2 and HMGB1 to RAG1 were compared to the standards (Figure 2D).
	0.95	RAG1 and the other pair to RAG2.
	0.95	RAG1 and RAG2 N-termini and nonamer exits on the SEC particle, we were able to generate a fairly detailed model of the RAG1-RAG2-DNA complex (Figure 7).
	0.94	RAG1 and RAG2 constructs used for preparing the SEC were fusions with MBP, it was possible to tag the SEC with monovalent anti-MBP Fab fragments, and thus localize the MBP moieties.
	0.94	RAG1 (R1/MR2) or RAG2 (MR1/R2) of the purified SEC using PreScission protease.
	0.91	RAG2s are most probably assigned as the "arms" in Figure 4B (i-iv), and the "tails" of the anchor-shaped SEC are most likely the MBPs linked to the N-termini of the RAG1 dimer.
	0.89	RAG1 and RAG2.
	0.85	RAG1 and RAG2, and independent measurements of its molecular mass by gel filtration, light scattering, and STEM all yield a value close to 500,000 Da, implying that the SEC is composed of a RAG1-RAG2 heterotetramer and two cleaved RSS DNAs (Figure 2-Figure 3).
	0.84	RAG1 and two RAG2 molecules in each SEC, four anti-MBP Fab extensions were observed for each SEC particle (Figure 4C).
	0.76	RAG1 and RAG2.
	0.75	RAG1 and RAG2 was adsorbed onto carbon-coated grids, negatively stained with uranyl acetate, and observed by transmission electron microscopy (EM).
	0.71	RAG1 and RAG2.
	0.69	RAG1:RAG2:HMGB1).
	0.63	RAG1 appear to be more flexible and assume more varied positions relative to the SEC than the MBPs attached to RAG2.
	0.60	RAG1 and RAG2 proteins with DNA containing a pair of cleaved recombination signal sequences (RSS).
	0.59	RAG1 and RAG2, we used the AR1 and MR2 variations and removed the MBPs fused to RAG1 by protease digestion after assembly and purification of SEC particles (Figure S2).
	0.57	RAG1 (384-1008 aa) and RAG2 (1-387 aa) are necessary for the basic recombination reaction and for in vitro RSS binding and cleavage.
	0.55	RAG2s and <=1 HMGB1 per RAG1 dimer.
	0.51	RAG1: 2 RAG2: 1 HMGB1.
	0.50	RAG1 and RAG2, a SEC would be 722 kDa or 960 kDa if 3 or 4 RAG1/2 heterodimers were present, far outside the experimentally measured range.
19912631	0.98	RAG1 and amino acids 1-387 for RAG2, are necessary and sufficient to rearrange artificial V(D)J recombination substrates in vitro.
	0.97	RAG1 or RAG2 can lead to partially impaired V(D)J recombinational activity resulting in Omenn syndrome (OS).
	0.97	RAG1 and RAG2, which can be either severe, leading to null alleles, or mild, leading to hypomorphic alleles that can still maintain a residual enzymatic activity.
	0.97	RAG1 or RAG2 mutations were detected (as will be described in the next section) only in 15 leaving four without a detectable mutation (mutation-free).
	0.97	RAG1 mutation, R559S, on the other hand is localized to the catalytic domain of RAG1 which interact with RAG2.
	0.96	RAG1, RAG2, or DCLRE1C.
	0.96	RAG1, and a fifth patient has a novel I444M mutation in RAG2.
	0.96	RAG1 or RAG2 mutations were confirmned as carriers (heterozygous) of the respective mutation.
	0.96	RAG1 and RAG2 mutations were confirmned as carriers of the respective mutation.
	0.96	RAG1 and RAG2 core regions.
	0.95	RAG1 or RAG2, and six (27%) in DCLRE1C.
	0.95	RAG1 and RAG2 mutations reported here, with the exception of I444M in OS2, are also associated with severe SCID or OS.
	0.94	RAG1 &RAG2) that are necessary for the somatic rearrangement of antigen receptor genes on T- and B-lymphocytes, or in DCLRE1C (Artemis), resemble all other forms of SCID in their infection susceptibility, however their lymphocyte phenotype is charecterized by predominantly circulating NK cells and undetectable B or T lymphocytes (T-B-NK+ SCID).
	0.94	RAG1, RAG2, or DCLRE1C.
	0.94	RAG1, RAG2, or DCLRE1C were also negative for LIG4 indicating that mutations in the latter are not a common cause of SCID or OS in Saudi patients.
	0.90	RAG1, RAG2, and DCLRE1C.
	0.89	RAG1-RAG2 interaction which occurs normally in the nucleus, and is required during T-cell receptor (TCR) and B-cell immunoglobulin (Ig) rearrangements.
	0.86	RAG1, RAG2, or DCLRE1C was found in OS3 (F2) patient.
	0.83	RAG1, RAG2, and DCLRE1C are the primary genes responsible for the T-B-NK+ SCID phenotype and in a recent report, mutations in LIG4 were also documented in patients with this phenotype who also have microcephaly and developmental delay.
	0.58	RAG1, RAG2 or DCLRE1C genes for any of the remaining 6 T-B-NK+ SCID patients (P16-P21; ~27%).
19492059	0.98	RAG-1 and the amino terminus of RAG-2 as well as the herpes DBP as a consequence of the original insertion event
	0.97	RAG-1/RAG-2 like locus for long periods of time until the present in the sea urchin in the absence of V(D)J recombination.
	0.97	RAG-1 and RAG-2 locus in the sea urchin, apparently predating V(D)J recombination; 2) co-relates the known functional properties of the current acquired immune system and the herpes viruses as well as numerous regulatory features shared between these elements; 3) provides an explanation for shared regulatory network and mutagenic potential of both herpes virus replication and V(D)J recombination and the complex and possibly intersecting roles of these pathways as co-factors in human malignancy through V(D)J recombination pathogenesis.
	0.96	RAG-1 and RAG-2 regulate site-specific recombination events in somatic immune B- and T-lymphocytes to generate the acquired immune repertoire.
	0.96	RAG-1/RAG-2 transposase or transposon and can also account for the experimental structure of the current RAG-1/RAG-2-like genes in the sea urchin and other deuterostomes that do not undergo V(D)J recombination.
	0.95	RAG-1/RAG-2 recombinase are functionally similar to cis-acting sequences regulating the current herpes recombinase protein termed the herpes major DNA binding protein (DBP) accounting in part for the previous regulatory interactions between the RAG proteins and herpes virus infection of lymphocytes Second, it is shown that the recently solved partial crystal structure of a conserved herpes virus recombinase, the DBP protein ICP-8 shares functional properties with the known structural features of both the RAG-1 recombinase and RISC (RNA induced silencing complex).
	0.95	RAG-1 and RAG-2 like proteins from promoters in flanking sequences.
	0.94	RAG-1 and RAG-2 in non-vertebrate organisms such as the sea urchin that lack an acquired immune system and V(D)J recombination.
	0.94	RAG-1/RAG-2 protein complex required for recombination of genes for immunoglobulin and T cell receptor genes in vivo can function as a transposase under some conditions in vitro (although apparently not at a high rate in vivo).
	0.94	RAG-1-like recombinase (denoted pR1) adjacent to a pre-existing RAG-2-like protein (denoted pR2).
	0.94	RAG-1 DDE site, at first blocked by the proto-RAG-2 protein co-expressed in immune somatic cells would over time evolve to form the nucleus of a somatic recombinase generating a variable repertoire against pathogens such as herpes viruses.
	0.91	RAG-1 denoted pR1) adjacent to a pre-existing RAG-2 like protein (denoted pR2) is shown.
	0.90	RAG-1 protein adjacent to a gene encoding a functional RAG-2 protein although the sea urchin does not have any evidence of an acquired immune system, favoring a gradual rather than "big bang" model.
	0.90	RAG-1 and RAG-2 proteins are closely linked in inverted orientation in the genome of vertebrates that have acquired immune systems and the genome of the sea urchin that does not have an acquired immune system.
	0.60	RAG-1 and proto-RAG-2 proteins (Figure 5).
30971819	0.98	RAG1/RAG2 recombinase and V(D)J recombination was a pivotal event in the evolution of the jawed vertebrate adaptive immune system.
	0.98	RAG1 and RAG2 evolved from the transposase genes of an ancient "RAG transposon" while disassembled ("split") immunoglobulin and T-cell receptor genes arose from transposon insertion into a receptor gene, with the inserted terminal inverted repeats (TIRs) of the transposon becoming the RSSs.
	0.97	RAG1 and an acidic region in RAG2:that together suppress RAG-mediated transposition more than 1000-fold.
	0.97	RAG1 catalytic core while BbRAG2L, like RAG2, adopts a structure consistent with a 6-bladed beta-propeller fold (Fig. 2b and Extended Data Fig. 3b-d).
	0.97	RAG1 R848M mutation, as WT RAG1 lacked detectable transposition activity when paired with RAG2 1-350 (Fig. 5g).
	0.97	RAG2 and is increased by the RAG1 R848M mutation.
	0.96	RAG2 1-350, a RAG1 E649V mutation boosted transposition while S963A had little effect (Fig. 5g).
	0.96	RAG1 and RAG2 1-350. f, Number (percent) of transposition events into the genome features indicated.
	0.95	RAG2 1-350, E649V/R848M RAG1, WT RAG1, and no RAG1 yielded 930, 16, and zero independent transposition events, respectively (Fig. 5h and Extended Data Fig. 9d).
	0.95	RAG2 1-383 (f) or 1-350 (g) and the indicated full length WT or mutant RAG1 protein, and with full length BbRAGL (mean +- SEM).
	0.92	RAG1 R848M (h) or R848M/E649V (i) and various forms of RAG2, beginning at amino acid 1 and ending with the amino acid indicated below the bars.
	0.82	RAG2 1-350 and either WT or R848M/E649V RAG1.
	0.76	RAG1 and RAG2 to provide two-tiered protection against RAG-mediated transposition.
25488578	0.98	RAG1-RAG2 transposase.
	0.97	RAG1-RAG2 locus in the sea urchin genome implies that this pair of closely linked genes was already present in the genome of the last common ancestor of the Deuterostomes.
	0.95	RAG1 and RAG2 genes in animal genomes suggests that this gene pair was already present in the ancestral Transib-like transposon, although no such gene combination has been detected in the currently identified transposons.
	0.95	RAG1-RAG2 gene pair, whereas insertion of a related non-autonomous element introduced the RSS into an ancestral immunoglobulin gene, which was an element of innate immunity.
	0.94	RAG1-RAG2 before the emergence of adaptive immunity is intriguing: is it possible that there may be additional mechanisms of naturally evolved genome engineering that remain to be discovered?
	0.92	RAG1 is the enzymatically active subunit, whereas RAG2 acts as a regulatory subunit and is superficially similar to the function of Cas2 in the Cas1-Cas2 duet.
	0.91	RAG1-RAG2 recombinase complex (FIG.
	0.90	RAG1-RAG2 gene pair.
	0.90	RAG1-RAG2) has been previously discussed.
	0.81	RAG1 and RAG2 proteins are not encoded in proximity of the cognate recombination sites.
	0.61	RAG1-RAG2 are similar, and there is significant sequence similarity between the TIRs of Transib and the recombination signal sequences (RSSs) of the immunoglobulin genes (FIG.
	0.60	RAG1-RAG2 gene block while leaving the native RSS-like TIRs within the immunoglobulin gene.
26996199	0.98	recombination-activating gene 1 (RAG1) and RAG2 proteins initiate the V(D)J recombination process, which ultimately enables the generation of T cells and B cells with a diversified repertoire of antigen-specific receptors.
	0.97	RAG1 and RAG2 genes are juxtaposed on chromosome 11p13.
	0.96	RAG1 and RAG2 (REFS ).
	0.96	RAG1 and M322T from RAG2 are partially exposed (shown in yellow), whereas V8I, F62L and T77N from RAG2 are buried inside the protein (shown in purple).
	0.95	RAG2 coordinately activate the transcription of RAG1 and RAG2 during T cell and B cell development.
	0.95	RAG2 core region folds into a six-bladed beta-propeller and associates primarily with the RAG1 domains downstream of the DDBD and inclusive of the CTD, creating the arms of the Y-shaped structure of the RAG complex (BOX 1).
	0.93	Recombination-activating gene 1 (RAG1) and RAG2 (referred to collectively here as RAG genes) encode lymphoid-specific proteins that are expressed during the early stages of T cell and B cell development and initiate the process of V(D)J recombination by introducing DNA double-strand breaks (DSBs) at the junction between the heptamer and a coding element.
	0.90	RAG1 and RAG2, crystallography and cryo-electron microscopy studies have helped to predict the structural and functional consequences of most mutations.
	0.85	RAG1 core subunits are shown in blue and grey, and two RAG2 core subunits are shown in purple and pink.
	0.72	RAG1 and RAG2 create a Y-shaped structure in which the NBDs of the two RAG1 molecules form the stem, and the DDBDs form the branch point.
	0.60	RAG1 and RAG2 have an important regulatory role.
	0.60	recombination-activating gene 1 (RAG1)-RAG2 heterotetramer.
18281312	0.98	RAG1 and RAG2, which mediate interactions with conserved recombination signal sequences (RSSs) that lie adjacent to each gene segment.
	0.97	RAG1/full-length RAG2 is also observed.
	0.97	RAG1 and RAG2 protein preparations shown in Figure 1B were incubated with a radiolabeled intact 12-RSS substrate in binding reactions containing Ca2+, and RAG-RSS complex formation was analyzed using an EMSA (Figure 1C).
	0.96	RAG1, but not truncated catalytically active 'core' RAG1 (residues 384-1040), when RAG1 is co-expressed with 'core' RAG2 (residues 1-387) in mammalian cells and recovered using a mild purification procedure.
	0.96	RAG1 and RAG2 in 293 cells in various combinations (cMR1/cMR2, cMR1/FLMR2, FLMR1/cMR2, see Figure 1A) and purified them following our standard procedure, or a modified protocol that uses a milder buffer containing 10% glycerol, 10 mM MgCl2 and 150 mM KCl.
	0.96	RAG1 and RAG2, protein yields are generally quite similar using either purification method (Figure 1B).
	0.95	RAG1 dimer and monomeric RAG2, whereas the less abundant and slower migrating SC2 complex differed from SC1 by the incorporation of a second RAG2 molecule.
	0.94	RAG1/RAG2 association imparted by the buffers and/or procedures used for purification, rather than any potential association with Ku70/Ku80.
	0.89	RAG2 association with RAG1 and/or the RSS.
	0.80	RAG1/full-length RAG2, but not full-length RAG1/core RAG2, appears to be DNA-dependent.
18831563	0.98	RAG1 or RAG1 pre-incubated with RAG2 was incubated with various DNA substrates in the presence of Ca2+ and deposited onto APS-mica for AFM imaging.
	0.98	RAG2 associates with RAG1, which in turn binds to RSS sequences with a higher specificity [Table 1 and ], we investigated the role of RAG2 in DNA bending.
	0.97	RAG1 and RAG2, which contain large deletions but retain enzymatic activity of DNA cleavage in vivo.
	0.97	RAG1 and RAG2 proteins are necessary for efficient binding and cleavage, DNA recognition is largely the function of RAG1.
	0.95	RAG1 dimer size does not change upon the addition of RAG2 (79 kDa, estimated size 170 nm3), the measured volume of RAG1/2 (938 nm3) is between a RAG1/2 tetramer (2RAG1:2RAG2, 459+340=799 nm3) and pentamer (2RAG1:3RAG2, 968 nm3).
	0.82	RAG1 with or without RAG2 induces a significant DNA bending at 12RSS.
	0.77	RAG1, to which RAG2 was added later.
	0.57	RAG2 may act through a conformational change of RAG1, which may change the DNA binding properties of RAG1/2 relative to RAG1 alone.
18775324	0.98	RAG1 and RAG2 proteins that generate double-strand DNA breaks at recombination signal sequences (RSS) associated with rearrangeable gene segments.
	0.97	RAG1 and RAG2 proteins.
	0.97	RAG1 and RAG2 provides one level of specificity, additional constraints at the level of substrate DNA are required to discriminate between the seven antigen receptor loci in the genome.
	0.96	RAG1, RAG2, and HMG2 for additional 2 hr.
	0.93	RAG1, which contains structural motifs as well as E3 ligase activity, may affect protein stability or association, while the C-terminal domain of RAG2 binds phosphoinositides, core histones, and H3K4me3 via a PHD domain.
	0.84	RAG1, GST-RAG2 core, and HMG2 proteins obtained as described in the Experimental Procedures.
24418478	0.98	RAG1 transcription level was correlated to RAG2 (Fig 1, C), indicating that the differences in severity of the precursor B-cell block were not caused by differences in expression of RAG1.
	0.95	RAG1 transcription level correlated with that of RAG2, we assume that all patients had similar expression of the mutant RAG1 protein (Fig 1, C).
	0.91	recombination-activating gene 1 (RAG1) and RAG2 result in loss or reduction of V(D)J recombination.
	0.84	recombination-activating gene (RAG) 1 and RAG2 proteins by creating double-stranded breaks in the immunoglobulin and TR loci.
	0.76	RAG1 expression levels correlated to RAG2 expression in all the analyzed RAG patients, as determined by using RQ-PCR.
	0.56	RAG1 and RAG2 transcription levels are correlated, and that RAG1 and RAG2 levels in BM mononuclear cells depend on the number of cells expressing RAG (pre-BI and pre-BII cells).
30905508	0.98	RAG1 and RAG2 binding maps precisely to broken signal ends detected by END-seq in thymocytes at the TCRalpha locus.
	0.95	RAG1 and full-length RAG2 are shown; equivalent data were obtained with core RAG2.
	0.93	RAG1 binds to the RSS nonamer and following capture of a partner RSS to form a synaptic complex, RAG2 directs the RAG1 DDE catalytic site to cleave the partner RSS precisely at the boundary between the heptamer and coding sequence.
	0.89	RAG1 and one of RAG2 and single complex 2 (SC2) that contains two molecules each of RAG1 and RAG2.
	0.70	RAG1 and RAG2, together with two substrate plasmids, that encode either a 12-RSS, a 23-RSS or a SJ (Figure S5A).
	0.59	RAG1 and RAG2, bind to the RSSs, which lie adjacent to V, D, and J gene segments and consist of conserved heptamer and nonamer sequences, separated by 12 +- 1 bp or 23 +- 1 bp non-conserved spacers.
31702817	0.98	RAG1 subunits each in association with a RAG2.
	0.97	RAG1 in complex with RAG2 and other accessory proteins, which recognize and cleave at specific sequences termed recombination signal sequence (RSS) bordering the V, D and J segments.
	0.96	RAG1 catalytic domain, while RAG2 is involved in heptamer binding, chromatin targeting and the stability of the reaction intermediate complexes.
	0.94	RAG2 is a 527 amino acids protein, essential for the proper function of RAG1, comprised of a core region (-387) and a C-terminal domain (388-527).
	0.93	RAG1 and RAG2, key enzymes for generating the diverse repertoire of adaptive immune system effectors.
28083621	0.98	RAG1 and RAG2 genes can lead to a range of phenotypes characterized by various clinical spectrum (Niehues et al.).
	0.93	RAG1 and RAG2 genes, including second and third exon, respectively.
20371343	0.98	RAG1 and RAG2), are transesterases that introduce double strand breaks (DSBs) at recombination signal sequences (shown in triangles) that flank V, D, and J gene segments.
31031743	0.98	RAG1, JAK3, ADA, IL7R, and CECR1 genes, 9 homozygous variants including ADA, RAG1, RAG2, CD3D, JAK3, ARPC1B, MYD88/CARD9, and JAGN1, 7 hemizygous variants in IL2RG, CD40LG, and XIAP, and only 1 heterozygous somatic variant in NRAS (Figure 4C).
9166431	0.97	RAG1 and RAG2.
	0.97	RAG1 and RAG2 proteins, which are directed in cis by recombination signal sequences (RSSs)1.
	0.97	RAG1 and RAG2 are required but not sufficient to regulate 12/23-dependent cleavage, and that other ubiquitously expressed cellular factors cooperate with RAGs to establish the 12/23 rule.
	0.97	RAG1 and RAG2, purified RAG1 and RAG2, and combinations of extracts and purified proteins.
	0.97	RAG1/RAG2 (R1/2) on the 12/23 substrate, in the absence or presence of purified high mobility group protein 1 or 2 (HMG1 or HMG2, respectively), recombinant HMG1 (rHMG1), integration host factor (IHF), and HU protein.
	0.96	RAG1 and RAG2 are not sufficient for 12/23 dependent cleavage, whereas RAG1 and RAG2 complemented with whole cell extract faithfully recapitulates the 12/23 rule.
	0.96	RAG1 and RAG2 can mediate 12/23 regulated cleavage in vitro.
	0.96	RAG1 and RAG2 proteins, suggesting that RAG1 and RAG2 alone may not be sufficient for strict adherence to the 12/23 rule.
	0.96	RAG1 and RAG2 Complemented with Whole Cell Extracts Show Strict 12/23 Regulation.
	0.96	RAG1 and RAG2 proteins have shown preferential, but incomplete 12/23-regulated cleavage by the isolated proteins.
	0.96	RAG1 and RAG2 strictly adhere to the 12/23 rule, whereas RAGs purified from the same extracts have only a two- to threefold preference for a 12/23 substrate.
	0.96	RAG1 and RAG2 was completely inhibited by the extracts of untransfected 293T cells (Fig. 2, D and E).
	0.96	RAG1, RAG2, DNA-bending proteins, and other factors can be completely analyzed.
	0.96	RAG1/ RAG2-cotransfected 293T whole cell extracts (R1/2 WCE) on 12/23 and 12/12 cleavage probes.
	0.95	RAG1 and RAG2 were prepared from 293T cells that were transiently transfected with plasmids that encode RAG1 and RAG2 GST fusion proteins.
	0.95	RAG1- and RAG2-mediated DNA cleavage.
	0.95	RAG1 and RAG2 on the 12/23 substrate.
	0.95	RAG1 and RAG2 and either HMG1, rHMG1, HMG2, or HU on both 23/23 and 23i substrates (Fig. 3 C; data not shown).
	0.95	RAG1/RAG2 (R1/2) on 12/23 and 23/23 cleavage probes, in the presence or absence of untransfected 293T whole cell extract (WCE), as indicated.
	0.94	RAG1 and RAG2 GST fusion proteins were copurified directly from the same transfected 293T cell extracts, and control extracts were from 293T cells that did not express RAG1 or RAG2.
	0.94	RAG1/RAG2-cotransfected 293T whole cell extract (R1/2 WCE) on 12/23 and 23/23 cleavage probes.
	0.93	RAG1 and RAG2 in the first phase of the V(D)J recombination reaction results in the production of signal and coding ends.
	0.92	RAG1- and RAG2-mediated cleavage of substrates containing 23 RSS but not of substrates containing only 12 RSS.
	0.92	RAG1 and RAG2 proteins with factors found in whole cell extracts, we combined control extracts from untransfected 293T cells with purified RAG proteins.
	0.88	RAG1/RAG2 (R1/2) on 23/23 and isolated 23 RSS (23i) substrate, in the absence or presence of rHMG.
	0.86	RAG1 and RAG2 are known to be involved in V(D)J recombination, but none of these proteins has been suggested as required for 12/23-regulated cleavage.
	0.82	RAG1 and RAG2.
	0.72	RAG1/RAG2.
	0.58	RAG1/RAG2 (R1/2) on the 12/12 substrate, in the absence or presence of purified HMG1 or HMG2, rHMG1, IHF, and HU protein.
	0.57	RAG1/RAG2 (R1/2) on 12/23 and 12/12 cleavage probes.
27574300	0.97	RAG1 and RAG2 are required for ATM's inhibition of signal (but not coding) end joining; the non-core N-terminus of RAG 1 is not.
	0.97	RAG1 and RAG2 as evidenced by partial inhibition in experiments with one core RAG component and one full length RAG component (yellow and orange bars).
	0.97	RAG1 and RAG2 were not present in the recombinant proteins used recently to determine the molecular structure of the RAG complex; although the C-termini of both RAG1 and RAG2 are present in the constructs used in recent cryo-EM studies of the RAG complex, 179 residues from RAG2's C-terminus and 26 residues from RAG1's C-terminus are not visible in the structures, presumably because of the flexibility of these regions relative to the core regions.
	0.97	RAG1 and RAG2 stabilize this interaction.
	0.97	RAG1, RAG2, and increasing concentrations of wild type ATM.
	0.97	RAG1 and RAG2 are required for maximal ATM inhibition of VDJ joining
	0.97	RAG1 or RAG2 as indicated.
	0.96	RAG1 and RAG2 are also required for ATM's capacity to limit signal (but not coding) joining.
	0.96	RAG1 and RAG2, with either GFP-tagged ATM or GFP-tagged DNA-PKcs or vector control were transfected as in episomal assays.
	0.96	RAG1 and RAG2 are required for maximal ATM-mediated inhibition of VDJ joining
	0.96	RAG1's C-terminus is much less well conserved than RAG2's.
	0.96	RAG1 and RAG2 has been shown to be important in limiting the hairpinning stage of RAG cleavage; of note these authors proposed that the C-termini of RAG1 and RAG2 increased stability of RSS binding by the RAG complex.
	0.95	RAG1 or RAG2 non-core regions result in somewhat less relative inhibition of coding joints, ATM still substantially inhibits coding end joining with all combinations of RAG expression constructs.
	0.95	RAG 1 and RAG2.
	0.94	RAG1 and RAG2 that lack their C-termini (Fig. 3C, red arrow, light green bars), indicating that the "non-core" C-terminus of RAG1 is required for the ability of ATM to limit signal end joining.
	0.94	RAG1, RAG2, or I-Sce1 as well as control plasmid, wild type DNA-PKcs, or wild type ATM.
	0.93	RAG2, and either full length RAG1, N-terminal deleted RAG1 (ndelR1), or C-terminal deleted RAG1 (cdelR1).
	0.90	RAG1 and RAG2 are requisite for ATM's capacity to limit signal (but not coding) end joining.
	0.90	RAG1 or C-terminal deleted RAG1 (cdelR1) in conjunction with full length RAG2, 4X, 5X, 11X, 12X, or core RAG2.
	0.87	RAG2 mutant and cdel/RAG1 were imprecise (with kinase dead ATM, data not shown) as compared to 1 of 80 with full length RAGs (Figure 2B).
	0.87	RAG1 or C-terminal deleted RAG1 (cdelR1) in conjunction with full length RAG2, 4X, 5X, 11X, 12X, or core RAG2.
	0.83	RAG1 or RAG2.
	0.83	RAG2's acidic hinge, the RAG1 C-terminus includes numerous negatively charged residues.
	0.81	RAG1 collaborates with the C-terminus of RAG2 to inhibit the hairpin stage of cleavage.
	0.77	RAG1's or RAG2's C-termini.
	0.77	RAG2 mutant and cdel/RAG1 are predominately precise (Fig.4D).
	0.75	RAG2 mutant and cdel/RAG1 RAGs affects end processing of signal joints.
	0.69	RAG1 nor core RAG2 functions fully in living animals.
	0.64	RAG1 and RAG2 cooperate to inhibit the hairpinning step during RAG RSS cleavage, and that "together the RAG1 and RAG2 C-terminal regions produce a tighter complex with 12/23RSS".
20004590	0.97	Rag1/Rag2 enzyme.
	0.97	Rag2 was never a part of them, and an ancestral Rag1-like Transib sequence simply integrated next to a prototypical Rag2 gene that served a different cellular function at that time (Fig. 2).
	0.97	Rag1/Rag2 complex.
	0.96	Rag1/Rag2 gene pair, all Transib and Transib-like elements identified thus far contain only a single open reading frame with similarity to Rag1.
	0.96	Rag1/Rag2 gene pair in evolution, considering that similarities with cut-and-paste transposases in lower organisms are limited to Rag1 by itself.
	0.96	Rag1 and Rag2?
	0.96	Rag1/Rag2 gene pair in an echinoderm species and in jawed vertebrates suggest that the transposon either entered the genome of a common ancestor of all living deuterostomes (Fig. 2), or that two related Rag1-like elements independently entered the genome of an ancestral jawed vertebrate and an ancestral echinoderm.
	0.96	Rag1/Rag2 complex will provide answers to at least some of these questions.
	0.96	Rag1/Rag2 gene cluster
	0.95	Rag1/Rag2 complex.
	0.95	Rag1/Rag2 gene locus.
	0.95	Rag1/Rag2 cluster (Fig. 2).
	0.95	Rag2 control the transposase activity [reviewed in ], it is likely that several other changes in Rag1 also contributed to these altered properties.
	0.94	Rag1 and Rag2 in jawed vertebrates
	0.94	Rag1/Rag2 genes?
	0.93	RAG1 and RAG2).
	0.93	Rag1 could also have originated from the integration of a Transib element into the 3'end of a ubiquitin ligase gene that was located next to the ancestral Rag2 (Fig. 2).
	0.91	Rag1/Rag2 complex but also require non-homologous end joining DNA repair factors.
	0.89	Rag1/Rag2 that theoretically could act as RSS, but their conservation in other species and whether they are indeed remnants of the ancestral TIRs remains to be determined.
	0.88	Rag1/Rag2) evolved into the V(D)J recombinase.
	0.86	Rag1/Rag2 complex uses the same reaction chemistry as many cut-and-paste transposases (including Tn5, Tn10, and Hermes), and cleaves the DNA at the RSS by a set of hydrolysis and transesterification reactions: an initial hydrolysis step creates a nick in the top strand of the DNA, followed by a transesterification using the 3'-OH group as the nucleophile (Fig. 1) [reviewed in, reviewed in ].
	0.86	Rag1 and Rag2 extends to their transcriptional control, namely that both genes are always coexpressed.
	0.85	Rag1/Rag2 from all other species as well.
	0.85	Rag1 and Rag2 (prot-Rag1 and prot-Rag2) proteins emerged, serving an unknown primitive function.
	0.81	Rag1 are well conserved: the three catalytic residues D548, D708, and E962, their immediate sequence environment, the zinc finger domain important for the interaction with Rag2, and parts of the N-terminus.
	0.77	RAG1 and RAG2).
	0.62	Rag2 is overall less well conserved than Rag1 (54% identity and 68% similarity between shark and human Rag2), but the hydrophobic residues that are important for the structural integrity of the beta-propeller and the PHD domain remain intact throughout all vertebrate Rag2 reported thus far.
19621044	0.97	RAG1-RAG2 recombinase functions within a specialized subnuclear compartment that we term the V(D)J recombination factory.
	0.97	RAG1-RAG2 complex seems to play a role in mediating allelic pairing during B cell development.
	0.97	RAG1-RAG2 promotes classical non-homologous end-joining
	0.97	RAG1 forms protein-protein interactions (either directly or indirectly) with two components of the cNHEJ machinery (Ku70 and Ku80), perhaps the C-terminal portion of RAG2 also interacts with components of the cNHEJ machinery.
	0.97	RAG1-RAG2 post-cleavage complex to the cNHEJ pathway.
	0.97	RAG1-RAG2 complex nucleates the factory, while arrows pointing towards the RAG1-RAG2 complex represent the recruitment of additional regulatory factors by the RAG1-RAG2 complex.
	0.96	RAG1-RAG2 complex.
	0.96	RAG2-H3K4me3 interaction may induce a conformational change in the RAG1-RAG2 complex, thereby allosterically activating the recombinase and stimulating chromosomal V(D)J cleavage.
	0.96	RAG1-RAG2 complex influences allelic pairing also remains.
	0.95	RAG2 in this conformation, the RAG1-RAG2 complex might exhibit suboptimal catalytic properties.
	0.95	RAG1-RAG2 complex is a talented and versatile molecular machine that does much more than simply catalyze the phosphoryl transfer reactions required to generate DNA double-strand breaks.
	0.94	RAG1-RAG2 complex plays a role in mediating allelic pairing of immunoglobulin loci during B cell development is very exciting and certainly expands our view of how the RAG1-RAG2 complex helps to regulate V(D)J recombination.
	0.91	RAG1-RAG2 complex also interacts with H3K4me3, plays a role in immunoglobulin allelic pairing, and helps determine whether the broken ends generated during V(D)J recombination are repaired via classical NHEJ, alternative NHEJ, or homologous recombination.
	0.89	RAG1-RAG2 can function as a recombinase, several recent studies have revealed that RAG1-RAG2 is actually a surprisingly multifaceted enzyme complex that plays an important role in ensuring that V(D)J recombination is faithfully executed and properly regulated in the cell.
	0.89	RAG2-H3K4me3 interaction may be required for recruiting and/or retaining the RAG1-RAG2 complex at poised antigen receptor loci.
	0.85	RAG1-RAG2 recombinase catalyzes all V(D)J recombination events, and yet only a limited subset of all recombinationally competent gene segments are actually rearranged in a given cell at a given time, V(D)J recombination must be regulated by modulating the accessibility of the various antigen receptor loci to the RAG proteins.
	0.81	RAG2-H3K4me3 interaction might stabilize the RAG1-RAG2 post-cleavage complex, helping the recombinase to bind cleaved signal and coding ends, thereby facilitating efficient 'hand-off' of V(D)J recombination intermediates to the NHEJ machinery.
	0.80	RAG1 expression, but independent of the RAG1-RAG2-catalyzed V(D)J cleavage because it still occurs with a catalytically inactive form of RAG1.
	0.73	RAG1-RAG2 'reads' marks of accessible chromatin
	0.51	RAG1-RAG2 complex.
25985233	0.97	RAG1 and RAG2) introduce DNA double-strand breaks and recombine V, D and J segments, AID deaminates cytosines in Ig V and switch regions thereby enabling somatic hypermutation (SHM) and class switch recombination (CSR) of Ig genes.
	0.97	RAG1-RAG2 is activated in response to infectious and inflammatory stimuli, both in early and mature B cells.
	0.97	RAG1-RAG2.
	0.97	Rag1-Rag2 mRNA and recombination of Igk V and J gene segments.
	0.97	Rag1, Rag2 and one empty vector control and, Aicda, Rag1 and Rag2, were analyzed.
	0.96	Rag1, Rag2 and Aicda transcription.
	0.96	RAG1-RAG2 and AID activity in all subgroups (Supplementary Tables 3-5).
	0.96	RAG1 and RAG2 after retroviral overexpression of these vectors in EBV-immortalized human cord blood B cells.
	0.93	Rag1, Rag2 and Aicda mRNA expression (Fig. 3c-e).
	0.92	Rag1 and Rag2 mRNA levels were measured by qRT-PCR following inducible deletion of Pten in Ptenfl/fl pre-B cells (n=3, mean +- s.d.).
	0.91	RAG1-RAG2 activity alone.
	0.91	RAG1-RAG2 but also upregulation of AID (Fig. 3a).
	0.89	RAG1 and RAG2 are constitutively expressed in pro- and pre-B cells and target recombination signal sequences (RSSs) in both Ig and non-Ig genes.
	0.85	Rag1-Rag2, while Akt phosphorylates and inactivates FOXO1, a potent transcriptional activator of Rag1 and Rag2.
	0.83	RAG1-RAG2-expressing pre-B cells, these findings did not establish that AID and RAG1-RAG2 are concurrently active in the same cells.
	0.81	RAG1-RAG2 and AID enzymes
	0.74	Rag1 (eGFP) and Rag2 (dsRedE2), either alone or in combination or empty vector controls for Aicda, Rag1 and Rag2 vectors (Figs. 5a,b; Supplementary Figs. 6,7).
	0.63	RAG1-RAG2-mediated deletions and rearrangements, we measured whether lesions in childhood ALL (data from clinical trial P9906) occur preferentially at genes bound by AID in normal B cells.
	0.56	RAG1-RAG2 activities in parallel at the single-cell level, we monitored mAID-GFP and de novo surface expression of Igkappa light chains after RAG-mediated Vkappa-Jkappa gene rearrangement (Fig.4a, Supplementary Fig. 3b).
	0.52	RAG1, RAG2 and AID promotes clonal evolution towards pre-B ALL
25707801	0.97	RAG1, which has been accurately mapped to the interface with RAG2 .
	0.96	RAG1/RAG2 complexes.
	0.96	RAG1/RAG2 (both long and short forms) complexed with DNA from Superdex-200 (S200) in a low salt buffer (50mM HEPES 7.0, 60 mM KCl, 1mM maltose and 2 mM DTT).
	0.96	RAG2 that interact with RAG1 are labeled.
	0.94	RAG1-RAG2 protein complex (RAG1/2) initiates this site-specific recombination by cutting DNA at specific sites flanking the coding segments.
	0.94	RAG1 and RAG2 have been characterized .
	0.94	RAG2 (1-387) and two further truncated RAG2 variants (1-351 and 1-367) were constructed with a non-cleavable N-terminal MBP tag and co-expressed with the tag-less core RAG1.
	0.93	RAG1 and RAG2.
	0.93	RAG1 and RAG2. (a) One side of the doughnut-shaped RAG2 interacts with the preR, RNH and ZnC2 domains of RAG1 (color-coded as in Fig. 3).
	0.86	RAG1 and RAG2, of 1040 and 527 residues, cooperate in all their known activities.
	0.79	RAG1 chains are shown in blue and green ribbon diagrams, and both RAG2 subunits are shown in magenta.
	0.77	RAG2, the major S200 eluant peak came out at the same time point and contained RAG1, RAG2 (1-351 or 1-387) and HMGB1 proteins, as shown in the SDS gel (right insert), as well as 12 and 23RSS oligonucleotides, as confirmed by a TBE-Urea gel stained by SYBR-Green (left insert).
	0.68	RAG1 and RAG2 is shown as an open book.
	0.65	RAG1/2 complex may explain why many mutations in the RAG1 and RAG2 interface impact DNA cleavage.
	0.59	RAG1 and RAG2 genes , RSS-dependent DNA cleavage by purified RAG1/2 has been reconstituted .
19396172	0.97	RAG1/RAG2/HMGB1.
	0.96	RAG1 and RAG2, which form the core of the recombinase machinery.
	0.95	RAG1 and RAG2, respectively, have yielded to structure determination, but they offer little direct information about DNA recognition and cleavage as they are outside of the core regions.
	0.95	RAG1 core hybrid protein (see Methods), substantially reduced 12RSS binding by RAG1/RAG2 as assayed by gel shift (Fig. 5a,c).
	0.95	RAG1/RAG2/HMGB1.
	0.95	RAG1 and HMGB1 in the absence of RAG2 supported substantial energy transfer, which again was strongly dependent on the nonamer but not the heptamer.
	0.95	RAG1 proteins contained RAG2, and the positions of the free and bound substrates are indicated with diagrams.
	0.94	RAG1-RSS interaction to the nonamer, while contacts in the heptamer and spacer are more dependent on RAG2 and HMGB1/2.
	0.75	RAG1, RAG2, and HMGB1, as indicated below the bars, with the A substrate pair, or the A substrate pair with mutant nonamer (NONmut), or mutant heptamer (HEPmut) sequences.
	0.59	RAG2, HMGB1/2, and other domains of RAG1, consistent with many previous studies of DNA binding by the RAG proteins.
	0.58	RAG1, we tested all of the mutants for their ability to interact with RAG2 using a GST-RAG2 pull-down assay and found that all of the RAG1 core mutants exhibited wild-type ability to interact with RAG2 (Supplementary Fig. 4).
	0.58	RAG1 proteins contained RAG2 and HMGB1.
	0.54	RAG1, with RAG2 and HMGB1/2 functioning as its co-factors.
18234093	0.97	RAG2 and a single RAG1 dimer is preferentially formed at physiological temperature.
	0.96	RAG1 in developing lymphocytes is complexed with RAG2, or if there is a separate pool of free RAG1.
	0.96	RAG2 protein levels, but not RAG1, are cell cycle regulated, with increasing degradation occurring at the transition from G1 to the S phase.
	0.96	RAG1 in the absence of RAG2.
	0.96	RAG1 subunits may be associated in a way that shields both the RSS and RAG2 binding sites.
	0.95	RAG1 dimer is preferentially stabilized over higher order oligomers in the presence of RAG2.
	0.93	RAG1 and RAG2, which is directed to appropriate DNA cleavage sites by recognition of the conserved recombination signal sequence (RSS).
	0.93	RAG2 at 37 C, the preferentially stabilized V(D)J recombinase:RSS complex contains a single dimer of RAG1.
	0.93	RAG2 and a single dimer of RAG1, in contrast to lower temperatures where multiple protein-DNA complexes were formed.
	0.93	RAG1:RAG2:RSS complexes 1 and 2 (in Figure 7A) as GST-core RAG2 bound to the 2-subunit and 4-subunit MCR1:12-RSS complexes, respectively.
	0.61	RAG2 could bind to both the 2-subunit MCR1:12-RSS and the 4-subunit MCR1:12-RSS complexes following incubation at 25 C. Since these complexes may be due to either one or two active RAG1 dimers bound to the 12-RSS, we asked if both of these complexes may be relevant to RAG1 function at 37 C. Here, we monitored the formation of the MCR1:RAG2:12-RSS complexes as a function of temperature.
	0.53	RAG1 preferentially interacts with the RSS, RAG2, and catalyzes DNA cleavage
23293004	0.97	RAG1 and HMGB1, and optimal in the presence of RAG2.
	0.97	RAG1-RAG2-HMGB1-23RSS (23SC) complex (yellow), as determined by Swanson, and sites of DNAse I hypersensitivity in the signal end complex (magenta).
	0.96	RAG1 and in and around the heptamer, probably by both RAG1 and RAG2.
	0.96	RAG1 and HMGB1, in the absence of RAG2, are able to synapse two RSSs in a manner that is strongly dependent on the nonamer but not the heptamer, raising the possibility that the FRET detected with 23RSSdR2a in the absence of RAG2 was due to trans interactions.
	0.96	RAG2 indicates that RAG1 and HMGB1 are capable of bending the 23RSS in such a way that the interfluorophore distance is reduced from 170-180 A to <90 A.
	0.96	RAG1/RAG2/HMGB1, well above the concentrations used in the standard FRET reaction (125/250/185 nM).
	0.95	RAG2; bar 11, omission of RAG1.
	0.94	RAG1, RAG2, HMGB1, the nonamer and heptamer, Mg2+ and partner 12RSS:everything known to be required for formation of a cleavage competent PC:argues that energy transfer derives primarily from active complexes.
	0.90	RAG1 and RAG2 (together referred to as RAG), which interact with one another and perform DNA binding and cleavage functions to initiate V(D)J recombination.
	0.87	RAG1 and RAG2 generate DNA double strand breaks within a paired complex (PC) containing two complementary recombination signal sequences (RSSs), the 12RSS and 23RSS, which differ in the length of the spacer separating heptamer and nonamer elements.
	0.78	RAG2 or the heptamer, together with these prior observations, suggest that RAG1 and HMGB1 interactions with the nonamer and nonamer proximal spacer, likely together with interactions at other locations on the DNA, are able to induce a large bend in the DNA.
	0.58	RAG1, RAG2 and HMGB1/2 is represented as the green shape, V and J coding segments as rectangles and the 12RSS and 23RSS as red and blue triangles, respectively.
26548953	0.97	RAG1-RAG2 monomer from SEC and later refitted directly with the mRAG1-RAG2 dimer from the crystal structure.
	0.96	RAG1-RAG2 Complex Structures
	0.96	RAG1 and RAG2) (Figure 1A).
	0.96	RAG1 from one RAG monomer and RAG2 from the symmetric RAG monomer and between the two RAG1 subunits (Figure 3F), which are completely absent in Apo-RAG.
	0.96	RAG1-RAG2 monomer interacts with one coding end DNA chain exclusively.
	0.96	RAG1 and RAG2, respectively.
	0.95	RAG1-RAG2 interaction is mostly mediated by polar contacts between the alpha15 helix in RAG1 and the alpha1 helix and the beta27-beta28 loop in RAG2 (Figures 3F, S3A, and S3B).
	0.91	RAG1 (light green and light cyan), RAG2 (green and cyan), and HMGB1 (orange) are represented as cartoons.
	0.89	RAG1-RAG2 monomers is dramatically different from that in the Apo-RAG (Figure 3D).
	0.81	RAG1-RAG2 complex (Apo-RAG) containing RAG1 (271-1031) and RAG2 (full-length) (Figure 1A), its complex with 12-RSS and 23-RSS signal ends (SEC) in the presence of Mg2+, and its complex with paired, nicked 12-RSS and 23-RSS intermediates (PC) in the presence of Ca2+, which was reported to inhibit RSS cleavage by RAG (Figure 1B).
	0.80	RAG1 and RAG2 from different vertebrate species using both insect and mammalian cell expression systems.
	0.74	RAG1-RAG2 monomer from the mRAG1-RAG2 crystal structure, the NBD of RAG1 in the PC exhibits a dramatically different orientation (Figure 3B).
29477728	0.97	RAG1 and RAG2 in a total of 692 PID patients from two separate cohorts, one from the United Kingdom (UK) and one from Austria (Vienna).
	0.97	RAG1/RAG2 to calculate the activity % of WT with mean +- SEM shown in Table 1.
	0.94	RAG1 and RAG2.
	0.93	RAG1 and/or RAG2 mutations (Table E3).
	0.93	RAG1 and RAG2 proteins with residual recombination activity in these patients likely provides antibody repertoire that may be sufficient during early childhood but immunodeficiency and progressive autoimmunity becomes apparent towards early adolescence.
	0.91	RAG1 and RAG2 proteins normally required for catalyzing V(D)J recombination events are shown in Table E2.
	0.91	RAG1 mutations in non-core and the catalytic RNase H (RNH) domain while presenting with CID-G/AI, and patients 6 and 7 (Table E1) reported as CID-G/AI due to compound heterozygous core/plant homeodomain (PHD) and homozygous core RAG2 mutations, respectively.
	0.88	Recombination-activating gene 1 (RAG1) and RAG2 encode lymphoid-specific proteins that are essential for V(D)J recombination and diversification the T and B cell repertoire in the thymus and bone marrow, respectively.
	0.86	RAG1 and RAG2; variants identified in non-coding regions were not expected to affect protein expression or function.
	0.86	RAG1 and RAG2.
	0.86	RAG1 and RAG2 adapted from Notarangelo et al. 2016 (ref E19).
	0.61	RAG1 and RAG2, respectively.
30800289	0.97	RAG) 1 and RAG2 initiate the molecular processes that lead to lymphocyte receptor formation through VDJ recombination.
	0.97	RAG1/ RAG2 cause the most profound immunodeficiency syndrome, severe combined immunodeficiency (SCID).
	0.97	RAG1 or RAG2 abolish the initiation of antigen receptor recombination, which prevents the progression of T- and B-lymphocyte progenitors beyond the DN3 and pre-B-1 stage of development, giving rise to a T-B-natural killer cell (NK)+ SCID phenotype .
	0.97	RAG1 or RAG2 severely disrupt the function of the recombinase proteins but permit occasional recombination events that maintain partial V(D)J recombination activity and lead to the expansion of oligoclonal T-lymphocyte populations .
	0.97	RAG1 or RAG2 disrupt the function of RAG endonucleases profoundly and result in complete failure to initiate antigen receptor V(D)J re-arrangement, which causes failure of progression of T- and B-lymphocyte progenitors beyond the DN3 and pre-B-1 stage of development.
	0.96	RAG) 1 and RAG2 encode endonuclease proteins, which are critical to initiate the molecular processes that lead to lymphocyte receptor formation.
	0.96	RAG1 or RAG2 .
	0.96	RAG1 and RAG2, which randomly incise DNA at highly conserved sequences of DNA (recombination signal sequences) that flank all variable (V), diversity (D), and joining (J) coding regions, initiate T-lymphocyte receptor gene segment re-arrangement in the thymic cortex, enabling the assembly of interspersed V(D)J gene elements, a process known as V(D)J recombination.
	0.95	RAG1/ RAG2 completely annul this process and abrogate T- and B-lymphocyte receptor formation, leading to the most profound immunodeficiency syndrome, severe combined immunodeficiency (SCID).
	0.94	RAG1 or RAG2.
	0.94	RAG1 or RAG2 is estimated to be much higher than is accounted for by the number of SCID or Omenn syndrome patients , suggesting that many more older patients with less-severe clinical manifestations, including combined immunodeficiency, autoimmune cytopenias, organ-specific autoimmune disease, and antibody deficiency, are yet to be identified.
	0.84	RAG1 or RAG2 , which permits some V(D)J recombination in less-severe mutations and permits the formation of a few T-lymphocyte clones which experience impaired positive and negative selection as they pass through the disrupted thymic structure.
25849362	0.97	Rag1-Rag2 complex formation, DNA binding, or RSS nicking; those that exhibit wild-type V(D)J cleavage activity in vitro but impaired V(D)J recombination in vivo:for example, mutants that are impaired in chromatin-binding or in rejoining the broken DNA ends generated during V(D)J cleavage.
	0.92	Rag1 and Rag2 genes.
	0.87	Rag1 or Rag2 genes, the protein products of which are critical members of the cellular apparatus for V(D)J recombination.
	0.84	Rag1 and Rag2.
	0.80	Rag1 and Rag2 initiate V(D)J recombination by cleaving DNA to generate double-strand breaks consisting of two hairpinned coding ends and two blunt signal ends.
	0.72	Rag1, Rag1V779M, or Rag1R142*, plus both full-length Rag2 and an exogenous recombination substrate to detect either signal joints (pGG49) or coding joints (pGG51).
	0.66	Rag1 and Rag2, or rarely by mutations in the NHEJ factor Artemis, in the IL-7 receptor alpha chain or in the RNase mitochondrial RNA processing (RMRP) gene.
	0.60	Rag1 and Rag2 mutants can confer susceptibility to Omenn Syndrome by impairing the post-cleavage stage of V(D)J recombination.
	0.55	Rag1 and Rag2.
	0.53	Rag1 and core Rag1V779M in the presence of recombinant full-length Rag2 and resolved by denaturing polyacrylamide gel electrophoresis.
26186701	0.97	recombination activating gene 1 (RAG1) and 2 (RAG2).
	0.97	RAG1 and RAG2 are known to impair V(D)J recombination, thereby causing T-B-NK+ severe combined immunodeficiency.
	0.96	RAG1 and RAG2 form the recombinase complex which binds and cleaves specific recombination signals that flank VDJ regions.
	0.96	RAG1 and RAG2 are tightly regulated, with two major peaks of expression occurring during T cell development, first in the double negative stage during TCR beta gene recombination, and subsequently in the double positive stage when the TCR alpha chain genes are rearranged.
	0.95	RAG1 and RAG2 have been reported to cause a T-B-NK+ type of severe combined immunodeficiency.
	0.94	RAG1 and RAG2 are known to cause a T-B-NK+ form of severe combined immunodeficiency.
	0.89	RAG1 and RAG2 has led to an expansion of the spectrum of disease to include Omenn syndrome, early onset autoimmunity, granuloma, chronic cytomegalovirus- or EBV-infection with expansion of gamma/delta T-cells, idiophatic CD4 lymphopenia and a phenotype resembling common variable immunodeficiency.
	0.87	RAG1 or RAG2 in the two patients described.
	0.83	RAG1/RAG2 is conserved throughout evolution.
	0.73	RAG1 (D) Schematic depiction of RAG2.
16004728	0.97	RAG-1 and RAG-2 protein complex.
	0.97	RAG-1/RAG-2 described in animals other than humans.
	0.96	RAG-1 and RAG-2 were first discovered when these authors attempted to identify the 'recombinase' responsible for V(D)J recombination.
	0.96	RAG-1 and RAG-2, it will be necessary to increase the number of full-length genes and proteins in the databases.
	0.95	RAG-1 (residues 384-1040) and RAG-2 (1-387), respectively.
	0.95	RAG-1 and/or RAG-2 genes.
	0.91	RAG-1 and RAG-2 genes are mapped in the same chromosome, separated by only a few kilobases and placed in opposite orientation to each other.
	0.80	RAG-1 and RAG-2 have been used to study phylogenetic relationships in deep nodes.
	0.55	RAG-1 and RAG-2 can be (at least for now) considered as 'perfect' orthologues, which adds another advantage of using them as molecular markers in phylogenetic studies.
30565244	0.97	RAG 1 and RAG2 proteins
	0.97	RAG2 core region folds in a six-bladed beta-propeller associates with the RAG1 domains downstream of the DDBD, creating the arms of the Y structure.
	0.96	RAG1 and RAG2 protein sequences are not related to each other.
	0.96	RAG1-RAG2 interaction and recombination signal recognition and cleavage.
	0.96	RAG1/RAG2 core proteins have revealed a Y shaped structure, with the RAG1 NBD dimer forming the stem of the Y, while additional regions along the central and C terminal region of RAG1 act as DNA-binding surfaces for the RSS heptamer and coding flank.
	0.94	RAG1 and RAG2 and suitable recombination substrates in which recognition of RSS by the RAG complex would allow DNA recombination and expression of antibiotic resistance genes or alternatively generation of coding and signal joint recombination products that can be identified by polymerase chain reaction amplification.
	0.92	RAG1 and RAG2, that recognizes and binds to a pair of RSSs, introducing a DNA double strand break at the junction with the coding gene segment.
	0.89	RAG1 (hRAG1) or hRAG2.
	0.81	Rag1 or Rag2 genes by homologous recombination leads to a lymphoid arrest at a stage prior to the recombination of the antigen receptor loci, corresponding to double negative 3 (DN3) and pre-B cells along T and B cell development, respectively.
22434887	0.97	RAG1 and RAG2 proteins, the RAG post-cleavage complex (PCC) may coordinate with either classical NHEJ or alternative NHEJ machineries for end resolution.
	0.97	RAG1 and RAG2 mutants have been suggested to alter PCC stability.
	0.97	RAG1-RAG2 to the 12RSS substrate.
	0.96	RAG1 and RAG2 mutants have features that resemble joints made by cells defective in NHEJ, like junctions with excessive nucleotide deletions and/or increased frequency of microhomologies.
	0.94	RAG1/RAG2 composition, sequence variations of the RSS and coding flanks have also been found to modulate PCC stability.
	0.89	RAG1-RSS interaction compared to Kd 25 nM in the RAG1/RAG2-RSS interaction, although the affinity determined here by anisotropy is slightly higher than the one obtained by EMSA.
	0.86	RAG1 and RAG2), to generate blunt-ended signal ends (SEs) and covalently sealed hairpin coding ends (HP-CEs).
18722175	0.97	RAG1/core RAG2, full-length RAG1/core RAG2 and core RAG1/full length RAG2 are adjusted to have the same amount of RAG1, and compared for coding joint formation.
	0.96	RAG1/core RAG2 complex was tested for signal joint formation in our biochemically defined system, with the addition of ubiquitination components with or without a proteasome fraction.
	0.94	RAG1/core RAG2 is capable of mediating signal joint formation in cellular V(D)J recombination assays.
	0.93	RAG1/core RAG2 and core RAG1/FL RAG2 showed comparable coding joint efficiency to core RAG1/core RAG2, and the pattern of coding joint products was also indistinguishable (Fig. 2D, lane 1 versus lanes 3 & 4).
	0.78	RAG1, RAG2 and TdT, whereas HMGB1, Ku70/86, Artemis, DNA-PKcs, pol mu, pol lambda, XLF, XRCC4, and DNA ligase IV are present in all vertebrate somatic cells.
	0.75	RAG1, RAG2, HMGB1, Ku70, Ku86, DNA-PKcs, Artemis, polymerase mu, polymerase lambda, TdT, XRCC4, DNA ligase IV and XLF.
19324890	0.97	RAG1 in the context of the RAG1/RAG2 complex situated on an RSS.
	0.92	RAG1 plus RAG2 do not recruit GMEB1-VP16 (line 5).
	0.89	RAG1 and RAG2 binding to the RSS.
	0.72	RAG1 protein (absent VP-16), coupled with RAG2, binds the RSS elements (line 4).
	0.55	RAG1 and RAG2 to address the occupancy of the RAG protein complex on DNA.
	0.53	RAG1 and RAG2 coexpression.
19524534	0.97	RAG1/RAG2 complex, and the rejoining phase done by the nonhomologous DNA end joining (NHEJ) pathway, which is required for the repair of general double-strand DNA breaks (DSBs).
	0.96	RAG1/GST-core RAG2 (1-387 a.a.), or MBP-full-length RAG1/GST-core RAG2, were also used (Suppl.
	0.93	RAG2 polypeptide of the RAG1/RAG2 complex binds to the histone H3 modification, trimethylated lysine 4 (H3K4me3), and in some manner increases V(D)J recombination.
	0.92	RAG1/full-length RAG2 (hereafter designated c/f) showed 3.3-fold stimulation of RSS cleavage (Fig. 2C, lane 16).
	0.90	RAG2 tagged with maltose binding protein (MBP) was co-expressed with glutathione-S-transferase (GST)-tagged core RAG1 (384-1008 aa) in 293T cells and affinity-purified with amylose resin.
	0.87	RAG1, RAG2 and HMGB1 form a complex (hereafter designated the RAG complex) that stably binds to DNA substrates containing a 12/23 RSS pair (synaptic complex) in the presence of divalent cations.
21655267	0.97	RAG1 and RAG2 promoters, the RAG gene has also other regulatory elements, such as the proximal enhancer (Ep), the distal enhancer (Ed) and the RAG enhancer (Erag).
	0.95	Recombination activating gene 1 (RAG1) and RAG2, which are essential enzymes for initiating variable-diversity-joining segment recombination, have also been found to be expressed in cancer cells.
	0.95	RAG1 and RAG2 proteins together were found to be sufficient to cleave recombination substrates in cell free systems.
	0.91	RAG1 and RAG2 expressions (Figure 4).
	0.86	RAG1 and RAG2 in these cancer cell lines (Figure 2).
	0.66	RAG1 and RAG2 in MCF-7 cells.
22201127	0.97	Rag1 and Rag2 as indicated.
	0.96	Rag1 and Rag2 mRNA transcripts in RAG1-GFPhigh cells infected with a Gfi1B-ER construct and treated (+) or not (-) with tamoxifen (4-OHT) for 12 h. Numbers 1-3 indicate biological replicates.
	0.96	Rag1 and Rag2, that showed significant differences in transcript levels (P < 0.01) when Gfi1b-ER-expressing cells were exposed to tamoxifen for 12 h, as measured by an ANOVA statistical test (; Fig. 4 A).
	0.94	Rag1 and Rag2 transcripts relative to HPRT in RAG1-GFPhigh cells infected with a retroviral Gfi1b-ER construct and treated (+) or not (-) with tamoxifen (4-OHT) for 12 h in the presence (+) or absence (-) of the DNA replication inhibitor aphidicolin.
	0.92	Rag1 and Rag2 transcripts were expressed at higher levels in Gfi1b-/- cells compared with their WT (Wt) counterparts in pools of Abelson-transformed mutant cells (Fig. 6 A).
	0.90	Rag1 and Rag2 proteins.
25400915	0.97	Rag1, Rag2, E2A, Pax5 and EBF1 using Taqman based Real-Time PCR.
	0.97	Rag1 and Rag2 mRNAs level was evaluated by RT-PCR as a ratio to 18S mRNA expression and the differences were compared using Student's t-test (**P < 0.01).
	0.95	Rag1 and Rag2 gene expression was up regulated (+130%, P < 0.01 and +251%, P < 0.01, respectively) following pre-BCR crosslinking, whereas in the presence of U0126 the pre-BCR-induced Rag1/Rag2 down-modulation remained unchanged (Fig. 5C).
	0.93	Rag1 and Rag2 expression (-66% P < 0.01 and -28%, P < 0.05, respectively; Fig. 4A).
	0.88	Rag1, Rag2, E2A and Pax5 transcripts occurred in a PI3K-dependent manner.
	0.64	Rag1, Rag2, Pax5 and E2A expression in a PI3K-dependent manner.
27293192	0.97	RAG1-like and RAG2-like genes.
	0.97	RAG1 and RAG2 proteins (referred to collectively as RAG), which form a complex that excises the DNA between the V, D, and J gene segments.
	0.97	RAG1 (G) and RAG2 (H) protein homologs.
	0.84	RAG1-like and RAG2-like proteins.
	0.82	RAG1 and RAG2 in the vertebrate and the sea urchin RAG-like loci (Figure 2C).
	0.76	RAG1 and RAG2 genes flanked by RSS-like TIRs, was the source of jawed vertebrate RAG genes and was responsible for creating the initial split antigen receptor gene.
29734775	0.97	RAG1 or RAG2 genes, autoimmunity associated with expansion of oligoclonal T cells and production of autoantibodies is also often observed in affected patients.
	0.96	RAG1 or RAG2 gene is genetically inactivated have contributed greatly to the understanding of SCID caused by the loss of function mutations in the RAG genes.
	0.93	RAG1 and RAG2 proteins have functional domain structures that can be divided into core and non-core domains, with the core domains being the minimal region required for catalyzing V(D)J recombination and the non-core domains exerting a variety of regulatory functions, including nuclear import, interaction with other cellular proteins, and protein turnover.
	0.89	RAG1 or RAG2 genes may lead to a failure of V(D)J recombination of Ig and TCR genes and are the prominent causes for severe combined immunodeficiency (SCID), such as Omenn syndrome, a form of primary immunodeficiency characterized by abnormal development of functional T cells and B cells.
	0.75	RAG1 and RAG2 proteins form a heterotetramer that recognizes the Recombination Signal Sequence (RSS) flanking the V, D, and J regions of Ig genes or TCR genes and nicks the DNA to induce the DNA recombination events.
	0.75	RAG1 or RAG2 gene, gene KO animal models alone cannot recapitulate the entire spectrum of genetics and pathologies of these patients.
12615895	0.97	RAG-1/RAG-2 form a complex with the RSS, which is in part stabilized by the interactions between the nonamer binding domain of RAG-1 and the nonamer motif.
	0.97	RAG-1/RAG-2 efficiently introduce a nick at each RSS via a hydrolysis reaction at the heptamer/coding flank border, generating a 3' hydroxyl end.
	0.82	RAG-1, RAG-2, and terminal deoxynucleotidyl transferase (TdT).
	0.78	RAG-1 and RAG-2 together constitute the recombinase.
	0.57	RAG-1/RAG-2, and MRN complex during opening and processing of the hairpin coding ends?
21599978	0.97	RAG2 is predicted to adopt a six-bladed propeller structure and functions to enhance sequence-specific interactions of RAG1 to the RSS, and possibly induce conformational changes in RAG1 to activate DNA cleavage activity.
	0.96	RAG1 and core RAG2 were significantly less efficient in the recombination of both exogenous plasmid substrates and endogenous genetic loci when compared to their full-length counterparts.
	0.86	RAG1 and RAG2 expression in Abelson-transformed pre-B cells, alpha-RAG1 immunofluorescence showed diffuse localization of RAG1 throughout the nucleoplasm, rather than at the nuclear periphery.
	0.71	RAG1 and RAG2.
	0.69	RAG1, like non-core RAG2, plays multiple roles in the recombination reaction and its regulation.
22424479	0.97	RAG1 and RAG 2 genes in SCID patients and the control group (Table 2) and compared them with the clinical phenotypes.
	0.93	RAG1base and RAG2base mutation databases
	0.85	RAG1 and RAG2 proteins are essential for V(D)J rearrangement of the B (BCR) and TCR during T and B cell development.
	0.54	RAG1 or RAG2 represent approximately 10% of all SCID cases and most of them are T-B-NK + SCID.
23325855	0.97	RAG2 core (RAG2c) (Figure 2B), while RAG1c did demonstrate an association with RAG2c (Figure 2B), a well-known RAG1 interaction partner.
	0.97	RAG2 is omitted from the reaction, indicating that RAG1 and HMBG1 are sufficient to induce a large bend in the 23RSS.
	0.97	RAG1, particularly in the absence of RAG2, it is reasonable to consider the possibility that binding of RAG1 is not limited to these antigen receptor loci.
	0.84	RAG2 expression after M phase, a RAG1-HMGB1-DNA complex might be capable of recruiting RAG2 to non-RSS locations throughout the genome, thereby creating the functional V(D)J recombinase complex at off-target sites and providing a pathway for chromosomal translocations.
31075127	0.97	RAG1 affects RAG2 interactions with H3K4me3 since targeting of RAG2 to H3K4me3-modified chromatin is independent of RAG1.
	0.94	RAG1 was present with RAG2 at H3K4me3-enriched sites, and thus we predict RAG1 is proximal with RAG2 to H3K4me3 puncta throughout the nucleus.
	0.73	RAG1 and RAG2 proteins, function by creating DNA double strand breaks at select recombination signal sequences (RSS) that are located at the border of each gene segment in the AR loci.
	0.52	RAG1, yet RAG2 is essential for relieving an autoinhibition of the recombinase through binding to H3K4me3 by a PHD region in the RAG2 noncore domain.
30778343	0.97	RAG1 or RAG2 genes.
	0.97	RAG1 mutations and 1 RAG2 mutation).
	0.91	RAG1, RAG2, ZAP70 gene depending on the immunophenotypic pattern.
31333681	0.97	RAG1 and RAG2 assembles on either a 12- or 23-RSS and subsequently captures a complementary RSS.
	0.95	RAG1 and RAG2), are essential for V(D)J recombination.
	0.78	RAG2 with H3K4me3 via its PHD finger has a further regulatory role, namely to overcome the auto-inhibition of RAG1 cleavage, imposed by RAG2.
20139091	0.97	RAG1 or RAG2, which allow cleavage but hinder the formation of signal joints, coding joints or both, clearly indicating important interactions with both types of DNA intermediates.
	0.78	RAG1 and core RAG2, which we then challenged by incubation at temperatures ranging from 37 C to 70 C. We measured SE release by native polyacrylamide gel electrophoresis.
26742581	0.97	RAG1 and RAG2 work as a heterodimer to generate a wide array of rearrangements in antigen receptors in T and B lymphocytes by rearranging V (variable), D (diversity), and J (joining) gene segments.
	0.77	RAG1 and RAG2 is a site-specific endonuclease responsible for the generation of antigen receptor diversity.
24472623	0.97	RAG1, at a RAG2 interaction site within the catalytic core.
25550426	0.96	RAG1 and HMGB1, in the absence of RAG2, were sufficient for substantial energy transfer with the 12RSSdR2a substrate (Figure 3C and E), a finding that parallels prior results with the 23RSSdR2a substrate.
	0.96	RAG1 and HMGB1 in the absence of RAG2.
	0.94	RAG1/RAG2/HMGB1 complex (black/dark gray shape).
	0.94	RAG2 core is important for RSS binding specificity and critical for catalysis by RAG1, the mechanism by which it facilitates these processes is not known, although its interaction with RAG1 is thought to be important.
	0.94	RAG1 monomers that diverge at the arms ('hooks') of the anchor and make contact with RAG2 monomers, which constitute the tips of the arms (see cartoon representation in Figure 1A).
	0.94	RAG1 was omitted from the reaction performed under SC conditions (RAG+HMGB1); (C-F) RAG2 was omitted from reactions with the fluorophores in cis [panels (C) and (E)] or in trans [panels (D) and (F)] performed under SC conditions (RAG+HMGB1) [panels (C) and (D)] or under PC conditions (RAG+HMGB1 and 23RSS partner DNA) [panels (E) and (F)].
	0.93	RAG1 and RAG2, which together with HMGB1 bind to a recombination signal sequence (12RSS or 23RSS) to form the signal complex (SC) and then capture a complementary partner RSS, yielding the paired complex (PC).
	0.93	RAG1, RAG2 and HMGB1 were maintained at a fixed molar ratio of 1:2:1.6, while PC analysis was similar but included a 3-fold molar excess of unlabeled 23RSS with respect to RAG1.
	0.93	RAG1, RAG2 and HMGB1, respectively) are below the concentrations required to reach plateau levels of diffusion time, indicating that the FRET assays were performed under non-saturating, dynamic equilibrium conditions.
	0.92	RAG2 does not bind DNA by itself, the RAG1-RAG2 complex has higher affinity and specificity for the RSS than does RAG1 alone.
	0.79	RAG1 and RAG2 (together referred to as RAG) and high mobility group box protein HMGB1 (or 2), in a process called V(D)J recombination.
	0.67	RAG1 and two subunits of RAG2 (Figure 1A, schematic diagram).
	0.59	RAG1-RAG2-12RSS complex lacking HMGB1 (Figure 4C).
	0.53	RAG1-RAG2-HMGB1-12RSS (12SC and PC)complexes (yellow) and the site of DNAse I hypersensitivity (pink, with arrow) in the 12SC, as determined by Swanson. (C-F) Ribbon diagrams showing a superposition of the models of the 12RSS in the SC and the PC from four orthogonal perspectives of the 'front' view in (A) and (B), with the SC in blue (heptamer in dark blue) and PC in pink (heptamer in red).
11257142	0.96	RAG1 and RAG2 to the RSSs.
	0.93	RAG1, and RAG2 (Fig. 1 B).
	0.92	RAG1 and RAG2, in BOSC 23 cells, a human embryonic kidney cell line.
	0.91	RAG1 and RAG2.
	0.89	RAG1, and RAG2.
	0.87	RAG1 and RAG2, which recognize the RSSs and introduce double-stranded DNA breaks at the coding signal sequence boundaries 3 4 5.
	0.83	RAG1 and RAG2 alone, rearrangements were not detectable (Fig. 1 B).
	0.80	RAG)1 and RAG2, each have the ability to activate TCR gamma and delta rearrangement in human kidney cells.
	0.80	RAG1 and RAG2 (Fig. 2).
	0.77	RAG1 and RAG2.
	0.61	RAG1, and RAG2 and analyzed by PCR for Vgamma8-Jgamma1.3/2.3 recombination.
9705958	0.96	RAG1, RAG2, lambda-like, and V-preB, and all of these mRNAs are maintained in cocultures of GC B cells and CD40L-expressing fibroblasts (Figs. 2 and 5, a and b).
	0.96	RAG1 and RAG2 downregulation was observed with 10 mug/ml of intact anti-kappa+lambda and as little as 2 mug/ml of Fab'2 fragments of anti-kappa+lambda antibody but was difficult to detect with 10 mug/ml of intact anti-kappa or anti-lambda alone (RAG1 expression was decreased by a factor of 6-8 after treatment with 10 mug/ml of intact anti-kappa+lambda antibody, and up to 20x after treatment with 10 mug/ml of Fab'2 fragments of anti-kappa+lambda; Fig. 5 b).
	0.95	RAG1 1 and RAG2 are essential for V(D)J recombination.
	0.95	RAG1 were also found in centroblasts (20% of the levels in centrocytes by phosphorimaging), but RAG2 was not detected in these cells (Fig. 2).
	0.93	RAG1, RAG2, TdT, lambda-like, and V-preB were not expressed in resting FM B cells or in mixtures of FM B cells and post-GC memory B cells (Fig. 2).
	0.92	RAG1, RAG2, TdT, lambda-like, and V-preB mRNAs in centrocytes are comparable to the levels of these mRNAs found in unfractionated adult bone marrow samples as measured by phosphorimaging.
	0.90	RAG1 and RAG2, B cell progenitors also express a series of other proteins that are developmentally restricted, B cell specific, and required for efficient antibody gene assembly.
	0.90	RAG1, RAG2, and TdT were specifically enriched in centrocytes (Fig. 2).
	0.78	RAG1, RAG2, lambda-like, or V-preB (Fig. 5 a).
25135298	0.96	RAG1-, RAG2-, and E47-expressing vectors (left) or with RAG1-, RAG2-, and RUNX1-expressing vectors (right).
	0.95	RAG1, showed that IP performed with an anti-RUNX1 antibody results in the Co-IP of RAG1, but not RAG2 (Fig. 5 B).
	0.95	RAG1/RAG2/E47-expressing vectors, we observed a nonclassical rearrangement between the upstream Ddelta2-12RSS and the downstream Ddelta3-23RSS, giving rise to Ddelta2-Ddelta3 SJ and elimination of the Ddelta2-Ddelta3 CJ as an episomal circle (Fig. 8, A [left] and B).
	0.93	RAG2, was necessary for RAG1 recruitment (unpublished data).
	0.69	RAG1-RAG2 complex (RAG1/2) which binds to a 12RSS/23RSS pair (12/23 rule) and then introduces double-strand breaks (DSBs) simultaneously at the two coding segment-RSS junctions.
28747913	0.96	RAG1 mutations, 8 RAG2 mutations, 7 JAK3 mutations, 4 DCLRE1C mutations, 4 IL7R mutations, 2 RFXANK mutations, and 2 ADA mutations).
	0.91	RAG1 (n = 7), RAG2 (n = 7), JAK3 (n = 5), DCLRE1C (n = 4), IL7R (n = 3), RFXANK (n = 2), and ADA (n = 1).
	0.91	RAG1, 3 in RAG2, 2 in JAK3, 1 in IL7R, and 1 in ADA).
	0.91	RAG1 mutations, 1 JAK3 mutation, 1 RAG2 mutation, and 1 RFXANK mutations (Table SE3 in Supplementary Material).
19118899	0.96	RAG1 and RAG2 proteins, which together bind DNA sequences flanking the antigen receptor gene segments and introduce double stranded breaks in the DNA.
19731809	0.96	RAG-1 and RAG-2 fragments catalyze RSS-specific nicking and transesterification of DNA substrates in vitro.
20705244	0.95	rag1 and rag2) gene expression leading to enhanced pro-B cell survival and augmented V(D)J recombinase activity.
	0.94	rag1 and rag2.
	0.94	rag1 and rag2 mRNA levels (Fig. 6a).
	0.92	rag1 and rag2 which associate and form the V(D)J recombinase.
	0.85	rag1 and rag2 are also regulated by FoxO1 in B cells.
	0.84	rag1, and rag2 in developing B cells.
	0.80	rag1, rag2 and il7r.
	0.79	rag1 and rag2 in proliferating B cells.
24068669	0.95	Rag1 and Rag2 transcription is repressed by IL-7R and pre-BCR signaling is ill-defined.
	0.95	Rag1, Rag2, and Foxo1, as Ebf1-deficient common lymphoid progenitors (CLPs) display reduced expression of these genes.
	0.94	RAG1 and RAG2 proteins form a complex that binds to conserved recombination signal sequences (RSSs) flanking a pair of Ag receptor gene segments and synchronously generates double-stranded DNA breaks (DSBs) between each RSS and its corresponding gene segment.
	0.87	Rag1 and Rag2.
	0.75	Rag1 and Rag2, and increased chromatin accessibility at the Ig kappa light-chain locus to allow light chain gene recombination and ultimately the assembly of a complete B cell receptor (BCR).
26196452	0.95	RAG1/RAG2 are thought to be segregated to early (RAG1/RAG2) and late (AID) stages of B cell development, respectively, others and we recently showed that the two enzymes could be concurrently expressed during early B-lymphopoiesis.
	0.89	RAG1-RAG2).
	0.78	RAG1-RAG2 can respond to an inflammatory stimulus, such as LPS.
	0.68	RAG1 and RAG2 induce DNA double-strand breaks during V(D)J recombination in pro- and pre-B cells and their role as drivers of pre-B leukemogenesis was recently elucidated.
28783691	0.95	RAG1 and RAG2 genes that affect various domains of the respective proteins.
	0.90	RAG1 and RAG2 genes in humans cause a broad spectrum of phenotypes, including severe combined immune deficiency (SCID) with lack of T and B cells, Omenn syndrome, leaky SCID, and combined immune deficiency with granulomas or autoimmunity (CID-G/AI).
	0.85	RAG1-RAG2 subunit is labeled for explicitness on the side view.
	0.82	RAG1 and RAG2 protein with the mutations of the 12 patients according to the severity of clinical presentation from top to bottom (A).
28769923	0.95	RAG1 and RAG2 mutations in humans are associated with a broad spectrum of clinical and immunological phenotypes, including T- B- severe combined immune deficiency (SCID), Omenn syndrome (OS), atypical SCID (AS), and combined immune deficiency with granuloma and/or autoimmunity (CID-G/A).
	0.94	RAG1 and RAG2) in humans are associated with a broad range of phenotypes.
	0.92	RAG1, 16 RAG2, 11 DCLRE1C, 4 LIG4, and 2 NHEJ distinct gene mutations (Table 1).
20600921	0.95	RAG1/RAG2 bound signal ends can direct strand transfer of the excised element into a "foreign" DNA target in a process equivalent to the integration step in transposition (Figure 2a).
	0.88	RAG1 and RAG2 direct chromosomal breakage at receptor gene loci.
23630348	0.95	RAG1 gene expression, but does not affect RAG2 gene expression (Supplementary Figure 2A).
	0.89	RAG1 and RAG2 may not be sufficient to initiate VH replacement in the EU12 muHC+ cells.
24290284	0.95	recombination-activating gene (RAG) 1 and RAG2 proteins initiate the VDJ recombination process by generating DNA double-strand breaks at the recombination signal sequences (RSSs) that flank the variable (V), diversity (D), and joining (J) gene segments of the immunoglobulin and T-cell receptor (TCR) genes.
	0.95	RAG1 and RAG2 genes result in the T-B- severe combined immune deficiency (SCID) phenotype.
29628308	0.95	RAG1-C and RAG2-D are shown after superimposing RAG2-Ds.
23720659	0.94	RAG1 (A), CMV-RAG2 (B), H2k-RAG1 (C), H2k-RAG2 (D), H2k-RAG2-ERTAM (E) plasmids.
	0.92	RAG1/2 transcription or RAG2 nuclear translocation (Figure 4) Variation in transcription efficiency was achieved by transfection of RAG1/2 expression vectors bearing different promoters, namely H2k or CMV (see Figure 1).
	0.84	RAG1 and 0.7 mug CMV-RAG2 (GFPi + RAG).
	0.79	RAG1 (A,C) and RAG2 (B,D) constructs contain genomic fragments spanning the whole RAG1 (white box) or RAG2 (black box) coding sequences (ATG and stop codons indicated).
23994475	0.94	RAG1 and RAG2 are marked with an asterisk (Student's t-test, unpaired, two tailed, equal variance).
30061602	0.93	RAG1-RAG2)2 endonuclease complex (RAG) is a DDE family member with RAG1 serving as the catalytic subunit (Fig. 1a).
	0.93	RAG1 and RAG2 is mediated by non-specific interactions with sugar phosphate backbones, the dramatic rotation is likely accommodated without a significant alteration of the binding energy.
	0.91	RAG1 and its associated RAG2 in complex with melted RSS and nicked RSS are colored in green and cyan, respectively.
	0.86	RAG1 molecules in the (RAG1-RAG2)2 complex, for a given RSS, we named the RAG1 that also mediates the phosphodiester bond hydrolysis of the RSS the first RAG (or 1st RAG), and the partner RAG1 that only binds the RSS the second RAG (or 2nd RAG).
	0.86	RAG1-RAG2 monomer that binds unmelted RSS (colored as in Fig. 1a) with the crystal structure of Apo-RAG (4WWX, gray) (b), the complex that binds melted RSS (green) (c) and the complex that binds nicked RSS (cyan) (d).
	0.85	RAG1-RAG2 dimer, intact RSSs dissociated from RAG when subjected to purification by gel filtration chromatography.
	0.85	RAG1: light green and light cyan; RAG2: green and cyan; alpha15-alpha16 loop in the 1st RAG1: magenta; beta4-beta5 loop in the RNH of 2nd RAG1: yellow; 12-RSS and 23-RSS: red and orange.
	0.84	RAG1-RAG2 monomer is defined as containing the RAG1 subunit that performs the catalysis on a given bound RSS.
	0.83	RAG1 in the second RAG1-RAG2 monomer (Fig. 6d).
	0.63	RAG1-RAG2 dimer, intact 12-RSS, intact 23-RSS and HMGB1 in an approximate 1:1:1:2 molar ratio (Supplementary Fig. 1b for the 12-RSS and 23-RSS sequences used).
27431763	0.93	RAG1 and RAG2 expression levels were 3.09- and 1.93-fold increased at relapse, respectively.
	0.92	RAG1 and RAG2 based on RSS-motif recognition and chromatin.
	0.91	RAG1 and RAG2 is limited to precursor stages of lymphocytes, the activity of the complex is attenuated during S-phase of cell cycle, and RAG cleavage is directed towards RSS pair containing sequences.
	0.89	RAG1 expression relative to other cases with annotated cytogenetic type (Wilcoxon rank sum test P<2.2e-16, 95% CI 8.6-13.6-fold, Figure 5A) and also high RAG2 expression (Figure 5B).
	0.83	RAG1, RAG2 and AICDA across a transcriptome data set with 1382 pre-B-ALL patients (Figure 5:source data 1, Figure 5).
	0.80	RAG1 (B) RAG2 and (C) AICDA across the pre-B-ALL subtypes (N = 153 BCR-ABL1, N = 153 ETV6-RUNX1, N = 151 hyperdiploid, N = 198 MLL rearrangement, N = 267 other, N = 82 TCF3-PBX1).
27368095	0.93	RAG1-induced rearrangement was very inefficient, and soon afterward a second enzyme, RAG2, was discovered after transfection of cells with genomic DNA that greatly enhanced the rearrangement; luckily, the two RAG enzymes were closely linked which made the experiment with genomic DNA possible.
	0.93	RAG1 has features consistent with several prokaryotic cut-and-paste transposases like Tn10, RAG2 contains elements/domains found only in eukaryotes.
31632441	0.93	RAG1 and RAG2 are, respectively, located at chromosome positions 11p12 and 11p13 and encode for the RAG1 and RAG2 proteins.
	0.86	RAG1 and RAG2 mutations.
22710321	0.93	RAG1 and are marked by H3K4me3 recognized by RAG2 and these activities together impart specificity for promoting restricted DNA cleavage.
28569776	0.93	RAG1 and RAG2) (b).
20015384	0.92	RAG1 and RAG2, play a crucial role in the immune response in vertebrates.
	0.79	Rag1 and Rag2, play an essential role in the host's active immune response to the different pathogens (see and references therein for specific different activity of each protein in the immunological response), starting the process that generates specific receptors on B and T lymphocytes.
29181194	0.92	RAG-1 and RAG-2, bind one RSS from each of the paired gene segments, to form RAG-RSS complexes associated with each signal sequence.
26921311	0.91	RAG1 and RAG2 or an I-Sce1 expression construct as specified.
	0.86	RAG1, and RAG2 ectopic expression in ATM deficient 293T cells, 72 hours after transfection of indicated plasmids.
	0.86	RAG1 and RAG2, or RAG1 and mutant RAG2, and a substrate (depicted in right panel) to detect VDJ coding joints that delete 8 or 9 bp from each end and are joined at a region of microhomology, and thus likely represent joints mediated by a-NHEJ.
	0.53	RAG1 nor RAG2 expression is impacted by co-transfection of the ATM expression plasmid (Fig. 4B).
31058115	0.91	RAG2 E170 is likely important in RAG1/2 dimerization as it contacts an arginine residue in RAG1 (R561).
	0.79	RAG1 and RAG2 are associated with many different immunodeficiencies including T-B-NK+ SCID, Omenn syndrome (OS), leaky SCID (LS) with gammadelta T cell expansion, and combined immunodeficiency with granulomas and/or autoimmunity (CID-G/AI).
	0.68	RAG1 and RAG2 proteins combine to form a heterotetrameric complex which acts as an endonuclease.
	0.60	RAG2 allele with Y277fs will not contribute any recombinase activity as truncation of RAG2 further than amino acid 350 leads to a non-functioning protein that is unlikely to form any complex with RAG1.
23530145	0.90	Rag-1-/- hosts (A) or co-transferred into Rag-2-/- gammac-/- hosts (B&C).
30588215	0.90	RAG1 and RAG2 and subsequent insights into their evolutionary origins.
28179379	0.88	RAG1/2core, we compared chromosomal rearrangements in RAG2core and RAG2-/- TC-Seq libraries.
	0.83	RAG1 and RAG2.
	0.68	RAG2core lacks the C-terminal plant homeodomain, which normally mediates RAG1/2 binding to H3K4me3.
29051008	0.85	RAG1, RAG2 or DCLRE1C, who accounted for 24% of combined immune deficiency cases in the Kuwait National Primary Immunodeficiency Disorders Registry.
	0.75	RAG1 and RAG2 to the recombination signal sequences (RSSs) flanking the variable (V), diversity (D) and joining (J) coding elements of the B cell receptor (BCR) and T cell receptor (TCR) genes and inducing a DNA double strand break, leaving hairpin structure at coding ends.
	0.68	RAG1-RAG2 complex.
	0.66	RAG2, which led to the conversion of guanine (G) to C at position 104 in the cDNA (c.104G>C), causing a change of glycine (G) to alanine (A) at position 35 (p.G35A) in the core region of RAG2, at the interface of the RAG1-RAG2 interacting domains.
22891620	0.84	RAG2) could fit the profile of laterally transferred genes because it has a paralogue:RAG1:and therefore is present in more than one copy.
19317908	0.67	RAG1 dimer and either one (SC1) or two (SC2) molecules of RAG2.
17105341	0.64	RAG1/core RAG2 (D) and core RAG1/full-length RAG2 (E) preparations.
26515615	0.63	RAG1 or RAG2 defects.
18380906	0.56	RAG1 and RAG2 are both necessary and sufficient to support cleavage of isolated RSS oligonucleotide substrates in vitro .
19233873	0.51	RAG1 and RAG2 assembled on long PCR-generated substrates containing RSSs positioned in cis.