Publication for PSMB8 and PSMB9

Species Symbol Function* Entrez Gene ID* Other ID Gene
coexpression		 CoexViewer
hsa PSMB8 proteasome 20S subunit beta 8 5696 [link]
hsa PSMB9 proteasome 20S subunit beta 9 5698

Pubmed ID Priority Text
25749172 0.98 LMP2 and LMP7 nuclear localization, while in liver cells their distribution of LMP2 and LMP7 between the cytoplasm and nucleus was more even.
0.97 LMP2, and LMP7 in these tumors in relation to HPV status, HLA class I expression, each other, and clinical outcome was therefore investigated.
0.97 LMP2 and LMP7 is not always associated with an increased antigen presentation.
0.96 LMP2, LMP7, and LMP10 are subunits of the immunoproteasome, responsible for the processing of proteins to peptides, while TAP1 and TAP2 transport peptides from the cytoplasm to the endoplasmic reticulum.
0.96 LMP2, and LMP7 in TSCC and BOTSCC was found, with the exception of TAP1, to be frequently reduced, irrespective of HPV status.
0.96 LMP2 and LMP7, the expression of all three genes is regulated by interferon-gamma.
0.96 LMP2, and LMP7, we have used commercially available antibodies and we have trusted the manufacturers' descriptions of their specificity.
0.95 LMP2 and LMP7 expression was also associated to HLA class I expression.
0.95 LMP2 nuclear expression in relation to DFS showed a very similar pattern to that of LMP7, although this result was not statistically significant (Figure 2).
0.95 LMP2, LMP7, and LMP10, the decline was likely not due to HPV.
0.94 LMP2 to LMP7.
0.94 LMP2, LMP7, TAP1, TAP2, and HLA class I correlated to clinical outcome in HNSCC.
0.94 LMP2, and LMP7 was absent or weak in a substantial fraction (33-59%) of the tumors, while LMP10 was reduced in even more (87%) of the tumors, whereas TAP1 only had a reduced expression in 9%.
0.90 LMP2 and LMP7 would thus enhance cell survival and proliferation, this way resulting in a poorer clinical outcome.
0.89 LMP2, and LMP7, between 127 and 147 of the 151 included TSCC and BOTSCC samples were stained and evaluated for nuclear and cytoplasmic expression.
0.88 LMP2 and LMP7 expression was correlated to HLA class I expression in HPV-positive tumors.
0.86 LMP2, and LMP7 expression in the HNSCC study by Meissner et al. were also somewhat higher than those presented here, but in line with our data, TAP1 was less frequently reduced than TAP2.
0.84 LMP2, LMP7, and LMP10 expression was absent or weak in 18% to 58% of the tumors, with the least for TAP1 and the most for LMP2 (Table 3).
0.82 LMP2 and LMP7 staining of the stroma and tumor-infiltrating lymphocytes were observed.
0.82 LMP2 and LMP7 was associated with an absence of lymph node metastasis, possibly due to a similar mechanism.
0.79 LMP2, and LMP7 in Tonsillar and Base of Tongue Cancer and Implications for Clinical Outcome1
0.72 LMP7 and possibly LMP2, as well as lower nuclear expression of LMP10 and a higher expression of TAP1 in TSCC as compared to BOTSCC (Table 2, Table 3).
0.64 LMP2, LMP7, and LMP10 also play a role with regard to cell survival and proliferation and protect cells against oxidative damage.
0.59 LMP7, and possibly also LMP2, can potentially be useful together with other biomarkers, including HPV status, for predicting clinical outcome.
0.58 LMP2 and LMP7 were, however, not associated to survival (data not shown).
29980604 0.98 LMP2 (B), and LMP7 (C) by RT-PCR and were normalized to GAPDH gene.
0.97 LMP2 and LMP7 were significantly up-regulated after 24 h of RV16 and RV1B infection as compared with the uninfected control.
0.97 LMP2 and LMP7 at 24 h p.i.
0.97 LMP2 deficiency and LMP7 inhibition on antiviral gene expression during viral infection deserves further investigation.
0.96 LMP2 and LMP7 mRNA levels (Figure 3B and C).
0.95 LMP2 and LMP7, antiviral genes MX1 and OAS1 and viral load were measured.
0.94 LMP2 (beta1i), MECL-1 (beta2i), and LMP7 (beta5i) upon exposure to pro-inflammatory stimuli such as interferon (IFN)-gamma or tumor necrosis factor alpha (TNF-alpha).
0.94 LMP2 and LMP7 expression in primary alveolar type II cells from patients with early stages of COPD.
0.93 LMP2 and LMP7 mRNA.
0.92 LMP2 and LMP7 protein expression (Figure 4B), and increased the viral load (Figure 4C).
0.90 LMP2 and LMP7 proteins (Figure 2D).
0.90 LMP2 and LMP7 expression, which was paralleled with increased viral load.
0.89 LMP2 and LMP7 mRNA and proteins, and IFN-lambda mRNA in HTBE cells.
0.88 LMP2, but not LMP7 mRNA expression (Figure 1D and E).
0.86 LMP2 and LMP7 expression warrants further investigation.
0.86 LMP2 protein, it likely reflects an accumulation of the LMP2 precursor protein including N-terminal amino acids that could not be cleaved by the inhibited LMP7 during proteasome maturation.
0.80 LMP2 subunit might be more involved in the induction of IP during RV infection compared with LMP7.
0.78 LMP2 and LMP7 have putative binding sites of STAT1.
0.73 LMP2 and LMP7 by IFN-lambda.
0.72 LMP2 and LMP7 proteins and representative Western blot images from two subjects.
0.59 LMP2 and LMP7 proteins were significantly increased after 48 h of RV1B or RV16 infection (Figure 1C).
0.53 LMP7 in RV-infected human airway epithelial cells by using the LMP7 inhibitor, we next aimed to assess the specific role of LMP2 subunit against viral infection by leveraging our ALI culture system of LMP2-deficient mTECs.
0.53 LMP2 or LMP7, but this hypothesis needs to be tested in our future experiments.
29073155 0.98 LMP2/LMP7 polymorphism affects susceptibility to numerous cancers.
0.97 LMP2/LMP7 gene single-nucleotide polymorphisms (SNPs).
0.96 LMP2/LMP7 genotyping.
0.96 LMP2/LMP7 polymorphism and the risk of ESCC in the Kazakh population remains unclear.
0.96 LMP2/LMP7 with ESCC risk in population subgroups (Table 3 and Table 4).
0.96 LMP2 /LMP7 and TAP1
0.96 LMP2/TAP1 and mutant LMP7, decreases susceptibility to ESCC in the Kazakh population (OR = 0.37, 95%CI = 0.23-0.59, p<0.001), whereas haplotype E, which includes wild-type homozygous LMP2/LMP7/TAP1, acts as a risk factor to increase susceptibility to ESCC in the Kazakh population (OR = 3.67, 95% CI = 1.85-7.28, p<0.001).
0.96 LMP2 and LMP7 polymorphisms and the risk of ESCC in the Kazakh population was investigated.
0.96 LMP2/LMP7 polymorphisms are associated with the risk of ESCC in the Kazakh population, a Chinese ethnic minority.
0.95 LMP2 R/C+C/C genotype and the wild-type homozygous LMP7 Q/Q genotype exhibited a higher risk of developing ESCC, further illustrating the existence of linkage disequilibrium in LMP polymorphisms.
0.95 LMP2/TAP1 and mutant LMP7, decreased the risk of ESCC in the Kazakh population.
0.95 LMP2 can be considered a risk factor for ESCC and LMP7 as a protective factor against ESCC in the Kazakh population.
0.93 LMP2/LMP7 have been linked to the occurrence, development, and prognosis of many diseases, including viral infection, autoimmune disease, and malignant tumors.
0.91 LMP2 and LMP7, they are transferred into the endoplasmic reticulum (ER) lumen by the transporter associated with antigen processing (TAP) protein, loaded onto MHC class I molecules, and presented to cytotoxic T lymphocytes.
0.89 LMP2, LMP7 and TAP1, and our results indicated that haplotypes A and E were more common in both the patients and control individuals.
0.83 LMP2/LMP7 polymorphism and ESCC in the Kazakh population with respect to clinical pathological parameters (p>0.05).
0.82 LMP2/LMP7 gene on gene expression, the results showed that SNP locus of LMP2 in esophageal tissues affected the expression of LMP2 (p = 1.30x10-7, S3 Fig).
0.75 LMP2/LMP7 polymorphism and HPV infection, though we found no association between these variables.
0.67 LMP2/LMP7 gene polymorphisms in cases and controls
0.66 LMP2/LMP7 and HPV infection in Kazakh patients with ESCC (p>0.05).
0.52 LMP2 plays a role in the growth of multiple myeloma and acute myeloid leukemia but that LMP7 is not associated with these hematological malignancies.
23932981 0.98 LMP2, LMP7 and MECL-1.
0.98 LMP2, LMP7 and MECL-1 cluster into three robust branches, indicating that these three genes from lungfish are counterparts of the same genes from mammals and other tetrapods.
0.98 LMP2 has diverged from the rest of the vertebrate LMP2s since the group formed by elasmobranch, teleost, coelacanth and tetrapod LMP2 sequences does not cluster with its lungfish counterpart 2) Lungfish and shark LMP7 are, in turn, closely related, the coelacanth sequence being closer to the teleost LMP7 and separated from the tetrapod LMP7 group 3) Finally, P. dolloi MECL-1 is more closely related to the coelacanth MECL-1, the other lobbed-fin fish species here analyzed.
0.97 LMP2), 5.5 times lower (LMP7) and 4 times lower (MECL-1) than those found in the kidney.
0.97 LMP2, LMP7 and MECL-1 amino acid sequences showed the presence of a signal peptide and a conserved motif (proteasome beta type 6, 5 and 7 respectively) that characterizes members of the N-terminal nucleophile (Ntn)-hydrolase superfamily (involved in peptide bond hydrolysis).
0.96 LMP2, LMP7 and MECL-1 were observed (Fig 5B).
0.96 LMP2, LMP7 and MECL-1 were constitutively expressed in all the tissues examined with the highest expression found in the kidney and post-pyloric spleen.
0.95 LMP2 and LMP7, closely clusters with the coelacanth MECL-1 sequence and groups with shark and tetrapod sequences whilst teleost MECL-1 form a different group.
0.95 LMP2, LMP7 and MECL-1 expression in both lung and kidney cells indicating an important role of these molecules in immune response against viral infections in lungfish and shedding light on the evolution of lung immunity.
0.93 LMP2, LMP7 and MECL-1 have experienced different evolutionary pressures leading to complex phylogenetic relationships with the rest of the vertebrate immunoproteasome subunits.
0.92 LMP2, LMP7 and MECL-1 was examined in five different tissues (pre-pyloric spleen, post-pyloric spleen, gut, kidney and lung) from healthy fish (n=4) by qPCR.
0.88 LMP2, LMP7 and MECL-1 a phylogenetic tree, using mature peptide amino acid sequences, was constructed using software MEGA 4.
0.87 LMP2, LMP7 and MECL-1 in a sarcopterygian fish, the Nigerian spotted lungfish (Protopterus dolloi)
0.85 LMP2 lungfish (KF241953), human (CAG46457), Xenopus (NP_001079339), trout (ADM95871), zebrafish (NP_571466), coelacanth (ENSLACG00000014279) and shark (AAL59852); LMP7 lungfish (KF241954), human (CAA47026), Xenopus (NP_001084323), trout (BAD89554), zebrafish (AAB87679), coelacanth (ENSLACG00000014047) and shark (BAA10933); MECL-1 lungfish (KF241955), human (CAG33263), Xenopus (NP_001079861), trout (ADM95869), zebrafish (AAI65548), coelacanth (ENSLACG00000013849) and shark (DR783428).
0.56 LMP2, LMP7 and MECL-1 was observed after 4 and 12 h following stimulation.
10662796 0.98 LMP2, LMP7, and MECL-1 are constitutively highly expressed in many cells of lymphoid origin, probably including APCs.
0.97 LMP2 and LMP7, whereas MECL-1 is expressed but not incorporated into the 20S proteasome due to the absence of LMP2 37.
0.97 LMP2 and MECL-1 active site subunits, as the presence of the constitutive subunits in these positions results in a relatively poor antigenic peptide liberation (compare T2 LMP7 and T2 LMP2[/MECL-1]+7 in Table ).
0.97 LMP2 and LMP7 in tumor cells was associated with enhanced immune escape.
0.96 LMP2 and MECL-1 and also, to a lesser extent, LMP7 incorporate interdependently into proteasomes 34 37 48.
0.89 LMP2, LMP7, and MECL-1 with proteasomes changes the cleavage site specificity and enhances the frequency of cleavages, leading to efficient production of HBcAg141-151 CTL epitopes.
0.82 LMP7 influences the structural features of 20S proteasomes, thereby enhancing the activity of the LMP2 and MECL-1 catalytic sites, which provide cleavage specificity.
0.77 LMP2/MECL-1 and LMP7 had only minor effects on the generation of the antigenic peptide, the concerted presence of LMP2, MECL-1, and LMP7 dramatically enhanced the production of the relevant peptides.
0.73 LMP7 for kinetics and relative abundance of peptide fragments generated, we performed time course experiments using proteasomes from T2 LMP2+7 and T2 LMP2+7 T1A transfectants.
0.66 LMP2+MECL-1-containing proteasomes generate none or only low quantities of HBcAg141-151, the proteasome populations containing either LMP7 or LMP7 T1A must be responsible for the efficient production of the antigenic peptide.
0.62 LMP2 in combination with MECL-1 or LMP7 alone was sufficient to induce the production of small amounts of antigenic peptide.
0.60 LMP2 and LMP7 is due to incomplete processing of the NH2-terminal prosequence, which is an autocatalytic process 33.
0.58 LMP2 or LMP2 T1A, each in combination with MECL-1 and with or without LMP7 or LMP7 T1A.
0.51 LMP)2, LMP7, and MECL-1 (multicatalytic endopeptidase complex-like 1), leading to the formation of immunoproteasomes.
24418325 0.98 beta1i protein was suppressed for 58% and 78% after 48 h of PSMB8 and PSMB9 silencing respectively, compared to non-target control siRNA (Figure 6C).
0.98 PSMB8 mRNA expression after PSMB8 siRNA with and without 100 U/ml IFN-gamma for 24h compared to non-target siRNA with and without 100 U/ml IFN-y, (B)PSMB9 mRNA expression after PSMB9 siRNA with and without 100 U/ml IFN-gamma for 24 h compared to non-target siRNA with and without 100 U/ml IFN-gamma.
0.97 PSMB8 and PSMB9 remained significantly (P = 0.03) suppressed for approximately 80%, even after exposure to IFN-gamma, compared to non-target siRNA (Figure 6A-B).
0.97 PSMB8 and PSMB9 silencing with or without IFN-gamma pre-exposure.
0.97 PSMB8 (beta5i) and PSMB9 (beta1i).
0.97 PSMB8/beta5i-downregulation resulted in a 50% decrease of chymotrypsin-like activity, whereas beta1i downregulation had no effect on any of the three catalytic activities (data not shown).
0.96 PSMB8, but not PSMB9, chymotrypsin-like proteasome catalytic activity significantly (P = 0.03) declined to 50% of its control and remained suppressed after exposure to IFN-gamma (Figure 6D).
0.96 PSMB8 or PSMB9 siRNA with and without 100 U/ml IFN-y for 24 h. Results are the means of 4 separate experiments.
0.95 LMP7) beta1i (LMP2), and beta2i (MECL-1).
0.94 PSMB8 and PSMB9 silencing on IFN-y sensitization of growth inhibition of THP1/BTZ200 cells to (C) bortezomib and (D) ONX 0914.
0.76 PSMB8, THP1/BTZ200 cells became slightly more resistant to bortezomib and ONX 0914, while PSMB9 silencing did not exert any effect (Figure 7A-B).
27098790 0.98 PSMB8, PSMB9, TAP1, and TAP2 genes in the Han Chinese population.
0.98 PSMB8 encodes beta2 subunit of immunoproteasome and shares a similar mechanism on the protein degradation and immune response like PSMB9.
0.97 PSMB8, PSMB9, TAP1, and TAP2 genes at chromosome 6 are located at an adjacent range from 32.859 Mb and 32.821 Mb and involved in the protein degradation and antigen presentation, suggesting a possible LD of the above SNPs with PD patients.
0.96 PSMB8, PSMB9, TAP1, and TAP2 genes in the Chinese population.
0.93 PSMB9 may increase a risk of PD for Chinese female besides other identified SNPs variants in PSMB8, PSMB9, TAP1, and TAP2 genes.
0.90 PSMB8, rs17587 in PSMB9, rs1135216 in TAP1, rs2228391, rs2228396, rs241447, rs241448, and rs4148876 in TAP2, respectively [Figure 1a].
0.90 PSMB8, TAP1, and TAP2 and PD (ii) the rs17587-G at PSMB9 may develop an increased risk of PD for Chinese female population.
0.81 PSMB8, PSMB9, TAP1, and TAP2 genes.
0.66 PSMB8, PSMB9, TAP1, and TAP2
21989738 0.98 LMP2 and LMP7 were up regulated in the CIITA over expression line.
0.98 LMP2 and LMP7.
0.97 LMP2 and LMP7 correlates with the degree of CIITA depletion in these cells (Supplemental Figure 4).
0.95 LMP2 and LMP7 in RD and SJRH30 cells (Figure 6C).
0.94 LMP2 and LMP7 following IFN-gamma stimulation.
0.91 LMP2 and LMP7.
0.83 LMP2 and LMP7 expression has been observed in several types of cancer, including head and neck squamous cell carcinoma (HNSCC) and colorectal carcinomas .
0.74 LMP2 and LMP7, these genes can also be activated by IFN-gamma in a non-CIITA dependent pathway.
22037302 0.98 LMP2 and LMP7 has also been observed in hepatocellular carcinoma.
0.97 LMP2 and LMP7 has been shown to be increased with an enhancement of antigen presentation in these cancer cell lines by expressing IFN-gamma following transfection.
0.94 LMP2, LMP7, and LMP10 can lead to a decrease in MHC class I-restricted peptide presentation, and cause an escape from immune surveillance, leading to cancer.
0.81 LMP2, LMP7, and LMP10 yields more types of peptides expressed on the cell surface.
0.65 beta1i (LMP2), beta2i (MECL1 or LMP10) and beta5i (LMP7) in the immunoproteasome.
0.65 LMP2, LMP7, and LMP10 are interchanged with the three components of the 20S catalytic core to form the immunoproteasome in the instance of IFN-gamma induction.
0.64 LMP2 and LMP7 upon viral transformation of the cell.
19756593 0.98 low-molecular weight protein (LMP) 2, LMP7 and LMP10]; the latter is induced by the action of inflammatory cytokines such as interferon-gamma and TNF-alpha.
0.98 LMP2 and LMP7 in normal renal tubular epithelium.
0.97 LMP2 and LMP7 proteins have been found at different levels in a variety of carcinomas.
0.96 LMP2, LMP7 and LMP10, were found in high-stage carcinomas when compared with low-stage tumors.
0.90 LMP2, LMP7 and LMP10 than low-stage UC.
0.87 LMP2, LMP7 and LMP10, the TAP subunits TAP1 and TAP2, and tapasin.
28129744 0.98 PSMB8 and PSMB9 (proteasome subunit, beta type, 8 and 9) coinciding with previously reported VL susceptibility loci.
0.98 PSMB8 (LMP7) and PSMB9 (LMP2).
0.97 PSMB8, PSMB9 and TAP1 (bold) on chromosome 6 reported previously as potential VL-associated genetic loci.
0.97 PSMB8 (chr6p21.3), PSMB9 (chr6p21.3) and TAP1 (chr6p21.3) overlap with putative VL susceptibility loci.
0.93 PSMB8, PSMB9 and TAP1) described as potential VL-associated genetic susceptibility loci.
0.92 PSMB9, PSMB8, PTPN6, MX1, MX2, IFIT1, TOMM34, IFIT3, SERPING1, NCF4, TAP1 and ISG15) in the VL-blood profile (representing TFs, receptors, kinases, proteases, phosphatases, enzymes and other general proteins) that are significantly "over-connected" with objects both within the VL-blood profile as well as the larger metabase (Table 2).
28438776 0.98 Psmb8 and Psmb9 and the 11S activator subunits Psme1 and Pmse2 were not counteracted by HDAC or STAT1 inhibition, suggesting that key components of the immuno-proteasome were regulated by NFkB and JAK/STAT1 independent pathways.
0.93 PSMB8, PSMB9 and PSMB10 was examined in human islets exposed to a) a combination of IL-1beta and IFNgamma (black bars) or b) only IL-1beta (grey bars) or IFNgamma (black bars).
0.81 Psmb8, Psmb9 nor Psmb10 suggests that IL-1beta upregulates Egr1, also known as Zif268 (zinc finger protein 225) or NGFI-A (nerve growth factor-induced protein A), which are known to suppress the response of the Psmb9 promoter to NFkappaB. Indeed, Egr1 is highly expressed in pancreatic islets and beta cells (2016) and upregulated after 4-8 h by cytokines in INS-1E cells in an NO independent manner, suggesting that the cGMP/cAMP -PKA/G-CREB pathways are not involved in regulating the beta-cell immunoproteasome in contrast to endothelial cells that have a high basal expression of the immunoproteasome.
0.80 Psmb 8, 9 and 10 or double KO of Psmb9 and 10 plus inhibition with ONX 914 to inhibit Psmb8, with consequential risks of transfection artefacts.
0.77 Psmb8, Psmb9 and Psmb10; however, the expression of the constitutive Psmb5, Psmb6 and Psmb7 proteasome components (Fig 2) was not altered.
28718425 0.98 LMP)2, LMP7 and transporter associated with antigen processing 1 (TAP1), pointed towards the idea that NLRC5 may play an important role in immune evasion of cancers.
0.90 LMP2, LMP7 and TAP1..
0.85 LMP2, LMP7 and TAP1.
0.82 LMP2, LMP7 and TAP1.
0.80 LMP2, LMP7, TAP1), was associated with poor survival in melanoma and bladder cancer patients, indicating that abnormal epigenetic changes in NLRC5 within cancer cells significantly impact clinical outcomes.
29240645 0.98 PSMB8 (LMP7), PSMB9 (LMP2) and PSMB10 (LMP10) were analyzed by qRT-PCR.
0.93 LMP7, LMP2 and LMP10 catalytic proteasome subunits, which are encoded by PSMB8, PSMB9 and PSMB10 genes, respectively.
0.92 LMP7, and LMP2.
0.88 LMP7, LMP2 and LMP10 subunits, for example PR-924 and ONX-0914 are LMP7-selective, while carfilzomib and oprozomib actively inhibit both X and LMP7 subunits.
0.67 LMP7 (beta5i), LMP2 (beta1i) and LMP10 (beta2i) after priming with pro-inflammatory cytokines, or LPS with an increase in CT-like and T-like activities.
27634283 0.98 PSMB8, and PSMB9 in both founder mice were further confirmed by using real-time PCR and western blotting, respectively (Fig. 1C,D).
0.92 PSMB8/PSMB9.
0.92 PSMB8, and PSMB9 in splenocytes from WT or hTAP-LMP mice as analyzed by qRT-PCR and normalized to 18S rRNA levels.
0.87 PSMB8, and PSMB9 genes (hTAP-LMP mice) was generated, and we found that reconstitution of the hTAP-LMP gene cluster notably improved human HLA-I antigen presentation and restricted CTL responses.
22612225 0.98 LMP7 to CT-L activity may obscure any effect of LMP2 induction.
0.96 LMP2 expression in resting hepatocytes is consistent with the observation that LMP2 and LMP7 are expressed in the hepatocytes of healthy human adults and children.
0.95 LMP2 inhibitor that does not inhibit the constitutive proteasome, as well as of a specific LMP7 inhibitor IPSI to inhibit IL-1-stimulated down-regulation.
27098648 0.98 LMP7 and LMP2 genes, respectively, encode the Immunoproteasome beta5i and beta1i subunits, while MECL-1 encodes the beta2i subunit.
0.94 beta1i (LMP2), beta2i (MECL-1), and beta5i (LMP7).
0.85 LMP2 were found to play a key role in the development of acute myeloid leukemia and multiple myelomas, whereas polymorphisms within LMP7 were not considered a risk factor.
29451304 0.98 PSMB8, PSMB9, PSMB10 and PSMB2) and appears to contribute to MuOC pathogenesis.
0.97 PSMB8, PSMB9, PSMB10 and PSMB2).
0.92 PSMB 8, PSMB 2, PSMB 9 and PSMB 10.
23181576 0.98 beta1i (LMP2, low molecular weight protein 2, PSMB9), beta2i (MECL1, multicatalytic endopeptidase complex-like 1, PSMB10), and beta5i (LMP7, low molecular weight protein 7, PSMB8), respectively.
27132469 0.97 LMP7 and LMP2, decreased proteasome activity, and enhanced proteasome inhibitor sensitivity in vitro and in vivo.
0.97 LMP7 and LMP2 expression, while its overexpression in MOLP-8 cells reduced their levels (Figure 3B).
0.97 LMP7 and LMP2 in RPMI 8226 (left) and U266 cells (middle) with suppressed TJP1, or in MOLP-8 cells with overexpressed TJP1 (right).
0.97 LMP7 or LMP2 overexpression were treated with vehicle or BTZ for 72 hr.
0.96 LMP7 and LMP2 expression, our data support the conclusion that resistance due to enhanced proteasome capacity is mediated mainly through TJP1 and its effects on EGFR/JAK/STAT3/LMP7/2.
0.96 LMP7 and LMP2 (B) determined by western blotting in RPMI 8226 (left) or U266 cells (right) with Con-shRNA, or a STAT3-shRNA.
0.94 LMP7 and LMP2 levels (Figure 3D) and greater ChT-L activity (Figure 3E), while reintroduction of TJP1 into KO mESCs reduced the ChT-L activity (Figure 3E).
0.94 LMP7 and LMP2 expression, which increases proteasome activity and PI resistance.
0.94 LMP7 and LMP2 (middle).
0.93 LMP7, LMP2, alpha-3, or beta-actin.
0.92 LMP7, LMP2, beta-actin, and alpha-3.
0.91 LMP7 and LMP2, thereby decreasing proteasome capacity.
0.91 LMP7 and LMP2 expression was sufficient to confer resistance by increasing proteasome capacity, and that EGFR/JAK/STAT3 modulated LMP7 and LMP2 levels.
0.85 LMP7 and LMP2.
0.77 LMP7 and LMP2, IGF-1 and IL-6 did not (Figure 6A), and only EGF enhanced proteasome ChT-L activity and, therefore, proteasome capacity (Figure 6B).
0.73 LMP7 or LMP2, and found that this by itself reduced bortezomib sensitivity (Figure 5E).
0.72 LMP7 and LMP2 levels (Figure 5B), which correlated with a reduction in ChT-L activity (Figure 5C).
0.67 LMP7 and LMP2 that are rate limiting, and that the TJP1/EGFR pathway is more important in determining PI sensitivity.
32060274 0.97 PSMB8 and PSMB9 and melanoma patient survival, we analyzed data from TCGA of 472 melanoma patients for whom RNA-seq data and patient outcome were available (Supplementary Table 1).
0.97 PSMB8 and PSMB9 levels.
0.97 PSMB8 and PSMB9 than for those with low levels (P = 0.006, Wilcoxon rank sum test).
0.97 PSMB8 expression and PSMB9 expression highly correlated (Spearman R = 0.81, P < 2.5E-6).
0.97 PSMB8 and PSMB9 (P = 0.03 for PSMB8 and P = 0.06 for PSMB9, Wilcoxon rank sum test), but the expression of the constitutive proteasome subunits showed no correlation (P = 0.5, Wilcoxon rank sum test) (Fig. 5c).
0.97 PSMB8 and PSMB9 and improved survival and enhanced response to immune-checkpoint inhibitors (both anti-CTLA4 and anti-PD1) in melanoma patients.
0.95 PSMB8 and PSMB9 overexpression was found to highly associate with CD4+ and CD8+ T-cell infiltration, regulatory T-cells, NK cells and M1-macrophages (Fig. 1c), in agreement with a role for IP subunit overexpression in enhancing the immune response in the tumor.
0.93 PSMB8 and PSMB9 are overexpressed in melanoma cell lines.
0.93 PSMB8 and PSMB9 expression is associated with better overall patient survival (Fig. 1a, logrank P < 0.005; the signal is robust with different subgrouping of patients, as shown in Supplementary Fig. 1).
0.92 PSMB8 and PSMB9, two major components of the immunoproteasome, is predictive of better survival and improved response to immune-checkpoint inhibitors of melanoma patients.
0.91 PSMB8 (Suc-LLVY-AMC) and a substrate that is specifically cleaved by PSMB9 (Suc-PAL-AMC) (Supplementary Fig. 7).
0.90 PSMB8 and PSMB9 expression, as observed in the TCGA cohort (Spearman R = 0.88, P < 1E-15).
0.84 PSMB8 and PSMB9 expression levels (Spearman R = 0.90, P < 1E-15) and a statistically significant co-occurrence of their overexpression (hypergeometric P < 4.9E-55, see Methods).
0.84 PSMB9 was within the top 1.5% (P < 0.01, Wilcoxon rank sum test) and PSMB8 within the top 4.4% (P < 0.04, Wilcoxon rank sum test) of genes that are significantly associated with durable clinical benefit after treatment with ipilimumab (Supplementary Table 12).
0.77 PSMB8 and PSMB9 can serve as biomarkers for predicting survival of melanoma patients and for identifying patients likely to favorably respond to immune-checkpoint inhibitors.
0.58 PSMB8 and PSMB9 expression levels are much stronger predictors of melanoma patients' immune response to checkpoint inhibitors than the tumors' mutational burden.
23526983 0.97 LMP-2 in 4 of 4 and deficiencies in LMP-7 in 3 of 4 HGB cell lines examined by RT-PCR and Western blot.
0.97 LMP-7 Peptides, and, Rescued Expression of TAP-2, LMP-2 Peptides and the B-7.1 Molecule
0.95 LMP-2 and LMP-7 components of the endogenous antigen presentation pathway.
0.94 LMP-2 and LMP-7 are multiple components of the endogenous, antigen presentation pathway machinery.
0.88 LMP-7, 174 bp; LMP-2, 312 bp; beta-actin, 289 bp except in experiments concerning expression of LMP-2 in which the primer pair for the 618 bp fragment was used.
0.88 LMP-2 and LMP-7 components of the endogenous antigen presentation pathway.
0.87 LMP-7; and D, LMP-2.
0.85 LMP-7, and that rescue in the expression of TAP-2 and LMP-2 occurred when compared to these cell lines cultured in medium minus the IGF-1R mAb.
0.84 LMP-2, LMP-7 and LMP-10 subunits of the proteasomes are inducible by interferon-gama (IFN-gamma).
0.84 LMP-2 and LMP-7, respectively.
0.81 LMP-2 and LMP-7 peptides were demonstrated when down-regulation of IGF-1 by IGF-1 antisense RNA or when blockade of the IGF-1 receptor (IGF-1R) by its monoclonal antibody occurred.
0.75 LMP-7 was enhanced in HG-2 (p<0.001), HG-5 and HG-9 (p<0.05); and, expression in LMP-2 was up-regulated in HG-2 (p<0.001), HG-5 and HG-9 (p<0,05).
0.56 LMP-7 and LMP-2 gene expression respectively.
25098831 0.97 PSMB8 and R = 0.80 for PSMB9.
0.96 PSMB8 and PSMB9 were significantly increased when compared to NIM patients (figure 2).
0.96 PSMB8 compared to actin in the patients with inflammatory muscle diseases and slightly weaker intensities for PSMB9.
0.95 PSMB8 and PSMB9 are higher expressed than expected in the majority of IBM and several of the PM muscle.
0.95 PSMB8, PSMB9 and/or PSMB10 in all investigated cellular subsets except CD4+ (figure 1).
0.94 PSMB8, PSMB9 and PSMB10.
0.89 PSMB8 and PSMB9 relative to beta actin in IM and NIM.
0.88 PSMB8 and PSMB9 proteins were investigated in muscle tissue of representative patients with dermatomyositis (P2 and P3), polymyositis (P9), overlap syndrom (P16) and non-inflammatory muscle diseases (P18, P19, P20, P24).
0.69 PSMB8 and PSMB9 was normalized to corresponding signals of the housekeeping protein beta actin, which was detected in a second staining procedure on the same membrane.
0.68 PSMB8 [0.302+-0.139 and 0.075+-0.041] and about 5-fold increase for PSMB9 [0.049+-0.029 and 0.009+-0.002] but less than 2-fold for PSMB10 [0.065+-0.064 and 0.036+-0.022].
21400024 0.97 LMP2, LMP10, and LMP7.
0.96 LMP2, LMP10, and LMP7 was confirmed by western blot in Figure 6B.
0.95 LMP2 (beta1i), and LMP7 (beta5i), in all three APCs (Figure 6A).
0.94 beta1i (LMP2), beta2i (LMP7) and beta 5i (MECL1, LMP10), which results in proteasomes with higher chymotrypsin-like activity.
0.82 LMP2 (center) and LMP7 (right).
0.74 LMP2, LMP10, and LMP7) in K562 cells.
0.70 LMP2 (beta1i) and LMP7 are poorly expressed in K562 cells in comparison to CD40B cells and dendritic cells
0.52 LMP2 and LMP7.
23554652 0.97 LMP2/LMP7 genes with chronic hepatitis C virus (HCV) infection, and to assess whether LMP2/LMP7 genes could influence the outcomes of HCV infection among drug users.
0.97 LMP2/LMP7 genes with chronic HCV infection.
0.93 LMP2/LMP7 genes may alter the activities of the proteasome and influence the clinical course of hepatitis C. The aim of the present study was to investigate a possible association of the LMP2/LMP7 genes with outcomes of HCV infection and determine whether these genes contribute to the susceptibility to HCV infection as a genetic risk factor among drug users.
0.91 LMP2/LMP7 genes and some diseases.
0.88 LMP2 and LMP7 that can alter the pool of peptides available for class I antigen presentation through enhanced substrate cleavage after basic and hydrophobic amino acid residues compared to the constitutive proteasome catalytic subunits.
0.86 LMP2/LMP7 gene SNPs did not show any deviation from the Hardy-Weinberg equilibrium (all P > 0.05 in controls).
0.84 LMP2/LMP7 and the outcomes of HCV infection among drug users
0.80 LMP2/LMP7 genes which are located in the human MHC class-II DNA-binding protein 1 loci have been shown to be important in the MHC class-I antigen presentation pathway.
25329802 0.97 LMP2 but independently from subunit LMP7.
0.96 LMP2, LMP7, Rpt6 in primary tumor and adjacent tissue.
0.95 LMP2 and/or LMP7 subunits was analyzed on the basis of the expression of these subunits.
0.95 LMP2 subunit in tumor, LMP7 subunit in adjacent tissue and Rpt6 subunit both in tumor and adjacent tissue on the simultaneous effect of the disease stage and factor of ERalpha absence or ERalpha presence, was revealed (Figs. 6 and 7).
0.92 LMP2 and LMP7 to the larger extent in comparison with other cells.
0.82 LMP7 possess chymotrypsin-like (ChTL) activity, subunits Y and LMP2 possess caspase-like activity, and subunits Z and MECL1- trypsin-like activity.
0.78 LMP2 and LMP7.
0.75 LMP2, LMP7 and Rpt6 in these tissues by Western blotting and analyzed the connection of these parameters with clinical-pathological factors.
28536458 0.97 LMP2 and LMP7 and the transporter complex which is composed of the subunits TAP1 and TAP2.
0.97 LMP2 and LMP7.
0.95 LMP2 (light green) and LMP7 (dark green) in 4 MCC cell lines was determined by RT-qPCR in triplicates using specific primers; CT values were normalized to RPLP0 and calibrated to a set of DeltaCTs of MKL-2; relative mRNA expression is depicted as mean + SEM.
0.93 LMP2 and LMP7 mRNA expression is shown in comparison to RPLP0.
0.87 LMP2 and LMP7 as well as TAP1 and TAP2.
0.81 LMP2 and LMP7 to allow the formation of the immunoproteasome.
0.74 LMP2 and LMP7 are simultaneously down-regulated by histone hypoacetylation.
0.66 LMP2 or LMP7 promoter specific primers.
22363101 0.97 LMP2 and LMP7, however, showed high signal intensity of the immunoproteasome proteins, likely reflecting a high concentration of immunoproteasome proteins in the BAL supernatant, in patients with ARDS but not in healthy controls.
0.96 LMP2 and LMP7) and proteasome subtypes by western blot, chromatographic purification, and 2D-dimensional gelelectrophoresis.
0.96 LMP 2 and LMP 7 in the extracellular alveolar space in all ARDS patients but not in healthy controls was associated with a change in the ratio of proteasomal enzyme activities as revealed following purification.
0.87 LMP2 and LMP7 immunoproteasome proteins in the BAL supernatant and also in their cell pellet lysate (Figures 1(a) and 1(b)).
0.87 beta 1i (LMP2), beta 2i (MECL-1), and beta 5i (LMP7) that are incorporated into a newly synthesized intermediate type and/or immunoproteasome.
0.83 beta 1i (LMP2), beta 2i (MECL-1), and beta 5i (LMP7) were detected in the two-dimensional polyacrylamide gelelectrophoresis (Figure 4) confirming the data derived from the western blots.
0.72 beta 1i (LMP2), beta 2i (MECL-1), and beta 5i (LMP7) that are incorporated cooperatively into newly synthesized proteasomes named "immunoproteasome".
21256843 0.97 LMP2, LMP7, MECL-1 or PA28beta.
0.96 LMP2, LMP7 and MECL-1 within the MDB.
0.96 LMP2, B- MECL-1, and C- LMP7 around the mitochondria (green) and FAT10 (Texas red) merged (yellow).
0.95 LMP2 or LMP7 around mitochondria (Fig 2).
0.94 LMP2 and LMP7 were found in the cell nuclei.
0.83 LMP2, LMP7 and MECL-1 cause the formation of the immunoproteasome, and consequently decrease the 26S proteasome activity.
23024775 0.97 LMP2, LMP7, ERAP1, tapasin and ERp57 from normal expression to partial loss or total loss of expression in cervical tissue specimens in Immunohistochemical analysis.
0.92 LMP2, LMP7, Tapasin, ERAP1, CNX, CRT and ERp57) were analyzed by Semi-quantitative RT-PCR in normal uterine cervix tissue, CIN and CSCC.
0.88 LMP2, LMP7, calnexin, calreticulin, ERp57, and tapasin staining shown in Figure S1), Panels A1-C1 depict normal uterine cervix tissue with normal protein expression.
0.82 LMP7, ERAP1, tapasin, and ERp57 protein expression positively associated with HLA-I expression in CIN lesions, whereas ss2-m, TAP1, TAP2, LMP2, LMP7, ERAP1, ERp57, and tapasin expression positively associated with HLA-I in the cancerous lesions.
0.80 LMP2, LMP7, Tapasin, ERAP1, CNX, CRT and ERp57) in cervical cancer.
0.70 LMP2 and LMP7), transporters associated with antigen processing 1 and 2 (TAP1 and TAP2), endoplasmic reticulum aminopeptidase 1 (ERAP1), and the ER chaperone proteins calnexin, calreticulin, and tapasin.
26885372 0.97 PSMB8 [Swiss-Prot:P28062], PSMB9 [Swiss-Prot:P28065], PSMB10 [Swiss-Prot:P40306]) in our database of 55 melanoma cell lines by gene expression array analysis (Fig. 1).
0.96 LMP2 or LMP7) and presence of CD3+ TILs.
0.78 LMP-2, LMP-7 and MECL1 replace the beta1, beta5 and beta2 subunits respectively, resulting in changes in enzymatic activity and production of an altered MHC class I epitope repertoire (reviewed in).
0.71 LMP2 and LMP7 expression was observed, which in all cell lines tested was upregulated following incubation with IFNgamma, (quantified by densitometry analysis, Fig. 2, bottom panel).
0.64 PSMB8 was variable, detected in some cell lines and not in others, while the third IP-specific subunit, PSMB9, was detected in only a few cell lines.
0.56 PSMB8, PSMB9, PSMB10, and thymus restricted subunit PSMB11
27833096 0.97 beta1i/LMP2, beta2i/MECL-1 and beta5i/LMP7 in non-immune cells and the assembly of the so called immunoproteasomes (i-proteasomes).
0.96 beta1i/LMP2 and beta5i/LMP7 into 20S proteasomes in IFN-gamma-treated, HCV-infected cells (Figure 5c).
0.95 beta1i/LMP2, beta2i/MECL-1 and beta5i/LMP7) and standard proteasome subunits (alpha4 and beta5) (d).
0.91 beta1i/LMP2, beta2i/MECL-1 and beta5i/LMP7 (Figure 5d).
0.89 beta1i/LMP2, beta2i/MECL-1 and beta5i/LMP7 at the protein level in a PKR-dependent manner.
0.87 beta1i/LMP2, beta2i/MECL-1 and beta5i/LMP7 in non-infected cells but did not alter the standard proteasome subunit beta5 expression and abundance of the non-replaceable subunit alpha4 (Figure 1b).
28543773 0.97 LMP2, LMP7) while progressively decreasing expression of constitutive catalytic proteasome subunits (beta1, beta2, beta5) and that the loss of constitutive proteasome subunits continues (15 days) beyond the time at which immunoproteasome induction is maximal (9 days).
0.96 LMP7, and LMP2 were significantly increased starting at 10 pg/mL IFNgamma, with significantly enhanced induction observed at 1 ng/mL IFNgamma (Fig 6B,C and Supp.
0.94 LMP7 and LMP2 increased through day 6 and then remained at the same elevated level.
0.93 LMP7 (Fig. 5C) and LMP2 (Fig. 5E) proteins were significantly increased by each of the immune activators (and combinations thereof).
0.86 LMP7 and LMP2 and decreased expression of the corresponding constitutive beta5 and beta2 subunits (Supp. Info.
0.83 LMP7 and beta5, (D) beta2 and (E) LMP2 and beta1 protein expression relative to vehicle after normalization.
27648699 0.97 LMP2 and LMP10, but did not express LMP7 proteasome subunits (Figure 1A, lane 1).
0.97 LMP7 and LMP2 in tolerized (LM), compared to non-tolerized cells (ML) (Figure 4E), and after 24h LPS treatment, all three LMP subunits were downregulated in tolerized THP1 cells (LM and LL; P < 0.05) (Figure 4F).
0.96 LMP7 (Figure 1B) and, in fact, contained proteasomes with immuno-subunits LMP2, LMP7 and LMP10, but no detectable X, Y, or Z subunits.
0.96 LMP7, LMP2, and LMP10 subunits after 4h and 24h of second LPS tolerance treatment in PMA-treated THP-1 cells.
0.84 LMP2 and LMP7, but not LMP10, X, Y, and Z (Figure 1C).
27659694 0.97 PSMB8 and PSMB9 in M5 AMLs were enriched in processes linked to mitochondrial activity and stress responses, respectively.
0.97 PSMB8, PSMB9 and PSMB10.
0.96 PSMB8 and PSMB9 orthologues is to help cells dealing with oxidative and proteotoxic stress.
0.95 PSMB8 for PSMB5, PSMB9 for PSMB6 and PSMB10 for PSMB7.
0.93 PSMB8 and PSMB9 orthologues have been found in invertebrates (who have no adaptive immune system), including the most basal branch of Metazoans:the placozoan Trichoplax adhaerens.
28051153 0.97 PSMB8/PSMB9/PSMB10) to form the immunoproteasome (IP).
0.96 PSMB8, PSMB9 and PSMB10) observed within a BM-MSC network are conserved across datasets representing breast cancer cells and tissue.
0.96 PSMB8, and PSMB9 and is also sensitive to retinoic acid.
0.95 PSMB8 and PSMB9.
0.83 PSMB8, PSMB9 and PSMB10), proteasome activators PSME1 and PSME2 and transporter genes TAP1 and TAP2 across cancer cells, and eight datasets representing breast cancer tumour tissue's.
28622390 0.97 PSMB8, PSMB9 at the RNA and protein level in a wider range of colon and ovarian cancer cell lines and treatment time points than had been described previously.
0.97 PSMB8, and PSMB9 at both the RNA and protein level in the colon and ovarian cancer cell lines.
0.97 PSMB9 (b1i), MECL-1 (b2i), and PSMB8 (b5i) during proteasome neosynthesis.
0.93 PSMB8, CALR, PSMB9/TAP1 (shared promoter), CD58, and TAPBP.
0.75 PSMB8, PSMB9, and TAP1).
30648121 0.97 LMP2, and LMP7 mRNA were quite low.
0.97 LMP2, and LMP7 genes may be insufficiently transcribed in sHCC cells in a coordinate fashion, in part because TAP1 and LMP2 genes are known to share a bidirectional promoter.
0.82 LMP2, LMP7, TAP1, and TAP2 were markedly lower in the sHCC29 and sHCC63 cells than those in the sHCC74 cells.
0.80 LMP2, and LMP7 were determined cytofluormetrically.
0.64 LMP2 was abundantly expressed in all of three cell lines, LMP7 expression was detectable only at a very low percentage of sHCC63 cells (Figure 3(c)).
19065646 0.97 LMP2, MECL1, and LMP7, we compared the expression profile of the various components of proteasome in immature and mature DC cultured in human serum conditioned media and differentiated in the presence of GM-CSF/IFN-alpha and of GM-CSF/IL-4.
0.95 LMP2, MECL1, and LMP7), that replace the corresponding constitutive homologs beta1, beta2, and beta5.
0.95 LMP2-specific mAb SY-1, MECL1-specific mAb TO-6, LMP7-specific mAb HB2, and rabbit polyclonal antisera to PA28alpha or PA28beta were tested in Western blotting with lysates of T2 cells and untreated or Type I/Type II IFN-treated Colo38 melanoma cells (A), with lysates of immature and mature IFNDC and IL-4DC (B), and with components immunoprecipitated by the alpha2-specific mAb from immature and mature IFNDC and IL-4DC (C).
0.93 LMP2 and LMP7 were not detectable, because T2 cells lack the encoding genes (Fig. 4A).
20221424 0.97 PSMB8, PSMB9, TAP1 and TAP2 as well as proteins involved in MHC class I and class II presentation.
0.95 PSMB8, PSMB9) and transporter 1, ATP-binding cassette sub-family B (MDR/TAP) (TAP1) and transporter 2, ATP-binding cassette sub-family B (MDR/TAP) (TAP2).
0.86 PSMB8 and PSMB9 are located next to TAP1 and TAP2 in the class II region and encodes the inducible catalytic components LMP7 and LMP2 of the immunoproteasome, a specialised proteasome complex expressed upon stimulation with inflammatory cytokines.
0.65 PSMB8, PSMB9, TAP1 and TAP2 and their interaction partners outside the HLA ( Figure 3B and C and Table 4 ).
24304442 0.97 beta1i (LMP2), beta5i (LMP7).
0.97 beta1i/LMP2 and beta5i/LMP7.
0.97 LMP2 and LMP7.
0.67 beta1i/LMP2, beta5i/LMP7 and LFA-1 activation of T cells by the calcium ionophore A23187 and CaCl2 results in increased generation of microparticles (Figs 2E and 4A).
25528575 0.97 LMP2 and LMP7 encode LMP.
0.94 LMP2, and LMP7 were associated with outcomes of HCV infection.
0.91 LMP2, LMP7, HLA-DMA, HLA-DMB, HLA-DOA, and HLA-DOB,.
0.83 LMP2, LMP7, and tapasin) in a Chinese population of paid blood donors with high risk of HCV infection.
29587858 0.97 beta1i (PSMB9, LMP2), beta2i (PSMB10, LMP10) and beta5i (PSMB8, LMP7).
0.95 PSMB8 (LMP7), PSMB9 (LMP2) and PSMB10 (LMP10) genes upon stimulation with INFgamma or TNFalpha.
0.94 PSMB8 (LMP7), PSMB9 (LMP2), PSMB10 (LMP10) from the immunoproteasome (blue) are depicted to estimate expression of the respective proteasome type across different tissues.
0.87 PSMB8 (LMP7), PSMB9 (LMP2) and PSMB10 (LMP10) in immune privileged tissues such as retina (2 RPKM), muscle (3 RPKM), testis (3.6 RPKM), whereas lymphoid tissues including spleen (101 RPKM), appendix (109 RPKM) and lymph node (129 RPKM) displayed highly abundant immunoproteasome levels (Fig. 5, Additional file 1: Table S3).
25127410 0.97 PSMB9/beta1i) and PK957 (PSMB8/beta5i), reduced the efficiency of cellular reprogramming, induced an exit of self-renewal and activated expression of somatic markers such as FGF5 and GATA4 (Table 2).
0.97 PSMB8/beta5i and PSMB9/beta1i are also expressed in human placenta.
0.82 PSMB9/beta1i and PSMB8/beta5i (Table 1).
27264839 0.97 LMP2, LMP7, TAP1, TAP2 and HLA class I predicts patient survival, where higher expression of APM components correlates with better survival.
0.96 LMP7 and single nucleotide polymorphisms for LMP2 and LMP7 have been detected in the case of cervix malignancies.
0.93 LMP2, LMP7, LMP10, TAP1, TAP2, Tapasin, Calreticulin, Calnexin, ERp57, beta2-microglobulin) and HLA class I loci (HLA-A, HLA-B and HLA-C).
30675634 0.97 PSMB8, PSMB9 and PSMB10 arose from PSMB6, PSMB5 and PSMB7, respectively, not by individual duplications, but by 2R-GWD (Fig. 3).
0.95 beta1i (also known as LMP2, PSMB9), beta2i (also known as MECL1, PSMB10) and beta5i (also known as LMP7, PSMB8) subunits instead of beta1, beta2 and beta5 subunits, respectively, have distinct cleavage specificities and produce peptides with C-terminal hydrophobic residues that fit well in the groove of MHC class I molecules more efficiently than standard 20S proteasomes.
0.86 beta1i and beta5i (PSMB9 and PSMB8 in humans, and Psmb9 and Psmb8 in mice) are in the class II region of the MHC on chromosomes 6 and 17, respectively.
20174631 0.97 Low Molecular Mass Polypeptide 2 (LMP2), Multicatalytic Endopeptidase Complex Subunit (MECL-1) and LMP7 into immunoproteasome].
0.92 LMP2 & LMP7) and PA28-alpha subunits.
23360169 0.97 LMP7 and TAP2, but not PSMB9, was correlated with levels of the HLA class I surface expression in melanoma cell lines.
0.97 LMP2, LMP7 and MECL-1 could stimulate the enhanced antimelanoma CTL activity.
31143302 0.97 PSMB8 and digenic mutations, those with a dominant POMP mutation, and those with recessive PSMB4 or PSMB9 and digenic mutations were registered as PRAAS1 (OMIM#256040), PRAAS2 (#618048), and PRAAS3 (#617591), respectively.
0.96 PSMB8 plus proteasome subunit alpha type 3 (PSMA3) encoding alpha7, PSMB8 plus PSMB4 encoding beta7, and PSMB9 encoding beta1i plus PSMB4 mutations, and to those with a heterozygous mutation in proteasome maturation protein (POMP) encoding a chaperon Ump1.
29259686 0.97 PSMB9 coding beta1i as well as PSMB8 and proteasome maturation protein (POMP) genes from 8 patients.
22216088 0.96 LMP7, LMP2, and MECL1.
0.96 LMP7 and LMP2, and one structural subunit (beta7) from multiple clones in each of the 2 resistant cells lines and compared them to the sequence of the subunits in the parental cells.
0.95 LMP7, LMP2, and MECL1) as analyzed by western blotting and quantitatively confirmed by ProCISE, an active site probe-based proteasome subunit ELISA (Figure 1B-C).
0.77 LMP2 levels did not increase in concordance with LMP7 and MECL1, as beta1 is capable of forming hybrid proteasomes with immunoproteasome subunits.
24490108 0.96 PSMB9 gene and a G/T polymorphism in the PSMB8 gene.
0.93 PSMB9 and LMP7-Q/Q (PSMB8) confers a higher relative risk than with HLA-B27 alone.
0.52 PSMB8 expression, PSMB9 gene expression is induced by IFN-gamma, resulting in the upregulation of the protein product of this gene beta1i, which replaces the constitutive catalytic subunit beta1 (PSMB6).
28381880 0.96 LMP7, LMP2 and LMP10 respectively, n = 3).
0.96 LMP2 and LMP7 in cells treated with FA and ONX-0914 (LMP7-i) for 3 h. (B) Westerns for cells treated with LMP7-i and MG132 (5 muM) for 4 h. (C) FACS profiles of EdU incorporation in cells treated with LMP7-i for 6 h. EdU was added during the last hour.
0.93 LMP2 or LMP7 (Fig. 2A).
20812720 0.96 LMP2/beta1i, MECL1/beta2i, and LMP7/beta5i, which replace the constitutive proteasome counterparts Y/beta1, Z/beta2, and X/beta5, respectively, to create the immunoproteasome.
0.96 LMP2/beta1i, MECL1/beta2i and LMP7/beta5i.
31702633 0.96 LMP2 or LMP7 genes may affect the expression of disease in HLA-B27 individuals by influencing the spectrum of peptides available, first by binding to HLA-B27 and then by presenting to autoreactive cytotoxic T cells.
0.87 LMP2 and LMP7) have been widely reported as genetic predisposing factors for AS.
27566410 0.96 beta1i (PSMB9; LMP2, low molecular weight protein 2), beta2i (PSMB10; LMP10, MECL-1, multicatalytic endopeptidase complex-like 1), and beta5i (PSMB8; LMP7, low molecular weight protein 7).
29182146 0.96 LMP2 (ibeta1), MECL-1 (ibeta2), and LMP7 (ibeta5) - that share respectively 62%, 59%, and 71% sequence identity with their cP counterparts.
29391047 0.96 PSMB8 and PSMB9 genes encoding two components of immunoproteasome (Figure 5).
32119722 0.96 beta1i (LMP2), beta2i (LMP10) and beta5i (LMP7) the so-called immune subunits, respectively.
19820934 0.95 LMP2-, LMP7-, TAP1-, TAP2-, tpn-, calnexin-, calreticulin, and ERp57-specific mAbs was found, but the percentage of stained tumor cells varied with a maximum reaching 39.7%, whereas a moderate to weak cytoplasmic staining of these lesions was detected with a percentage of stained tumor cells ranging between 17.2 and 65.5% in 52 to 59 PC lesions analyzed (Table 3, pFigs.
0.93 LMP2, LMP7, calnexin, calreticulin, tpn (p < 0.001), and ERp57 (p = 0.002) was significantly lower in PC lesions than in normal prostate tissues.
0.91 LMP2 and LMP7 expression in normal prostate tissues is a primarily unexpected finding since these immunoproteasome subunits are generally only expressed in cells upon IFN-gamma treatment.
0.91 LMP2 loss in PC; d LMP7 downregulation in PC; e weak TAP1 expression in normal prostate gland and TAP1 loss in PC; f positive staining for TAP2 in normal prostate gland and PC; g tpn downregulation in PC; h comparable high calnexin expression in normal prostate gland and PC;
0.88 LMP2 and LMP7 appear to be coordinately downregulated in prostate cancer cells.
0.84 LMP2 and LMP7, TAP1, TAP2, calnexin, calreticulin, ERp57, and tapasin are strongly expressed in the cytoplasm of normal prostate cells, whereas HLA class I heavy chain (HC) and beta2-microglobulin are expressed on the cell surface.
0.78 LMP2-, LMP7-, TAP1-, TAP2-, calnexin-, calreticulin-, ERp57-, tpn-, HLA class I HC-, and beta2-m-specific mAb.
22807337 0.95 LMP2 (beta1i), MECL1 (beta2i) and LMP7 (beta5i), which replace their constitutive counterparts Y (beta1), Z (beta2) and X (beta5), respectively, to form the immunoproteasome.
0.93 LMP7, we examined whether the fluorescent signals from LKS01-B650 would overlap with those from UK101-Fluor, a fluorescent probe targeting the catalytic active LMP2.
0.93 LMP7 signals are colocalized with signals from LMP2, indicating LKS01-B650-bound LMP7 is located in fully assembled immunoproteasomes.
26876939 0.94 beta1i (LMP2), beta2i (MECL1) and beta5i (LMP7) - that replace the c-proteasomal beta1, beta2 and beta5 to form immunoproteasomes (i-proteasomes, the term used here for any type of proteasomes that contains at least one of the three i-proteasome-specific beta (ibeta) subunits).
28848544 0.94 PSMB8 mutations, but others are compound heterozygous for PSMB4, or are heterozygous for combinations such as PSMA3/PSMB8, PSMB9/PSMB4, or PSMB8/PSMB4.
28977958 0.93 LMP2, LMP7) and of transporter subunits (TAP1 and TAP2) are documented.
0.83 LMP2/LMP7 polymorphisms and cancer risk.
0.81 LMP2/LMP7.
0.69 LMP2/LMP7 polymorphisms.
0.60 LMP2 rs17587 and LMP7 rs2071543 polymorphisms may act as risk factors for cancer, especially for Asian populations.
24480782 0.92 LMP2, LMP7, TAP2, or tapasin expression were observed between both treatments, suggesting that radiation therapy modulates the expression of APM components regardless of dosing regimen (data not shown).
25548428 0.92 PSMB8 (LMP7) and PSMB9 (LMP2).
25796583 0.92 LMP2, LMP7 and ERAP1 genes were genotyped in cervical carcinoma patients and healthy controls from two distinct Indonesian populations (Balinese and Javanese).
31576159 0.92 beta1i (PSMB9), beta2i (PSMB10), and beta5i (PSMB8).
22588558 0.90 LMP2, LMP7, TAP1, TAP2 and HLA class I alleles on NPC tumour cells have been described in one study, others have shown heterogeneous expression with a partial loss of HLA-ABC in almost 50% of NPC cases.
22677907 0.90 LMP7 and LMP2 are responsible for ~50-70% and ~30-50% of the CT-L activity of the purified immunoproteasome, respectively.
29104774 0.89 beta1i/PSMB9) and PK957 (beta5i/PSMB8) activates the expression of differentiation markers and loss of hESC pluripotency, which indicates the role of IPs in the maintenance of pluripotency.
27213585 0.88 LMP7 expression and HLA class I expression, but not with LMP2 or TAP1/2.
17622526 0.87 LMP2 and LMP7 down-regulation with an absence of lymph node metastasis; this finding is seemingly corroborated by reports that certain immunogenic peptides in melanoma and renal-cell carcinoma are not generated by immunoproteasomes and that presentation of these peptides is reduced upon up-regulation of the immunoproteasomal subunits.
9584142 0.86 LMP2 (ibeta1) and LMP7 (ibeta5) are encoded within the MHC class II region in the direct neighborhood of the TAP1 and TAP2 peptide transporter genes.
0.82 LMP2)1 (ibeta1), LMP7 (ibeta5), and MECL-1 (ibeta2) during proteasome assembly.
27071340 0.83 low-molecular mass polypeptide 7 (LMP7), LMP2 and multicatalytic endopeptidase complex-like 1 (MECL1) replace beta5, beta1 and beta2, respectively.
0.78 LMP7, MECL1 and LMP2 was increased by 7 9%, 23 1% and 33 6%, respectively, relative to patients receiving 15 or 20 mg/m2 (see Fig 3A and B; P < 0 05, P <0 001 and P < 0 01, respectively).
0.72 LMP2) was also observed in PBMCs at doses of 15 and 20 mg/m2, albeit at lower levels than LMP7 inhibition (31-46% inhibition of MECL1 and 22-33% inhibition of LMP2).
22355695 0.82 LMP2, LMP7, and LMP10/MECL-1 subunits have been reported to contribute to the initiation and development of disorders.
31428085 0.79 PSMB8-TAP1-PSMB9 locus in the MHC region.
20919990 0.74 beta1i (Lmp2), beta2i (Mecl-1), and beta5i (Lmp7) subunits, thus forming the so called 'Immunoproteasome.
0.61 beta1i (or Lmp2), beta2 (or Mecl-1), and beta5i (or Lmp7).
32053590 0.63 Psmb8), beta2i (Psmb9) and beta1i (Psmb10) compared to the untreated islets (Table 3).
25412285 0.59 LMP2 (beta1i), MECL-1 (beta2i) and LMP7 (beta5i), are expressed and incorporated into the proteasome in place of their constitutive counterparts, beta1, beta2 and beta5, to form another particle called the immunoproteasome (Figure 1A).



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