Publication for SFTPA1 and SFTPA2

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
hsa	SFTPA1	surfactant protein A1	653509			[link]
hsa	SFTPA2	surfactant protein A2	729238

Pubmed ID	Priority	Text
31475015	1.00	SP-A gene products, we wished to investigate the combined effect of co-expressed SP-A1/SP-A2 (co-ex) in response to O3 induced OxS on AM miRNome.
	0.97	SP-A1 and SP-A2 and among variants in survival and lung function mechanics in response to bacterial infection, and SP-A1 compared to SP-A2 exhibits a higher efficiency in pulmonary surfactant reorganization.
	0.96	SP-A1 with arginine or the arginine of SP-A2 with cysteine resulted in a reversal pattern of SP-A oligomerization and functional activity of both mutants of SP-A1 and SP-A2.
	0.91	SP-A1/SP-A2 and sex on the AM miRNome.
	0.83	SP-A1 or SP-A2 gene, on the AM miRNome after OxS, and found that SP-A2 (but not SP-A1) had a significant impact on AM in males.
	0.80	SP-A1 has a cysteine and SP-A2 has an arginine.
	0.77	SP-A1 and SP-A2.
	0.77	SP-A locus consists of two functional genes, SFTPA1 and SFTPA2 and encodes two functional proteins, SP-A1 and SP-A2, respectively, and each is identified with several genetics variants.
	0.72	SP-A2 males but not in SP-A2 females or in SP-A1 males and females in response to OxS.
	0.69	SP-A1 and SP-A2 genes, expression of target genes to mitigate the OxS injury is lacking, indicating that other hormone dependent mechanisms are involved.
	0.67	SP-A1 and SP-A2 mRNA content was found to vary in explant cultures under different conditions.
	0.64	SP-A1/SP-A2 Protein on AM miRNome; Sex Differences
	0.64	SP-A1/SP-A2) product and of single gene product (SP-A2) on the regulation AM miRNome on both males and females, and males respectively.
	0.62	SP-A1/SP-A2 (6A2/1A0, co-ex) after O3 exposure and compared it to that of KO mice lacking SP-A. In response to OxS, AM miRNome changes were observed in both males and females (with or without normalization to KO), although after multiple comparison analysis, AM miRNAs significantly changed only in females.
27835691	1.00	SP-A gene locus is located on chromosome 10 10q22-q23), and consists of two functional and quasi identical genes, the SFTPA1 (SP-A1) and SFTPA2 (SP-A2), approximately 40 kb pair apart.
	0.97	SP-A1 haplotypes (coded 6A, 6A2, 6A3, 6A4) and six SP-A2 haplotypes (coded 1A, 1A0, 1A1, 1A2, 1A3, 1A5) are the most prevalent.
	0.97	SP-A1/SP-A2 haplotypes and/or SP-B Ile131Thr polymorphic alleles are associated with RDS in infants born late-preterm, after taking into account the effect of other perinatal risk or protective factors.
	0.96	SP-A1 and SP-A2 haplotypes in the two late-preterm groups are presented in Fig 1.
	0.96	SP-A1 6A4 and SP-A2 1A5 haplotypes were significantly overrepresented in infants who developed RDS as compared to late-preterm controls.
	0.94	SP-A1 and SP-A2 haplotypes were noted (Fig 1).
	0.88	SP-A1 and SP-A2 haplotypes between the population of late-preterm infants and the reference population of healthy term newborns ([haplotype: Pearson chi-square, p-value] 6A: 0.0005, 0.983; 6A2: 0.521, 0.481; 6A3: 0.220, 0.639; 6A4: 0.915, 0.339; 1A: 0.027, 0.871; 1A0: 0.033, 0.857; 1A1: 0.614, 0.433; 1A2: 0.055, 0.815; 1A5: 0.133, 0.715).
	0.87	SP-A1 6A4 or/and SP-A2 1A5 haplotype was present in 20 newborns with RDS (35.7%) and in 7 without RDS (11.7%), resulting in a 4.21-fold (95% CI 1.61-11.0) higher probability of RDS in carriers of these haplotypes (P = 0.003, estimated power 89.9%).
	0.80	SP-A1 6A4 and SP-A2 1A5 haplotypes was preserved when adjusting for known risk or protective factors, such as male gender, smaller gestational age, smaller weight, complications of pregnancy, and administration of antenatal corticosteroids.
	0.73	SP-A1 6A4 and SP-A2 1A5 haplotypes was preserved when adjusting for known risk or protective factors, such as male gender, smaller gestational age, smaller size (weight) for gestational age, complications of pregnancy and administration of antenatal corticosteroids, with the carriers of the 6A4 and 1A5 haplotypes having a 4- and 5-fold higher probability for RDS, respectively (Table 4).
	0.68	SP-A gene locus is located on chromosome 10 10q22-q23), and consists of two functional and quasi identical genes, the SFTPA1 (SP-A1) and SFTPA2 (SP-A2), approximately 40 kb pair apart.
	0.59	SP-A1 and SP-A2 haplotypes or the SP-B Ile131Thr polymorphism alleles.
30333828	0.98	SFTPA1 and 4 for SFTPA2) (Figure 1A) and seven with SFTPD (Figure 1B).
	0.97	SFTPA1 and SFTPA2.
	0.97	SFTPA1 (n = 3), one SNP in SFTPA2, one SNP in SFTPC, and one SNP in SFTPD.
	0.97	SFTPA2 gene is associated with CF through 9 intergenic SNP-SNP interactions with SFTPA1 (n = 2), SFTPB (n = 4), and SFTPC (n = 3) (X2 is 2.4172-6.4974, p = 0.0485-0.0038, Figure 1A).
	0.97	SFTPA1 or SFTPA2.
	0.97	SFTPA1 and SFTPA2 interaction are likely to be markers for mild and moderate/severe pulmonary disease in CF, respectively.
	0.96	SFTPA1 or SFTPA2 and SFTPD.
	0.96	SFTPA1/SFTPA2 (n = 7) and SP-B and SFTPD (n = 7).
	0.96	surfactant protein A (SP-A), in humans SP-A consists of SP-A1 and SP-A2 encoded by SFTPA1 and SFTPA2, respectively; each gene has been identified with several genetic variants, and these have been shown to associate with several pulmonary diseases.
	0.96	SFTPA1 and SFTPA2 encoding the hydrophilic surfactant proteins, SP-A1 and SP-A2 and on the right SNPs of the surfactant genes SFTPB and SFTPC, encoding the hydrophobic proteins, SP-B and SP-C, are shown (B).
	0.96	SFTPA1 SNPs are associated with CF through 13 intergenic SNP-SNP interactions with SNPs in SFTPA2 (n = 2), SFTPB (n = 3), and SFTPC (n = 8) (X2 is 2.2285-7.8947, p = 0.0487-0.0007) (Table 4, Figure 1A).
	0.96	SFTPA1, no interaction of SFTPA2 with SFTPD was found to be associated with CF.
	0.95	SFTPA1, SFTPA2, SFTPB, SFTPC, and SFTPD With Cystic Fibrosis
	0.95	SFTPA1, 3 for SFTPA2, and 3 for SFTPD).
	0.95	SFTPA1, SFTPA2, SFTPB (Figure 1A), and SFTPD (Figure 1B).
	0.95	SFTPA2 SNP rs1059046 appears to stand out from the other SFTPA2 SNPs studied, as this SNP (1) is associated with CF via five of the total nine interactions observed with the other SP genes, (2) is the only SNP that shows interactions with two SFTPA1 SNPs, and (3) shows interactions with both hydrophobic surfactant proteins SFTPB and SFTPC (Figure 1A).
	0.93	SFTPA1 and SFTPA2) encoding the hydrophilic SP-A1 and SP-A2.
	0.93	SP-A1, SP-A2, and SP-D mediate innate immunity in the lung and via interactions with the alveolar macrophage the sentinel cell of innate lung host defense, promote, among others, bacterial and viral phagocytosis, and cytokine production, as well as affect lung inflammatory processes.
	0.91	SFTPA1 SNP-SNP interactions, 11 are with SFTPB and SFTPC encoding the hydrophobic surfactant proteins, and only two interactions are with SFTPA2 that encodes the hydrophilic surfactant protein A2 (Figure 1A), whereas no interactions are observed with SFTPD.
	0.90	SFTPA1, three are with SFTPA2, four are with SFTPB (Figure 1A), and three are with SFTPD (Figure 1B).
	0.85	SFTPA1 and SNP rs1059046 (aa 9 Thr/Asn) of SFTPA2.
	0.82	SFTPA1, SFTPA2, SFTPC, and SFTPD (X2 is 2.2285-8.4508, p = 0.0487-0.0007) (Table 4).
	0.80	SP-A1, shown previously to form higher size oligomers compared to SP-A2, was shown recently to affect more efficiently (than SP-A2) the structural organization of surfactant, which in turn may affect lung function.
	0.79	SFTPA1 and one of SFTPB) to associate with CF; c) A total of 34 intergenic interactions of different combinations between the various genes studied, except between SFTPD and SFTPA1 or SFTPA2, to associate with CF; A summary of all the significant intragenic and intergenic interactions is shown in Supplementary Table 3, and Figure 2.
	0.79	SFTPA1, three with SFTPA2 and only 3 with SFTPD.
	0.76	SFTPA1 or SFTPA2, whereas the SNP-SNP intergenic interactions between SFTPB and SFTPD include three of the four SFTPB SNPs studied.
	0.65	SFTPA1 has two intergenic interactions with SFTPA2, as well as intragenic interactions.
	0.58	SFTPA1 (5), SFTPA2 (4), SFTPB (4), SFTPC (2), and SFTPD (2)), and identified SP SNP associations by applying quantitative genetic principles.
	0.53	SP-A1 has been shown to more efficiently affect surfactant reorganization (than SP-A2) in the alveolar space.
	0.51	SFTPA1 and SFTPA2 with CF have been observed.
30459763	0.98	SP-A. Expression of SP-A binding proteins such as CD14 and TLR2 on the cell surface of the AMs isolated from SP-A1 (6A2), or SP-A2 (1A0) mice were measured by flow cytometry.
	0.97	SFTPA1 and SFTPA2 genes encode SP-A1 and SP-2 proteins, and each gene has been identified with numerous genetic variants.
	0.97	SP-A2 binding to the phagocytic cells and the differential expression of cell surface proteins that bind SP-A by AM from SP-A1 and SP-A2 mice play a role in this process.
	0.96	SP-A2 (1A0, 1A3), SP-A1/SP-A2 (6A2/1A0, co-ex), and SP-A KO male and female mice were infected with K. pneumoniae, and monitored for 14 days for survival.
	0.96	SP-A2 (co-ex) exhibited significant differences in survival compared to SP-A single gene variants in both males and females, as shown in Figures 5A,B. The co-ex males and females exhibited significantly higher survival compared to 1A3 (Figure 5A) and 6A2, and 6A4 males (Figure 5B) males.
	0.96	SP-A1 and SP-A2 genes differs within the coding region.
	0.96	SP-A gene expression in fetal lung tissues of various species to be regulated by a variety of hormones and factors, including retinoids, insulin, growth factors and cytokines, glucocorticoids and cAMP, estrogen related receptor -alpha, which is an important mediator of SP-A gene expression and its induction by cAMP, and testosterone to positively regulate the expression of SP-A. Moreover, human SP-A1 and SP-A2 genes are differentially regulated during development by cAMP and glucocorticoids.
	0.95	SP-A2 differentially affected the AM proteome of SP-A KO mice.
	0.94	SP-A1 and SP-A2 may further contribute to the observed differences in lung function mechanics and/or survival.
	0.93	SP-A binding proteins from AMs of hTG SP-A1 (6A2) and SP-A2 (1A0) mice.
	0.93	SP-A2 > SP-A1 > KO (male and female together); (b) Variant-specific survival co-ex (6A2/1A0) = 1A0 > 1A3 = 6A2 > 6A4 (male and female together); (c) Sex differences in survival in SP-A variants and KO mice, with females showing better survival than males; (d) The co-ex (6A2/1A0) did not exhibit sex differences; (e) exogenous treatment of KO mice with SPs (SP-A1 or SP-A2) proteins significantly improved the overall survival; (f) Differential gene-specific SP-A1 and SP-A2 binding was observed with phagocytic but not with non-phagocytic cells, as well as differential expression of cell surface proteins in AM from SP-A1 and SP-A2 mice.
	0.93	SP-A in infection and hat SP-A1 and SP-A2 differ in their activities in several lung processes/function and these may in part explain differences observed in the survival of SP-A1 and SP-A2 hTG mice.
	0.91	SP-A2 (1A0, 1A3) (C,D), SP-A KO (E), and SP-A1/SP-A2 [6A2/1A0, (co-ex)] (F) male and female mice over a period of 14 days after infection.
	0.91	SP-A2 vs. SP-A1 (p = 0.0007) to AM was seen as was for the phagocytic THP-1 cells (p = 0.0015), but no differences were observed with the non-phagocytic CHO cells.
	0.89	SP-A2 variant or both SP-A1 and SP-A2 (co-ex) variants and lacking SP-A (KO).
	0.89	SP-A2 bound THP-1, a phagocytic cell line, significantly more than SP-A1 but no differences were observed when CHO cells, a non-phagocytic cell line was used (Figure 8A).
	0.60	SP-A2 variant or both SP-A1/SP-A2 (co-ex) as well as mice lacking SP-A (i.e., KO) with K. pneumoniae and studied their daily survival over a 14 day period; (b) Rescued K. pneumoniae infected KO mice with exogenous SP-A1 or SP-A2 treatment prior to and/or at the time infection; (c) Carried out pilot binding studies of SP-A1 (6A2) and SP-A2 (1A0) to the AM as well as expression of cell surface proteins from AMs of SP-A1 (6A2) and SP-A2 (1A0) mice.
31781112	0.98	SP-A1 or SP-A2 in the presence (A,C,E) or absence of calcium (B,D,F).
	0.97	hSP-A1 and hSP-A2 represent Ca++-independent binding sites (Figure 6F).
	0.97	SP-A isoforms, SP-A1 and SP-A2, and changes in the CRD produced four variants, two for SP-A1 and two for SP-A2.
	0.96	SP-A protein whereas humans express two: SP-A1 and SP-A2 with core intra- and inter-species differences in the collagen-like domain.
	0.96	hSP-A1 (6A2) and hSP-A2 (1A0) isoforms in vivo revealed that mouse SP-A is a functional hybrid of hSP-A1 and hSP-A2 in regulating SP-A receptor occupancy and binding affinity.
	0.96	SP-A1 and SP-A2 variants in survival after infection and lung function.
	0.96	hSP-A2 also improved the binding potential of hSP-A1 by increasing binding affinity.
	0.96	hSPA1 did not bind SP-A-/- AMs and its expression alone induced only low affinity binding of hSPA1 compared to high affinity binding for hSP-A2, although at lower Bmax compared to the hSPA2 expression.
	0.96	hSP-A1 was observed only in AMs from hSP-A2 or WT mice.
	0.96	hSP-A2 and endogenous mouse SP-A shaped the positive cooperativity binding phenotype of AMs (Figures 6A,B, and Table 6), whereas hSP-A1 did not.
	0.96	SP-A1 and SP-A2 is polymorphic resulting in diverse allelic combinations of SP-A1 and SP-A2 variants.
	0.95	SP-A genes SFTPA1 (6A2) or SFTPA2 (1A0) via the alveolar epithelial Sftpc promoter.
	0.94	hSP-A2 was 3-fold higher in adult AMs than newborn AMs compared to a 1.6-fold increase for hSP-A1.
	0.93	SP-A1 and SP-A2 with AMs is developmentally regulated.
	0.91	hSP-A1 binding was 2-3-fold lower than that of hSP-A2 binding to murine AMs, indicating that the CDM is responsible for differences in receptor binding capacity of hSP-A isoforms with identical CRD.
	0.82	hSP-A2 resulted in ligand-induced upregulation of hSPA2 binding to AMs compared to SP-A-/- and hSP-A1 exposed AMs as demonstrated by the 2-2.5 increase in Bmax (Table 6).
	0.75	hSP-A1 and hSP-A2 proteins and their respective variants differ at four core amino acids in the collagen-like domain and the variants of each gene are distinguished among themselves by additional amino acid differences present in domains other than the collagen-like domain.
30123671	0.98	SP-A1 and SP-A2.
	0.96	SP-A2 suggests an important link between SP-A and the modulation of eosinophils, an immune cell associated with Type 2 asthma and asthma severity.
	0.93	SP-A function dependent on genetic variation in SP-A2 with the presence of either Q or K present at position 223 could offer mechanistic insight to explain why some SP-A is more effective in attenuating phenotypes associated with asthma.
	0.86	SP-A2 at position 223 that results in a glutamine (Q) to a lysine (K) substitution alters the ability of SP-A to inhibit EPO release and may offer a mechanistic explanation as to why some SP-A extracted from subjects with asthma is unable to carry out normal immune regulatory functions.
	0.85	SP-A to inhibit EPO release with rSP-A with either the major (223Q) or minor (223K) allele present in SP-A2, we see a striking and significant difference in activity between the two rSP-As (Figure 2).
	0.78	SP-A forms a 650-kDa octadecamer of six trimers, each trimer believed to be formed by two SP-A1 and one SP-A2 molecules.
	0.77	SP-A2 alters the ability of SP-A to inhibit eosinophil EPO release, which could lead to worse asthma exacerbations upon pathogen infection in those asthmatics harbouring the minor allele (223K).
	0.74	SP-A1 and SP-A2 exert differential effects on alveolar macrophages, a potential mechanism of the persistent inflammation in asthmatics proposed is that the altered SP-A ratio is contributing to the defect in macrophage function.
	0.54	SP-A derived from asthmatics was dysfunctional in mediating inflammation compared to SP-A derived from non-asthmatics and it has been suggested that dysfunction may be a consequence of an alteration in the SP-A1:SP-A2 ratio.
32218785	0.98	SP-A1 and SP-A2 differentially bind and regulate neonatal and adult human alveolar macrophages (AMs) (Thorenoor, Umstead et al.).
	0.96	SP-A1 and SP-A2 exhibit differential expression of cell surface proteins (Thorenoor, Kawasawa et al.) Rodents express only one SP-A variant; thus, Nalian et al. have compared the rodent and human SP-A with respect to structural determinants of the function.
	0.96	SP-A1 and SP-A2.
	0.93	SP-A1 and SP-A2 seem to differentially bind to phagocytic, but not to non-phagocytic cells (Thorenoor, Umstead et al.).
	0.80	SP-A variants differing in the collagen region, SP-A1 and SP-A2, encoded by SFTPA1 and SFTPA2, respectively, and produced by the alveolar type II cells in the lung.
19082436	0.98	SP-A1 and SP-A2 differences on macrophage function depends on SP-A protein concentration and functional integrity, an altered SP-A expression or SP-A dysfunction, as it occurs after SP-A is exposed to ozone, may adversely affect macrophage host defense function.
26292924	0.98	SFTPA1 and SFTPA2 genes, accurately distinguished lung cancer from other cancer samples, the predictive accuracy of LOOCV for TCGA and GSE5364 data were 95.68% and 100%, respectively.
30972061	0.97	SP-A locus consists of two functional genes, SFTPA1 and SFTPA2 encoding SP-A1 and SP-A2, respectively, plus a pseudogene and is located on chromosome 10q22-23.
	0.97	SP-A2 mice in response to ozone not only express a higher level of SP-A protein compared to SP-A1 mice (Figure 5A), but they appear to directly or indirectly regulate/influence the expression of other proteins (also see Figure 4).
	0.97	SP-A2 mice the SP-A content is significantly increased (p < 0.05) by 137.3% compared to SP-A1 female mice, but no differences were observed in SP-A levels between SP-A1 and SP-A2 female mice after ozone exposure (Figure 3B).
	0.97	SP-A1 and SP-A2 and SP-A KO mice, and studied in vivo the effect of human SP-A1 and SP-A2 genotypes on BAL proteomic profile and associated signaling pathways in response to bacterial infection in the presence or absence of ozone.
	0.97	SP-A2 and SP-A1 mice compared with SP-A KO mice showed a regulatory effect on BAL protein expression that are associated with the activation of APR (ERK1/2 and NF-IL6) signaling pathways.
	0.97	SP-A1 and SP-A2 male mice, but not females, could maintain this regulatory ability (Figure 9).
	0.97	SP-A1 and SP-A2 infected mice exhibit higher levels of Nrf2-related protein expression than KO mice, suggesting that SP-A plays protective roles against infection and oxidative stress.
	0.96	SP-A2 > SP-A1 KO, with the majority being increases in male mice and decreases in female mice.
	0.96	SP-A2 and SP-A1 exhibit differential genotype-and sex-dependent innate immune responses to microbial pathogens and/or ozone-induced oxidative stress by modulating proteomic patterns and signaling pathways in the lung.
	0.96	SP-A1 male mice and 30 proteins (83%) in SP-A2 male mice, exhibited marked increases (% change >25%; pink highlighting).
	0.96	SP-A2 and SP-A1 female mice
	0.96	SP-A1 and SP-A2 mice may reflect regulatory differences in the translation between SP-A1 and SP-A2 and/or qualitative functional differences between SP-A1 and SP-A2 remains to be determined.
	0.96	SP-A2 male mice compared to ozone-exposed SP-A1 male mice (Table 1S).
	0.96	SP-A1 and SP-A2 mice reduced (for male) or abrogated (for female) the ability to enhance APR (ERK1/2 and NF-IL6) signaling pathway activation.
	0.96	SP-A1/SP-A2 genotype-sex interaction.
	0.96	SP-A2 mice showed higher levels of annexin A5, SP-A, 14-3-3 zeta protein, and glutathione S-transferase A4 than SP-A1 and KO mice in response to ozone and infection (Figure 4).
	0.95	SP-A1 and SP-A2 in vitro and in vivo have been observed.
	0.95	SP-A2 (1A3); (2) hTG SP-A1 (6A4) mice; (3) SP-A KO mice.
	0.95	SP-A2 female mice are profoundly affected and more responsive to ozone exposure than the infected SP-A1 female mice.
	0.95	SP-A2 mice had higher level of glutathione S-transferase A1 than ozone-exposed KO mice and had higher levels of glutathione S-transferase, omega 1, and Rho GDP dissociation inhibitor, alpha, than ozone-exposed SP-A1 male mice.
	0.95	SP-A1 and SP-A2 genetic variants in response to environmental insults.
	0.94	SP-A1 or SP-A2 vs. KO male mice
	0.94	SP-A1 or SP-A2 vs. KO male mice
	0.93	SP-A locus consists of two functional genes, SFTPA1 and SFTPA2 encoding surfactant proteins SP-A1 and SP-A2, respectively.
	0.93	SP-A1 and SP-A2 male mice in response to a single insult (infection) is the same, but in response to a double insult (infection and ozone exposure) the SP-A content in the SP-A2 mice is significantly higher (p < 0.05) than that in SP-A1 mice (Figure 5A).
	0.93	SP-A1 and SP-A2 variants.
	0.92	SP-A1 male mice and complement component 3 in SP-A2 male mice were markedly decreased (% change > -25%; green highlighting) compared to KO male mice.
	0.92	SP-A1 and SP-A2 mice, with SP-A2 mice exhibiting a more robust response.
	0.91	SP-A1 was found to more efficiently affect surfactant structural organization compared to SP-A2.
	0.89	SP-A1 and SP-A2 mice, and SP-A KO mice to study in vivo effects of SP-A1 and SP-A2 on the bronchoalveolar lavage (BAL) proteomic profile and associated signaling pathways in response to ozone or filtered air (FA) exposure and Klebsiella pneumoniae infection.
	0.89	SP-A2 (compared to SP-A1) male mice directly or indirectly regulate levels of many proteins in response to FA and ozone.
	0.89	SP-A2 > SP-A1 > KO in male mice, and SP-A2 SP-A1 > KO in female mice, and after ozone exposure and infection, SP-A2 > SP-A1 KO in male mice, and SP-A2 > SP-A1 KO (decrease) in female mice.
	0.88	SP-A1 and SP-A2 on the BAL Proteome and Signaling Pathways in Response to Klebsiella pneumoniae and Ozone Exposure
	0.88	SP-A1 variants (6A, 6A2, 6A3, 6A4) and the SP-A2 variants (1A, 1A0, 1A1, 1A2, 1A3, 1A5) are the most frequently found variants in the population.
	0.88	SP-A1 comparison vs. 9 in the SP-A2 comparison described above).
	0.87	SP-A1 or SP-A2 vs. KO female mice
	0.87	SP-A1 and SP-A2 mice, respectively, showed marked decreases, and only two proteins (annexin A5 with increase of 145.3% and glutathione S-transferase A4 with increase of 55.3%) in infected SP-A2 female mice were expressed at higher levels than infected KO female mice.
	0.84	SP-A1 or SP-A2 genetic variants have been associated with several human pulmonary diseases.
	0.84	SP-A1 and SP-A2 mice and SP-A KO mice) were exposed to ozone (3 ppm) or filtered air for 3 h and then intratracheally infected with 50 mul of bacterial solution (containing about 450 CFU of K. pneumoniae, control with 50 mul of saline).
	0.84	SP-A1 and SP-A2 female mice, respectively, showed profound increases compared to KO female mice (data shown in the second set of Table 1S).
	0.80	SP-A1 and SP-A2 proteins expressed in vitro by insect or mammalian cells and in vivo, ex vivo, or in vitro.
	0.80	SP-A2 variants had a higher ability than SP-A1 variants to stimulate cytokine production by macrophage-like THP-1 cells, to enhance phagocytosis of bacteria by macrophages, and to interact with LPS and phospholipids.
	0.78	SP-A1 (A1), SP-A2(A2), KO] after exposure to O3 or filtered air (FA) following bacterial infection.
	0.70	SP-A1 and SP-A2 mice was studied in response to ozone-induced oxidative stress and/or infection.
	0.69	SP-A2 female mice showed increases in 3 proteins (annexin A5, glutathione S-transferase A4, and SP-A), and decreases in 5 proteins (complement component 3, heat shock protein 1A, Kpnb1 protein, murinoglobulin-1, and Serpin A1 compared to infected SP-A1 female mice (Tables 1S, 2S).
	0.65	SP-A1 or SP-A2 variant, in response to K. pneumoniae infection and in the presence or absence of ozone.
	0.63	SP-A1 and SP-A2 was shown to have diverged in terms of tubular myelin (TM) formation, an extracellular form of pulmonary surfactant.
	0.55	SP-A2 mice the 14-3-3 zeta protein level was higher than in infected SP-A1 and KO mice (Figure 4C).
	0.53	SP-A1 and SP-A2 and among in vitro expressed SP-A genetic variants have been observed using several different approaches.
	0.53	SP-A1 and SP-A2 mice (except for SP-A2 female where it may decrease) compared to the FA-exposed KO mice; SP-A2 males showed an increase compared to SP-A1 males with no differences between SP-A1 and SP-A2 females.
	0.51	SP-A2 and SP-A1 mice under the same conditions.
19392648	0.97	SP-A gene locus, and in primates a gene duplication event occurred generating two genes, SP-A1 and SP-A2.
	0.97	SP-A1 and SP-A2 genes and/or variants have been identified and studied.
	0.97	SP-A2 variants (1A2 vs 1A or 1A0) or mammalian cell-expressed SP-A1 variants (6A4 vs 6A or 6A2) to enhance TNF-alpha production by a macrophage-like cell line; (2) in the ability of insect cell-expressed SP-A1 (6A2, 6A4) and SP-A2 (1A, 1A0), or mammalian cell-expressed SP-A1 (6A2, 6A4) and SP-A2 (1A0, 1A1) to enhance phagocytosis by alveolar macrophages; (3) in the ability of insect cell-expressed SP-A1 (6A2, 6A4) and SP-A2 (1A0, 1A2) to aggregate LPS.
	0.97	SP-A1 variants, SP-A2 gene-specific variants as noted above, were uniformly more active than SP-A1 in most of the activities investigated.
	0.97	hSP-A1 and hSP-A2 from an evolutionary point of view could be another future endeavor.
	0.96	SP-A1, the most frequently observed variant is the AD', and for SP-A2, the ABD' and ABD.
	0.96	SP-A1 and GER for SP-A2) is postulated to contribute to differences in local structural stability between the two gene products.
	0.96	SP-A1 and SP-A2.
	0.96	SP-A protein consists of two SP-A1 molecules and one SP-A2, the available data indicate that in vitro- or in vivo-expressed single gene products are functional, although with some functional and structural differences between the two gene products.
	0.96	SP-A2 variants enhanced bacterial phagocytosis by either rat or human alveolar macrophages at higher levels than SP-A1, although a considerably higher protein concentration was required for the insect cell-expressed proteins.
	0.96	SP-A1 or SP-A2 variants may be due entirely or in part to differences other than the "core" amino acids that distinguish the two gene products.
	0.95	SP-A protein content, without distinction between SP-A1 and SP-A2 content or SP-A genotype among individuals, have been observed in several lung diseases or in physiological changes of lung activity.
	0.95	SP-A1 AND SP-A2 AND/OR AMONG THEIR RESPECTIVE VARIANTS
	0.95	SP-A function (i.e., phagocytosis, inhibition of surfactant secretion, cytokine production), they are not responsible for the observed differences between SP-A1 and SP-A2 because these differences are maintained regardless of the presence or absence of post-translational modifications.
	0.94	SP-A1 and SP-A2, except for Arg-197 (+20 precursor), which is Ala in both human sequences.
	0.94	SP-A2 to bind with higher affinity to a wider variety of sugars than SP-A1 indicates that the structural pattern or other attributes of SP-A2 make it more favorable for more diverse carbohydrate binding.
	0.94	SP-A1 and SP-A2; structural differences, in turn, may have an impact on the functional capabilities not only of the collagen-like region where amino acid 85 resides but also of the CRD region.
	0.94	SP-A1 and SP-A2 most likely by affecting the structure and subsequently the function of the two SP-A gene products.
	0.93	SP-A1 and SP-A2 in vitro-expressed variants include differences (see Table 1) in their ability to enhance phagocytosis by alveolar macrophages, enhance production of proinflammatory cytokines (TNF-alpha and IL-8) by macrophage-like THP-1 cells, and inhibit surfactant secretion by epithelial type II cells.
	0.93	SP-A1 and SP-A2 with respect to IAV appears to depend principally on the type of sialic acid linkage and not on sequence or oligomerization patterns of SP-A1 and SP-A2.
	0.93	SP-A complexity is associated with differences in function and structure of SP-A1 and SP-A2, there is much to be learned about the mechanisms by which these occur.
	0.90	SP-A1 and SP-A2 gene products are necessary for the formation of the extracellular structural form of surfactant, the tubular myelin (TM).
	0.90	SP-A1 or SP-A2 variants have been observed.
	0.89	SP-A structure through the crystal structure analysis of an SP-A fragment consisting of the neck and CRD are similar between SP-A1 and SP-A2, and, therefore, the residues in neck and CRD are not expected to contribute to structural or functional differences between the two hSP-A genes.
	0.88	SP-A1 or SP-A2 variants are located within the sequence for the signal peptide, collagen-like region, and CRD.
	0.87	SP-A1 and one SP-A2 molecules, recent evidence of in vitro- and in vivo-expressed SP-A variants indicate that homotrimers or homo-oligomers exist and/or that these are functional.
	0.87	SP-A1 or SP-A2 alone to form TM and the need of both for formation is perhaps the first example of complete functional divergence of the two SP-A genes.
	0.87	SP-A1 may be involved in the formation of an SP-A intertrimeric or intratrimeric disulfide bond and account, in part, for the observed oligomerization pattern differences between SP-A1 and SP-A2 variants.
	0.82	SP-A1 and SP-A2 variants are located in the collagenlike domain (reviewed in Ref.).
	0.78	SP-A1 and SP-A2 intragenic haplotypes or variants (see below) of the NCBI database are 6A3 (SP-A1) and 1A0 (SP-A2), and those of the Celera database are 6A3 (SP-A1) and 1A2 (SP-A2), indicating that different genomic samples were used in the NCBI and Celera databases.
	0.78	SP-A1 and SP-A2 variants.
	0.77	SP-A sequences, including all SP-A1 and SP-A2 variants, indicating that no differences in structure among various SP-As are expected to occur by means of these contacts.
	0.72	SP-A1 and SP-A2 sequences, in Figure 3.
	0.69	SP-A1 and SP-A2 5' UTR splice variants were recently shown to differentially affect mRNA stability and translation.
	0.69	SP-A1 and SP-A2 basal mRNA levels and in response to various hormones and to dexamethasone, in particular, have been observed in several studies, it has been challenging to determine if these mRNA differences reflect differences in the protein content of SP-A1, SP-A2, or both.
	0.68	SP-A1 (6A, 6A2, 6A3, 6A4) and six SP-A2 variants (1A, 1A0, 1A1, 1A2, 1A3, 1A5) have been observed in higher frequency of > 0.01 in the general population.
	0.65	SP-A1 and SP-A2 affect the function of SP-A1 and SP-A2 is not well understood.
	0.63	SP-A1 and SP-A2, and the results from both reports were obtained using primer extension.
	0.60	SP-A1, SP-A2, SP-A3) and the chicken genome to have an SP-A and an SP-A-like gene.
	0.59	SP-A consists of two functional genes, SFTPA1 (or SP-A1) and SFTPA2 (or SP-A2), as well as a pseudogene.
	0.54	SP-A1 and SP-A2 have been described.
	0.53	Surfactant Protein A1 (SP-A1) and SP-A2:Impact on Function
23069847	0.97	SP-A1 and SP-A2 in the inhibition of hemagglutination activity of influenza A virus.
	0.97	SP-A1 and SP-A2 in oligomerization properties, aggregation, structural stability, sugar-binding capacity, and ability to form phospholipids monolayers and tubular myelin have also been observed.
	0.97	SFTPA1 genomic sequence (Gene ID: 653509) is located between positions 81370695-81375199 of the positive strand, whereas the SFTPA2 (Gene ID: 729238) is located in the complement strand, positions 81315608-81320163.
	0.97	SFTPA1 and SFTPA2 genes results in a variety of mRNA transcripts.
	0.97	SP-A1 and SP-A2 mRNA variants also show sequence differences at the 3'UTRs.
	0.97	SP-A genes SFTPA1 and SFTPA2 are located in opposite transcriptional orientation, flanking a pseudogene (SFTPA3P).
	0.97	SP-A1 and SP-A2 expression
	0.96	SP-A1, and Thr66, Asn73, Val81, and Arg85 for SP-A2.
	0.96	SFTPA1 and SFTPA2.
	0.96	SFTPA1 and SFTPA2 genetic variants and acute and chronic lung disease have been identified in several populations and study groups including neonates, children, and adults.
	0.95	SP-A1 and SP-A2 genes and among their corresponding variants are located in the collagen-like domain.
	0.95	SFTPA1 and SFTPA2, as assessed by the protein ratio of SP-A1 to total SP-A, have been observed in human bronchoalveolar lavage samples as a function of age and lung health status (e.g. healthy vs. cystic fibrosis, culture positive vs. negative; asthmatic vs. control).
	0.95	SP-A2 variants contain two AU-rich elements (AUUUA), whereas the SP-A1 sequences contain only one.
	0.94	SP-A1 and SP-A2 monomers composed of six trimeric structural subunits of 105kDa.
	0.94	SP-A1 and SP-A2 variants by glucocorticoids.
	0.93	SFTPA1 or SFTPA2 variants are located within the sequence for the signal peptide, collagen-like region, and CRD.
	0.93	SP-A1 and SP-A2 in a variety of innate immunity and surfactant related functions including cytokine production, modulation of surfactant secretion, phagocytosis by alveolar macrophages, as well as other structural characteristics.
	0.93	SFTPA1 and SFTPA2 based on various combinations of single nucleotide polymorphisms (SNPs) within the coding region that may or may not change the encoded amino acids.
	0.93	SP-A 5'UTR splice variants is not a random process as there are major, minor, and rare splice-variants for SP-A1 and SP-A2 transcripts.
	0.91	SFTPA1 and SFTPA2 by primer extension in two independent studies; these identified three transcription start sites for SFTPA1, and one common transcript start site for SFTPA2, although some minor discrepancies observed between the two studies were attributed to variations in the individual lung RNA samples, and/or the limited number of clones tested.
	0.90	SP-A1 and SP-A2, and some of the structural differences between SP-A1 and SP-A2 may be responsible for functional differences.
	0.90	SFTPA1 (6A, 6A2, 6A3, 6A4), and six SFTPA2 (1A, 1A0, 1A1, 1A2, 1A3, 1A5) variants have been observed in higher frequency in the general population.
	0.89	SP-A monomer is a 35kDa protein composed by 248 amino acids, and the two gene products (SP-A1 and SP-A2) differ in four amino acids at the coding region.
	0.88	SP-A2 variants and the SP-A1 variant 6A2 has been shown to negatively affect translation efficiency, by mechanisms that involve formation of secondary structures with different stabilities, as well as differences in predicted miRNA binding to this element.
	0.79	SP-A1 and SP-A2 variants
	0.70	SP-A1, and SP-A2 monomers), and homo-oligomers (i.e. consisting of SP-A1 or SP-A2 monomers) are functional, and both gene products are required for tubular myelin formation.
	0.67	SP-A1 and SP-A2 variants remains to be determined.
	0.66	SFTPA1 and SFTPA2 and their genetic complexity, differences in the regulation of expression among SP-A variants may underlie individual susceptibility in response to different insults such as oxidative stress and disease.
	0.58	SP-A1 and SP-A2 protein content in certain lung diseases or conditions, as well as gain insight into the basis of individual disease susceptibility.
	0.57	SFTPA1 and SFTPA2).
	0.53	SFTPA2 in alveolar epithelial cells, as well as TTF-1 binding elements (TBE), important for hormonal regulation of lung development, as well as temporal and spatial control of SP-A gene expression.
	0.53	SP-A1 and SP-A2 mRNAs in a variety of physiological and pathological conditions.
21310059	0.97	SFTPA1, SFTPA2 and SFTPD observed in our study were similar to those previously reported in European populations.
	0.96	SFTPA1 was found to be in LD with SFTPD aa11, but only a marginal LD was found between SFTPA2 1A and SFTPD aa11 (see Table E3 in Additional File 1).
	0.95	SFTPA1, SFTPA2 and SFTPD
	0.95	SFTPA1, SFTPA2 and SFTPD genes
	0.95	SFTPA1, and SFTPA2 in infectious diseases.
	0.94	SFTPA1 codons 19, 50, 62, 133 and 219, and at the SFTPA2 codons 9, 91, 140 and 223 have been used to define the SP-A haplotypes, which are conventionally denoted as 6An for the SFTPA1 gene and 1An for the SFTPA2 gene (see Table E1 in Additional File 1).
	0.94	SFTPA1 and SFTPA2, whereas SFTPD aa11 was only observed in LD with SFTPA1 aa19 (see Figure 1).
	0.94	SFTPA1 and SFTPA2 genes.
	0.92	SFTPA1-SFTPA2 haplotype, 6A2-1A0, was underrepresented in patients (P = 0.0005, OR = 0.77; 95% CI 0.66 to 0.90), whereas 6A3-1A was overrepresented (P = 0.0007, OR = 3.92; 95% CI 1.63 to 10.80) (see Table 3).
	0.92	SFTPA1 and SFTPA2, as well as of haplotypes encompassing these genes, with the susceptibility, severity and outcome of CAP.
	0.91	SFTPA1 and SFTPA2 were previously found to be in LD.
	0.91	SP-A2 shows higher biological activity than SP-A1.
	0.89	SFTPA1 and SFTPA2 were respectively TGC and AGC, which correspond mainly with the 6A2 and 1A0 haplotypes respectively.
	0.88	SFTPA1, SFTPA2 and SFTPD gene variants
	0.85	SFTPA1 aa50-G, aa219-C as well as SFTPA2 aa9-A and aa91-G or genotypes carrying these alleles were associated with protection against CAP.
	0.79	SFTPA1 and SFTPA2 genes (Table 1).
	0.77	SFTPA2 1A0 (P = 0.002, OR = 0.79), SFTPA1-SFTPA2 6A2-1A0 (P = 0.0005, OR = 0.77), and SFTPD-SFTPA1-SFTPA2 C-6A2-1A0 (P = 0.00001, OR = 0.62) were underrepresented in patients, whereas haplotypes SFTPA2 1A10 (P = 0.00007, OR = 6.58) and SFTPA1-SFTPA2 6A3-1A (P = 0.0007, OR = 3.92) were overrepresented.
	0.77	SFTPA1 and SFTPA2 were reported to be in strong LD, and several haplotypes of these loci tend to segregate together, being 6A2-1A0 the major haplotype.
	0.73	SFTPA2 aa9-A, and a recessive effect of SFTPA1 aa50-G and aa219-C as well as SFTPA2 aa223-C were associated with a lower risk of CAP (see Table 1).
	0.58	SFTPA1, SFTPA2 and SFTPD are associated with susceptibility to CAP, and that several haplotypes also influence severity and outcome of CAP.
	0.57	SFTPA1 and SFTPA2 haplotypes 6A2, 1A0 and 6A2 to 1A0, and the SFTPD-SFTPA1-SFTPA2 haplotype C-6A2 to 1A0 are associated with a protective role against the development of Community-acquired pneumonia (CAP).
	0.55	SFTPA1 are in LD with SFTPD aa11 in our population, but only a marginal LD between SFTPA2 and SFTPD aa11 was observed.
	0.54	SP-A1 and SP-A2 are poorly understood.
	0.50	SFTPA1, SFTPA2 and SFTPD) are located in a cluster at 10q21-24.
23311887	0.97	SP-A1 and SP-A2 transcripts are expressed in adult human alveolar type II cells.
	0.96	SP-A1 and SP-A2, 295 bp).
	0.96	SP-A1 and SP-A2 mRNA and protein were detected (Figure 7).
	0.94	SP-A1 and SP-A2 mRNA after exposure to 5 mug/mL of LPS at different time points.
	0.94	SP-A1 and SP-A2.
	0.93	SP-A1 and SP-A2 genes are differentially expressed in different tissues.
	0.89	SP-A1 and SP-A2 mRNA after exposure to different concentrations of LPS for 8 h. (C) Comparison of the SP-A protein after exposure to different concentrations of LPS for 8 h. Each value represents the mean +- SEM for n = 3.
	0.83	SP-A1 and SP-A2, which share 96% and 97% similarities in amino acid and nucleotide sequences, respectively, encode SP-A. SP-A also has characteristic structures similar to those of the C-type lectin superfamily, which forms a flower bouquet structure composed of six trimeric subunits, each of which consists of 26 kDa to 35 kDa monomers.
	0.76	SP-A mRNA is encoded by the SP-A2 gene, whereas only 35% is derived from the SP-A1 gene in the lungs.
	0.75	SP-A1 and SP-A2 mRNA.
	0.73	SP-A mRNA and for gel electrophoresis of SP-A1 and SP-A2 mRNA.
	0.70	SP-A1 and SP-A2 mRNA and SP-A protein syntheses compared with those exposed to 0 and 0.1 mug/mL of LPS (P < 0.05).
	0.61	SP-A1 and SP-A2 mRNA and protein were significantly increased within 2 h (P < 0.05) and maintained beyond 24 h (Figure 8).
	0.59	SP-A2 gene is predominantly detected in the trachea and submucosal gland cells in the airway, whereas SP-A1 and SP-A2 transcript expressions are both detected in the small and large intestines of humans.
	0.58	SP-A1 and SP-A2 mRNA and protein syntheses in time- and concentration-dependent manners.
	0.57	SP-A1 and SP-A2 genes were expressed in the renal tissues and HK-2 cells in the same way as in the alveolar type II cells.
	0.55	SP-A1 (Lane 3) and SP-A2 (Lane 4) mRNA transcripts were detected in human renal tissues.
24729982	0.97	SP-A2 regulates many macrophage proteins in a manner similar to that of native mouse SP-A, whereas SP-A1 may be less effective or may alter the expression of proteins that are not affected by either native mouse SP-A or human SP-A2.
	0.96	SP-A KO mice or WT mice with several mouse lines containing human SP-A transgenes to determine the effects of endogenous expression of the human SP-A transgenes on the AM proteome.
	0.95	SP-A KO mice in order to determine how the presence of human SP-A in the transgenics altered the proteome of the alveolar macrophage (Table 2).
	0.95	SP-A (both SP-A1 and SP-A2), and scanned.
	0.94	SP-A1 gene, one expressing the 6A4 variant at low levels and another expressing the 6A2 variant at higher levels, and those expressing the human SP-A2 gene (1A0 variant) at low levels and at high levels.
	0.94	SP-A (in WT mice) vs those produced by the expressed human SP-A transgene or differences in the levels of SP-A regardless of type.
	0.93	SP-A bands from the 6A2 (SP-A1) and 1A0 (SP-A2) mice used in this study are plotted on a log scale.
	0.93	SP-A and the specific receptors involved, similarities in the effects of human SP-A on phagocytosis in human and rat alveolar macrophages and mouse alveolar macrophages (our unpublished data) confirm that at least some of the SP-A effects are SP-A-specific, rather than species-specific.
	0.92	SP-A2 on phagocytosis in vitro we found that SP -A2 enhanced phagocytosis of Pseudomonas aeruginosa more than SP-A1 did.
	0.91	SP-A2 were similar to each other but different from KO indicating a lack of variant-specific effects at very low levels of SP-A.
	0.90	SP-A1 to total SP-A in humans varies as a function of lung disease and age.
	0.87	SP-A1/total SP-A ratios and found a range of 0.003 to .999 (mean 0.21; SD 0.241).
	0.82	SP-A2, low levels of SP-A1, and low levels of SP-A2, with wild type (WT) and SP-A KO mice.
	0.63	SP-A1 and SP-A2
	0.62	SP-A2 transgene had very similar protein expression patterns suggesting that responses to low levels of SP-A are independent of SP-A genotype, whereas the responses to higher amounts of SP-A are genotype-dependent.
12908879	0.97	SP-A1 and SP-A2 marker loci.
	0.95	SP-A2 and SP-A1.
	0.94	SP-A1 and SP-A2 using GDA software.
	0.94	SP-A1 with SP-A2.
	0.92	SP-A1 and SP-A2 markers.
	0.87	SP-A1 with SP-A2.
	0.71	SP-A1 and SP-A2 in the German study group and SP-A2 in the White American study group deviate from HWE, the estimates of haplotype frequencies may be biased and significant associations between SP-A1 and SP-A2 could be also due to departure from HWE in these two study groups.
25957169	0.97	SP-A in human lung tissue (positive control), D) WT murine distal airway (negative control), E) SP-A-/- murine distal airway (negative control), F) SP-A2 223K targeted mice alveolar macrophages and distal airway, G) SP-A2 223Q targeted mice alveolar macrophages and distal airway.
	0.96	SP-A2 transgenes gave positive reactions to the antibody in the alveolar regions and in alveolar macrophages (which are known to internalize SP-A) for both of the SP-A223K/- (Fig. 3F) and SP-A223Q/- (Fig. 3G) mice.
	0.94	SP-A2 at position Q223K (1A0 versus 1A3) can dramatically impair SP-A2 from binding the pathogen (MMF), which consequently leads to a heightened innate response that was not significantly different than when SP-A is absent altogether.
	0.93	SP-A that may be associated with lung disease, and our findings demonstrate that allelic differences in SP-A2 (Gln223Lys) affect the binding to MMF.
	0.92	SPA-/- background to yield experimental animals SP-A2 223K/- and SP-A2 223Q/-.
	0.89	SP-A is encoded by two genes designated, SP-A1 and SP-A2.
22553125	0.97	SP-A1 and SP-A2, consisting of single nucleotide polymorphisms (SNPs), haplotypes, and other variations have been associated with acute and chronic lung disease throughout life in several populations and study groups.
	0.97	SP-A expression has also been postulated, and alternative splicing at the SP-A 5'UTR is a major regulatory mechanism for differential SP-A1 and/or SP-A2 variant expression.
	0.97	SP-A expression, both the total and the relative levels of SP-A1 and SP-A2.
	0.88	SP-A is encoded by two functional genes, SFTPA1 (SP-A1) and SFTPA2 (SP-A2).
	0.87	SP-A1 and SP-A2 is affected, resulting in altered immune and inflammatory responses.
28727907	0.97	SP-A genes (SFTP-A1 and SFTP-A2) that encode two different proteins SP-A1 and SP-A2 that have biochemical and functional differences.
	0.88	SP-A2 (+/-) mice but not in SP-A KO (-/-) mice.
	0.87	SP-A1 and SP-A2) rather than the total SP-A plays a role in lung disease susceptibility.
	0.86	SP-A2 (+/-) and the SP-A KO (-/-) mouse models.
16356236	0.97	SP-A1 and SP-A2.
	0.95	SP-A2 gene and haploptype 6A/1A3 in RSV-infected infants, whereas allele 1A of SP-A2 and allele 6A of SP-A1 were under-represented.
	0.93	SP-A is encoded by two genes (SP-A1 and SP-A2), which are located on chromosome 10.
27793398	0.97	SP-A2 and compare its efficacy in neutralising RSV with the trimeric rfhSP-A of SP-A1 used in this study.
	0.91	SP-A1 and SP-A2 have been found, including the capacity of SP-A2 to bind various sugars with a higher affinity than SP-A1.
	0.76	SP-A forms functional heterotrimeric units composed of Sftpa1 and Sftpa2 gene products (SP-A1 and SP-A2), the composition of which varies in different disease states.
25278226	0.97	SFTPA1 and SFTPA2 in fetal lung explants (cell culture was exposed to 2500 ng/ml insulin for 6 days) and SFTPA1 only in H441 cells (cell culture was exposed to 2500 ng/ml insulin for 24 hours).
	0.96	SFTPA1, SFTPA2, SFTPB, SFTPC, or SFTPD.
30293076	0.97	SP-A is comprised of 2 proteins, SP-A1 and SP-A2, and their ratio in the native SP-A protein has been found to vary amongst individuals.
22815690	0.96	SP-A1 and SP-A2 decreased (p = 0.6, p<0.01) and no further correlation could be observed.
	0.95	SP-A expression cultures were grouped according their basal median expression of SP-A1/SP-A2 (low level SP-A1<1436, SP-A2<2500, black bars; high level SP-A1>1436 and SP-A2>2500, hatched bars; C, D).
	0.94	SPA-1 and SP-A2 mRNA level.
	0.94	SP-A1 mRNA expression level, stimulation with roflumilast-N-oxide 1 microM induced an insignificant trend towards augmentation in SP-A1 mRNA expression, but not in SP-A2 mRNA (Figure 3C and D).
	0.93	SP-A1, SP-A2 and SP-C mRNA expression remain constant (Figure 2).
	0.93	SP-A1 and SP-A2 mRNA with a Low Intracellular Basal Level
	0.92	SP-A1, SP-A2; SP-B; SP-C and SP-D mRNA were measured by real-time PCR after culture.
	0.92	SP-A1 and six alleles of SP-A2 have been identified until now.
	0.89	SP-A1 level is higher than SP-A2 which turns to the opposite in adult lung.
	0.88	SP-A1 (A) and SP-A2 (B) mRNA was measured by real-time PCR.
	0.88	SP-A1 mRNA was more sensitive to regulation by roflumilast-N-oxide than SP-A2 mRNA.
	0.73	SP-A expression, we divided the cells in such with low (values SP-A1: rE <1436; SP-A2: rE <2500) and high baseline intracellular mRNA expression (values SP-A1: rE >1436; SP-A2: rE >2500).
	0.67	SP-A2, SP-B, SP-C and SP-D expression significantly by 50-70% of the controls without Indomethacin whereas the reduction in SP-A1 expression did not reach statistical significance (Figure 4A).
	0.66	SP-A levels are found in lung diseases as exemplified by higher SP-A1/SP-A2 levels in patients suffering from adenocarcinoma which correlates with tumour-grading, higher level in patients with alveolar proteinosis or reduced levels in diseases such as the Acute Respiratory Distress Syndrome (ARDS).
	0.66	SP-A1 and SP-A2 mRNA expression.
	0.55	SP-A is encoded by two functional genes, SFTPA1 coding for SP-A1 and SFTPA2 coding for SP-A2 and one SP-A pseudogen.
32152944	0.96	SP-A, which is made up of highly homologous SPA-1 and SPA-2 polypeptides.
	0.96	SP-A2, which both affect the amino acids in CRD region of SP-A, may alter binding to M. tuberculosis and thus were found to be strongly linked with tuberculosis susceptibility (Malik et al.).
	0.94	SP-A1 and SP-A2 genes have been described which indicate protection or susceptibility toward pulmonary TB in the populations studied in Mexico, Ethiopia, India and China (Floros et al.; Madan et al.; Malik et al.; Vaid et al.; Yang et al.).
	0.92	SP-A exists in two isoforms, SP-A1 and SP-A2, which are encoded by distinct genes.
	0.88	SP-A1 alleles (SFTPA1 307A, SFTPA1 776T) and two SP-A2 alleles (SFTPA2 355C and SFTPA2 751C) were associated with tuberculosis susceptibility in Ethiopia (Malik et al.).
	0.79	SP-A2 1649G leads to a transversion (proline to alanine), affecting the triple helical structure of SP-A (Yang et al.).
19287351	0.96	SP-A2 1A0/SP-A1 6A2).
	0.94	SP-A1 and SP-A2 gene products, it is unknown whether differences in the surfactant protein-mediated host response to RSV exists.
	0.93	SP-A locus consists of two functional genes (SP-A1 and SP-A2) in opposite transcriptional orientation.
	0.73	SP-A2 1A0/SP-A1 6A2) were identified to potentially associate with protection of severe RSV disease.
	0.65	SP-A2 1A0/SP-A1 6A2) were associated with severe RSV disease, with two being protective.
21504569	0.96	SP-A was confirmed to represent SP-A2, but the assay used in the present study is known to detect both SP-A1 and SP-A2 isoforms.
	0.96	SP-A levels, and also if SP-A1 and SP-A2 predict disease progression or whether these changes are related to smoking alone.
31354704	0.96	SP-A1 and SP-A2, encoded by SFTPA1 and SFTPA2, respectively, which are produced by the alveolar type II cells (T2C).
	0.93	SFTPA1 and SFTPA2, encoding SP-A1 and SP-A2 proteins, respectively.
25184962	0.95	SFTPA2 in the control of pandemic H1N1, although the mechanism by which SP-A may act is still ambiguous.
	0.78	SP-A gene SFTPA2 that positively correlated with flu severity.
20439915	0.95	Surfactant protein-A (SP-A) is a C-type lectin encoded by SFTPA1 and SFTPA2, with a triple helical collagen region on the N-terminus and a carbohydrate recognition domain (CRD) on the C-terminus.
21945366	0.95	SP-A1 and SP-A2 that encode for SP-A1 and SP-A2 proteins.
24954098	0.94	SP-A gene products, SP-A1 and SP-A2, have distinct roles.
	0.54	SP-A genes, SP-A1 and SP-A2, plus several variants for each gene, indicates that SP-A regulation and function is more complex than in animals.
	0.53	SP-A2 hTG mice with human SP-A1, SP-A2, or mixtures of both gene products and studying the resultant changes in the AM proteome.
25058539	0.93	SP-A1 and SP-A2 mRNA expression following Dicer and Argonaut-2 knockdown in ATII cells
	0.85	SP-A1 and SP-A2, some of which have been associated with lung disease susceptibility and/or pathogenesis in neonates, children, and adults.
	0.85	SP-A transcripts (3 for SP-A1, 3 for SP-A2, and 5 for both genes), and 52 miRNAs expressed only in ATI cells had predicted binding to SP-A 3'UTRs (14 for SP-A1, 13 for SP-A2, and 15 for both genes) (Table 2).
	0.85	Surfactant protein A, the most abundant protein of this complex, plays an important role in innate immunity, and its function appears to be dependent on the relative content of two gene products (SP-A1 and SP-A2).
	0.84	SP-A1 and SP-A2 mRNAs, as well as total SP-A protein than cells transfected with the control siRNA.
	0.83	SP-A1 and SP-A2 genotype.
	0.67	SP-A 3'UTR sequences (5 miRNAs for SP-A1, 4 miRNAs for SP-A2, and 2 miRNAs for both genes) (Table 3).
	0.53	SP-A1 and SP-A2 variants in several experimental models.
28351530	0.93	SP-A1, SP-A2 and TNF-alpha expression were significantly increased in HK-2 cells after treatment with LPS.
	0.87	SFTPA2, MBL3 and SFTPA1 are in order upstream of SFTPD, which is then followed by MBL1.
	0.79	SP-A1 and SP-A2 and Allelic Variants
	0.60	SP-A1 gene products and one SP-A2 product per trimer.
	0.52	SP-A is a result of the expression of two distinct but similar genes, SP-A1 and SP-A2.
19284609	0.93	SP-A1 and SP-A2 on the other hand display several different alleles and splicing variants, moreover different oligomeric states have been described.
	0.84	SP-A gene was diverged into SP-A1 and a second gene which subsequently emerged to SP-A2 and the SP-A pseudogene.
	0.77	SP-A1 and SP-A2 up to date prevents a differential analysis of the two gene products in situ.
17407567	0.93	SFTPA may play a role in the pathogenesis of asthma, and infants in our cohort, by virtue of their family histories of asthma, may differ in SFTPA1 and SFTPA2 hapylotype distributions compared to the general population.
24950659	0.92	SFTPA1 and SFTPA2 has been shown; and LD among variants at these genes could influence the results of genetic-association studies.
	0.92	SFTPA1, SFTPA2, and SFTPD genes in H1N1pdm IAV infection in humans.
	0.88	SFTPA1 and SFTPA2 on respiratory gas exchange in 52 hospitalized patients.
	0.66	SFTPA1 allele rs1136450-G was also associated, although to a lower extent, with the development of ARF (P = 0.038; OR, 2.64) and the use of MV (P = 0.040; OR, 2.55); these associations may be secondary to the existence of LD between SFTPA1 and SFTPA2 variants (Figure 2).
21613931	0.92	SFTPA1 and SFTPA2 in an additional 58 FIP kindreds led to the discovery of a second SFTPA2 mutation in one additional family.
	0.67	Surfactant protein A has two isoforms encoded by adjacent genes (SFTPA1, SFTPA2).
	0.63	SFTPA1 and SFTPA2.
29152081	0.92	SFTPA1, SFTPA2 and SFTPC, surfactant genes which have been reported to express exclusively in type II penumocytes, have showed their unique roles in LUAD.
	0.81	SFTPA2, SFTPA1, CHIPA2, SFTPC, and RPL13AP17) with high diagnostic power in LUAD across 27 types of cancer
23169704	0.92	SP-A proteins (SP-A1 versus SP-A2) or by different combinations and/or proportions of SP-A1:SP-A2 and their respective genetic variants.
11806849	0.91	SP-A1 gene (designated 6A to 6A20), and 15 haplotypes have been identified in the SP-A2 gene (designated 1A to 1A13).
	0.88	SP-A1 (6A2) and SP-A2 (1A0) haplotypes.
26641881	0.91	SP-A1, SP-A2 and SP-D mRNA expression at 6 h at 5 and 10 mug/ml.
32082572	0.91	Sftpa1 and Sftpa2, encoding SP-A1 and SP-A2, respectively, and these two gene products have been shown to have a differential impact on several AM functions.
25025725	0.90	SP-A1, a change in the relative levels of SP-A1 versus SP-A2 might skew our assay when implemented across a heterogeneous cohort.
	0.85	SP-A. Thus, additional genotyping at this SNP (rs1059046) would be required to fully correlate SP-A2 and Lys223 variant levels with a specific allelic variant.
	0.76	SP-A1 allelic variants (6A, 6A2, 6A3, 6A4) and six SP-A2 allelic variants (1A, 1A0, 1A1, 1A2, 1A3, and 1A5) are observed with a frequency of greater than 1% in the general population.
	0.53	SP-A2 223 genotypes which does not utilize the pan-SP-A Gln223 peptide.
30774012	0.88	SP-A1, SP-A2, or SP-B promoter plasmids containing luciferase reporter gene and then treated with medium or medium containing dust extract (1%) for 24 h. Luciferase activities in cell lysates were determined and normalized to total protein concentration of cell lysates.
	0.78	SP-A1, SP-A2, and SP-B mRNA levels with 0.25% or 1% dust extract causing maximal inhibition (Figure 1g-i).
	0.77	SP-A1, SP-A2, and SP-B mRNAs
	0.67	SP-A1 promoter activity, but inhibited SP-A2 and SP-B promoter activities (Figure 2).
	0.64	SP-A1, SP-A2, and SP-B mRNA levels were quantified by real-time qRT-PCR and normalized to 18S rRNA levels.
26966339	0.86	SP-A1 and SP-A2 SNPs, which affect splicing and/or mRNA maturation, had associations with tuberculosis.
26998217	0.85	SP-A KO mice as described above, we added SP-A1, SP-A2 (10 mug each), or both (low dose 5 mug each or high dose 10 mug each) to the cultured macrophages for 1 h before fixing and staining the cells.
30854216	0.83	SFTPA1 and SFTPA2 genes, we designed a specific primer set corresponding to the differences in the nucleotide sequence (forward primer: 5 -TGGTCAGTGGCCTGACCC-3 and reverse primer: 5 -AGAGTCAGGGCCCATCAGA-3 ).
23328842	0.82	SP-A2 haplotype alone or in combination with an SP-A1 haplotype was also associated with increased risk of meningococcal disease and respiratory symptoms in infants at risk for asthma .
	0.77	SP-A1, SP-A2, and SP-D marker SNPs (Table 1).
24868212	0.82	SP-A2 1A0 variant and SP-A1/SP-A2 6A2/1A0 haplotype have frequently been reported as being associated risk factors for the development of RDS, and the SP-A1 6A3 variant as a protective factor for RDS, in Finnish and North American studies.
	0.53	SP-A (SFTPA1 and SFTPA2) are located on chromosome 10q22-q23.
27250970	0.79	SP-A1 gene are 6A, 6A2, 6A3, and 6A4, and those for the SP-A2 gene are 1A, 1A0, 1A1, 1A2, 1A3, and 1A5.
16884531	0.64	SP-A1 and SP-A2 allele haplotypes were also in linkage disequilibrium (P < 0.0001).
25621661	0.61	SFTPA2 likely disrupt normal routing and processing of the protein, supporting the concept that, like mutations in SFTPC, SP-A-related disease results from misfolding of the protein in alveolar type II epithelial cells.
28485325	0.58	SP-A1 and SP-A2).