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TNFSF15 (tumor necrosis factor (ligand) superfamily, member 15)

Written2009-08Gui-Li Yang, Jian-Wei Qi, Zhi-Song Zhang, Lu-Yuan Li
Department of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15213, USA (LYL); College of Pharmacy, College of Life Sciences, Nankai University, 94 Wei Jin Road, 300071 Tianjin, China (LYL, GLY, JWQ, ZSZ)

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Alias (NCBI)MGC129934
HGNC Alias symbTL1
HGNC Alias namevascular endothelial cell growth inhibitor
 TNF superfamily ligand TL1A
 TNF ligand-related molecule 1
 vascular endothelial growth inhibitor-192A
HGNC Previous nametumor necrosis factor (ligand) superfamily, member 15
LocusID (NCBI) 9966
Atlas_Id 42638
Location 9q32  [Link to chromosome band 9q32]
Location_base_pair Starts at 114784652 and ends at 114806039 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping TNFSF15.png]
Local_order TNFSF15 gene at 9q32, near the CD30L gene at 9q33.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)


  Boxes with roman numerals above represent exons and horizontal lines represent intronic sequence. The putative transcription start site is indicated by a double arrowhead. R denotes the 5' untranslated sequence unique to each respective transcript, and stippled boxe represents the common 3' untranslated region.
Description The human VEGI gene spans about 17 kb and consists of four exons.
Transcription The size of VEGI mRNA is approximately 6.5 kb. It is unusual for a human gene of 6.5 kb to contain only a small open reading frame of 522 nucleotides. Multiple VEGI transcripts generated by the use of cryptic splice sites and alternate exons.
Pseudogene Not known.


  Figure A. All three isoforms.
Figure B. A ribbon diagram of the TL1A trimer. (Jin et al. BBRC 364:1, 2007).
Description Hydrophobicity analysis of VEGI predicts a 13 amino acid hydrophobic region that follows the amino terminal segment of 12 amino acids, suggesting a structure characteristic of a type II transmembrane protein, with residues 26-174 constituting an extracellular domain analogous to domains found in other TNF family members.
VEGI isoforms exhibit a carboxyl terminal domain of 151 amino acid residues, which is encoded by part of the fourth exon, termed IVb. The initially characterized VEGI isoform, designated VEGI-174, is encoded by the fourth exon (parts IVa and IVb) alone, which includes both the putative transmembrane domain and the conserved extracellular domain. There are two additional endothelial-specific transcripts of 7.5 and 2.0 kb, which encode peptides of 251 (VEGI-251) and 192 (VEGI-192) residues, respectively. The VEGI-251 and -192 isoforms differ in their amino terminal regions, but share the conserved 151-amino acid residue carboxy terminal domain. VEGI-251 possesses a putative secretory signal peptide and its overexpression causes apoptosis of endothelial cells and inhibition of tumor growth.
  Amino acid sequence alignment of three VEGI isoforms. The putative hydrophobic regions of VEGI-251 and VEGI-174 are underlined. Asterisk denotes the start of shared sequences for all three isoforms.
Expression VEGI is specifically expressed in endothelial cells. Analysis of total RNA preparations from many cell lines and primary cell cultures by Northern blot analysis confirmed the specificity of VEGI expression, with only HUVEC and human venous endothelial cells demonstrating detectable levels of expression. Using multiple tissue Northern blots, the VEGI transcript was found in many adult human tissues, including placenta, lung, skeletal muscle, kidney, pancreas, spleen, prostate, small intestine, and colon, suggesting that the gene product may play a role in the function of a normal vasculature.The failure to detect the transcripts of this new gene in some of the human tissues probably is due to relatively small proportion of endothelial cells in these tissues. Using isoform-specific probes, we have determined that the distribution profiles of VEGI isoforms in human organs and tissues appear to be different. The 7.5 kb transcript encoding VEGI-251 was expressed at high levels in the placenta, kidney, lung and liver, whereas the 2 kb transcript corresponding to VEGI-174 was observed in liver, kidney, skeletal muscle and heart. VEGI-174 mRNA was more abundant in heart, skeletal muscle, pancreas, adrenal gland, and liver, while VEGI-251 was more abundant in fetal kidney and fetal lung. Overlapping expression of VEGI-251 and VEGI-174 mRNA was detected in prostate, salivary gland and placenta, whereas VEGI-192 mRNA was not readily detected by Northern blot. These expression patterns suggest the possibility of tissue or developmentally specific functions for VEGI isoforms. Alternatively, this expression pattern also supports the view that one VEGI isoform is the functional cytokine,while the others act in regulatory roles to modulate the activity of the active isoform. In this case, it is possible that the non-functional isoforms do not exist at the protein level. VEGI isoform expression has also been examined in cultured cells by RNase protection assay. All three known VEGI isoforms were detected in human endothelial cells, including coronary artery endothelial (HCAE), HUVE cells, and human microvascular endothelial (HMVE) cells. Very low levels are sometimes detected in adult bovine aortic endothelial (ABAE) cells. Little VEGI expression was detectable in human coronary artery smooth muscle (CASM) and mouse endothelioma bEND.3 cells. More than one isoform is detectable simultaneously, with VEGI-251 being the most abundant. The expression of this protein is inducible by TNF and IL-1 alpha, but not by gamma-interferon.
Localisation Endothelial cells and monocytes. However, VEGI was not expressed in either B or T cells.
Function VEGI is an endogenous inhibitor of angiogenesis produced largely by vascular endothelial cells and exerts a specific inhibitory activity on the proliferation of endothelial cells. VEGI enforces growth arrest of endothelial cells in G0 and early G1 phases of the cell cycle but induces apoptosis in proliferating endothelial cells. The MAPKs p38 and jun N-terminal kinase (JNK) are required for VEGI-mediated endothelial inhibition. Engineered overexpression of secreted VEGI by cancer cells or systemic administration of recombinant VEGI to tumor-bearing mice inhibits tumor growth in numerous tumor models. Recent studies show that VEGI helps modulate the immune system by activating T cells and stimulating dendritic cell maturation, suggesting that VEGI is directly involved in modulating the interaction between the endothelium and the immune system. Recombinant VEGI has an inhibitory activity on mouse bone marrow-derived EPCs in culture, preventing their differentiation toward endothelial cells.
Interaction of TL1A with DR3 promotes T cell expansion during an immune response (Migone et al., 2002).
Homology VEGI exhibits 20-30% sequence homology to human TNF-alpha, TNF-beta, and the Fas ligand, similar to that among other TNF family members.

Implicated in

Entity Colon carcinoma
Note Local production of a secreted form of VEGI via gene transfer caused complete suppression of the growth of MC-38 murine colon cancers in syngeneic C57BL/6mice. Histological examination showed marked reduction of vascularization in MC-38 tumors that expressed soluble but not membrane-bound VEGI or were transfected with control vector. The conditioned media from soluble VEGI-expressing cells showed marked inhibitory effect on in vitro proliferation of adult bovine aortic endothelial cells.
Entity Breast cancer
Note The anticancer potential of VEGI was examined in a breast cancer xenograft tumor model in which the cancer cells were co-injected with Chinese hamster ovary cells overexpressing a secreted form of the protein. The co-injection resulted in potent inhibition of xenograft tumor growth. Our findings are consistent with the view that VEGI is an endothelial cell-specific negative regulator of angiogenesis.
Entity Mucosal vaccine adjuvant
Note Kayamuro et al., (2009) reported that TL1A induced the strongest immune response and augmented OVA-specific IgG and IgA responses in serum and mucosal compartments, respectively. The OVA-specific immune response of TL1A was characterized by high levels of serum IgG1 and increased production of IL-4 and IL-5 from splenocytes of immunized mice, suggesting that TL1A might induce Th2-type responses. These findings indicate that TL1A has the most potential as a mucosal adjuvant among the TNFS cytokines.
Entity Inflammatory bowel disease
Note Bamias et al., (2003) provided evidence that the novel cytokine TL1A may play an important role in a Th1-mediated disease such as Crohn's disease. Takedatsu et al., (2008) revealed that TL1A is an important modulator in the development of chronic mucosal inflammation by enhancing T(H)1 and T(H)17 effector functions. The central role of TL1A represents an attractive, novel therapeutic target for the treatment of Crohn's disease patients.
Entity Inflammatory arthritis
Note Bull et al., (2008) demonstrated that the DR3-TL1A pathway regulates joint destruction in two murine models of arthritis and represents a potential novel target for therapeutic intervention in inflammatory joint disease. Bamias et al., (2008) concluded that TL1A may serve as an inflammatory marker in rheumatoid arthritis. Interactions between TL1A and its receptors may be important in the pathogenesis of rheumatoid arthritis.
Entity Renal inflammation and injury
Note Al-Lamki et al., (2008) suggested that TL1A may contribute to renal inflammation and injury through DR3-mediated activation of NF-kappaB and caspase-3, respectively, but that an unidentified receptor may mediate the NF-kappaB-independent induction of TNFR2 in tubular epithelial cells.


TL1A both promotes and protects from renal inflammation and injury.
Al-Lamki RS, Wang J, Tolkovsky AM, Bradley JA, Griffin JL, Thiru S, Wang EC, Bolton E, Min W, Moore P, Pober JS, Bradley JR.
J Am Soc Nephrol. 2008 May;19(5):953-60. Epub 2008 Feb 20.
PMID 18287561
Endothelial progenitor cells for postnatal vasculogenesis.
Asahara T, Kawamoto A.
Am J Physiol Cell Physiol. 2004 Sep;287(3):C572-9. (REVIEW)
PMID 15308462
Expression, localization, and functional activity of TL1A, a novel Th1-polarizing cytokine in inflammatory bowel disease.
Bamias G, Martin C 3rd, Marini M, Hoang S, Mishina M, Ross WG, Sachedina MA, Friel CM, Mize J, Bickston SJ, Pizarro TT, Wei P, Cominelli F.
J Immunol. 2003 Nov 1;171(9):4868-74.
PMID 14568967
Role of TL1A and its receptor DR3 in two models of chronic murine ileitis.
Bamias G, Mishina M, Nyce M, Ross WG, Kollias G, Rivera-Nieves J, Pizarro TT, Cominelli F.
Proc Natl Acad Sci U S A. 2006 May 30;103(22):8441-6. Epub 2006 May 12.
PMID 16698931
Circulating levels of TNF-like cytokine 1A (TL1A) and its decoy receptor 3 (DcR3) in rheumatoid arthritis.
Bamias G, Siakavellas SI, Stamatelopoulos KS, Chryssochoou E, Papamichael C, Sfikakis PP.
Clin Immunol. 2008 Nov;129(2):249-55. Epub 2008 Aug 30.
PMID 18757243
The Death Receptor 3-TNF-like protein 1A pathway drives adverse bone pathology in inflammatory arthritis.
Bull MJ, Williams AS, Mecklenburgh Z, Calder CJ, Twohig JP, Elford C, Evans BA, Rowley TF, Slebioda TJ, Taraban VY, Al-Shamkhani A, Wang EC.
J Exp Med. 2008 Oct 27;205(11):2457-64. Epub 2008 Sep 29.
PMID 18824582
Preparation and characterization of a novel chimeric protein VEGI-CTT in Escherichia coli.
Cai J, Wei R, Cheng J.
J Biomed Biotechnol. 2008;2008:564969.
PMID 18769489
A novel secreted splice variant of vascular endothelial cell growth inhibitor.
Chew LJ, Pan H, Yu J, Tian S, Huang WQ, Zhang JY, Pang S, Li LY.
FASEB J. 2002 May;16(7):742-4. Epub 2002 Mar 26.
PMID 11923219
Endothelial progenitor cells control the angiogenic switch in mouse lung metastasis.
Gao D, Nolan DJ, Mellick AS, Bambino K, McDonnell K, Mittal V.
Science. 2008 Jan 11;319(5860):195-8.
PMID 18187653
VEGI-192, a new isoform of TNFSF15, specifically eliminates tumor vascular endothelial cells and suppresses tumor growth.
Hou W, Medynski D, Wu S, Lin X, Li LY.
Clin Cancer Res. 2005 Aug 1;11(15):5595-602.
PMID 16061878
Purification and crystallization of recombinant human TNF-like ligand TL1A.
Jin T, Kim S, Guo F, Howard A, Zhang YZ.
Cytokine. 2007 Nov;40(2):115-22. Epub 2007 Oct 1.
PMID 17905596
TNF superfamily member, TL1A, is a potential mucosal vaccine adjuvant.
Kayamuro H, Yoshioka Y, Abe Y, Katayama K, Yoshida T, Yamashita K, Yoshikawa T, Hiroi T, Itoh N, Kawai Y, Mayumi T, Kamada H, Tsunoda S, Tsutsumi Y.
Biochem Biophys Res Commun. 2009 Jul 3;384(3):296-300. Epub 2009 May 4.
PMID 19406102
Vascular endothelial growth inhibitor (VEGI), an endogenous negative regulator of angiogenesis.
Metheny-Barlow LJ, Li LY.
Semin Ophthalmol. 2006 Jan-Mar;21(1):49-58. (REVIEW)
PMID 16517446
TL1A is a TNF-like ligand for DR3 and TR6/DcR3 and functions as a T cell costimulator.
Migone TS, Zhang J, Luo X, Zhuang L, Chen C, Hu B, Hong JS, Perry JW, Chen SF, Zhou JX, Cho YH, Ullrich S, Kanakaraj P, Carrell J, Boyd E, Olsen HS, Hu G, Pukac L, Liu D, Ni J, Kim S, Gentz R, Feng P, Moore PA, Ruben SM, Wei P.
Immunity. 2002 Mar;16(3):479-92.
PMID 11911831
TL1A (TNFSF15) regulates the development of chronic colitis by modulating both T-helper 1 and T-helper 17 activation.
Takedatsu H, Michelsen KS, Wei B, Landers CJ, Thomas LS, Dhall D, Braun J, Targan SR.
Gastroenterology. 2008 Aug;135(2):552-67. Epub 2008 May 7.
PMID 18598698
Characterization of a novel TNF-like ligand and recently described TNF ligand and TNF receptor superfamily genes and their constitutive and inducible expression in hematopoietic and non-hematopoietic cells.
Tan KB, Harrop J, Reddy M, Young P, Terrett J, Emery J, Moore G, Truneh A.
Gene. 1997 Dec 19;204(1-2):35-46.
PMID 9434163
The endothelial cell-produced antiangiogenic cytokine vascular endothelial growth inhibitor induces dendritic cell maturation.
Tian F, Grimaldo S, Fujita M, Cutts J, Vujanovic NL, Li LY.
J Immunol. 2007 Sep 15;179(6):3742-51.
PMID 17785811
Inhibition of endothelial progenitor cell differentiation by VEGI.
Tian F, Liang PH, Li LY.
Blood. 2009 May 21;113(21):5352-60. Epub 2009 Mar 27.
PMID 19329781
Modulation of endothelial cell growth arrest and apoptosis by vascular endothelial growth inhibitor.
Yu J, Tian S, Metheny-Barlow L, Chew LJ, Hayes AJ, Pan H, Yu GL, Li LY.
Circ Res. 2001 Dec 7;89(12):1161-7.
PMID 11739281
TL1, a novel tumor necrosis factor-like cytokine, induces apoptosis in endothelial cells. Involvement of activation of stress protein kinases (stress-activated protein kinase and p38 mitogen-activated protein kinase) and caspase-3-like protease.
Yue TL, Ni J, Romanic AM, Gu JL, Keller P, Wang C, Kumar S, Yu GL, Hart TK, Wang X, Xia Z, DeWolf WE Jr, Feuerstein GZ.
J Biol Chem. 1999 Jan 15;274(3):1479-86.
PMID 9880523
VEGI, a novel cytokine of the tumor necrosis factor family, is an angiogenesis inhibitor that suppresses the growth of colon carcinomas in vivo.
Zhai Y, Ni J, Jiang GW, Lu J, Xing L, Lincoln C, Carter KC, Janat F, Kozak D, Xu S, Rojas L, Aggarwal BB, Ruben S, Li LY, Gentz R, Yu GL.
FASEB J. 1999 Jan;13(1):181-9.
PMID 9872942
Inhibition of angiogenesis and breast cancer xenograft tumor growth by VEGI, a novel cytokine of the TNF superfamily.
Zhai Y, Yu J, Iruela-Arispe L, Huang WQ, Wang Z, Hayes AJ, Lu J, Jiang G, Rojas L, Lippman ME, Ni J, Yu GL, Li LY.
Int J Cancer. 1999 Jul 2;82(1):131-6.
PMID 10360832
Structure and inhibitory effects on angiogenesis and tumor development of a new vascular endothelial growth inhibitor.
Zilberberg L, Shinkaruk S, Lequin O, Rousseau B, Hagedorn M, Costa F, Caronzolo D, Balke M, Canron X, Convert O, Lain G, Gionnet K, Goncalves M, Bayle M, Bello L, Chassaing G, Deleris G, Bikfalvi A.
J Biol Chem. 2003 Sep 12;278(37):35564-73. Epub 2003 Jul 1.
PMID 12837752


This paper should be referenced as such :
Yang, GL ; Qi, JW ; Zhang, ZS ; Li, LY
TNFSF15 (tumor necrosis factor (ligand) superfamily, member 15)
Atlas Genet Cytogenet Oncol Haematol. 2010;14(7):665-669.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)TNFSF15   11931
Entrez_Gene (NCBI)TNFSF15    TNF superfamily member 15
AliasesTL1; TL1A; TNLG1B; VEGI; 
GeneCards (Weizmann)TNFSF15
Ensembl hg19 (Hinxton)ENSG00000181634 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000181634 [Gene_View]  ENSG00000181634 [Sequence]  chr9:114784652-114806039 [Contig_View]  TNFSF15 [Vega]
ICGC DataPortalENSG00000181634
TCGA cBioPortalTNFSF15
Genatlas (Paris)TNFSF15
SOURCE (Princeton)TNFSF15
Genetics Home Reference (NIH)TNFSF15
Genomic and cartography
GoldenPath hg38 (UCSC)TNFSF15  -     chr9:114784652-114806039 -  9q32   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)TNFSF15  -     9q32   [Description]    (hg19-Feb_2009)
GoldenPathTNFSF15 - 9q32 [CytoView hg19]  TNFSF15 - 9q32 [CytoView hg38]
Genome Data Viewer NCBITNFSF15 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AF039390 AF520785 AK291642 AK313721 AW014795
RefSeq transcript (Entrez)NM_001204344 NM_005118
Consensus coding sequences : CCDS (NCBI)TNFSF15
Gene ExpressionTNFSF15 [ NCBI-GEO ]   TNFSF15 [ EBI - ARRAY_EXPRESS ]   TNFSF15 [ SEEK ]   TNFSF15 [ MEM ]
Gene Expression Viewer (FireBrowse)TNFSF15 [ Firebrowse - Broad ]
GenevisibleExpression of TNFSF15 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)9966
GTEX Portal (Tissue expression)TNFSF15
Human Protein AtlasENSG00000181634-TNFSF15 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtO95150   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtO95150  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProO95150
Domaine pattern : Prosite (Expaxy)TNF_2 (PS50049)   
Domains : Interpro (EBI)TNF    TNF_dom    TNFSF15    Tumour_necrosis_fac-like_dom   
Domain families : Pfam (Sanger)TNF (PF00229)   
Domain families : Pfam (NCBI)pfam00229   
Domain families : Smart (EMBL)TNF (SM00207)  
Conserved Domain (NCBI)TNFSF15
PDB (RSDB)2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
PDB Europe2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
PDB (PDBSum)2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
PDB (IMB)2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
Structural Biology KnowledgeBase2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
SCOP (Structural Classification of Proteins)2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
CATH (Classification of proteins structures)2O0O    2QE3    2RE9    2RJK    2RJL    3K51    3MI8   
AlphaFold pdb e-kbO95150   
Human Protein Atlas [tissue]ENSG00000181634-TNFSF15 [tissue]
Protein Interaction databases
IntAct (EBI)O95150
Ontologies - Pathways
Ontology : AmiGOsignaling receptor binding  cytokine activity  tumor necrosis factor receptor binding  protein binding  extracellular space  plasma membrane  plasma membrane  integral component of plasma membrane  apoptotic process  activation of cysteine-type endopeptidase activity involved in apoptotic process  activation of cysteine-type endopeptidase activity involved in apoptotic process  immune response  signal transduction  activation of NF-kappaB-inducing kinase activity  integral component of membrane  tumor necrosis factor-mediated signaling pathway  
Ontology : EGO-EBIsignaling receptor binding  cytokine activity  tumor necrosis factor receptor binding  protein binding  extracellular space  plasma membrane  plasma membrane  integral component of plasma membrane  apoptotic process  activation of cysteine-type endopeptidase activity involved in apoptotic process  activation of cysteine-type endopeptidase activity involved in apoptotic process  immune response  signal transduction  activation of NF-kappaB-inducing kinase activity  integral component of membrane  tumor necrosis factor-mediated signaling pathway  
Pathways : KEGGCytokine-cytokine receptor interaction   
REACTOMEO95150 [protein]
REACTOME PathwaysR-HSA-5669034 [pathway]   
NDEx NetworkTNFSF15
Atlas of Cancer Signalling NetworkTNFSF15
Wikipedia pathwaysTNFSF15
Orthology - Evolution
GeneTree (enSembl)ENSG00000181634
Phylogenetic Trees/Animal Genes : TreeFamTNFSF15
Homologs : HomoloGeneTNFSF15
Homology/Alignments : Family Browser (UCSC)TNFSF15
Gene fusions - Rearrangements
Fusion : QuiverTNFSF15
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerTNFSF15 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)TNFSF15
Exome Variant ServerTNFSF15
GNOMAD BrowserENSG00000181634
Varsome BrowserTNFSF15
ACMGTNFSF15 variants
Genomic Variants (DGV)TNFSF15 [DGVbeta]
DECIPHERTNFSF15 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisTNFSF15 
ICGC Data PortalTNFSF15 
TCGA Data PortalTNFSF15 
Broad Tumor PortalTNFSF15
OASIS PortalTNFSF15 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICTNFSF15  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DTNFSF15
Mutations and Diseases : HGMDTNFSF15
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)TNFSF15
DoCM (Curated mutations)TNFSF15
CIViC (Clinical Interpretations of Variants in Cancer)TNFSF15
NCG (London)TNFSF15
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry TNFSF15
NextProtO95150 [Medical]
Target ValidationTNFSF15
Huge Navigator TNFSF15 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDTNFSF15
Pharm GKB GenePA36623
Clinical trialTNFSF15
DataMed IndexTNFSF15
PubMed163 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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