CLEC4M: Difference between revisions

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{{Infobox_gene}}
{{Infobox_gene}}
'''C-type lectin domain family 4 member M''' is a [[protein]] that in humans is encoded by the ''CLEC4M'' [[gene]].<ref name="pmid10072769">{{cite journal | vauthors = Yokoyama-Kobayashi M, Yamaguchi T, Sekine S, Kato S | title = Selection of cDNAs encoding putative type II membrane proteins on the cell surface from a human full-length cDNA bank | journal = Gene | volume = 228 | issue = 1-2 | pages = 161–7 |date=Apr 1999 | pmid = 10072769 | pmc =  | doi =10.1016/S0378-1119(99)00004-9  }}</ref> CLEC4M has also been designated as '''CD299''' ([[cluster of differentiation]] 299).
'''C-type lectin domain family 4 member M''' is a [[protein]] that in humans is encoded by the ''CLEC4M'' [[gene]].<ref name="pmid10072769">{{cite journal | vauthors = Yokoyama-Kobayashi M, Yamaguchi T, Sekine S, Kato S | title = Selection of cDNAs encoding putative type II membrane proteins on the cell surface from a human full-length cDNA bank | journal = Gene | volume = 228 | issue = 1–2 | pages = 161–7 |date=Apr 1999 | pmid = 10072769 | pmc =  | doi =10.1016/S0378-1119(99)00004-9  }}</ref> CLEC4M has also been designated as '''CD299''' ([[cluster of differentiation]] 299).


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*{{cite journal  | vauthors=Baribaud F, Doms RW, Pöhlmann S |title=The role of DC-SIGN and DC-SIGNR in HIV and Ebola virus infection: can potential therapeutics block virus transmission and dissemination? |journal=Expert Opin. Ther. Targets |volume=6 |issue= 4 |pages= 423–31 |year= 2006 |pmid= 12223058 |doi= 10.1517/14728222.6.4.423 }}
*{{cite journal  | vauthors=Baribaud F, Doms RW, Pöhlmann S |title=The role of DC-SIGN and DC-SIGNR in HIV and Ebola virus infection: can potential therapeutics block virus transmission and dissemination? |journal=Expert Opin. Ther. Targets |volume=6 |issue= 4 |pages= 423–31 |year= 2006 |pmid= 12223058 |doi= 10.1517/14728222.6.4.423 }}
*{{cite journal  | author=Becker Y |title=HIV-1 gp120 binding to dendritic cell receptors mobilize the virus to the lymph nodes, but the induced IL-4 synthesis by FcepsilonRI+ hematopoietic cells damages the adaptive immunity--a review, hypothesis, and implications. |journal=Virus Genes |volume=29 |issue= 1 |pages= 147–65 |year= 2004 |pmid= 15215692 |doi= 10.1023/B:VIRU.0000032797.43537.d3 }}
*{{cite journal  | author=Becker Y |title=HIV-1 gp120 binding to dendritic cell receptors mobilize the virus to the lymph nodes, but the induced IL-4 synthesis by FcepsilonRI+ hematopoietic cells damages the adaptive immunity--a review, hypothesis, and implications. |journal=Virus Genes |volume=29 |issue= 1 |pages= 147–65 |year= 2004 |pmid= 15215692 |doi= 10.1023/B:VIRU.0000032797.43537.d3 }}
*{{cite journal  | vauthors=Lalor PF, Lai WK, Curbishley SM |title=Human hepatic sinusoidal endothelial cells can be distinguished by expression of phenotypic markers related to their specialised functions in vivo. |journal=World J. Gastroenterol. |volume=12 |issue= 34 |pages= 5429–39 |year= 2006 |pmid= 17006978 |doi=  |display-authors=etal}}
*{{cite journal  | vauthors=Lalor PF, Lai WK, Curbishley SM |title=Human hepatic sinusoidal endothelial cells can be distinguished by expression of phenotypic markers related to their specialised functions in vivo. |journal=World J. Gastroenterol. |volume=12 |issue= 34 |pages= 5429–39 |year= 2006 |pmid= 17006978 |doi=  10.3748/wjg.v12.i34.5429|display-authors=etal}}
*{{cite journal  | vauthors=Curtis BM, Scharnowske S, Watson AJ |title=Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp120. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 17 |pages= 8356–60 |year= 1992 |pmid= 1518869 |doi=10.1073/pnas.89.17.8356  | pmc=49917  }}
*{{cite journal  | vauthors=Curtis BM, Scharnowske S, Watson AJ |title=Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp120. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 17 |pages= 8356–60 |year= 1992 |pmid= 1518869 |doi=10.1073/pnas.89.17.8356  | pmc=49917  }}
*{{cite journal  | vauthors=Gattegno L, Ramdani A, Jouault T |title=Lectin-carbohydrate interactions and infectivity of human immunodeficiency virus type 1 (HIV-1). |journal=AIDS Res. Hum. Retroviruses |volume=8 |issue= 1 |pages= 27–37 |year= 1992 |pmid= 1736938 |doi=10.1089/aid.1992.8.27  |display-authors=etal}}
*{{cite journal  | vauthors=Gattegno L, Ramdani A, Jouault T |title=Lectin-carbohydrate interactions and infectivity of human immunodeficiency virus type 1 (HIV-1). |journal=AIDS Res. Hum. Retroviruses |volume=8 |issue= 1 |pages= 27–37 |year= 1992 |pmid= 1736938 |doi=10.1089/aid.1992.8.27  |display-authors=etal}}

Latest revision as of 11:31, 2 March 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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C-type lectin domain family 4 member M is a protein that in humans is encoded by the CLEC4M gene.[1] CLEC4M has also been designated as CD299 (cluster of differentiation 299).

This gene encodes L-SIGN (liver/lymph node-specific intracellular adhesion molecules-3 grabbing non-integrin), a type II integral membrane protein that is 77% identical to CD209 antigen, an HIV gp120-binding protein. This protein, like CD209, efficiently binds both intercellular adhesion molecule 3 (ICAM3) and HIV-1 gp120, and enhances HIV-1 infection of T cells. This gene is mapped to 19p13.3, in a cluster with the CD209 and CD23/FCER2 genes. Multiple alternatively spliced transcript variants have been found for this gene, but the biological validity of some variants has not been determined.[2]

References

  1. Yokoyama-Kobayashi M, Yamaguchi T, Sekine S, Kato S (Apr 1999). "Selection of cDNAs encoding putative type II membrane proteins on the cell surface from a human full-length cDNA bank". Gene. 228 (1–2): 161–7. doi:10.1016/S0378-1119(99)00004-9. PMID 10072769.
  2. "Entrez Gene: CLEC4M C-type lectin domain family 4, member M".

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.