Biology:Kinase insert domain receptor
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Kinase insert domain receptor (KDR, a type IV receptor tyrosine kinase) also known as vascular endothelial growth factor receptor 2 (VEGFR-2) is a VEGF receptor. KDR is the human gene encoding it. KDR has also been designated as CD309 (cluster of differentiation 309). KDR is also known as Flk1 (Fetal Liver Kinase 1).
The Q472H germline KDR genetic variant affects VEGFR-2 phosphorylation and has been found to associate with microvessel density in NSCLC.[1]
Interactions
Kinase insert domain receptor has been shown to interact with SHC2,[2] Annexin A5[3] and SHC1.[4][5]
See also
- Cluster of differentiation
- VEGF receptors
References
- ↑ "Novel functional germline variants in the VEGF receptor 2 gene and their effect on gene expression and microvessel density in lung cancer". Clinical Cancer Research 17 (16): 5257–67. August 2011. doi:10.1158/1078-0432.CCR-11-0379. PMID 21712447.
- ↑ "The Shc-related adaptor protein, Sck, forms a complex with the vascular-endothelial-growth-factor receptor KDR in transfected cells". The Biochemical Journal 347 (Pt 2): 501–9. April 2000. doi:10.1042/0264-6021:3470501. PMID 10749680.
- ↑ "Lipocortin V may function as a signaling protein for vascular endothelial growth factor receptor-2/Flk-1". Biochemical and Biophysical Research Communications 258 (3): 713–21. May 1999. doi:10.1006/bbrc.1999.0678. PMID 10329451. https://zenodo.org/record/1229498.
- ↑ "Vascular endothelial growth factor induces SHC association with vascular endothelial cadherin: a potential feedback mechanism to control vascular endothelial growth factor receptor-2 signaling". Arteriosclerosis, Thrombosis, and Vascular Biology 22 (4): 617–22. April 2002. doi:10.1161/01.ATV.0000012268.84961.AD. PMID 11950700.
- ↑ "16K human prolactin inhibits vascular endothelial growth factor-induced activation of Ras in capillary endothelial cells". Molecular Endocrinology 13 (5): 692–704. May 1999. doi:10.1210/mend.13.5.0280. PMID 10319320.
Further reading
- "Vascular endothelial growth factor receptor-2: structure, function, intracellular signalling and therapeutic inhibition". Cellular Signalling 19 (10): 2003–12. October 2007. doi:10.1016/j.cellsig.2007.05.013. PMID 17658244.
- "Signaling via vascular endothelial growth factor receptors". Experimental Cell Research 253 (1): 117–30. November 1999. doi:10.1006/excr.1999.4707. PMID 10579917.
- "Bone marrow mononuclear cell transplantation promotes therapeutic angiogenesis via upregulation of the VEGF-VEGFR2 signaling pathway in a rat model of vascular dementia". Behavioural Brain Research 265: 171–80. May 2014. doi:10.1016/j.bbr.2014.02.033. PMID 24589546.
- "Properties of two VEGF receptors, Flt-1 and KDR, in signal transduction". Annals of the New York Academy of Sciences 902 (1): 201–5; discussion 205–7. May 2000. doi:10.1111/j.1749-6632.2000.tb06314.x. PMID 10865839. Bibcode: 2000NYASA.902..201S.
- "Signaling transduction mechanisms mediating biological actions of the vascular endothelial growth factor family". Cardiovascular Research 49 (3): 568–81. February 2001. doi:10.1016/S0008-6363(00)00268-6. PMID 11166270.
- "HIV-Tat dependent chemotaxis and invasion, key aspects of tat mediated pathogenesis". Clinical & Experimental Metastasis 18 (7): 533–8. 2001. doi:10.1023/A:1011991906685. PMID 11688957.
- "VEGFR-2 (KDR/Flk-1)". Journal of Biological Regulators and Homeostatic Agents 16 (3): 227–32. 2003. PMID 12456025.
- "Signal transduction via vascular endothelial growth factor (VEGF) receptors and their roles in atherogenesis". Journal of Atherosclerosis and Thrombosis 13 (3): 130–5. June 2006. doi:10.5551/jat.13.130. PMID 16835467.
External links
- Kinase+insert+domain+receptor at the US National Library of Medicine Medical Subject Headings (MeSH)
- Overview of all the structural information available in the PDB for UniProt: P35968 (Vascular endothelial growth factor receptor 2) at the PDBe-KB.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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