Dimerization of VEGF receptors and implications for signal transduction: a computational study
F Mac Gabhann, AS Popel - Biophysical chemistry, 2007 - Elsevier
Vascular endothelial growth factor (VEGF) is a potent cytokine involved in the induction of
neovascularization. Secreted as a cysteine-linked dimer, it has two binding sites at opposite …
neovascularization. Secreted as a cysteine-linked dimer, it has two binding sites at opposite …
Structural determinants of growth factor binding and specificity by VEGF receptor 2
VM Leppänen, AE Prota, M Jeltsch… - Proceedings of the …, 2010 - National Acad Sciences
Vascular endothelial growth factors (VEGFs) regulate blood and lymph vessel formation
through activation of three receptor tyrosine kinases, VEGFR-1,-2, and-3. The extracellular …
through activation of three receptor tyrosine kinases, VEGFR-1,-2, and-3. The extracellular …
Direct measurements of VEGF–VEGFR2 binding affinities reveal the coupling between ligand binding and receptor dimerization
C King, K Hristova - Journal of Biological Chemistry, 2019 - ASBMB
Vascular endothelial growth factor receptor 2 (VEGFR2) controls angiogenesis and is
critically important for normal human development and cancer progression. A recent finding …
critically important for normal human development and cancer progression. A recent finding …
[HTML][HTML] Monte Carlo simulations of VEGF binding to cell surface receptors in vitro
The vascular endothelial growth factor (VEGF) family binds multiple endothelial cell surface
receptors. Our goal is to build comprehensive models of these interactions for the purpose of …
receptors. Our goal is to build comprehensive models of these interactions for the purpose of …
Transmembrane domain‐mediated orientation of receptor monomers in active VEGFR‐2 dimers
DDE Dosch, K Ballmer-Hofer - The FASEB journal, 2010 - Wiley Online Library
Vascular endothelial growth factors (VEGFs) activate cellular receptor tyrosine kinases
(RTKS) such as VEGFR‐1,‐2, and‐3. These receptors are activated upon ligand binding to …
(RTKS) such as VEGFR‐1,‐2, and‐3. These receptors are activated upon ligand binding to …
Structure of the Full-length VEGFR-1 Extracellular Domain in Complex with VEGF-A
Vascular endothelial growth factors (VEGFs) regulate blood and lymph vessel development
upon activation of three receptor tyrosine kinases: VEGFR-1,-2, and-3. Partial structures of …
upon activation of three receptor tyrosine kinases: VEGFR-1,-2, and-3. Partial structures of …
Structure–function analysis of VEGF receptor activation and the role of coreceptors in angiogenic signaling
FS Grünewald, AE Prota, A Giese… - Biochimica et Biophysica …, 2010 - Elsevier
Vascular endothelial growth factors (VEGFs) constitute a family of six polypeptides, VEGF-A,-
B,-C,-D,-E and PlGF, that regulate blood and lymphatic vessel development. VEGFs …
B,-C,-D,-E and PlGF, that regulate blood and lymphatic vessel development. VEGFs …
Site-specific phosphorylation of VEGFR2 is mediated by receptor trafficking: insights from a computational model
LW Clegg, F Mac Gabhann - PLoS computational biology, 2015 - journals.plos.org
Matrix-binding isoforms and non-matrix-binding isoforms of vascular endothelial growth
factor (VEGF) are both capable of stimulating vascular remodeling, but the resulting blood …
factor (VEGF) are both capable of stimulating vascular remodeling, but the resulting blood …
Structural insights into the binding of vascular endothelial growth factor-B by VEGFR-1D2: Recognition and specificity
S Iyer, PI Darley, KR Acharya - Journal of Biological Chemistry, 2010 - ASBMB
The formation of blood vessels (angiogenesis) is a highly orchestrated sequence of events
involving crucial receptor-ligand interactions. Angiogenesis is critical for physiological …
involving crucial receptor-ligand interactions. Angiogenesis is critical for physiological …
Structure of a VEGF–VEGF receptor complex determined by electron microscopy
Receptor tyrosine kinases are activated upon ligand-induced dimerization. Here we show
that the monomeric extracellular domain of vascular endothelial growth factor (VEGF) …
that the monomeric extracellular domain of vascular endothelial growth factor (VEGF) …