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 …

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 …

[HTML][HTML] 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 …

[HTML][HTML] Monte Carlo simulations of VEGF binding to cell surface receptors in vitro

F Mac Gabhann, MT Yang, AS Popel - Biochimica et Biophysica Acta (BBA) …, 2005 - Elsevier
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 …

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 …

[PDF][PDF] Structure of the Full-length VEGFR-1 Extracellular Domain in Complex with VEGF-A

S Markovic-Mueller, E Stuttfeld, M Asthana, T Weinert… - Structure, 2017 - cell.com
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 …

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 …

[HTML][HTML] 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 …

[HTML][HTML] 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 …

Structure of a VEGF–VEGF receptor complex determined by electron microscopy

C Ruch, G Skiniotis, MO Steinmetz, T Walz… - Nature structural & …, 2007 - nature.com
Receptor tyrosine kinases are activated upon ligand-induced dimerization. Here we show
that the monomeric extracellular domain of vascular endothelial growth factor (VEGF) …