[图书][B] Structural and Functional Analysis of the Heparin-binding Domain of VEGF164
D Krilleke - 2006 - search.proquest.com
Several of the multitude of functions attributed to Vascular Endothelial Growth Factor-A
(VEGF-A) are coordinated by its various isoforms, which are generated as a result of …
(VEGF-A) are coordinated by its various isoforms, which are generated as a result of …
[HTML][HTML] Molecular mapping and functional characterization of the VEGF164 heparin-binding domain
D Krilleke, A DeErkenez, W Schubert, I Giri… - Journal of Biological …, 2007 - ASBMB
The longer splice isoforms of vascular endothelial growth factor-A (VEGF-A), including
mouse VEGF164, contain a highly basic heparin-binding domain (HBD), which imparts the …
mouse VEGF164, contain a highly basic heparin-binding domain (HBD), which imparts the …
The heparin-binding domain confers diverse functions of VEGF-A in development and disease: a structure–function study
D Krilleke, YSE Ng, DT Shima - 2009 - portlandpress.com
The longer splice isoforms of VEGF (vascular endothelial growth factor)-A, including
VEGF164 (165), contain a highly basic HBD (heparin-binding domain). This domain allows …
VEGF164 (165), contain a highly basic HBD (heparin-binding domain). This domain allows …
A Functional Heparin–Binding Domain is Required for Vegf164–Induced Retinal Leukostasis
K Nishijima, D Krilleke, GS Robinson… - … & Visual Science, 2006 - iovs.arvojournals.org
Purpose:: The heparin–binding domain (HBD) in the C–terminus of VEGF164 confers VEGF
isoform–specific biological activities in vascular development and disease. We have …
isoform–specific biological activities in vascular development and disease. We have …
[HTML][HTML] VEGF162, a new heparin-binding vascular endothelial growth factor splice form that is expressed in transformed human cells
T Lange, N Guttmann-Raviv, L Baruch… - Journal of Biological …, 2003 - ASBMB
The splice forms of vascular endothelial growth factor (VEGF) differ in biological properties
such as the receptor types that they recognize and their interaction with heparan sulfate …
such as the receptor types that they recognize and their interaction with heparan sulfate …
Disulfide structure of the heparin binding domain in vascular endothelial growth factor: characterization of posttranslational modifications in VEGF
RG Keck, L Berleau, R Harris, BA Keyt - Archives of biochemistry and …, 1997 - Elsevier
Preparations of recombinant human vascular endothelial growth factor (VEGF165)
expressed in Chinese hamster ovary (CHO) cells andEscherichia coliwere compared using …
expressed in Chinese hamster ovary (CHO) cells andEscherichia coliwere compared using …
[HTML][HTML] Production of Soluble Human Vascular Endothelial Growth Factor VEGF-A165-Heparin Binding Domain in Escherichia coli
A Seyedarabi, L Cheng, I Zachary, S Djordjevic - PloS one, 2013 - journals.plos.org
We report a method for production of soluble heparin binding domain (HBD) of human
vascular endothelial growth factor VEGF-A165. Recombinant VEGF-A165-HBD that contains …
vascular endothelial growth factor VEGF-A165. Recombinant VEGF-A165-HBD that contains …
[图书][B] Structural characterisation of the binding site for VEGF165 within heparan sulphate
CJ Robinson - 2002 - search.proquest.com
Vascular endothelial growth factor (VEGF) is a highly specific mitogen for cultured
endothelial cells and a potent stimulator of angiogenesis in vivo. Among the widely …
endothelial cells and a potent stimulator of angiogenesis in vivo. Among the widely …
[HTML][HTML] VEGF121, a vascular endothelial growth factor (VEGF) isoform lacking heparin binding ability, requires cell-surface heparan sulfates for efficient binding to the …
T Cohen, H Gitay-Goren, R Sharon, M Shibuya… - Journal of Biological …, 1995 - ASBMB
Four vascular endothelial growth factor (VEGF) splice variants containing 121, 165, 189, and
206 amino acids are produced from a single human gene as a result of alternative splicing …
206 amino acids are produced from a single human gene as a result of alternative splicing …
[HTML][HTML] Solution structure of the heparin-binding domain of vascular endothelial growth factor
WJ Fairbrother, MA Champe, HW Christinger, BA Keyt… - Structure, 1998 - cell.com
Background: Vascular endothelial growth factor (VEGF) is an endothelial cell-specific
mitogen and is a potent angiogenic and vascular permeabilizing factor. VEGF is also an …
mitogen and is a potent angiogenic and vascular permeabilizing factor. VEGF is also an …