Structure-function studies of two synthetic anti-vascular endothelial growth factor Fabs and comparison with the Avastin Fab. (Q33230191)

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14 January 2020

title

Structure-function studies of two synthetic anti-vascular endothelial growth factor Fabs and comparison with the Avastin Fab (English)

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14 January 2020

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14 January 2020

Germaine Fuh

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14 January 2020

Ping Wu

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14 January 2020

Wei-Ching Liang

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14 January 2020

Mark Ultsch

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14 January 2020

Chingwei V Lee

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14 January 2020

Barbara Moffat

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14 January 2020

language of work or name

English

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publication date

22 December 2005

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Journal of Biological Chemistry

14 January 2020

published in

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14 January 2020

volume

281

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14 January 2020

issue

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14 January 2020

page(s)

6625-6631

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Cross-species vascular endothelial growth factor (VEGF)-blocking antibodies completely inhibit the growth of human tumor xenografts and measure the contribution of stromal VEGF.

14 January 2020

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Inhibition of vascular endothelial growth factor-induced angiogenesis suppresses tumour growth in vivo

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Vascular endothelial growth factor D (VEGF-D) is a ligand for the tyrosine kinases VEGF receptor 2 (Flk1) and VEGF receptor 3 (Flt4)

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Identification of the KDR tyrosine kinase as a receptor for vascular endothelial cell growth factor

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The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 Å resolution: multiple copy flexibility and receptor binding

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Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site

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Crystal Structure at 1.7 Å Resolution of VEGF in Complex with Domain 2 of the Flt-1 Receptor

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High-affinity human antibodies from phage-displayed synthetic Fab libraries with a single framework scaffold

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X-ray structures of the antigen-binding domains from three variants of humanized anti-p185HER2 antibody 4D5 and comparison with molecular modeling

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Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?

21 January 2018

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Crystallization of the receptor binding domain of vascular endothelial growth factor

21 January 2018

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VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 A resolution and mutational analysis of the interface

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Processing of X-ray diffraction data collected in oscillation mode

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Solution structure of a phage-derived peptide antagonist in complex with vascular endothelial growth factor

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Receptor-selective variants of human vascular endothelial growth factor. Generation and characterization

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Selection and analysis of an optimized anti-VEGF antibody: crystal structure of an affinity-matured Fab in complex with antigen

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The Cystine-Knot Growth-Factor Superfamily

21 January 2018

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Requirements for binding and signaling of the kinase domain receptor for vascular endothelial growth factor

21 January 2018

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The atomic structure of protein-protein recognition sites

21 January 2018

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The subunit interfaces of oligomeric enzymes are conserved to a similar extent to the overall protein sequences

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Conservation helps to identify biologically relevant crystal contacts

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21 January 2018

Identifiers

DOI

10.1074/JBC.M507783200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16373345%20AND%20SRC:MED&resulttype=core&format=json

14 January 2020

1 reference

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