Structure of the Discoidin Domain Receptor 1 Extracellular Region Bound to an Inhibitory Fab Fragment Reveals Features Important for Signaling-Reference-Cited by-同舟云学术

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Structure of the Discoidin Domain Receptor 1 Extracellular Region Bound to an Inhibitory Fab Fragment Reveals Features Important for Signaling

Published:2012-04 Issue:4 Volume:20 Page:688-697
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Carafoli Federico,Mayer Marie Cathrin,Shiraishi Kazushige,Pecheva Mira Anguelova,Chan Lai Yi,Nan Ruodan,Leitinger Birgit,Hohenester Erhard

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference44 articles.

1. Identification of disulfide-linked dimers of the receptor tyrosine kinase DDR1;Abdulhussein;J. Biol. Chem.,2008

2. Monoclonal antibody therapy of cancer;Adams;Nat. Biotechnol.,2005

3. The crystal structure of activated protein C-inactivated bovine factor Va: implications for cofactor function;Adams;Proc. Natl. Acad. Sci. USA,2004

4. Trafficking defects and loss of ligand binding are the underlying causes of all reported DDR2 missense mutations found in SMED-SL patients;Ali;Hum. Mol. Genet.,2010

5. Standard conformations for the canonical structures of immunoglobulins;Al-Lazikani;J. Mol. Biol.,1997

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