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A.M. de Vos
Researcher at Genentech
Publications - 27
Citations - 7745
A.M. de Vos is an academic researcher from Genentech. The author has contributed to research in topics: Receptor & Protein structure. The author has an hindex of 21, co-authored 27 publications receiving 7593 citations.
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Journal ArticleDOI
Human Growth Hormone and Extracellular Domain of Its Receptor: Crystal Structure of the Complex
TL;DR: Examination of the 2.8 angstrom crystal structure of the complex between the hormone and the extracellular domain of its receptor (hGHbp) showed that the complex consists of one molecule of growth hormone per two molecules of receptor.
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Selection and analysis of an optimized anti-VEGF antibody: crystal structure of an affinity-matured Fab in complex with antigen.
Yongmei Chen,Christian Wiesmann,Germaine Fuh,Bing Li,H.W. Christinger,P. Mckay,A.M. de Vos,Henry B. Lowman +7 more
TL;DR: The final antibody has improved affinity for several VEGF variants as compared with the parental antibody; however, some contact residues on V EGF differ in their contribution to the energetics of Fab binding.
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Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
Brian C. Cunningham,Mark Ultsch,A.M. de Vos,Michael G. Mulkerrin,Karl R. Clauser,James A. Wells +5 more
TL;DR: Human growth hormone forms a 1:2 complex with the extracellular domain of its receptor-binding protein (hGHbp) as studied by crystallization, size exclusion chromatography, calorimetry, and a previously undescribed fluorescence quenching assay.
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Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5.
Sarah G. Hymowitz,H.W. Christinger,Germaine Fuh,M.H. Ultsch,Mark P. O'Connell,Robert F. Kelley,Avi Ashkenazi,A.M. de Vos +7 more
TL;DR: The crystal structure of the complex between Apo2L and the ectodomain of DR5 suggests general principles of binding and specificity for ligand recognition in the TNF receptor superfamily.
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Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor
TL;DR: The structure of human NGF in complex with human TrkA-d5 is consistent with results from mutagenesis experiments for all neurotrophins, and indicates that the first patch may constitute a conserved binding motif for all family members, whereas the second patch is specific for the interaction between NGF and TrKA.