M
Mark Ultsch
Researcher at Genentech
Publications - 88
Citations - 10440
Mark Ultsch is an academic researcher from Genentech. The author has contributed to research in topics: Binding site & Receptor. The author has an hindex of 43, co-authored 83 publications receiving 9816 citations. Previous affiliations of Mark Ultsch include University of California, San Francisco.
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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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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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Mapping of the C1q Binding Site on Rituxan, a Chimeric Antibody with a Human IgG1 Fc
Esohe Ekinaduese Idusogie,L.G. Presta,H. Gazzano-Santoro,Klara Totpal,Pin Yee Wong,Mark Ultsch,Y.G. Meng,Michael G. Mulkerrin +7 more
TL;DR: The results demonstrate that the previously described C1q binding motif in murine IgG2b constituting residues E318, K320, and K322 is not applicable to a human IgG1 when challenged with either human, rabbit, or guinea pig complement and suggest that there are species-specific differences in the C 1q binding site of Igs.
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Convergent solutions to binding at a protein-protein interface.
TL;DR: Juxtaposition of the available Fc-complex crystal structures showed that the convergent binding surface is highly accessible, adaptive, and hydrophobic and contains relatively few sites for polar interactions, which may promote cross-reactive binding, which is common to protein-protein interactions and especially hormone-receptor complexes.
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Bcl10 activates the NF-κB pathway through ubiquitination of NEMO
Honglin Zhou,Ingrid E. Wertz,Ingrid E. Wertz,Karen O'Rourke,Mark Ultsch,Somasekar Seshagiri,Michael Eby,Wei Xiao,Vishva M. Dixit +8 more
TL;DR: The adaptor protein Bcl10 promotes activation of NF-κB transcription factors through paracaspase- and UBC13-dependent ubiquitination of NEMO.