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Deborah Fass
Researcher at Weizmann Institute of Science
Publications - 98
Citations - 7503
Deborah Fass is an academic researcher from Weizmann Institute of Science. The author has contributed to research in topics: Protein disulfide-isomerase & Endoplasmic reticulum. The author has an hindex of 36, co-authored 89 publications receiving 6908 citations. Previous affiliations of Deborah Fass include Massachusetts Institute of Technology.
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Core structure of GP41 from the HIV envelope glycoprotein
TL;DR: The crystal structure of this complex, composed of the peptides N36 and C34, is a six-helical bundle that shows striking similarity to the low-pH-induced conformation of influenza hemagglutinin and likely represents the core of fusion-active gp41.
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Generating disulfides enzymatically: Reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p
Einav Gross,Carolyn S. Sevier,Nimrod Heldman,Elvira Vitu,Moran Bentzur,Chris A. Kaiser,Colin Thorpe,Deborah Fass +7 more
TL;DR: Reduced Ero1p can catalyze reduction of exogenous FAD in solution and drive disulfide bond formation under anaerobic conditions in the endoplasmic reticulum.
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Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module.
TL;DR: The structure of ligand-binding repeat 5 (LR5) of the LDLR, determined to 1.7 å resolution by X-ray crystallography and presented here, contains a calcium ion coordinated by acidic residues that lie at the carboxy-terminal end of the domain and are conserved among LDL-A modules.
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Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography
TL;DR: 3D structural information regarding the prefusion conformation of an intact unstained retrovirus surface protein is provided, and tentative docking of the x-ray crystal structure of the receptor-binding domain is allowed.
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Structure of ero1p, source of disulfide bonds for oxidative protein folding in the cell.
TL;DR: The X-ray crystallographic structure of Ero1p is presented, which reveals the molecular details of the catalytic center, the role of a CXXCXXC motif, and the spatial relationship between functionally significant cysteines and the bound cofactor.