H
Hermann Schindelin
Researcher at University of Würzburg
Publications - 144
Citations - 9253
Hermann Schindelin is an academic researcher from University of Würzburg. The author has contributed to research in topics: Ubiquitin & Gephyrin. The author has an hindex of 47, co-authored 132 publications receiving 8533 citations. Previous affiliations of Hermann Schindelin include Stony Brook University & California Institute of Technology.
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Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction.
TL;DR: The crystal structure has been determined for the complex between the Fe-protein and MoFe-protein components of nitrogenase stabilized by ADP·AIF4–, previously used as a nucleoside triphosphate analogue in nucleotide-switch proteins.
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Molybdenum-Cofactor–Containing Enzymes: Structure and Mechanism
TL;DR: Four families of molybdenum-cofactor-containing enzymes have been identified on the basis of sequence alignments and spectroscopic properties, and the available crystallographic structures for members of these families are discussed within the framework of the active site structure and catalytic mechanisms.
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Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase.
Caroline Kisker,Hermann Schindelin,Andrew Pacheco,William A Wehbi,Robert M. Garrett,K.V. Rajagopalan,John H. Enemark,Douglas C. Rees +7 more
TL;DR: Four variants associated with sulfite oxidase deficiency have been identified: two mutations are near the sulfate binding site, while the other mutations occur within the domain mediating dimerization.
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Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination.
TL;DR: In this article, the crystal structure of DMSO reductase from Rhodobacter sphaeroides reveals a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically coordinate the metal through their dithiolene groups.
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The Crystal Structure of Yeast Protein Disulfide Isomerase Suggests Cooperativity between Its Active Sites
TL;DR: Biochemical studies demonstrate that all domains of PDI, including the C-terminal tail, are required for full catalytic activity and defines a framework for rationalizing the differences between the two active sites and their respective roles in catalyzing the formation and rearrangement of disulfide bonds.