R
Robert Zwilling
Researcher at Heidelberg University
Publications - 24
Citations - 1015
Robert Zwilling is an academic researcher from Heidelberg University. The author has contributed to research in topics: Astacin & Bone morphogenetic protein 1. The author has an hindex of 18, co-authored 24 publications receiving 990 citations.
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Journal ArticleDOI
Structure of astacin with a transition-state analogue inhibitor
Frank Grams,Vincent Dive,Athanasios Yiotakis,Irene Yiallouros,Stamatia Vassiliou,Robert Zwilling,Wolfram Bode,Walter Stöcker +7 more
TL;DR: The structure of the zinc peptidase astacin in complex with a phosphinic peptide suggests that a special role is played by the side chain of a zinc-bound tyrosine, which is shifted to form a hydrogen bond to the phosphinyl group—a mimic of the carboxyanion of the transition state.
Journal ArticleDOI
Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin.
TL;DR: The astacin structure has been solved by multiple isomorphous replacement using six heavy-atom derivatives, and refined to a crystallographic R-value of 0.158 applying stringent constraints.
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Biosynthesis of Astacus protease, a digestive enzyme from crayfish.
TL;DR: The mechanism of enzyme production observed in Astacus differs considerably from vertebrates suggesting an alternative model for synthesis and storage of digestive enzymes.
Journal ArticleDOI
Implications of the three‐dimensional structure of astacin for the structure and function of the astacin family of zinc‐endopeptidases
TL;DR: The topology of residues forming the zinc-binding active site of astacin corresponds to almost identical arrangements in all other astacins, suggesting that these are likewise metalloproteinases.
Journal ArticleDOI
The astacin protein family in Caenorhabditis elegans
TL;DR: Based on structural differences of the regulatory unit, six NAS subgroups were established, which seemingly represented different functional and evolutionary clusters, perfectly reflected in an evolutionary tree constructed solely from amino acid sequence information of the catalytic chain.