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Robert Huber

Researcher at Technische Universität München

Publications -  742
Citations -  76282

Robert Huber is an academic researcher from Technische Universität München. The author has contributed to research in topics: Active site & Protein structure. The author has an hindex of 139, co-authored 671 publications receiving 73557 citations. Previous affiliations of Robert Huber include Munich University of Applied Sciences & Russian Academy of Sciences.

Papers
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Journal ArticleDOI

Structural basis of the endoproteinase-protein inhibitor interaction.

Wolfram Bode, +1 more
- 07 Mar 2000 - 
TL;DR: Three zinc endopeptidase inhibitors directed against metzincins and thermolysin have been characterised in the free and complexed state, displaying novel mechanisms of inhibition with their target proteinases.
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Crystal Structures of Catalytic Subunit of cAMP-dependent Protein Kinase in Complex with Isoquinolinesulfonyl Protein Kinase Inhibitors H7, H8, and H89 STRUCTURAL IMPLICATIONS FOR SELECTIVITY

Richard Engh, +4 more
- 18 Oct 1996 - 
TL;DR: The crystal structures of corresponding complexes with the cAPK catalytic subunit are determined and the conservation of the ATP-binding site of protein kinases allows evaluation of factors governing general selectivity of these inhibitors among kinases.
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X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor.

Wolfram Bode, +5 more
- 01 Oct 1986 - 
TL;DR: Orthorhombic crystals diffracting beyond 1.7 A resolution, have been grown from the stoichiometric complex formed between human leukocyte elastase and the third domain of turkey ovomucoid inhibitor (OMTKY3), the first serine proteinase glycoprotein analysed.
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Crystal structure of the first dissimilatory nitrate reductase at 1.9 A solved by MAD methods.

João M. Dias, +12 more
- 15 Jan 1999 - 
TL;DR: The polypeptide fold of NAP and the arrangement of the cofactors is related to that of Escherichia coli formate dehydrogenase (FDH) and distantly resembles dimethylsulphoxide reductase.
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A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans

Vitali Svetlitchnyi, +7 more
- 13 Jan 2004 - 
TL;DR: The functional cluster A of ACS(Ch) contains a Ni-Ni-[4Fe-4S] site, in which the positions proximal and distal to the cubane are occupied by Ni ions, which is apparent from a positive correlation of the Ni contents and negative correlations of the Cu or Zn contents with the acetyl-CoA/CO exchange activities of different preparations of monomeric ACS.