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Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.
- I. Sinning, G. Kleywegt, +7 authors P. Board
- Chemistry, Medicine
- Journal of molecular biology
- 5 July 1993
The crystal structure of human alpha class glutathione transferase A1-1 has been determined and refined to a resolution of 2.6 A. There are two copies of the dimeric enzyme in the asymmetric unit.… Expand
X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function.
- H. Dirr, P. Reinemer, R. Huber
- Chemistry, Medicine
- European journal of biochemistry
- 1 March 1994
Crystal structures of cytosolic glutathione S-transferases (EC 2.5.1.18), complexed with glutathione or its analogues, are reviewed. The atomic models define protein architectural relationships… Expand
Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate.
- M. P. Egloff, P. Cohen, P. Reinemer, D. Barford
- Chemistry, Medicine
- Journal of molecular biology
- 15 December 1995
Protein phosphatase 1 (PP1) is a serine/threonine protein phosphatase that is essential in regulating diverse cellular processes. Here we report the crystal structure of the catalytic subunit of… Expand
Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer.
- S. Steinbacher, R. Seckler, S. Miller, B. Steipe, R. Huber, P. Reinemer
- Biology, Medicine
- Science
- 15 July 1994
The tailspike protein (TSP) of Salmonella typhimurium phage P22 is a part of the apparatus by which the phage attaches to the bacterial host and hydrolyzes the O antigen. It has served as a model… Expand
Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a…
- P. Reinemer, L. Prade, +8 authors B. Bieseler
- Biology, Medicine
- Journal of molecular biology
- 1996
Glutathione S-transferases (GST) are a family of multifunctional enzymes involved in the metabolization of a broad variety of xenobiotics and reactive endogenous compounds. The interest in plant… Expand
The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases
- W. Stöcker, F. Grams, +4 authors David B. Mckay
- Biology, Medicine
- Protein science : a publication of the Protein…
- 1 May 1995
The three‐dimensional structures of the zinc endopeptidases human neutrophil collagenase, adamalysin II from rattle snake venom, alkaline proteinase from Pseudomonas aeruginosa, and astacin from… Expand
Discovery of the novel antithrombotic agent 5-chloro-N-({(5S)-2-oxo-3- [4-(3-oxomorpholin-4-yl)phenyl]-1,3-oxazolidin-5-yl}methyl)thiophene- 2-carboxamide (BAY 59-7939): an oral, direct factor Xa…
- S. Röhrig, A. Straub, +5 authors E. Perzborn
- Chemistry, Medicine
- Journal of medicinal chemistry
- 18 August 2005
Despite recent progress in antithrombotic therapy, there is still an unmet medical need for safe and orally available anticoagulants. The coagulation enzyme Factor Xa (FXa) is a particularly… Expand
The X‐ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity.
- W. Bode, P. Reinemer, R. Huber, T. Kleine, S. Schnierer, H. Tschesche
- Biology, Medicine
- The EMBO journal
- 1 March 1994
Matrix metalloproteinases are a family of zinc endopeptidases involved in tissue remodelling. They have been implicated in various disease processes including tumour invasion and joint destruction.… Expand
Refined crystal structure of porcine class Pi glutathione S-transferase (pGST P1-1) at 2.1 A resolution.
- H. Dirr, P. Reinemer, R. Huber
- Chemistry, Medicine
- Journal of molecular biology
- 13 October 1994
The crystal structure of class Pi glutathione S-transferase from porcine lung (pGST P1-1) in complex with glutathione sulphonate has been refined at 2.11 A resolution, to a crystallographic R-factor… Expand
The three‐dimensional structure of class pi glutathione S‐transferase in complex with glutathione sulfonate at 2.3 A resolution.
- P. Reinemer, H. Dirr, R. Ladenstein, J. Schaeffer, O. Gallay, R. Huber
- Biology, Medicine
- The EMBO journal
- 1 August 1991
The three‐dimensional structure of class pi glutathione S‐transferase from pig lung, a homodimeric enzyme, has been solved by multiple isomorphous replacement at 3 A resolution and preliminarily… Expand