Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Carlos Fernandez-Catalan"'
Autor:
David Reverter, Tad A. Holak, Carlos Fernandez-Catalan, Roland Baumgartner, Francesc X. Avilés, Ruth Pfänder, Josep Vendrell, Wolfram Bode, Robert Huber
Publikováno v:
Nature Structural Biology. 7:322-328
Leech carboxypeptidase inhibitor (LCI) is a novel protein inhibitor present in the medicinal leech Hirudo medicinalis. The structures of LCI free and bound to carboxypeptidase A2 (CPA2)have been determined by NMR and X-ray crystallography, respective
Autor:
Wolfram Bode, Carlos Fernandez-Catalan, Koichi Suzuki, Akihiro Irie, Marianne Braun, Kazuhiro Nakagawa, Hans D. Bartunik, Robert Huber, Stefan Strobl, Hiroyuki Sorimachi, Hajime Masumoto, Gleb Bourenkow
Publikováno v:
Proceedings of the National Academy of Sciences. 97:588-592
Calpains (calcium-dependent cytoplasmic cysteine proteinases) are implicated in processes such as cytoskeleton remodeling and signal transduction. The 2.3-Å crystal structure of full-length heterodimeric [80-kDa (dI-dIV) + 30-kDa (dV+dVI)] human m-
Autor:
Wolfram Bode, F.X. Gomis-Ruth, Hideaki Nagase, Frank Grams, Carlos Fernandez-Catalan, Klaus Maskos, Harald Tschesche
Publikováno v:
Annals of the New York Academy of Sciences. 878:73-91
The proteolytic activity of the matrix metalloproteinases (MMPs) involved in extracellular matrix degradation must be precisely regulated by their endogenous protein inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). Disruption of this
Autor:
Frank Grams, Wolfram Bode, Hideaki Nagase, Carlos Fernandez-Catalan, Klaus Maskos, Harald Tschesche
Publikováno v:
Cellular and Molecular Life Sciences (CMLS). 55:639-652
Matrix metalloproteinases (MMPs) are involved in extracellular matrix degradation. Their proteolytic activity must. be precisely regulated by their endogenous protein inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). Disruption of this
Autor:
Ulrich Bergmann, Ylva Lindqvist, Ari Tuuttila, Wolfram Bode, Karl Tryggvason, Carlos Fernandez-Catalan, Gunter Schneider, Ekaterina Morgunova, Klaus Maskos
Publikováno v:
Journal of Molecular Biology. 284:1133-1140
The three-dimensional structure of human tissue inhibitor of metalloproteinases-2 (TIMP-2) was determined by X-ray crystallography to 2.1 A resolution. The structure of the inhibitor consists of two domains. The N-terminal domain (residues 1-110) is
Autor:
Marina A. A. Parry, Wolfram Bode, Robert Huber, Bernhard Schlott, Andreas Bergner, Carlos Fernandez-Catalan, Karl-Heinz Gührs, Karl-Peter Hopfner
Publikováno v:
Nature Structural Biology. 5:917-923
The serine proteinase plasmin is the key fibrinolytic enzyme that dissolves blood clots and also promotes cell migration and tissue remodeling. Here, we report the 2.65 A crystal structure of a ternary complex of microplasmin-staphylokinase bound to
Autor:
Tad A. Holak, Carlos Fernandez-Catalan, Robert Huber, Astar Winoto, Roland Baumgartner, Richard A. Engh
Publikováno v:
Structure. 6(10):1279-1290
Background: The four members of the INK4 gene family (p16 INK4a , p15 INK4b , p18 INK4c and p19 INK4d ) inhibit the closely related cyclin-dependent kinases CDK4 and CDK6 as part of the regulation of the G 1 →S transition in the cell-division cycle
Autor:
Wolfram Bode, Andrea Lichte, Carlos Fernandez-Catalan, Klaus Maskos, Dušan Turk, Robert Huber, Harald Tschesche, Juan J. Calvete
Publikováno v:
The EMBO Journal. 17:5238-5248
The proteolytic activity of matrix metalloproteinases (MMPs) towards extracellular matrix components is held in check by the tissue inhibitors of metalloproteinases (TIMPs). The binary complex of TIMP-2 and membrane-type-1 MMP (MT1-MMP) forms a cell
Autor:
Melissa Petersen, Carl J. March, Martin F. Wolfson, George A. Ellestad, Wolfram Bode, Gleb Bourenkov, Douglas P. Cerretti, Klaus Maskos, Charles Rauch, Pranitha Reddy, Hans D. Bartunik, Carlos Fernandez-Catalan, Beverly J. Castner, Raymond J. Davis, Raymond J. Paxton, Roy A. Black, Howard R. G. Clarke, Jeffrey N. Fitzner, Robert Huber
Publikováno v:
Proceedings of the National Academy of Sciences. 95:3408-3412
Tumor necrosis factor-α (TNFα) is a cytokine that induces protective inflammatory reactions and kills tumor cells but also causes severe damage when produced in excess, as in rheumatoid arthritis and septic shock. Soluble TNFα is released from its
Autor:
Stefan Strobl, Hiroyuki Sorimachi, Marianne Braun, Wolfram Bode, David Reverter, Carlos Fernandez-Catalan
Publikováno v:
Biological chemistry. 383(9)
The calpains form a growing family of structurally related intracellular multidomain cysteine proteinases containing a papain-related catalytic domain, whose activity depends on calcium. The calpains are believed to play important roles in cytoskelat