Zobrazeno 1 - 10
of 45
pro vyhledávání: '"J. Uppenberg"'
Autor:
Zhihe Kuang, Panagis Filippakopoulos, Raymond S. Norton, Alex N. Bullock, J. Uppenberg, Pavel Savitsky, Timothy Sharpe, Shenggen Yao, Andrew Low, Sandra E. Nicholson, Rowena S. Lewis
Publikováno v:
Journal of Molecular Biology
The mammalian SPRY domain- and SOCS box-containing proteins, SPSB1 to SPSB4, belong to the SOCS box family of E3 ubiquitin ligases. Substrate recognition sites for the SPRY domain are identified only for human Par-4 (ELNNNL) and for the Drosophila or
Autor:
Susanne van den Berg, Martin Högbom, R. Collins, J. Uppenberg, Lovisa Holmberg Schiavone, Tobias Karlberg, Martin Hammarström, A. Flores
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 64:279-286
Argininosuccinate synthetase catalyzes the transformation of citrulline and aspartate into argininosuccinate and pyrophosphate using the hydrolysis of ATP to AMP and pyrophosphate. This enzymatic process constitutes the rate-limiting step in both
Publikováno v:
Journal of Molecular Biology. 290:201-211
Tartrate-resistant acid phosphatase (TRAP) is a mammalian di-iron-containing enzyme that belongs to the family of purple acid phosphatases (PAP). It is highly expressed in a limited number of tissues, predominantly in bone-resorbing osteoclasts and i
Autor:
M Norin, N Ohrner, T.A. Jones, Karl Hult, Shamkant Anant Patkar, Gerard J. Kleywegt, T Anthonsen, Waagen, J. Uppenberg
Publikováno v:
Biochemistry. 34:16838-16851
Many lipases are potent catalysts of stereoselective reactions and are therefore of interest for use in chemical synthesis. The crystal structures of lipases show a large variation in the shapes of their active site environments that may explain the
Publikováno v:
Journal of Molecular Biology. 235:790-792
Lipase B from Candida antarctica has been crystallized in five different crystal forms. The space groups and cell dimensions have been determined by X-ray diffraction methods. Four of the crystal forms have been judged to be of good quality for furth
Publikováno v:
Structure (London, England : 1993). 9(8)
Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose without requiring any cofactors, such as pyridoxal phosphate. The enzyme is part of operons th
Publikováno v:
Journal of molecular biology. 290(1)
Tartrate-resistant acid phosphatase (TRAP) is a mammalian di-iron- containing enzyme that belongs to the family of purple acid phosphatases (PAP). It is highly expressed in a limited number of tissues, predominantly in bone-resorbing osteoclasts and
Publikováno v:
Drug News & Perspectives. 12:389
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Akademický článek
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