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Autor:
Péter Medveczky, László Gráf, Zoltán Boldizsár Simon, András Málnási-Csizmadia, László Szilágyi, Linda Gombos, Júlia Tóth
Publikováno v:
Journal of Biological Chemistry. 281:12596-12602
Human trypsin 4 is an unconventional serine protease that possesses an arginine at position 193 in place of the highly conserved glycine. Although this single amino acid substitution does not affect steady-state activity on small synthetic substrates
Autor:
Thor Las Holtet, Troels Wind, Lisa Mathiasen, Peter A. Andreasen, Signe Kjelgaard, Anni Christensen, Grant E. Blouse, Helle H. Petersen, Martin Ejnar Hansen
Publikováno v:
Journal of Biological Chemistry. 280:38424-38437
To find new principles for inhibiting serine proteases, we screened phage-displayed random peptide repertoires with urokinase-type plasminogen activator (uPA) as the target. The most frequent of the isolated phage clones contained the disulfide bridg
Publikováno v:
Journal of Biological Chemistry. 280:35424-35432
The functional form of ClpP, the proteolytic component of ATP-dependent Clp proteases, is a hollow-cored particle composed of two heptameric rings joined face-to-face forming an aqueous chamber containing the proteolytic active sites. We have found t
Autor:
Gurdyal S. Besra, Kevin J. C. Gibson, Bénédicte Sichi, Patricia Constant, Germain Puzo, Martine Gilleron, Jérôme Nigou
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2005, 280 (31), pp.28347-28356. ⟨10.1074/jbc.M505498200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2005, 280 (31), pp.28347-28356. ⟨10.1074/jbc.M505498200⟩
Lipomannans (LMs) are powerful pro-inflammatory lipoglycans found in mycobacteria and related genera, however the molecular bases of their activity are not fully understood. We report here the isolation and the structural and functional characterizat
Publikováno v:
Journal of Biological Chemistry. 280:27832-27838
Kunitz domain 1 (KD1) of tissue factor pathway inhibtor-2 inhibits trypsin, plasmin, and factor VIIa (FVIIa)/tissue factor with Ki values of 13, 3, and 1640 nm, respectively. To investigate the molecular specificity of KD1, crystals of the complex of
Publikováno v:
Journal of Biological Chemistry. 280:23523-23530
Studies of the mechanisms of blood coagulation zymogen activation demonstrate that exosites (sites on the activating complex distinct from the protease active site) play key roles in macromolecular substrate recognition. We investigated the importanc
Autor:
Birgit Christine Bønsager, Peter Kresten Nielsen, Birte Svensson, Mette Prætorius-Ibba, Maher Abou Hachem, Kenji Fukuda
Publikováno v:
Journal of Biological Chemistry. 280:14855-14864
The barley alpha-amylase/subtilisin inhibitor (BASI) inhibits alpha-amylase 2 (AMY2) with subnanomolar affinity. The contribution of selected side chains of BASI to this high affinity is discerned in this study, and binding to other targets is invest
Publikováno v:
Journal of Biological Chemistry. 279:48262-48269
The S1 site (Asp(189)) of factor Xa (fXa) is located on a loop (residues 185-189) that contains three solvent-exposed charged residues (Asp(185), Lys(186), and Glu(188)) below the active-site pocket of the protease. To investigate the role of these r
Autor:
Judy Barnett-Norris, Sean D. McAllister, Mary E. Abood, Diane L. Lynch, Patricia H. Reggio, Dow P. Hurst
Publikováno v:
Journal of Biological Chemistry. 279:48024-48037
In this study, we tested the hypothesis that a CB(1) TMH3-4-5-6 aromatic microdomain, which includes F3.25(190), F3.36(201), W5.43(280), and W6.48(357), is centrally involved in CB(1) receptor activation, with the F3.36(201)/W6.48(357) interaction ke
Publikováno v:
Journal of Biological Chemistry. 279:38519-38524
Previous studies have suggested that the conformation of the activation peptide of protein C is influenced by the binding of Ca(2+). To provide direct evidence for the linkage between Ca(2+) binding and the conformation of the activation peptide, we