Comparative Trajectories of Active and S195A Inactive Trypsin upon Binding to Serpins-Reference-Cited by-同舟云学术

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Comparative Trajectories of Active and S195A Inactive Trypsin upon Binding to Serpins

Published:2002-10 Issue:41 Volume:277 Page:38901-38914
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Mellet Philippe,Mély Yves,Hedstrom Lizbeth,Cahoon Marguerite,Belorgey Didier,Srividya Narayanan,Rubin Harvey,Bieth Joseph G.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference44 articles.

1. The Serpins Are an Expanding Superfamily of Structurally Similar but Functionally Diverse Proteins

2. Assessing the protease and protease inhibitor content of the human genome

3. Structure of a serpin–protease complex shows inhibition by deformation

4. Serpin-Protease Complexes Are Trapped as Stable Acyl-Enzyme Intermediates

5. The Inhibition Mechanism of Serpins

Cited by 9 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. THERMOLYSIN DAMAGES ANIMAL LIFE THROUGH DEGRADATION OF PLASMA PROTEINS ENHANCED BY RAPID CLEAVAGE OF SERPINS AND ACTIVATION OF PROTEASES;Archives of Insect Biochemistry and Physiology;2014-07-10

2. Common architecture of nuclear receptor heterodimers on DNA direct repeat elements with different spacings;Nature Structural & Molecular Biology;2011-04-10

3. Determining Serpin Conformational Distributions with Single Molecule Fluorescence;Methods in Enzymology;2011

4. Local environment perturbations in alpha1-antitrypsin monitored by a ratiometric fluorescent label;Photochemical & Photobiological Sciences;2009

5. Short-lived protease-serpin complexes: Partial disruption of the rat trypsin active site;Protein Science;2007-11

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