Interaction of cysteine proteinases with recombinant kininogen domain 2, expressed inEscherichia coli
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(94)01380-J/fullpdf
Reference33 articles.
1. Isolation of a human cDNA for .alpha.2-thiol proteinase inhibitor and its identity with low molecular weight kininogen
2. Human plasma kininogens are identical with α-cysteine proteinase inhibitors
3. A new function of kininogens as thiol-proteinase inhibitors: inhibition of papain and cathepsins B, H and L by bovine, rat and human plasma kininogens
4. Human high molecular weight kininogen as a thiol proteinase inhibitor: presence of the entire inhibition capacity in the native form of heavy chain
5. Role of High Molecular Weight Kininogen in Contact Activation
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1. Kininogens: More than cysteine protease inhibitors and kinin precursors;Biochimie;2010-11
2. Role of Nucleic Acid and Protein Manipulation Technologies in High‐throughput Structural Biology Efforts;Biopolymers Online;2003-01-27
3. The kallikrein-kininogen-kinin system: lessons from the quantification of endogenous kinins;Peptides;2000-12
4. Purification and Characterization of Low Molecular Weight Kininogen from Pig Plasma;Journal of Food Science;2000-01
5. Contact System: A Vascular Biology Modulator With Anticoagulant, Profibrinolytic, Antiadhesive, and Proinflammatory Attributes;Blood;1997-11-15
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