Structural arrangement in the α2 -macroglobulin-thrombin complex
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(83)80728-5/fullpdf
Reference19 articles.
1. Characterization of alkylamine-sensitive site in alpha 2-macroglobulin.
2. A thiol-ester in α2 -macroglobulin cleaved during proteinase complex formation
3. Sequence location of the reactive thiol ester in human α2 -macroglobulin
4. Reactive site in human alpha 2-macroglobulin: circumstantial evidence for a thiolester.
5. Trypsin-induced activation of the thiol esters in α2-macroglobulin generates a short-lived intermediate (‘nascent’ α2M) that can react rapidly to incorporate not only methylamine or putrescine but also proteins lacking proteinase activity
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1. Active but inoperable thrombin is accumulated in a plasma protein layer surrounding Streptococcus pyogenes;Thrombosis and Haemostasis;2015
2. Role of Internal Thiol Esters in the ?-Macroglobulin-Proteinase Binding Mechanism;Annals of the New York Academy of Sciences;1994-09
3. Identification of alpha 2-macroglobulin conformational intermediates by electron microscopy and image analysis. Comparison of alpha 2-macroglobulin-thrombin and alpha 2-macroglobulin reacted with cis-dichlorodiammineplatinum(II) and trypsin.;Journal of Biological Chemistry;1992-03
4. Image processing of proteinase- and methylamine-transformed human α2-macroglobulin;Journal of Biological Chemistry;1989-07
5. Human Fibroblast Collagenase-α-Macroglobulin Interactions;Journal of Biological Chemistry;1989-01
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