Interaction between separated consecutive complement control modules of human C1r: Implications for dimerization of the full-length protease-Reference-Cited by-同舟云学术

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Interaction between separated consecutive complement control modules of human C1r: Implications for dimerization of the full-length protease

Published:2010-10-21 Issue:22 Volume:584 Page:4565-4569
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Láng András,Major Balázs,Szilágyi Katalin,Gáspári Zoltán,Gál Péter,Závodszky Péter,Perczel András

Funder

ICGEB

Hungarian Scientific Research Fund

East-NMR/FP-7

János Bolyai Fellowship

The European Union and the European Social

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2010.10.033/fullpdf

Reference21 articles.

1. Purified proenzyme C1r. Some characteristics of its activation and subsequent proteolytic cleavage;Arlaud;Biochim. Biophys. Acta,1980

2. Molecular characterization of the catalytic domains of human complement serine protease C1r;Arlaud;Biochemistry,1986

3. NH2-terminal calcium-binding domain of human complement C1s- mediates the interaction of C1r- with C1q;Busby;Biochemistry,1990

4. Activation of human complement serine-proteinase C1r is down-regulated by a Ca2+-dependent intramolecular control that is released in the C1 complex through a signal transmitted by C1q;Thielens;Biochem. J.,1994

5. Identification of the peptide bond cleaved during activation of human C1r;Arlaud;FEBS Lett.,1985

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