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Article

Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: Structure of the active catalytic region of C1r

1 Dec 2007

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Share to Blood Coagulation and Thrombosis Mechanisms
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Identifiers

PMID: 17996945
DOI: 10.1016/j.molimm.2007.09.031

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Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: Structure of the active catalytic region of C1rPMID 17996945Read ↗

Structural biology of the C1 complex of complement unveils the mechanisms of its activation and proteolytic activitySemantic proximity Read ↗

Structure and activation of the C1 complex of complement: unraveling the puzzleSemantic proximity Read ↗

Structural biology of C1: dissection of a complex molecular machinerySemantic proximity Read ↗

Deciphering the Fine Details of C1 Assembly and Activation Mechanisms: â€œMission Impossibleâ€?Semantic proximity Read ↗

Structure of the C1r–C1s interaction of the C1 complex of complement activationSemantic proximity Read ↗

The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complexSemantic proximity Read ↗

Structural and functional anatomy of the globular domain of complement protein C1qSemantic proximity Read ↗

Factor B structure provides insights into activation of the central protease of the complement systemSemantic proximity Read ↗

Crystal structure of the catalytic domain of human complement C1s: a serine protease with a handleSemantic proximity Read ↗

Identification of the C1q-binding Sites of Human C1r and C1s: a refined three-dimensional model of the C1 complex of complement.Semantic proximity Read ↗

C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement FunctionsSemantic proximity Read ↗

The Molecular Mechanisms of Complement Receptor 1—It Is ComplicatedSemantic proximity Read ↗

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