Baculovirus-mediated expression of truncated modular fragments from the catalytic region of human complement serine protease C1s. Evidence for the involvement of both complement control protein modules in the recognition of the C4 protein substrate.

Baculovirus-mediated expression of truncated modular fragments from the catalytic region of human complement serine protease C1s. Evidence for the involvement of both complement control protein modules in the recognition of the C4 protein substrate.

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Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2 Structural basis for activation of the complement system by component C4 cleavage Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle Paths reunited: Initiation of the classical and lectin pathways of complement activation Structural insights into the innate immune recognition specificities of L- and H-ficolins Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch A Molecular Switch Governs the Interaction between the Human Complement Protease C1s and Its Substrate, Complement C4 The Serine Protease Domain of MASP-3: Enzymatic Properties and Crystal Structure in Complex with Ecotin Crystal Structure of the Tetrameric Fibrinogen-like Recognition Domain of Fibrinogen C Domain Containing 1 (FIBCD1) Protein Microarray reveals complement components are regulated in the serum-deprived rat retinal ganglion cell line Deciphering the fine details of c1 assembly and activation mechanisms: "mission impossible"?Elucidation of the substrate specificity of the C1s protease of the classical complement pathway.The recognition unit of FIBCD1 organizes into a noncovalently linked tetrameric structure and uses a hydrophobic funnel (S1) for acetyl group recognition.Topology of the membrane-bound form of complement protein C9 probed by glycosylation mapping, anti-peptide antibody binding, and disulfide modification.The N-terminal CUB-epidermal growth factor module pair of human complement protease C1r binds Ca2+ with high affinity and mediates Ca2+-dependent interaction with C1s.Structural and Functional Characterization of a Single-Chain Form of the Recognition Domain of Complement Protein C1q.A recombinant chimeric epidermal growth factor-like module with high binding affinity for integrins.Functional characterization of complement proteases C1s/mannan-binding lectin-associated serine protease-2 (MASP-2) chimeras reveals the higher C4 recognition efficacy of the MASP-2 complement control protein modules.Molecular interactions between MASP-2, C4, and C2 and their activation fragments leading to complement activation via the lectin pathway.Studies on the interactions between C-reactive protein and complement proteins.The emerging role of complement lectin pathway in trypanosomatids: molecular bases in activation, genetic deficiencies, susceptibility to infection, and complement system-based therapeutics.

P2860

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P2860

Baculovirus-mediated expression of truncated modular fragments from the catalytic region of human complement serine protease C1s. Evidence for the involvement of both complement control protein modules in the recognition of the C4 protein substrate.

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http://www.wikidata.org/entity/Q32155073

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1998 nî lūn-bûn

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1998 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի հունվարին հրատարակված գիտական հոդված

@hy

1998年の論文

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1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

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