Extensive Basal Level Activation of Complement Mannose-Binding Lectin-Associated Serine Protease-3: Kinetic Modeling of Lectin Pathway Activation Provides Possible Mechanism.

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Complement in the Initiation and Evolution of Rheumatoid Arthritis.Be on Target: Strategies of Targeting Alternative and Lectin Pathway Components in Complement-Mediated Diseases

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P2860

Extensive Basal Level Activation of Complement Mannose-Binding Lectin-Associated Serine Protease-3: Kinetic Modeling of Lectin Pathway Activation Provides Possible Mechanism.

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2017 nî lūn-bûn

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2017年学术文章

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Extensive Basal Level Activati ...... n Provides Possible Mechanism.

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Extensive Basal Level Activati ...... n Provides Possible Mechanism.

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Extensive Basal Level Activati ...... n Provides Possible Mechanism.

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Extensive Basal Level Activati ...... n Provides Possible Mechanism.

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Extensive Basal Level Activati ...... n Provides Possible Mechanism.

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Extensive Basal Level Activati ...... n Provides Possible Mechanism.

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P1476

Extensive Basal Level Activati ...... n Provides Possible Mechanism.

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P2093

Gábor Oroszlán

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József Dobó

http://www.w3.org/2001/XMLSchema#string

Péter Gál

http://www.w3.org/2001/XMLSchema#string

Péter Závodszky

http://www.w3.org/2001/XMLSchema#string

Ráhel Dani

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P2860

Proteolytic activities of two types of mannose-binding lectin-associated serine protease

MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway

Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: a study on recombinant catalytic fragments

Structures of C3b in complex with factors B and D give insight into complement convertase formation

A novel mannose-binding lectin/ficolin-associated protein is highly expressed in heart and skeletal muscle tissues and inhibits complement activation

Complement factor D, a novel serine protease

MASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificity

Quantitative Characterization of the Activation Steps of Mannan-binding Lectin (MBL)-associated Serine Proteases (MASPs) Points to the Central Role of MASP-1 in the Initiation of the Complement Lectin Pathway

The X-ray Crystal Structure of Mannose-binding Lectin-associated Serine Proteinase-3 Reveals the Structural Basis for Enzyme Inactivity Associated with the Carnevale, Mingarelli, Malpuech, and Michels (3MC) Syndrome

The Serine Protease Domain of MASP-3: Enzymatic Properties and Crystal Structure in Complex with Ecotin

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1821

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scholarly article

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10.3389/FIMMU.2017.01821

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Steffen Thiel

Andras Szilagyi

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2017-12-18T00:00:00Z

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29326707

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Extensive Basal Level Activation of Complement Mannose-Binding Lectin-Associated Serine Protease-3: Kinetic Modeling of Lectin Pathway Activation Provides Possible Mechanism.

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P2860

P2860

Extensive Basal Level Activation of Complement Mannose-Binding Lectin-Associated Serine Protease-3: Kinetic Modeling of Lectin Pathway Activation Provides Possible Mechanism.

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