Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

MASP-1, a Promiscuous Complement Protease: Structure of Its Catalytic Region Reveals the Basis of Its Broad Specificity

29 Jun 2009

Abstract excerpt

Mannose-binding lectin (MBL)-associated serine protease (MASP)-1 is an abundant component of the lectin pathway of complement. The related enzyme, MASP-2 is capable of activating the complement cascade alone. Though the concentration of MASP-1 far exceeds that of MASP-2, only a supporting role of MASP-1 has been identified regarding lectin pathway activation. Several non-complement substrates, like fibrinogen and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Blood Coagulation and Thrombosis Mechanisms
Share to Coagulation, Bradykinin, Polyphosphates, and Angioedema
Share to Complement system in diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 19564340
DOI: 10.4049/jimmunol.0901141

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

MASP-1, a Promiscuous Complement Protease: Structure of Its Catalytic Region Reveals the Basis of Its Broad SpecificityPMID 19564340Read ↗

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.Semantic proximity Read ↗

Mannan-Binding Lectin-Associated Serine Protease (MASP)-1 Is Crucial for Lectin Pathway Activation in Human Serum, whereas neither MASP-1 nor MASP-3 Is Required for Alternative Pathway FunctionSemantic proximity Read ↗

Crystal Structure and Functional Characterization of the Complement Regulator Mannose-binding Lectin (MBL)/Ficolin-associated Protein-1 (MAP-1)Semantic proximity Read ↗

A novel mannose-binding lectin-associated serine protease 1/3 gene variant.Semantic proximity Read ↗

Polymorphisms in mannan-binding lectin (MBL)-associated serine protease 2 affect stability, binding to MBL, and enzymatic activity.Semantic proximity Read ↗

Mannose-binding lectin serine proteases and associated proteins of the lectin pathway of complement: Two genes, five proteins and many functions?Semantic proximity Read ↗

Investigation of the mechanism of interaction between Mannose-binding lectin-associated serine protease-2 and complement C4.Semantic proximity Read ↗

Structural basis for activation of the complement system by component C4 cleavage.Semantic proximity Read ↗

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

Interaction of mannose-binding protein with associated serine proteases: effects of naturally occurring mutations.Semantic proximity Read ↗

Deciphering Complement Receptor Type 1 Interactions with Recognition Proteins of the Lectin Complement PathwaySemantic proximity Read ↗

Multiple domains of MASP-2, an initiating complement protease, are required for interaction with its substrate C4.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.