Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2.
Modular organization of the carboxyl-terminal, globular head region of human C1q A, B, and C chains.
The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties.
Characterization and organization of the genes encoding the A-, B- and C-chains of human complement subcomponent C1q. The complete derived amino acid sequence of human C1q.
C1q binds phosphatidylserine and likely acts as a multiligand-bridging molecule in apoptotic cell recognition.
Interaction of human C1q with IgG and IgM: revisited.
CD91 interacts with mannan-binding lectin (MBL) through the MBL-associated serine protease-binding site.
Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability.
Expression of recombinant human complement C1q allows identification of the C1r/C1s-binding sites.
Complement is activated by IgG hexamers assembled at the cell surface.
Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver.
Analysis of the Interaction between Globular Head Modules of Human C1q and Its Candidate Receptor gC1qR.
Structure and activation of C1, the complex initiating the classical pathway of the complement cascade.
Evidence for C1q-mediated crosslinking of CD33/LAIR-1 inhibitory immunoreceptors and biological control of CD33/LAIR-1 expression.
Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics.
Structures of C1-IgG1 provide insights into how danger pattern recognition activates complement.
Molecular modelling of human complement subcomponent C1q and its complex with C1r2C1s2 derived from neutron-scattering curves and hydrodynamic properties.
A reference map of the human binary protein interactome.
The binding site for C1q on IgG.
C1q binding to surface-bound IgG is stabilized by C1r(2)s(2) proteases.
Activation of a complex of C1r and C1s subcomponents of human complement C1 by the third subcomponent C1q.
The Clq receptor site on immunoglobulin G.
Ultrastructure of the first component of human complement: electron microscopy of the crosslinked complex.
Amino acid sequence of the N-terminal 108 amino acid residues of the B chain of subcomponent C1q of the first component of human complement.
Isolation, by partial pepsin digestion, of the three collagen-like regions present in subcomponent Clq of the first component of human complement.
Conversion of C4 into C4a and C4b
Conversion of C2 into C2a and C2b
C1-Inh binds Antigen: antibody: C1 complex activated C1r, C1s
Antigen:IgG:C1Q:2xActivated C1R:SERPING1:2xActivated C1S:SERPING1 dissociates
C1-Inh binds and inactivates C1r, C1s
The classical complement cascade mediates CNS synapse elimination.
Complement and microglia mediate early synapse loss in Alzheimer mouse models.
UniProtKB P02746 human complement C1q subcomponent subunit B