Activation of the first component of complement.

No abstract is available for this paper.

• Publication year

  1987

• Venue

  Annual Review of Immunology

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1146/ANNUREV.IY.05.040187.000321PMID 3036181
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Kinetics of the reaction between human C1-esterase inhibitor and C1r or C1s.

  2005cited by this paper
• Initiation of complement activation

  2005cited by this paper
• The first component of human complement (C1): Activation and control

  2004cited by this paper
• Kinetics of interaction of C1 inhibitor with complement C1s.

  1986cited by this paper
• Human inhibitor of the first component of complement, C1: characterization of cDNA clones and localization of the gene to chromosome 11.

  1986cited by this paper
• A molecular mechanism for the activation of the first component of complement by immune complexes.

  1986cited by this paper
• Activator-bound C1 is less susceptible to inactivation by C1 inhibition than is fluid-phase C1.

  1986cited by this paper
• Activation of the first component of human complement, C1, by monoclonal antibodies directed against different domains of subcomponent C1q.

  1986cited by this paper
• Molecular characterization of the catalytic domains of human complement serine protease C1r.

  1986cited by this paper
• Molecular cloning of human C1 inhibitor: sequence homologies with alpha 1-antitrypsin and other members of the serpins superfamily.

  1986cited by this paper
• Domain structure and associated functions of subcomponents C1r and C1s of the first component of human complement.

  1985cited by this paper
• Efficiency of activation of complement by anti-hapten antibodies at the red cell surface: effect of patchy vs random distribution of hapten.

  1985cited by this paper
• Immunoglobulin G antibody bound to the C1q subcomponent of human complement exhibits segmental flexibility.

  1985cited by this paper
• Primary structure of the reactive site of human C1-inhibitor.

  1985cited by this paper
• Demonstration of the interaction of native C1 with monomeric immunoglobulins and C1 inhibitor.

  1985cited by this paper
• Molecular modelling of human complement subcomponent C1q and its complex with C1r2C1s2 derived from neutron-scattering curves and hydrodynamic properties.

  1985cited by this paper
• Primary structure of the A chain of human complement-classical-pathway enzyme C1r. N-terminal sequences and alignment of autolytic fragments and CNBr-cleavage peptides.

  1985cited by this paper
• Activation of complement pathways by univalent antibody derivatives with intact Fc zones.

  1985cited by this paper
• Nature of the interaction between the C1q and C1r2S2 subunits of the first component of human complement.

  1985cited by this paper
• Immunoglobulin M possesses two binding sites for complement subcomponent C1q, and soluble 1:1 and 2:1 complexes are formed in solution at reduced ionic strength.

  1985cited by this paper
• Activation of the human classical complement pathway by a mouse monoclonal hybrid IgG1-2a monovalent anti-TNP antibody bound to TNP-conjugated cells.

  1985cited by this paper
• Identification of the peptide bond cleaved during activation of human Clr

  1985cited by this paper
• Structural model of the collagen-like region of C1q comprising the kink region and the fibre-like packing of the six triple helices.

  1985cited by this paper
• Segmental flexibility of the C1q subcomponent of human complement and its possible role in the immune response.

  1985cited by this paper
• The classical complement pathway: activation and regulation of the first complement component.

  1985cited by this paper
• The role of immune complexes in the activation of the first component of human complement.

  1984cited by this paper
• Neutron scattering studies of subcomponent C1q of first component C1 of human complement and its association with subunit C1r2C1s2 within C1.

  1984cited by this paper
• Structure and activation of C1: current concepts.

  1984cited by this paper
• Detection of intermediary Clr with complete active site, using a synthetic proteinase inhibitor

  1984cited by this paper
• Activation of C1.

  1984cited by this paper
• The C1q receptor site on human immunoglobulin G.

  1984cited by this paper
• Kinked DNA in crystalline complex with EcoRI endonuclease

  1984cited by this paper
• Conformation and restricted segmental flexibility of C1, the first component of human complement.

  1983cited by this paper
• The mechanism of synergistic complement‐mediated lysis of rat red cells by monoclonal IgG antibodies

  1983cited by this paper
• Neutron scattering studies of the isolated C1r2C1s2 subunit of first component of human complement in solution.

  1983cited by this paper
• The serine proteinase chain of human complement component C1s. Cyanogen bromide cleavage and N-terminal sequences of the fragments.

  1983cited by this paper
• Complete amino acid sequence of the catalytic chain of human complement subcomponent C1-r.

  1983cited by this paper
• Human C1 inhibitor: improved isolation and preliminary structural characterization.

  1983cited by this paper
• Proteins involved in the activation and control of the two pathways of human complement.

  1983cited by this paper
• Heparin-stimulated modification of C1-inhibitor by subcomponent C1s of human complement.

  1983cited by this paper
• Measurement of the association constants of the complexes formed between intact C1q or pepsin-treated C1q stalks and the unactivated or activated C1r2C1s2 tetramers.

  1983cited by this paper
• A new role for C-1-inhibitor in homeostasis: control of activation of the first component of human complement.

  1982cited by this paper
• Spontaneous activation of the first component of human complement (C1) by an intramolecular autocatalytic mechanism.

  1982cited by this paper
• Fluid phase activation of proenzymic C1r purified by affinity chromatography.

  1982cited by this paper
• Kinetics of activation of the first component of complement (C1) by IgG oligomers.

  1982cited by this paper
• Formation of a conformationally changed C1r, a subcomponent of the first component of human complement, as an intermediate of its autoactivation reaction

  1982cited by this paper
• Completion of the amino acid sequences of the A and B chains of subcomponent C1q of the first component of human complement.

  1982cited by this paper
• Fluid-phase interaction of C1 inhibitor (C1 Inh) and the subcomponents C1r and C1s of the first component of complement, C1.

  1982cited by this paper
• The classical complement pathway: mechanism of activation of the first component by antigen-antibody complexes.

  1982cited by this paper
• Ultrastructure of the first component of human complement: electron microscopy of the crosslinked complex.

  1982cited by this paper
• Electron microscopy of the first component of human complement

  1982cited by this paper
• C1q binding to antibody-coated cells: predictions from a simple multivalent binding model.

  1981cited by this paper
• Distinction between fixation of C1 and the activation of complement by natural IgM anti-hapten antibody: effect of cell surface hapten density.

  1981cited by this paper
• Size and shape of human C1-inhibitor.

  1981cited by this paper
• Size and shape of human CI‐inhibitor

  1981cited by this paper
• Increase of conformational stability of homogeneous rabbit immunoglobulin G after hapten binding.

  1981cited by this paper
• Activation of the early components of the classical complement pathway under physiologic conditions.

  1981cited by this paper
• Semi-flexible joint in the C1q subunit of the first component of human complement.

  1981cited by this paper
• Stoichiometry and sedimentation properties of the complex formed between the C1q and C1r2C1s2 subcomponents of the first component of complement.

  1981cited by this paper
• Development of an immunochemical test to assess C1 inactivator function in human serum and its use for the diagnosis of hereditary angioedema.

  1980cited by this paper
• Kinetics of reaction of human C1-inhibitor with the human complement system proteases C1r and C1s.

  1980cited by this paper
• Antigen‐independent activation of the first component of complement C1 by chemically crosslinked rabbit IgG‐oligomers

  1980cited by this paper
• Assembly of subcomponents C1r and C1s of first component of complement: electron microscopic and ultracentrifugal studies.

  1980cited by this paper
• The conformation of subcomponent C1q of the first component of human complement

  1980cited by this paper
• Purified proenzyme C1r. Some characteristics of its activation and subsequent proteolytic cleavage.

  1980cited by this paper
• Calcium binding properties of the C1 subcomponents C1q, C1r and C1s

  1980cited by this paper
• The binding of human complement component C4 to antibody-antigen aggregates.

  1980cited by this paper
• Activation of a complex of C1r and C1s subcomponents of human complement C1 by the third subcomponent C1q.

  1980cited by this paper
• A study on the structure and interactions of the C1 sub-components C1r and C1s in the fluid phase.

  1980cited by this paper
• Hydroxylysine-linked glycosides of human complement subcomponent C1q and various collagens.

  1979cited by this paper
• Structures and mechanisms of DNA restriction and modification enzymes

  1979cited by this paper
• Interaction of a bivalent ligand with IgM anti-lactose antibody.

  1979cited by this paper
• Active disassembly of the first complement component, C-1, by C-1 inactivator.

  1979cited by this paper
• Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement.

  1979cited by this paper
• Activation of the first component of human complement (C1) by antibody-antigen aggregates.

  1978cited by this paper
• Gross conformation of C1q: a subcomponent of the first component of complement.

  1978cited by this paper
• Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate.

  1978cited by this paper
• The subunit composition and sedimentation properties of human C1.

  1977cited by this paper
• The unactivated form of the first component of human complement, C1.

  1976cited by this paper
• Activation of C1r by proteolytic cleavage.

  1976cited by this paper
• Isolation, by partial pepsin digestion, of the three collagen-like regions present in subcomponent Clq of the first component of human complement.

  1976cited by this paper
• Physicochemical and functional characterization of the C1r subunit of the first complement component.

  1976cited by this paper
• Ultracentifuge studies of the binding of IgG of different subclasses to the Clq subunit of the first component of complement.

  1976cited by this paper
• Ultracentifuge studies of the binding of IgG of different subclasses to the Clq subunit of the first component of complement.

  1976cited by this paper
• Isolation and characterization of the proenzyme form of the C1s subunit of the first complement component.

  1974cited by this paper
• The activation of Cls with purified Clr.

  1974cited by this paper
• Isolation and characterization of C1q, a subcomponent of the first component of complement, from human and rabbit sera.

  1972cited by this paper
• Ein Beitrag zur Isolierung und Charakterisierung des C‐Inaktivators aus Humanplasma

  1970cited by this paper
• [Isolation and characterization of C1-Inactivator from human plasma].

  1970cited by this paper
• Nature of the active site of a subunit of the first component of human complement.

  1969cited by this paper
• Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase.

  1965cited by this paper

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