Formation of covalent complexes between the fourth component of human complement and IgG immune aggregates.

No abstract is available for this paper.

• Publication year

  1987

• Venue

  Complement

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1159/000463004PMID 3568629
• 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.

• No references are available for this paper.

• Release of Arachidonic Acid by Stimulation of Opsonic Receptors in Human Monocytes

  2003cites this paper
• The internal thioester and the covalent binding properties

  2002cites this paper
• Activation of the Complement Classical Pathway (C1q Binding) by Mesophilic Aeromonas hydrophila Outer Membrane Protein

  1998cites this paper
• The internal thioester and the covalent binding properties of the complement proteins C3 and C4

  1997cites this paper
• C1q binding and activation of the complement classical pathway by Klebsiella pneumoniae outer membrane proteins

  1993cites this paper
• The structure of immunoglobulins and their interaction with complement

  1993cites this paper
• Human antibody effector function.

  1992cites this paper
• Identification of virus components in circulating immune complexes isolated during hepatitis a virus infection

  1990cites this paper
• Substitution of a single amino acid (aspartic acid for histidine) converts the functional activity of human complement C4B to C4A.

  1990cites this paper
• Role of the fourth complement component (C4) in the regulation of contact sensitivity. II. Qualitative differences between C4 molecules from high- and low-C4 mouse strains.

  1989cites this paper
• Separation of active and inactive forms of the third component of human complement, C3, by fast protein liquid chromatography (FPLC).

  1989cites this paper
• The fluid-phase binding of human C4 and its genetic variants, C4A3 and C4B1, to immunoglobulins.

  1988cites this paper