"Opsonin Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Proteins that bind to particles and cells to increase susceptibility to PHAGOCYTOSIS, especially ANTIBODIES bound to EPITOPES that attach to FC RECEPTORS. COMPLEMENT C3B may also participate.
Descriptor ID |
D009895
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MeSH Number(s) |
D12.776.124.486.485.114.767 D12.776.124.486.657 D12.776.124.790.651.114.767 D12.776.377.715.548.114.767
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Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Opsonin Proteins".
Below are MeSH descriptors whose meaning is more specific than "Opsonin Proteins".
This graph shows the total number of publications written about "Opsonin Proteins" by people in this website by year, and whether "Opsonin Proteins" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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1997 | 0 | 1 | 1 |
2008 | 0 | 1 | 1 |
2012 | 0 | 1 | 1 |
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Below are the most recent publications written about "Opsonin Proteins" by people in Profiles.
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Fully human monoclonal antibodies from antibody secreting cells after vaccination with Pneumovax®23 are serotype specific and facilitate opsonophagocytosis. Immunobiology. 2013 May; 218(5):745-54.
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Cryptococcus neoformans enters the endolysosomal pathway of dendritic cells and is killed by lysosomal components. Infect Immun. 2008 Oct; 76(10):4764-71.
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Immune complex size and complement regulate cytokine production by peripheral blood mononuclear cells. Clin Immunol. 1999 Dec; 93(3):274-82.
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Tromp1, a putative rare outer membrane protein, is anchored by an uncleaved signal sequence to the Treponema pallidum cytoplasmic membrane. J Bacteriol. 1997 Aug; 179(16):5076-86.
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Roles of complement and complement receptor type 3 in phagocytosis of Listeria monocytogenes by inflammatory mouse peritoneal macrophages. Infect Immun. 1991 Aug; 59(8):2645-52.
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Protective and heart-crossreactive epitopes located within the NH2 terminus of type 19 streptococcal M protein. J Exp Med. 1988 Jun 01; 167(6):1849-59.