"Rosette Formation" 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.
The in vitro formation of clusters consisting of a cell (usually a lymphocyte) surrounded by antigenic cells or antigen-bearing particles (usually erythrocytes, which may or may not be coated with antibody or antibody and complement). The rosette-forming cell may be an antibody-forming cell, a memory cell, a T-cell, a cell bearing surface cytophilic antibodies, or a monocyte possessing Fc receptors. Rosette formation can be used to identify specific populations of these cells.
| Descriptor ID |
D012397
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| MeSH Number(s) |
E01.370.225.812.706 E05.200.812.706 E05.478.594.730
|
| Concept/Terms |
Rosette Formation- Rosette Formation
- Formation, Rosette
- Formations, Rosette
- Rosette Formations
- Immunocytoadherence
- Immunocytoadherences
|
Below are MeSH descriptors whose meaning is more general than "Rosette Formation".
Below are MeSH descriptors whose meaning is more specific than "Rosette Formation".
This graph shows the total number of publications written about "Rosette Formation" by people in this website by year, and whether "Rosette Formation" was a major or minor topic of these publications.
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Below are the most recent publications written about "Rosette Formation" by people in Profiles.
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Recombinant human IgG molecules lacking Fcgamma receptor I binding and monocyte triggering activities. Eur J Immunol. 1999 08; 29(8):2613-24.
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Interaction of human monocyte Fc gamma receptors with rat IgG2b. A new indicator for the Fc gamma RIIa (R-H131) polymorphism. J Immunol. 1995 Feb 15; 154(4):1852-60.
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Transfected NA1 and NA2 forms of human neutrophil Fc receptor III exhibit antigenic and structural heterogeneity. Blood. 1991 Jun 15; 77(12):2682-7.
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Molecular basis for a polymorphism involving Fc receptor II on human monocytes. J Immunol. 1989 Sep 01; 143(5):1731-4.
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Molecular basis for a polymorphism involving Fc receptor II on human monocytes. Trans Assoc Am Physicians. 1989; 102:252-9.
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Excessive binding of the natural anti-alpha-galactosyl IgG to sickle red cells: enhancement of red cell destruction by a physiological process. Trans Assoc Am Physicians. 1985; 98:158-65.