| R' | in electrocardiography, the second positive deflection during the QRS complex |
|---|---|
| ROCF | Rey-Osterrieth Complex Figure |
| rSr | an electrocardiographic complex |
| SFMC | soluble fibrin monomer complex |
| TAT | tetanus antitoxin; thematic apperception test; thematic aptitude test; thrombin-antithrombin complex... |
Ni
| paraluteal cell | A steroid secretory cell of the corpus luteum that comes from the theca interna of the ovarian follicle at the time of ovulation. Synonym: paraluteal cell, paralutein cell. (05 Mar 2000) |
|---|---|
| paralutein cell | A steroid secretory cell of the corpus luteum that comes from the theca interna of the ovarian follicle at the time of ovulation. Synonym: paraluteal cell, paralutein cell. (05 Mar 2000) |
| reactive cell | <cell biology> A round to oval astrocyte cell with abundant cytoplasm containing glial filaments and an eccentric nucleus; may contain two nuclei in the cell hypertrophy of astrocytes. Synonym: gemistocyte, gemistocytic cell, reactive astrocyte, reactive cell. (05 Mar 2000) |
| genes, T-cell receptor | DNA sequences, in cells of the t-lymphocyte lineage, that code for T-cell receptors. The tcr genes are formed by somatic rearrangement (see gene rearrangement, t-lymphocyte and its children) of germline gene segments, and resemble ig genes in their mechanisms of diversity generation and expression. (12 Dec 1998) |
| genes, T-cell receptor alpha | DNA sequences encoding the alpha chain of the T-cell receptor. The genomic organization of the tcr alpha genes is essentially the same in all species and is similar to the organization of ig genes. (12 Dec 1998) |
| genes, T-cell receptor beta | DNA sequences encoding the beta chain of the T-cell receptor. The genomic organization of the tcr beta genes is essentially the same in all species and is similar to the organization of ig genes. (12 Dec 1998) |
| genes, T-cell receptor delta | DNA sequences encoding the delta chain of the T-cell receptor. The delta-chain locus is located entirely within the alpha-chain locus. (12 Dec 1998) |
| genes, T-cell receptor gamma | DNA sequences encoding the gamma chain of the T-cell receptor. The human gamma-chain locus is organised similarly to the tcr beta-chain locus. (12 Dec 1998) |
| Marchand's wandering cell | A cell of the mononuclear phagocyte system. (05 Mar 2000) |
| receiver cell | <plant biology> Cells in the photosynthetic tissues of plants into which the solutes from xylem are pumped. (18 Nov 1997) |
| receptors, antigen, B-cell | Immunoglobulin molecules on the surface of B-lymphocytes that recognise and bind antigen. (12 Dec 1998) |
| receptors, antigen, T-cell | Molecules on the surface of T-lymphocytes that recognise and combine with antigens. The receptors are non-covalently associated with a complex of several polypeptides collectively called CD3 antigens (antigens, CD3). Recognition of foreign antigen and the major histocompatibility complex is accomplished by a single heterodimeric antigen-receptor structure, composed of either alpha-beta (receptors, antigen, T-cell, alpha-beta) or gamma-delta (receptors, antigen, T-cell, gamma-delta) chains. (12 Dec 1998) |
| receptors, antigen, T-cell, alpha-beta | T-cell receptors composed of CD3-associated alpha and beta polypeptide chains and expressed primarily in CD4+ or CD8+ T-cells. Unlike immunoglobulins, the alpha-beta T-cell receptors recognise antigens only when presented in association with major histocompatibility (MHC) molecules. (12 Dec 1998) |
| receptors, antigen, T-cell, gamma-delta | T-cell receptors composed of CD3-associated gamma and delta polypeptide chains and expressed primarily in CD4-/CD8- T-cells. The receptors appear to be preferentially located in epithelial sites and probably play a role in the recognition of bacterial antigens. The T-cell receptor gamma/delta chains are separate and not related to the gamma and delta chains which are subunits of CD3 (see antigens, CD3). (12 Dec 1998) |
| receptors, cell surface | Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behaviour of the target cell. Cell surface receptors, unlike enzymes, do not chemically alter their ligands. (12 Dec 1998) |