| viral regulatory proteins | Proteins which regulate the rate of transcription of viral structural genes. (12 Dec 1998) |
|---|---|
| viral structural proteins | Viral proteins that do not regulate transcription. They are coded by viral structural genes and include nucleocapsid core proteins (gag proteins), enzymes (pol proteins), and membrane components (env proteins). Transcription of viral structural genes is regulated by viral regulatory proteins. (12 Dec 1998) |
| viral tail proteins | Proteins found in the tail sections of DNA and RNA viruses. It is believed that these proteins play a role in directing chain folding and assembly of polypeptide chains. (12 Dec 1998) |
| cell cycle proteins | Proteins that control the cell division cycle. This family of proteins includes a wide variety of classes, including cyclin-dependent kinases, mitogen-activated kinases, cyclins, and phosphoprotein phosphatases (phosphoprotein phosphatase) as well as their putative substrates such as chromatin-associated proteins, cytoskeletal proteins, and transcription factors. (12 Dec 1998) |
| glue proteins, drosophila | Glycosylated proteins which are part of the salivary glue that drosophila larvae secrete as a means of fixing themselves to an external substrate for the duration of the pre-pupal and pupal period. The proteins which consist of at least eight polypeptides are encoded in the third larval instar by the sgs-3, sgs-4, sgs-7 and sgs-8 genes. (12 Dec 1998) |
| repressor proteins | Proteins which are normally bound to the operator locus of an operon, thereby preventing transcription of the structural genes. In enzyme induction, the substrate of the inducible enzyme binds to the repressor protein, causing its release from the operator and freeing the structural genes for transcription. In enzyme repression, the end product of the enzyme sequence binds to the free repressor protein, the resulting complex then binds to the operator and prevents transcription of the structural genes. (12 Dec 1998) |
| cerebrospinal fluid proteins | Proteins in the cerebrospinal fluid, normally albumin and globulin present in the ratio of 8 to 1. Increases in protein levels are of diagnostic value in neurological diseases. (brain and bannister's clinical neurology, 7th ed, p221) (12 Dec 1998) |
| membrane proteins | Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. (12 Dec 1998) |
| retroviridae proteins | Proteins from the family retroviridae. The most frequently encountered member of this family is the rous sarcoma virus protein. (12 Dec 1998) |
| retroviridae proteins, oncogenic | Retroviral proteins that have the ability to transform cells. They can induce sarcomas, leukaemias, lymphomas, and mammary carcinomas. Not all retroviral proteins are oncogenic. (12 Dec 1998) |
| chimeric proteins | Proteins in individuals that are derived from genetically different zygotes. (12 Dec 1998) |
| peripheral proteins | Pathways that can be easily removed from a biomembrane (e.g., by altering the pH or the ionic strength). Synonym: extrinsic proteins. (05 Mar 2000) |
| periplasmic binding proteins | Transport proteins located within the periplasmic space. Some act as receptors for bacterial chemotaxis, interacting with MCPs. Their mode of action is unclear. (18 Nov 1997) |
| ribosomal proteins | Proteins found in ribosomes. They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits. (12 Dec 1998) |
| growth associated proteins | <growth factor> Group of developmentally regulated polypeptides thought to be critical for the formation of neural circuitry. The acidic membrane phosphoprotein GAP 43 is synthesised and transported down regenerating and developing axons, pp46 localised in growth cone membranes during embryogenesis, B 50 in mature presynaptic membranes in the regulation of phosphotidylinositol turnover and F1 in the hippocampus during long-term potentiation, are now all known to be the same protein. (18 Nov 1997) |