| AIF | anemia-inducing factor; anti-inflammatory; anti-invasion factor |
|---|---|
| AIHA | American Industrial Hygiene Association; autoimmune hemolytic anemia |
| AISA | acquired idiopathic sideroblastic anemia |
| APA | action potential amplitude; aldosterone-producing adenoma; Ambulatory Pediatric Association; America... |
| APAF | antipernicious anemia factor |
| iron-sulfur proteins | A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation. (12 Dec 1998) |
|---|---|
| oncogene proteins | Proteins coded by oncogenes. They include proteins resulting from the fusion of an oncogene and another gene (oncogene proteins, fusion). (12 Dec 1998) |
| oncogene proteins, fusion | The translation products of the fusion between an oncogene and another gene. The latter may be of viral or cellular origin. (12 Dec 1998) |
| oncogene proteins v-abl | Transforming proteins encoded by the abl oncogenes. Oncogenic transformation of c-abl to v-abl occurs by insertional activation that results in deletions of specific n-terminal amino acids. (12 Dec 1998) |
| oncogene proteins v-erba | Transforming proteins encoded by erba oncogenes from the avian erythroblastosis virus. They are truncated versions of c-erba, the thyroid hormone receptor (receptors, thyroid hormone) that have retained both the DNA-binding and hormone-binding domains. Mutations in the hormone-binding domains abolish the transcriptional activation function. V-erba acts as a dominant repressor of c-erba, inducing transformation by disinhibiting proliferation. (12 Dec 1998) |
| oncogene proteins v-erbb | Transforming proteins encoded by erbb oncogenes from the avian erythroblastosis virus. The protein is a truncated form of the egf receptor (receptors, epidermal growth factor-urogastrone) whose kinase domain is constitutively activated by deletion of the ligand-binding domain. (12 Dec 1998) |
| oncogene proteins v-fos | Transforming proteins coded by fos oncogenes. These proteins have been found in the finkel-biskis-jinkins (fbj-msv) and finkel-biskis-reilly (fbr-msv) murine sarcoma viruses which induce osteogenic sarcomas in mice. The fbj-msv v-fos gene encodes a p55 kD protein and the fbr-msv v-fos gene encodes a p75 kD fusion protein. (12 Dec 1998) |
| oncogene proteins, viral | Products of viral oncogenes, most commonly retroviral oncogenes. They usually have transforming and often protein kinase activities. (12 Dec 1998) |
| oncogene proteins v-mos | Transforming proteins coded by mos oncogenes. The v-mos proteins were originally isolated from the moloney murine sarcoma virus (mo-msv). (12 Dec 1998) |
| tau proteins | One of the two major classes of microtubule-associated proteins isolated from the brain. The proteins have two domains: one that binds to microtubules and a second that binds to other cell components. By binding to several unpolymerised tubulin molecules simultaneously, tau proteins speed up the nucleation process in tubulin polymerization. Chemically modified tau proteins also appear to be involved in the formation and/or composition of the neurofibrillary tangles and neuropil threads found in alzheimer disease. (12 Dec 1998) |
| thyroxine-binding proteins | A group of proteins that includes thyroxine-binding globulin, a glycoprotein that serves as the major and specific carrier of thyroxine in plasma, accounting for 70-75% of the bound thyroxine; thyroxine-binding prealbumin, an albumin that serves as the secondary carrier, accounting for between 20 and 25% of the bound thyroxine; and serum albumin, which accounts for the remaining bound thyroxine. (12 Dec 1998) |
| egg proteins | Proteins which are found in eggs or ova from any species. (12 Dec 1998) |
| egg proteins, dietary | Proteins found in eggs which are consumed as a food. (12 Dec 1998) |
| extracellular matrix proteins | Macromolecular organic compounds that contain carbon, hydrogen, oxygen, nitrogen, and usually, sulfur. These macromolecules (proteins) form an intricate meshwork in which cells are embedded to construct tissues. Variations in the relative types of macromolecules and their organization determine the type of extracellular matrix, each adapted to the functional requirements of the tissue. The two main classes of macromolecules that form the extracellular matrix are: glycosaminoglycans, usually linked to proteins (proteoglycans), and fibrous proteins (e.g., collagen, elastin, fibronectins and laminin). (12 Dec 1998) |
| extrinsic 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) |