| PC | avoirdupois weight [Lat. pondus civile]; packed cells; paper chromatography; paracortex; parent cell... |
|---|---|
| TIC | Toxicology Information Center; trypsin inhibitory capability; tubulointerstitial cell; tumor-inducin... |
| AMC | academic medical center; acetylmethyl carbinol; Animal Medical Center; antibody-mediated cytotoxicit... |
| CDC | calculated date of confinement; cancer diagnosis center; capillary diffusion capacity; cell division... |
| CPC | central posterior curve; cerebellar Purkinje cell; cerebral palsy clinic; cerebral performance categ... |
| insect proteins | Proteins found in any species of insect. (12 Dec 1998) |
|---|---|
| insulin-like growth-factor-binding proteins | A family of soluble proteins that bind insulin-like growth factors and modulate their biological actions at the cellular level. (int j gynaecol obstet 1992;39(1):3-9) (12 Dec 1998) |
| integral proteins | Proteins that cannot be easily separated from a biomembrane. Synonym: intrinsic proteins. (05 Mar 2000) |
| intermediate filament proteins | Filaments 7-11 nm in diameter found in the cytoplasm of all cells. Many specific proteins belong to this group, e.g., desmin, vimentin, prekeratin, decamin, skeletin, neurofilin, neurofilament protein, and glial fibrillary acid protein. (12 Dec 1998) |
| intrinsic proteins | Proteins that cannot be easily separated from a biomembrane. Synonym: intrinsic proteins. (05 Mar 2000) |
| 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) |