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  • plasma thromboplastin inhibitor
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  • plasmin activation inhibitor
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  • protease inhibitor
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  • protease inhibitor type
  • reductase, 5-alpha-reductase inhibitor
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  • reversible inhibitor of MAO-A
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  • selective serotonin reuptake inhibitor(SSRI)
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  • serotonin-nonselective reuptake inhibitor
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  • serpin inhibitor
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  • specific inhibitor
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  • specific serotonin reuptake inhibitor(SSRI)
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  • tissue inhibitor
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  • tissue inhibitor of metalloprotainase
  • tissue inhibitor of metalloproteinase
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  • tissue plasminogen activation inhibitor
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OMI Oocyte Maturation Inhibitor
ACEI angiotensin-converting enzyme inhibitor
ACI acceleration index; acoustic comfort index; acute cardiac ischemia; acute coronary infarction; acute...
AI accidental injury; accidentally incurred; adiposity index; aggregation index; allergy and immunology...
AIA allylisopropylacetamide; amylase inhibitor activity; anti-immunoglobulin antibody; anti-insulin anti...
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TRD Temporal Response Differentiation
MNDA myeloid cell nuclear differentiation antigen
APP Acute phase proteins
ABP Albumin-binding proteins
CENP CENtromere proteins
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tissue inhibitor of metalloproteinases <chemical> A family of secreted proteins (timp-1, timp-2, and timp-3) that play a crucial role in regulating the activity of the secreted metalloproteinases (collagenases, stromelysins, gelatinases). Of the three characterised, only timp-1 and timp-2 appear to have related primary structures and inhibitory properties. They influence the activation of the prometalloproteinase and act to modulate proteolysis of extracellular matrix, notably during tissue remodeling and inflammatory processes. On certain cell types, they can exhibit growth factor-like activity, and they can inhibit the tumourigenic and metastatic phenotype in cancer cells. (pharmacol ther 1993;59:329-41)
Pharmacological action: antineoplastic agent, protease inhibitors.
(12 Dec 1998)
trypsin inhibitor A peptide hydrolyzed off trypsinogen under the catalytic influence of enteropeptidase, with trypsin produced as a result; so called because the peptide masks or inhibits the active site of the trypsin molecule, one of the polypeptides, from various sources (e.g., human and bovine colostrum, soybeans, egg white), that inhibit the action of trypsin.
Compare: Bowman-Birk inhibitor.
(05 Mar 2000)
trypsin inhibitor, bowman-birk soybean <chemical> A low-molecular-weight protein (minimum molecular weight 8000) which has the ability to inhibit trypsin as well as chymotrypsin at independent binding sites. It is characterised by a high cystine content and the absence of glycine.
Pharmacological action: trypsin inhibitors.
(12 Dec 1998)
trypsin inhibitor, kazal pancreatic <chemical> A pancreatic trypsin inhibitor common to all mammals. It is secreted with the zymogens into the pancreatic juice. It is a protein composed of 56 amino acid residues and is different in amino acid composition and physiological activity from the kunitz bovine pancreatic trypsin inhibitor (aprotinin).
Chemical name: Trypsin inhibitor, pancreatic secretory
(12 Dec 1998)
trypsin inhibitor, kunitz soybean <chemical> A high-molecular-weight protein (approximately 22,500) containing 198 amino acid residues. It is a strong inhibitor of trypsin and human plasmin.
Pharmacological action: trypsin inhibitors.
Chemical name: Trypsin inhibitor, Kunitz soybean
(12 Dec 1998)
familial lipoprotein lipase inhibitor An inhibitor found in certain individuals that inhibits lipoprotein lipase resulting in accumulation of chylomicrons, VLDL, and triacylglycerols; similar in symptoms to familial lipoprotein lipase deficiency.
(05 Mar 2000)
lipoprotein-associated coagulation inhibitor Formerly known as anticonvertin; a protein that inhibits the extrinsic pathway of coagulation by binding to the tissue factor III-factor VII-Calcium-factor Xa complex.
(05 Mar 2000)
lupus coagulation inhibitor An antiphospholipid antibody found in association with systemic lupus erythematosus (lupus erythematosus, systemic), antiphospholipid syndrome, and in a variety of other diseases as well as in healthy individuals. In vitro, the antibody interferes with the conversion of prothrombin to thrombin and prolongs the partial thromboplastin time. In vivo, it exerts a procoagulant effect resulting in thrombosis mainly in the larger veins and arteries. It further causes obstetrical complications, including foetal death and spontaneous abortion, as well as a variety of haematologic and neurologic complications.
(12 Dec 1998)
adenovirus e1a proteins Proteins transcribed from the e1a region of adenovirus which are involved in positive regulation of transcription of the early genes.
(12 Dec 1998)
adenovirus e1b proteins Proteins transcribed from the e1b region of adenovirus which are involved in regulation of the levels of early and late gene expression.
(12 Dec 1998)
adenovirus e1 proteins The very first viral gene products synthesised after cells are infected with adenovirus. The e1 region of the genome has been divided into two major transcriptional units, e1a and e1b, each expressing proteins of the same name (adenovirus e1a proteins and adenovirus e1b proteins).
(12 Dec 1998)
adenovirus e2 proteins Proteins transcribed from the e2 region of adenovirus. Several of these are required for viral DNA replication.
(12 Dec 1998)
adenovirus e3 proteins Proteins transcribed from the e3 region of adenovirus but not essential for viral replication. The e3 19k protein mediates adenovirus persistence by reducing the expression of class I major histocompatibility complex antigens on the surface of infected cells.
(12 Dec 1998)
adenovirus e4 proteins Proteins transcribed from the e4 region of adenovirus. The e4 19k protein transactivates transcription of the adenovirus e2f protein and complexes with it.
(12 Dec 1998)
adenovirus early proteins <molecular biology, protein, virology> Proteins encoded by adenoviruses that are synthesised prior to, and in the absence of, viral DNA replication.
The proteins are involved in both positive and negative regulation of expression in viral and cellular genes, and also affect the stability of viral mRNA. Some are also involved in oncogenic transformation.
(12 Dec 1998)
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