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  • radiation weighting factor
    ¹æ»ç¼±°¡Áß°è¼ö
  • realization factor
    ½ÇÇöÀÎÀÚ(ãùúÞì×í­).
  • recruitment factor
    ´©°¡¿äÀÎ(׫ʥé©ì×).
  • reducing factor
    ȯ¿øÀÎÀÚ.
  • relaxing factor
    ÀÌ¿ÏÀÎÀÚ(ì¬èÐì×í­).
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  • factor VIII-related antigen
    Á¦ VIII-°ü·ÃÇ׿ø
  • factor VIIa
    Á¦ VIIa ÀÎÀÚ
  • factor X
    Á¦ X ÀÎÀÚ
  • factor XI
    Á¦ XI ÀÎÀÚ
  • factor XII
    Á¦ XII ÀÎÀÚ
  • factor XIII
    Á¦ XIII ÀÎÀÚ
  • factor XIIIa
    Á¦ XIIIaÀÎÀÚ
  • factor XIIa
    Á¦ XIIa ÀÎÀÚ
  • factor XIa
    Á¦ XIa ÀÎÀÚ
  • factor Xa
    Á¦ Xa ÀÎÀÚ
  • factor deficiency
    Á¦ÀÎÀÚ°áÇÌÁõ(ð¯ì×í­ÌÀù¹ñø).
  • factor ii(prothrombin)
    Á¦2ÀÎÀÚ(ÇÁ·ÎÆ®·Òºó)
  • factor ix deficiency
    Á¦9ÀÎÀÚ °áÇÌ(Áõ)
  • factor theory
    ¿äÀÎÀÌ·Ð(é©ì×ìµÖå)
  • factor vii
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  • separation factor
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  • stringent factor
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  • Stuart factor
    ½ºÆ©¾Æ¸£Æ® ÀÎÀÚ(ì×í­)
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EIF erythrocyte initiation factor; eukaryotic initiation factor
FF degree of fineness of abrasive particles; fat-free; father factor; fecal frequency; fertility factor...
GF gastric fistula; gastric fluid; germ-free; glass factor; glomerular filtration; gluten-free; grandfa...
GIF gastric intrinsic factor; growth hormone-inhibiting factor
HGF hepatocyte growth factor; hyperglycemic-glucogenolytic factor
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(125I)-EGF 125I)-labeled epidermal growth factor
125-I-EGF 125I-labelled epidermal growth factor
CBF 2/core binding factor
CSF Colony Stimulating Factor
APRF 3/acute phase response factor
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receptors, somatotropin Cell surface proteins that bind somatotropin with high affinity and trigger intracellular changes influencing the behaviour of cells. Activation of growth hormone receptors regulates amino acid transport through cell membranes, RNA translation to protein, DNA transcription, and protein and amino acid catabolism in many cell types. Many of these effects are mediated indirectly through stimulation of the release of somatomedins.
(12 Dec 1998)
receptors, steroid Proteins found usually in the cytoplasm or nucleus that specifically bind steroid hormones and trigger changes influencing the behaviour of cells. The steroid receptor-steroid hormone complex regulates the transcription of specific genes.
(12 Dec 1998)
receptors, tachykinin Cell surface proteins that bind tachykinins with high affinity and trigger intracellular changes influencing the behaviour of cells. Three classes of tachykinin receptors have been characterised, the nk-1, nk-2, and nk-3, which prefer, respectively, substance p, neurokinin a (substance k, neurokinin alpha, neuromedin l), and neurokinin b (neurokinin beta, neuromedin k).
(12 Dec 1998)
receptors, thrombin Cell surface proteins that specifically bind thrombin and trigger changes in the behaviour of blood cells. There are at least two types of thrombin receptors on platelets. The higher affinity receptors mediate the inhibition of stimulated adenylate cyclase, the secretion of acid hydrolases, and the activation of phospholipase a2. The lower affinity receptors are linked to phospholipase c and trigger platelet aggregation and exposure of fibrinogen binding sites. A human platelet thrombin receptor has been cloned and is a member of the family of peptide receptors. There are also thrombin receptors on endothelial cells and smooth muscle cells.
(12 Dec 1998)
receptors, thromboxane Cell surface proteins that bind thromboxanes with high affinity and trigger intracellular changes influencing the behaviour of cells. at least a subset of thromboxane receptors act via the inositol phosphate and diacylglycerol second messenger systems.
(12 Dec 1998)
receptors, thyroid hormone Proteins, usually found in the nucleus, that specifically bind thyroid hormones and regulate DNA transcription. These proteins, termed c-erba, are activated by hormones and cause differentiation of erythroid progenitor cells which irreversibly lose proliferative potential. Thus c-erba proteins act as growth suppressors. The c-erba proteins are encoded by at least two genes, c-erba alpha and c-erba beta. Each of these has two isoforms. Mutations in the ligand-binding domain of the beta form causes thyroid hormone resistance syndrome.
(12 Dec 1998)
receptors, thyrotropin Cell surface proteins that bind thyrotropin and trigger intracellular changes influencing the behaviour of cells. These receptors are present in the nervous system and on cells in the thyroid gland. Autoantibodies to these receptors are implicated in graves', hashimoto's, and other thyroid diseases.
(12 Dec 1998)
receptors, thyrotropin-releasing hormone Cell surface receptors that bind thyrotropin releasing hormone (trh) with high affinity and trigger intracellular changes which influence the behaviour of cells. Activated trh receptors in the anterior pituitary stimulate the release of thyrotropin (thyroid stimulating hormone, tsh). Trh receptors on neurons mediate neurotransmission by trh.
(12 Dec 1998)
receptors, transferrin Membrane glycoproteins found in high concentrations on iron-utilizing cells. They specifically bind iron-bearing transferrin, are endocytosed with its ligand and then returned to the cell surface where transferrin without its iron is released.
(12 Dec 1998)
receptors, vasoactive intestinal peptide Cell surface proteins that bind vasoactive intestinal peptide (vip) with high affinity and trigger intracellular changes which influence the behaviour of cells.
(12 Dec 1998)
receptors, vasopressin Specific molecular sites or structures on or in cells that vasopressins react or to which they bind in order to modify the function of the cells. Two types of vasopressin receptor exist, the v1 receptor and the v2 receptor. The v1 receptor can be subdivided into v1a and v1b (formerly v3) receptors.
(12 Dec 1998)
receptors, very late antigen Members of the integrin family appearing late after T-cell activation. They are a family of proteins initially identified at the surface of stimulated T-cells, but now identified on a variety of cell types. At least six vla antigens have been identified as heterodimeric adhesion receptors consisting of a single common beta-subunit and different alpha-subunits.
(12 Dec 1998)
receptors, virus Specific molecular components of the cell capable of recognizing and interacting with a virus, and which, after binding it, are capable of generating some signal that initiates the chain of events leading to the biological response.
(12 Dec 1998)
receptors, vitronectin Alpha-v beta-3 integrins that bind vitronectin with high affinity and play a role in cell migration. They also bind fibrinogen, von willebrand factor, osteopontin, and thrombospondin. The highly homologous alpha-v beta-5 integrin also binds vitronectin, but mediates simple adhesion.
(12 Dec 1998)
cholinergic receptors Chemical sites in effector cells or at synapses through which acetylcholine exerts its action.
(05 Mar 2000)
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