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  • scatter factor
    »ê¶õ°è¼ö
  • stroma factor
    ¹öÆÀÁúÀÎÀÚ, °£ÁúÀÎÀÚ
  • sunprotective factor
    Àϱ¤º¸È£Áö¼ö
  • sebotropic factor
    Áö·çÃËÁøÀÎÀÚ
  • safety factor
    ¾ÈÀü°è¼ö
  • skin vascular permeability factor
    ÇǺÎÇ÷°üÅõ°úÀÎÀÚ
  • vascular endothelial growth factor
    Ç÷°ü³»ÇǼºÀåÀÎÀÚ
  • vascular permeability factor
    Ç÷°üÅõ°úÀÎÀÚ
  • virulence factor
    µ¶¼ºÀÎÀÚ, ¹ßº´ÀÎÀÚ
  • virus inhibitory factor
    ¹ÙÀÌ·¯½º¾ïÁ¦ÀÎÀÚ
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  • ¿µ¹®
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  • virus inhibitory factor
    ¹ÙÀÌ·¯½º¾ïÁ¦ÀÎÀÚ
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  • plasma thromboplastic factor
    Ç÷À寮·Òº¸ÇÃ¶ó½ºÆ¾ÀÎÀÚ.
  • plasma thromboplastin factor
    Ç÷À寮·Òº¸ÇÃ¶ó½ºÆ¾ÀÎÀÚ.
  • platelet activating factor
    Ç÷¼ÒÆÇ Ȱ¼º ÀÎÀÚ
  • platelet factor 4
    Ç÷¼ÒÆÇÀÎÀÚ(úìá³÷ùì×í­) 4
  • platelet factor 4=PF4
    Ç÷¼ÒÆÇÀÎÀÚ 4
  • platelet factor III
    Ç÷¼ÒÆÇÁ¦»ïÀÎÀÚ.
  • platelet-activating factor (PAF)
    Ç÷¼ÒÆÇ Ȱ¼ºÈ­ÀÎÀÚ
  • platelet-activating factor (paf)
    Ç÷¼ÒÆÇȰ¼ºÈ­ÀÎÀÚ(úìá³÷ùüÀàõûùì×í­)
  • platelet-derived growth factor
    Ç÷¼ÒÆÇÀ¯·¡ Áõ½ÄÀÎÀÚ
  • platelet-derived growth factor(PDGF)
    Ç÷¼ÒÆÇ À¯·¡ ¼ºÀå ÀÎÀÚ
  • platelet-derived growth factor(pdgf)
    ÆÇ-À¯µµ¼ºÀåÀÎÀÚ(úìá³÷ù-ë¯Óôà÷íþì×í­)
  • power factor
    Ãâ·Â·ü(õóæ³ëÒ), ¿ª·ü(æ³ëÒ).
  • predisposing factor
    ¼ÒÀμº ¿äÀÎ, ¼±Çà¿äÀÎ.
  • prognostic factor
    ¿¹ÈÄÀÎÀÚ
  • prolactin inhibiting factor
    ÇÁ·Ñ¶ôƾ(ºÐºñ)¾ïÁ¦ÀÎÀÚ.
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  • environmental factor
    ȯ°æÀÎÀÚ.
  • eosinophil chemotactic factor
    È£»ê±¸ È­ÇÐÁÖ¼ºÀÎÀÚ
  • eosinophil chemotactic factor =ECF
    È£»ê±¸ È­ÇÐÁÖ¼ºÀÎÀÚ.
  • eosinophilic chemotactic factor
    È£»ê±¸¼º È­ÇÐÁÖ¼ºÀÎÀÚ
  • epidermal growth factor
    Ç¥ÇǼºÀåÀÎÀÚ
  • epidermal growth factor
    Ç¥ÇǼºÀåÀÎÀÚ(øúù«à÷íþì×í­)
  • epidermal growth factor
    Ç¥ÇǼºÀå ÀÎÀÚ(¡­à÷íþ ì×í­)
  • epidermal growth factor (EGF)
    ÇǺÎÁõ½ÄÀÎÀÚ
  • epidermal growth factor = EGF
    Ç¥ÇÇ ¼ºÀå ÀÎÀÚ
  • epidermoid growth factor
    Ç¥ÇÇ¾ç ¼ºÀåÀÎÀÚ(¡­à÷íþì×í­)
  • erythrocyte maturation factor
    ÀûÇ÷±¸¼º¼÷ÀÎÀÚ(?ËÛËàËöËö).
  • erythrocyte maturation factor
    ÀûÇ÷±¸¼º¼÷ÀÎÀÚ(¡­à÷âÙì×í­).
  • essential growth factor
    ÇʼöÁõ½ÄÀÎÀÚ
  • excess factor
    °úÀ×ÀÎÀÚ(¡­ì×í­).
  • exposure calibration factor
    ÇÇÆøÃøÁ¤°è¼ö
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  • pyruvate oxidation factor
    ÆÄÀÌ·çºê»ê(ß«) »êÈ­ÀÎÀÚ(ß«ûùì×í­)
  • rat antispectacle eye factor
    Áã Ç׾ȱ¸ µ¹ÃâÁõ ÀÎÀÚ(ù÷äÑϹÔÍõóñøì×í­)
  • recruitment factor
    º¸ÃæÀÎÀÚ(ÜÍõöì×í­)
  • regulatory factor
    Á¶Àý ÀÎÀÚ(ðàï½ì×í­)
  • Reid factor
    ¶óÀ̵å ÀÎÀÚ(ì×í­)
  • relaxing factor
    ÀÌ¿Ï ÀÎÀÚ(ì¬èÐì×í­)
  • release factor
    À¯¸® ÀÎÀÚ(ë´×îì×í­)
  • resistance factor
    ÀúÇ× ÀÎÀÚ(ì×í­)
  • resistance-transfer factor
    ÀúÇ×ÀüÀÌ ÀÎÀÚ(ï®ì¹ì×í­)
  • R factor
    R ÀÎÀÚ(ì×í­)
  • Rhesus factor
    ·¹¼­½º ÀÎÀÚ(ì×í­)
  • rheumatoid factor
    ·ù¸¶ÅäÀ̵å ÀÎÀÚ
  • Rh factor
    Rh ÀÎÀÚ
  • rho factor
    rho ÀÎÀÚ
  • ribosome dissociating factor
    ¶óÀ̺¸¼Ø ÇØ¸®ÀÎÀÚ(ú°×îì×í­)
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CGP N-carbobenzoxy-glycyl-L-phenylalanine; chorionic growth hormone-prolactin; choline glycerophosphatid...
GA Gamblers Anonymous; gastric analysis; gastric antrum; general anesthesia; general angiography; gener...
Ga gallium; granulocyte agglutination
GCP geriatric cancer population; granulocyte chemotactic protein
G/E granulocyte/erythroid [ratio]
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PR Progestin receptors
PRL-R Prolactin receptors
PAR Protease activated receptors
RACK Receptors for activated C kinase
SARs Slowly adapting pulmonary stretch receptors
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  • vascular endothelial growth factor
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  • vascular permeability factor
    Ç÷°ü Åõ°ú ÀÎÀÚ
  • Ven blood factor
    Ææ Ç÷¾× ÀÎÀÚ
  • virus inhibitory factor
    ¹ÙÀÌ·¯½º ¾ïÁ¦ ÀÎÀÚ
  • vitamin B12-intrinsic factor
    ºñŸ¹Î B12-³»Àμº ÀÎÀÚ
  • wall correction factor
    º®±³Á¤ °è¼ö
  • wedge factor
    ½û±â ÀÎÀÚ
  • weighting factor
    °¡Áß°è¼ö
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receptors, parathyroid hormone Cell surface proteins that bind parathyroid hormone with high affinity and trigger intracellular changes which influence the behaviour of cells. Parathyroid hormone receptors on bone, kidney, and gastrointestinal cells mediate the hormone's role in calcium and phosphate homeostasis.
(12 Dec 1998)
receptors, peptide Cell surface receptors that bind peptide messengers with high affinity and regulate intracellular signals which influence the behaviour of cells.
(12 Dec 1998)
receptors, phencyclidine Specific sites or molecular structures on cell membranes or in cells with which phencyclidine reacts or to which it binds to elicit the specific response of the cell to phencyclidine. Studies have demonstrated the presence of multiple receptor sites for pcp. These are the pcp/sigma site, which binds both pcp and psychotomimetic opiates but not certain antipsychotics, and the pcp site, which selectively binds pcp analogs.
(12 Dec 1998)
receptors, pituitary hormone Cell surface proteins that bind pituitary hormones with high affinity and trigger intracellular changes influencing the behaviour of cells. Since many pituitary hormones are also released by neurons as neurotransmitters, these receptors are also found in the nervous system.
(12 Dec 1998)
receptors, pituitary hormone-regulating hormone Cell surface receptors that bind the hypothalamic hormones regulating pituitary cell differentiation, proliferation, and hormone synthesis and release, including the pituitary-releasing and release-inhibiting hormones. The pituitary hormone-regulating hormones are also released by cells other than hypothalamic neurons, and their receptors also occur on non-pituitary cells, especially brain neurons, where their role is less well understood. Receptors for dopamine, which is a prolactin release-inhibiting hormone as well as a common neurotransmitter, are not included here.
(12 Dec 1998)
receptors, polymeric immunoglobulin Specialised fc receptors (receptors, fc) for polymeric immunoglobulins, which mediate transcytosis of polymeric IgA and IgM into external secretions. They are found on the surfaces of epithelial cells and hepatocytes. After binding to IgA, the receptor-ligand complex undergoes endocytosis, transport by vesicle, and secretion into the lumen by exocytosis. Before release, the part of the receptor (secretory component) that is bound to IgA is proteolytically cleaved from its transmembrane tail.
(12 Dec 1998)
receptors, presynaptic Neurotransmitter receptors located on or near presynaptic terminals or varicosities. Presynaptic receptors which bind transmitter molecules released by the terminal itself are termed autoreceptors.
(12 Dec 1998)
receptors, progesterone Specific proteins found in or on cells of progesterone target tissues that specifically combine with progesterone. The cytosol progesterone-receptor complex then associates with the nucleic acids to initiate protein synthesis. There are two kinds of progesterone receptors, a and b. Both are induced by oestrogen and have short half-lives.
(12 Dec 1998)
receptors, prolactin Labile proteins on or in prolactin-sensitive cells that bind prolactin initiating the cells' physiological response to that hormone. Mammary casein synthesis is one of the responses. The receptors are also found in placenta, liver, testes, kidneys, ovaries, and other organs and bind and respond to certain other hormones and their analogs and antagonists. This receptor is related to the growth hormone receptor.
(12 Dec 1998)
receptors, prostaglandin Cell surface receptors that bind prostaglandins with high affinity and trigger intracellular changes which influence the behaviour of cells. Prostaglandin receptor subtypes have been tentatively named according to their relative affinities for the endogenous prostaglandins. They include those which prefer prostaglandin d2 (dp receptors), prostaglandin e2 (ep1, ep2, and ep3 receptors), prostaglandin f2-alpha (fp receptors), and prostacyclin (ip receptors).
(12 Dec 1998)
receptors, prostaglandin e Cell surface receptors which bind prostaglandins with a high affinity and trigger intracellular changes which influence the behaviour of cells. Prostaglandin e receptors prefer prostaglandin e2 to other endogenous prostaglandins. They are subdivided into ep1, ep2, and ep3 types based on their effects and their pharmacology.
(12 Dec 1998)
receptors, purinergic Cell surface proteins that bind purines with high affinity and trigger intracellular changes which influence the behaviour of cells. The best characterised classes of purinergic receptors in mammals are the p1 receptors, which prefer adenosine, and the p2 receptors, which prefer ATP or ADP.
(12 Dec 1998)
receptors, purinergic p1 A class of cell surface receptors that prefers adenosine to other endogenous purines. Purinergic p1 receptors are widespread in the body including the cardiovascular, respiratory, immune, and nervous systems. There are at least two pharmacologically distinguishable types (a1 and a2, or ri and ra). The methylxanthines, e.g., caffeine, bind to these receptors, but also have other unrelated effects.
(12 Dec 1998)
receptors, purinergic p2 A class of cell surface receptors for purines that prefer ATP or ADP over adenosine. P2 purinergic receptors are widespread in the periphery and in the central and peripheral nervous system. Subtypes have been proposed, usually designated p2 x, y, z, and t. P2x receptors may mediate fast synaptic transmission by ATP. The ADP-preferring p2t receptors in platelets stimulate aggregation.
(12 Dec 1998)
receptors, retinoic acid Proteins in the nucleus or cytoplasm that specifically bind retinoic acid or retinol and trigger changes in the behaviour of cells. Retinoic acid receptors, like steroid receptors, are ligand-activated transcription regulators. Several types have been recognised.
(12 Dec 1998)
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