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"early pregnancy factor"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
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  • ¿µ¹®
    ÇѱÛ
  • radiation weighting factor
    ¹æ»ç¼±°¡Áß°è¼ö
  • resistance factor
    ³»¼ºÀÎÀÚ, ÀúÇ×ÀÎÀÚ
  • resistance transfer factor
    ³»¼ºÀü´ÞÀÎÀÚ
  • reticuloendothelial depressant factor
    ±×¹°³»Çǰè¾ïÁ¦ÀÎÀÚ, ¸Á»ó³»Çǰè¾ïÁ¦ÀÎÀÚ
  • rheumatoid factor
    ·ù¸¶Æ¼½ºÀÎÀÚ
  • risk factor
    À§ÇèÀÎÀÚ
  • roentgen-to-rad conversion factor
    ·ÛÆ®°Õ´ë·¡µåº¯È¯°è¼ö
  • somatotropin release inhibiting factor
    ¼ºÀåÈ£¸£¸óºÐºñ¾ïÁ¦ÀÎÀÚ
  • spreading factor
    È®»êÀÎÀÚ
  • stable factor
    ¾ÈÁ¤ÀÎÀÚ
  • scatter factor
    »ê¶õ°è¼ö
  • stroma factor
    ¹öÆÀÁúÀÎÀÚ, °£ÁúÀÎÀÚ
  • sunprotective factor
    Àϱ¤º¸È£Áö¼ö
  • sebotropic factor
    Áö·çÃËÁøÀÎÀÚ
  • safety factor
    ¾ÈÀü°è¼ö
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  • ¿µ¹®
    ÇѱÛ
  • time-dose factor
    ½Ã°£¼±·®ÀÎÀÚ
  • tissue factor
    Á¶Á÷ÀÎÀÚ
  • transfer factor
    Àü´ÞÀÎÀÚ
  • transforming growth factor
    Àüȯ¼ºÀåÀÎÀÚ
  • transmission factor
    Åõ°ú°è¼ö
  • tumor angiogenesis factor
    Á¾¾çÇ÷°üÇü¼ºÀÎÀÚ
  • tumor necrosis factor
    Á¾¾ç±«»çÀÎÀÚ
  • 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®
    ÇѱÛ
  • reducing factor
    ȯ¿øÀÎÀÚ.
  • relaxing factor
    ÀÌ¿ÏÀÎÀÚ(ì¬èÐì×í­).
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  • ¿µ¹®
    ÇѱÛ
  • antistiffness factor
    Ç×°­Á÷ÀÎÀÚ(ù÷Ë­òÁ ì×í­).
  • asialo von Willebrand factor
    ¹«Å¸¾×Æùºô·¹ºê¶õµåÀÎÀÚ
  • atomic factor
    ¿øÀÚÀÎÀÚ(¡­ì×í­).
  • atrial natriuretic factor
    ½É¹æ¼º ³ªÆ®·ýÀÌ´¢ÀÎÀÚ
  • atrial natriuretic factor
    Atrial natriuretic factor
  • attenuation factor
    °¨¾à ¿ä¼Ò, °¨¼è ¿äÀÎ
  • autocrine motility factor
    Autocrine motility factor
  • back scatter factor
    ÈĹæ»ê¶õ°è¼ö
  • beam scattering factor
    ºö»ê¶õÀÎÀÚ
  • biotic factor
    »ý¹°ÀÎÀÚ(¡­ì×í­), »ýȰ¿ä¼Ò(ßæüÀé©áÈ).
  • biotic factor
    »ý¹°ÀÎÀÚ(¡­ì×í­), »ýȰ¿ä¼Ò(ßæüÀé©áÈ).
  • blood factor
    Ç÷¾×ÀÎÀÚ(?ËöËö).
  • carcinogenic factor
    ¹ß¾ÏÀÎÀÚ(ËÑËâËöËö).
  • cavaliere blood factor
    Ä«¹ß¸®¿¡ Ç÷¾×ÀÎÀÚ.
  • cavity-gas calibration factor
    °­-±âü ±³Á¤°è¼ö, ºó±¸¸Û-
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    ÇѱÛ
  • somatotropin factor
    ¼Ò¸¶Å䯮·ÎÇÉ ÀÎÀÚ(ì×í­)
  • specificity factor
    ƯÀ̼º ÀÎÀÚ(÷åì¶àõì×í­)
  • spreading factor
    ÆÛÁü ÀÎÀÚ(ì×í­)
  • stable factor
    ¾ÈÁ¤ÀÎÀÚ(äÌïÒì×í­)
  • steric factor
    ÀÔü ÀÎÀÚ(Ø¡ô÷ì×í­)
  • stringent factor
    ¾ö°Ý ÀÎÀÚ (åñÌ«ì×í­)
  • Stuart factor
    ½ºÆ©¾Æ¸£Æ® ÀÎÀÚ(ì×í­)
  • sulfation factor
    Ȳ»êÈ­ ÀÎÀÚ (üÜß«ûùì×í­)
  • surface factor
    Ç¥¸éÀÎÀÚ (øúØüì×í­)
  • T cell growth factor
    T ¼¼Æ÷¼ºÀåÀÎÀÚ (á¬øàà÷íþì×í­)
  • termination factor
    Á¾·áÀÎÀÚ (ðûÖõì×í­)
  • T factor
    T ÀÎÀÚ (ì×í­)
  • third factor
    Á¦»ïÀÎÀÚ (ð¯ß²ì×í­)
  • three-factor cross
    »ïÀÎÀÚ ±³Â÷ (ß²ì×í­Îßó©)
  • thymic humoral factor
    Èä¼± ü¾×ÀÎÀÚ (ýØàÊô÷äûì×í­)
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EMU early morning urine; energy-mode ultrasound
EMVC early mitral valve closure
END early neonatal death; endocrinology; endorphin; endothelin
EOCA early onset cerebellar ataxia
EOGBS early onset group B streptococcal [infection]
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IEG Immediate Early Gene
IE Immediate early
ICER Inducible cAMP early repressor
MIE Major Immediate Early
PEBV Pea early browning virus
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    ÇѱÛ
    ¼³¸í
  • 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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vascular endothelial growth factor A growth factor that is responsible for the growth of blood vessels.
(12 Dec 1998)
mammotropic factor <protein> Pituitary lactogenic hormone (23 kD) Synthesised on endoplasmic reticulum bound ribosomes as preprolactin that has an N terminal signal peptide that is cleaved from the mature form. The conversion of preprolactin to prolactin has been much used as an assay for membrane insertion.
(18 Nov 1997)
receptors, atrial natriuretic factor Cell surface proteins that bind atrial natriuretic factor with high affinity and trigger intracellular changes influencing the behaviour of cells.
(12 Dec 1998)
receptors, colony-stimulating factor Cell surface receptors for colony-stimulating factors, local mediators, and hormones that regulate the survival, proliferation, and differentiation of haemopoietic cells.
(12 Dec 1998)
receptors, epidermal growth factor-urogastrone Glycoproteins of about 170 kD that have protein kinase activity and span the plasma membranes of growing cells, including tumours. They are activated by the binding of epidermal growth factor-urogastrone which then initiates DNA and protein synthesis. They are not found on mitotically quiescent cells except in the stomach where they control the synthesis and release of digestive enzymes and gastric acid. Transforming growth factor alpha also binds to and activates these receptors.
(12 Dec 1998)
receptors, fibroblast growth factor Specific molecular sites or structures on cell membranes that react with fibroblast growth factors (both the basic and acidic forms), their analogs, or their antagonists to elicit or to inhibit the specific response of the cell to these factors. These receptors frequently possess tyrosine kinase activity.
(12 Dec 1998)
receptors, granulocyte-colony-stimulating factor Receptors that bind and internalise granulocyte-colony-stimulating factor. Their mw is believed to be 150 kD. These receptors are found mainly on a subset of myelomonocytic cells.
(12 Dec 1998)
receptors, granulocyte-macrophage colony-stimulating factor Receptors that bind and internalise the granulocyte-macrophage stimulating factor. Their mw is believed to be 84 kD. The most mature myelomonocytic cells, specifically human neutrophils, macrophages, and eosinophils, express the highest number of affinity receptors for this growth factor.
(12 Dec 1998)
receptors, growth factor Cell surface receptors that bind growth or trophic factors with high affinity, triggering intracellular responses which influence the growth, differentiation, or survival of cells.
(12 Dec 1998)
receptors, insulin-like-growth factor I Specific proteins on or in cells to which insulin-like growth factor I (somatomedin c) binds and thereby modifies the function of the cells. These receptors contain transmembrane and cytosolic domains, bind igf-I preferentially, and have high-affinity sites for igf-II. The alpha-subunit has a mw of 130 kD and the beta subunit possesses tyrosine kinase activity.
(12 Dec 1998)
receptors, insulin-like-growth-factor II Specific proteins on or in cells to which insulin-like growth factor II and mannose-6-phosphate bind and thereby modify the function of the cells. These receptors have a mw of 250 kD and possess no tyrosine kinase activity.
(12 Dec 1998)
receptors, macrophage colony-stimulating factor Glycoproteins of mw 165 kD which are encoded by the c-fms proto-oncogene. The binding of csf-1 to its receptors activates an intrinsic tyrosine kinase activity resulting in autophosphorylation of the receptors on tyrosine, rapid receptor down-regulation, and phosphorylation of as yet unidentified physiologic substrates that initiate a mitogenic response.
(12 Dec 1998)
receptors, nerve growth factor Cell surface receptors that bind nerve growth factor (ngf) and trigger intracellular changes influencing the behaviour of cells. Nerve growth factor receptors mediate the effects of nerve growth factor on the survival and growth of neurons.
(12 Dec 1998)
receptors, platelet-derived growth factor Specific molecular sites or structures on cell membranes that react with platelet-derived growth factor, its analogs, or antagonists, to elicit or to inhibit the specific response of the cell to this factor. Pdgf binds with different affinities and specificities to two structurally related receptors, the alpha-receptor and the beta-receptor. Both of these receptors are transmembrane proteins with an intracellular, ligand-stimulatable protein kinase domain.
(12 Dec 1998)
receptors, transforming growth factor beta Cell-surface proteins that bind transforming growth factor beta and trigger changes influencing the behaviour of cells. Two types of transforming growth factor receptors have been recognised. They differ in affinity for different members of the transforming growth factor beta family and in cellular mechanisms of action. Transforming growth factor alpha binds to the same receptors as epidermal growth factor (see receptors, epidermal growth factor-urogastrone).
(12 Dec 1998)
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