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"time factor effect"¿¡ ´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
  • ketogenic factor
    ÄÉÅæ»ý¼ºÀÎÀÚ
  • labile factor
    1. ºÒ¾ÈÁ¤ÀÎÀÚ 2. ºÒ¾ÈÁ¤¿ä¼Ò
  • leukocyte inhibitory factor
    ¹éÇ÷±¸¾ïÁ¦ÀÎÀÚ
  • leukotaxic factor
    ¹éÇ÷±¸½ò¸²ÀÎÀÚ
  • luteinizing hormone releasing factor
    Ȳ(»ö)üÇü¼ºÈ£¸£¸óºÐºñÀÎÀÚ
  • luteotrophic hormone inhibitory factor
    Ȳ(»ö)üÀÚ±ØÈ£¸£¸ó¾ïÁ¦ÀÎÀÚ
  • lymphocyte activating factor
    ¸²ÇÁ±¸È°¼ºÀÎÀÚ
  • lymphocyte inhibitory factor
    ¸²ÇÁ±¸¾ïÁ¦ÀÎÀÚ
  • lactogenic factor
    Á¥ÃËÁøÀÎÀÚ
  • lymphocytosis stimulating factor
    ¸²ÇÁ±¸Áõ°¡ÀÚ±ØÀÎÀÚ
  • migration inhibition factor
    À̵¿ÀúÁöÀÎÀÚ
  • mitogenic factor
    ºÐ¿­ÃËÁøÀÎÀÚ
  • myocardial depressant factor
    ½É(Àå)±Ù(À°)¾ïÁ¦ÀÎÀÚ
  • macrophage aggregating factor
    Å«Æ÷½Ä¼¼Æ÷ÀÀÁýÀÎÀÚ, ´ë½Ä¼¼Æ÷ÀÀÁýÀÎÀÚ
  • macrophage arming factor
    Å«Æ÷½Ä¼¼Æ÷¹«ÀåÀÎÀÚ, ´ë½Ä¼¼Æ÷¹«ÀåÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • conglutinogen activating factor
    ±³Âø¿øÈ°¼ºÀÎÀÚ
  • conversion factor
    º¯È¯ÀÎÀÚ, º¯È¯°è¼ö
  • corticotropin releasing factor
    ºÎ½Å°ÑÁúÀÚ±ØÈ£¸£¸ó¹æÃâÀÎÀÚ
  • decay accelerating factor
    ºØ±«ÃËÁøÀÎÀÚ
  • dermonecrotic factor
    ÇǺα«»çÀÎÀÚ
  • diabetogenic factor
    ´ç´¢À¯¹ßÀÎÀÚ
  • dilution factor
    ¹±ÈûÀÎÀÚ, Èñ¼®ÀÎÀÚ
  • drug resistance factor
    ¾àÁ¦ÀúÇ×ÀÎÀÚ
  • elongation factor
    ´ÃÀÓÀÎÀÚ, ¿¬ÀåÀÎÀÚ
  • endothelium-derived contracting factor
    ³»ÇǼ¼Æ÷¼öÃàÀÎÀÚ
  • endothelium-derived relaxing factor
    ³»ÇǼ¼Æ÷ÀÌ¿ÏÀÎÀÚ
  • endurance factor
    Áö¼ÓÀÎÀÚ
  • eosinophil chemotactic factor
    È£»ê±¸È­ÇÐÁÖ¼ºÀÎÀÚ, È£»ê±¸È­Çнò¸²ÀÎÀÚ
  • epidermal growth factor
    Ç¥ÇǼºÀåÀÎÀÚ
  • exogenous factor
    ¿ÜÀοä¼Ò
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  • ¿µ¹®
    ÇѱÛ
  • genetic factor
    À¯ÀüÀÎÀÚ(¡­ì×í­).
  • genetic factor
    À¯ÀüÀÎÀÚ.
  • granulocyte colony-stimulating factor
    °ú¸³±¸Áý¶ôÀÚ±ØÀÎÀÚ
  • granulocyte colony-stimulating factor=G-CSF
    °ú¸³±¸Áý¶ôÀÚ±ØÀÎÀÚ
  • granulocyte-macrophage coloneystimulating factor(gm-csf)
    °ú¸³±¸-´ë½Ä±¸ Áý¶ô ÀÚ±ØÀÎÀÚ
  • granulocyte-macrophage colony- stimulating factor
    °ú¸³±¸´ë½Ä¼¼Æ÷Áý¶ôÀÚ±ØÀÎÀÚ
  • granulocyte-macrophage colony-stimulating factor=GM-CSF
    °ú¸³±¸-´ë½Ä¼¼Æ÷Áý¶ôÀÚ±ØÀÎÀÚ
  • growth factor
    ¼ºÀå ÀÎÀÚ
  • growth factor
    ¼ºÀåÀÎÀÚ(à÷íþì×í­).
  • growth factor
    Áõ½ÄÀÎÀÚ
  • growth factor
    ¼ºÀå ÀÎÀÚ(à÷íþ ì×í­)
  • growth factor, B cell (BCGF)
    B¼¼Æ÷ Áõ½ÄÃËÁøÀÎÀÚ
  • growth hormone-releasing factor
    ¼ºÀåÈ£¸£¸óÀ¯¸®ÀÎÀÚ<--¹æÃâÀÎÀÚ>
  • growth promoting factor
    ¼ºÀåÃËÁøÀÎÀÚ(à÷íþõµòäì×í­), ¹ßÀ°ÃËÁø¹°Áú(Û¡ëÀõµòäÚªòõ)
  • hageman factor
    ÇϰԸ¸ ÀÎÀÚ, Hageman ÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • clotting time of whole blood
    ÀüÇ÷ÀÀ°í½Ã°£(îïúìëêͳãÁÊà)
  • clotting time of whole blood
    [³»°ú,ÀÓº´]ÀüÇ÷ÀÀÇ÷½Ã°£(îïúìëêúìãÁÊà).
  • clotting time of whole blood
    [³»°ú,ÀÓº´]ÀüÇ÷ÀÀÇ÷½Ã°£(ËøÌ´ËôÌ´Ëà˧).
  • coagulation time
    ÀÀ°í½Ã°£(¡­ãÁÊà) ¡ìÇ÷¾×ÀÇ¡í.
  • corrected sinus node recovery time
    ±³Á¤ µ¿°áÀý ȸº¹½Ã°£.
  • correlation time
    »ó°ü ½Ã°£
  • data acquisition time
    ÀÚ·á ȹµæ ½Ã°£
  • death time, thermal
    ¿­»ç¸ê½Ã°£
  • delay time
    Áö¿¬ ½Ã°£
  • dextrinizing time
    ÀüºÐÀüÈ­½Ã°£(îþÝÏï®ûùãÁÊà).
  • diastolic filling time
    È®Àå±âÃæ¸¸½Ã°£.
  • diffusion time
    È®»ê½Ã°£
  • disappearance time =DT
    ¹æ»ç ¼Ò½Ç½Ã°£.
  • dodging time
    ºÒ±ÔÄ¢Àû Åë°æ±â°£¡ì¿ÏÀü¿ù°æÆóÁö±îÁöÀÇ ºÎÁ¤±â¡í.
  • dose rate ; dosage rate ; dose per unit time
    ¹æ»ç ÀÓº´,ÇÙÀÇ,¾à¸®¼±·®·ü, ¿ë·®.
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  • ¿µ¹®
    ÇѱÛ
  • pellagra-preventaive factor
    Æç¶ó±×¶ó ¿¹¹æÀÎÀÚ(çãÛÁì×í­)
  • permeability factor
    Åõ°ú ÀÎÀÚ(÷âΦì×í­)
  • plasma factor
    Ç÷ÀåÀÎÀÚ(úìíìì×í­)
  • plasma thromboplastic factor
    Ç÷Àå Ç÷ÀüÇü¼ºÀÎÀÚ(úìíìúìîûû¡à÷ì×í­)
  • plasma thromboplastic factor B
    Ç÷Àå Ç÷ÀüÇü¼ºÀÎÀÚ B
  • platelet-activating factor
    Ç÷¼ÒÆÇȰ¼º ÀÎÀÚ(úìá³÷ùüÀàõì×í­)
  • platelet-derived growth factor
    Ç÷¼ÒÆÇÀ¯·¡(úìá³÷ùë¦ÕÎ) ¼ºÀåÀÎÀÚ(à÷íþì×í­)
  • PP factor
    PP ÀÎÀÚ(ì×í­)
  • preexponential factor
    Áö¼ö(ò¦â¦)¾ÕÀÚ¸® ÀÎÀÚ(ì×í­)
  • protein factor
    ´Ü¹éÁú ÀÎÀÚ(Ó±ÛÜòõì×í­)
  • protein release factor
    ´Ü¹éÁú ¹æÃâÀÎÀÚ(Ó±ÛÜòõÛ¯õóì×í­)
  • protein synthesis factor
    ´Ü¹éÁú ÇÕ¼ºÀÎÀÚ(Ó±ÛÜòõùêà÷ì×í­)
  • prothrombin factor
    ÇÁ·ÎÆ®·Òºó ÀÎÀÚ(ì×í­)
  • Prower factor
    ÇÁ¶ó¿ö ÀÎÀÚ(ì×í­)
  • psi factor
    »çÀÌ ÀÎÀÚ(ì×í­)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 15
ROESY rotating frame Overhauser effect spectroscopy
SDE specific dynamic effect; subdural empyema
SE saline enema; sanitary engineering; side effect; smoke exposure; solid extract; sphenoethmoidal; spi...
TEE thermic effect of exercise; total energy expenditure; transesophageal echocardiography; tyrosine eth...
TOE tender on examination; tracheoesophageal; transesophageal echography; transferred nuclear Overhauser...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 15
BUT Break-up Time
BHT Breath-holding time
t C)-time
CCT Central Conduction Time
CMCT Central Motor Conduction Time
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • Hageman factor
    ÇϰԸ¸ ÀÎÀÚ
    factor ?.
  • hormonal factor
    È£¸£¸ó ¿äÀÎ
  • hunter blood factor
    ÇåÅÍ Ç÷¾× ÀÎÀÚ
  • hypoglycemic producing factor
    ÀúÇ÷´çÁõ À¯¹ß ¿äÀÎ
  • hypophosphatemia-producing factor

    hypophosphatemic rickets (ÀúÀλê Ç÷¼º ±¸·çº´, ÀúÀλ꿰 Ç÷¼º ±¸·çº´

  • initiating factor
    À¯¹ß ¿äÀÎ
    ÁúȯÀ̳ª Àå¾ÖÀÇ ¹ßº´¿¡ ¿øÀÎÀÌ µÇ´Â ¿ä¼Òµé.
  • intrinsic factor antibody
    ³»Àμº ÀÎÀÚ Ç×ü
  • irritating factor
    ÀÚ±Ø ¿ä¼Ò
  • labile factor
    ºÒ¾ÈÁ¤ ÀÎÀÚ, ºÒ¾ÈÁ¤ ¿ä¼Ò
  • lactogenic factor
    ÃÖÀ¯ ÀÎÀÚ
  • latent factor
    ÀáÀçÀû ¿ä¼Ò
  • leucopenic factor
    ¹éÇ÷±¸ °¨¼Ò ÀÎÀÚ
  • leukotaxic factor
    ¹éÇ÷±¸ ÃßÈ­¼º ÀÎÀÚ
  • limiting factor
    ÇѰè ÀÎÀÚ, Á¦ÇÑ ÀÎÀÚ, ÇÑÁ¤ ÀÎÀÚ
  • local etiologic factor
    ±¹¼ÒÀû ¿øÀÎ ¿ä¼Ò
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 15
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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