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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
  • reticuloendothelial depressant factor
    ¼¼¸Á³»Çǰè¾ïÁ¦ÀÎÀÚ, ±×¹°³»Çǰè¾ïÁ¦ÀÎÀÚ
  • rheumatoid factor
    ·ù¸¶Æ¼½ºÀ¯»çÀÎÀÚ
  • risk factor
    À§ÇèÀÎÀÚ
  • roentgen-to-rad conversion factor
    ·ÛÆ®°Õ¶óµåº¯È¯°è¼ö
  • safety factor
    ¾ÈÀü°è¼ö
  • scatter factor
    »ê¶õ°è¼ö
  • sebotropic factor
    Áö·çÃËÁøÀÎÀÚ
  • skin vascular permeability factor
    ÇǺÎÇ÷°üÅõ°úÀÎÀÚ
  • somatotropin release inhibiting factor
    ¼ºÀåÈ£¸£¸óÀ¯¸®¾ïÁ¦ÀÎÀÚ
  • spreading factor
    È®»êÀÎÀÚ
  • stable factor
    ¾ÈÁ¤ÀÎÀÚ
  • stroma factor
    ¹öÆÀÁúÀÎÀÚ
  • sunprotective factor
    Àϱ¤º¸È£Áö¼ö
  • testis-determining factor
    °íȯ°áÁ¤ÀÎÀÚ
  • therapeutic gain factor
    Ä¡·áÀ̵æ°è¼ö
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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
  • genetic factor
    À¯ÀüÀÎÀÚ
  • 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
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  • ¿µ¹®
    ÇѱÛ
  • antihemophllic factor
    Ç×Ç÷¿ìº´ÀÎÀÚ
  • antiinsulin factor
    Ç×Àν¶¸°ÀÎÀÚ.
  • antineuritic factor
    Ç׽Ű濰ÀÎÀÚ(ù÷ãêÌèæúì×í­).
  • antinuclear factor =ANF
    Ç×ÇÙÀÎÀÚ.
  • antipellagra factor
    Çׯç¶ó±×¶óÀÎÀÚ.
  • antiphagocytic factor
    Ç׎½ÄÀÎÀÚ, Ç׽ıÕÀÎÀÚ
  • antirachitic factor
    Ç×±¸·çº´ÀÎÀÚ(¡­ì×í­).
  • antiscorbutic factor
    Ç×±«Ç÷º´ÀÎÀÚ.
  • antisterility factor
    Ç׺ÒÀÓÀÎÀÚ(ù÷ÝÕìôì×í­).
  • 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
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  • ¿µ¹®
    ÇѱÛ
  • 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)
  • 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)
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MF magnetic field; meat free; medium frequency; megafarad; membrane filler; merthiolate-formaldehyde [s...
MSF macrophage slowing factor; macrophage spreading factor; Medicins sans Frontieres [Doctors without Bo...
PIF paratoid isoelectric focusing variant protein; peak inspiratory flow; proinsulin-free; prolactin-inh...
SPF skin protection factor; specific-pathogen free; spectrophotofluorometer; S-phase fraction; split pro...
TGF T-cell growth factor; transforming growth factor; tuboglomerular feedback; tumor growth factor
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2-DG 2-Deoxy-D-[3H]-glucose
2-DG 2-Deoxy-[14C]glucose
2-DOG 2-Deoxy-D-glucose
DOG 2-Deoxy-D-glucose
dGlc 2-Deoxy-D-glucose
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • somatic factor
    ü¼º ¿äÀÎ
  • spreading factor
    È®»ê ÀÎÀÚ
  • stem cell factor
    °£ ¼¼Æ÷ ¿ä¼Ò
  • systemic etiologic factor
    Àü½ÅÀû ¿øÀÎ ¿ä¼Ò
  • transfer factor
    Àü´Þ ÀÎÀÚ, ÀüÀÌ ¿äÀÎ
  • tumor necrosis factor
    Á¾¾ç ±«»ç ÀÎÀÚ
    TNF. Á¾¾ç¿¡ °ü°èÇϰí ÀÖ´Â ¸é¿ª°èÀÇ ¼¼Æ÷ÀÎ Á¾¾ç ħÀ±¼º ¸²ÇÁ±¸
  • tumor necrotizing factor
    Á¾¾ç ±«»ç ÀÎÀÚ
  • turbo factor
    Åͺ¸ ÀÎÀÚ
  • V-factor
    V-ÀÎÀÚ
    Ç캸Çʷ罺¼ÓÀÇ ±ÕÀÇ ÀÌ¿­¼º ÀÎÀÚ.
  • variable factor
    °¡º¯ ÀÎÀÚ
  • vascular endothelial growth factor
    ¸Æ°ü ³»ÇǼ¼Æ÷ ¼ºÀå ÀÎÀÚ, Ç÷°ü ³»ÇǼ¼Æ÷ ¼ºÀå ÀÎÀÚ
  • 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
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 11
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)
receptors, tumour necrosis factor Cell surface receptors that bind tumour necrosis factor and trigger changes which influence the behaviour of cells. The two recognised tumour necrosis factor receptors are designated alpha and beta receptors. Both receptors bind both alpha and beta tumour necrosis factors with high affinity, and both are members of the nerve growth factor receptor family.
(12 Dec 1998)
G factor The single common variance or factor that is common to (i.e., empirically intercorrelates with) different intelligence tests (general).
A substance required for the growth of a specific organism.
(05 Mar 2000)
Castle's intrinsic factor A mucoprotein normally secreted by the epithelium of the stomach and that binds vitamin B12, the intrinsic factor/B12 complex is selectively absorbed by the distal ileum, though only the vitamin is taken into the cell.
(18 Nov 1997)
maturation factor <biochemistry> Member of the water soluble B vitamin group, important in the proper function of the nervous system and important in proper carbohydrate, protein and fat metabolism.
(27 Sep 1997)
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    ±¸ºÐ/º¸Çè±Þ¿©
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