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"Transforming Growth Factor beta1"¿¡ ´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
  • 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
  • skin vascular permeability factor
    ÇǺÎÇ÷°üÅõ°úÀÎÀÚ
  • vascular permeability factor
    Ç÷°üÅõ°úÀÎÀÚ
  • virulence factor
    µ¶¼ºÀÎÀÚ, ¹ßº´ÀÎÀÚ
  • virus inhibitory factor
    ¹ÙÀÌ·¯½º¾ïÁ¦ÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • tissue factor
    Á¶Á÷ÀÎÀÚ
  • transfer factor
    Àü´ÞÀÎÀÚ
  • transmission factor
    Åõ°ú°è¼ö
  • tumor angiogenesis factor
    Á¾¾çÇ÷°üÇü¼ºÀÎÀÚ
  • tumor necrosis factor
    Á¾¾ç±«»çÀÎÀÚ
  • vascular permeability factor
    Ç÷°üÅõ°úÀÎÀÚ
  • virulence factor
    µ¶¼ºÀÎÀÚ, ¹ßº´ÀÎÀÚ
  • virus inhibitory factor
    ¹ÙÀÌ·¯½º¾ïÁ¦ÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • 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)
  • 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.
  • prolactin inhibiting factor
    ÇÁ·Î¶ôƾ¾ïÁ¦ÀÎÀÚ
  • prolactin-inhibitory factor(PIF)
    ÇÁ·Î¶ôƾ ºÐºñ ¾ïÁ¦ ÀÎÀÚ
  • prolactin-releasing factor(PRF)
    ÇÁ·Î¶ôƾ ºÐºñ À¯¹ß ÀÎÀÚ
  • protein synthesis factor
    ´Ü¹éÇÕ¼ºÀÎÀÚ(Ó±ÛÜùêà÷ì×í­).
  • psychogenic factor
    ½ÉÀμº ¿ä¼Ò(¡­é©áÈ).
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  • ¿µ¹®
    ÇѱÛ
  • carcinogenic factor
    ¹ß¾ÏÀÎÀÚ(ËÑËâËöËö).
  • cavaliere blood factor
    Ä«¹ß¸®¿¡ Ç÷¾×ÀÎÀÚ.
  • cavity-gas calibration factor
    °­-±âü ±³Á¤°è¼ö, ºó±¸¸Û-
  • cell loss factor
    ¼¼Æ÷¼Ò½Ç°è¼ö
  • certainty factor
    È®½Ç¿äÀÎ
  • chamber calibration factor
    Àü¸®ÇÔ ÃøÁ¤°è¼ö, »óÀÚÃøÁ¤°è¼ö
  • chemotactic factor
    È­ÇÐÁÖ¼ºÀÎÀÚ(¡­ì×í­).
  • chemotactic factor
    (È­ÇÐ)ÁÖÈ­ÀÎÀÚ, È­ÇÐÁÖ¼ºÀÎÀÚ(¡­ì×í­).
  • chemotactic factor
    (È­ÇÐ)ÁÖÈ­ÀÎÀÚ, È­ÇÐÁÖ¼ºÀÎÀÚ(¡­ì×í­).
  • chemotactic factor
    (È­ÇÐ)ÁÖÈ­ÀÎÀÚ, È­ÇÐÁÖ¼ºÀÎÀÚ(¡­ì×í­)
  • cholestatic factor
    (Ãé)´äÁó¿ïüÀÎÀÚ.
  • circumstance factor
    »óȲÀÎÀÚ(íîüÏì×í­).
  • citrovorum factor
    ½ÃÆ®·Îº¸·ë <ÀÎÀÚ>
  • clotting factor
    ÀÀ°íÀÎÀÚ, ÀÀÇ÷ÀÎÀÚ(¡­ì×í­)
  • clotting factor
    ÀÀ°íÀÎÀÚ, ÀÀÇ÷ÀÎÀÚ(?ËöËö).
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  • ¿µ¹®
    ÇѱÛ
  • rho factor
    rho ÀÎÀÚ
  • ribosome dissociating factor
    ¶óÀ̺¸¼Ø ÇØ¸®ÀÎÀÚ(ú°×îì×í­)
  • separation factor
    ºÐ¸®ÀÎÀÚ(ÝÂ×îì×í­)
  • serum prothrombin converting factor
    Ç÷û(úìôè) ÇÁ·ÎÆ®·Òºó ÀüȯÀÎÀÚ(ï®üµì×í­)
  • serum sulfation factor
    Ç÷û À¯È²È­ÀÎÀÚ(úìôè×¼üÜûùì×í­)
  • serum thymic factor
    Ç÷û °©»ó¼±ÀÎÀÚ(úìôèË£ßÒàÍì×í­)
  • sex factor
    ¼ºÀÎÀÚ(àõì×í­)
  • shape factor
    ¸ð¾çÀÎÀÚ(Ù¼åÆì×í­)
  • sigma factor
    ½Ã±×¸¶ÀÎÀÚ(ì×í­)
  • SLR factor
    SLRÀÎÀÚ(ì×í­)
  • 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)
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FGF father's grandfather; fibroblast growth factor; fresh gas flow
FGFA fibroblast growth factor, acidic
FGFB fibroblast growth factor, basic
FGFR fibroblast growth factor receptor
GCF growth-rate-controlling factor
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EGF Epithelial growth factor
EDGF Eye Derived Growth Factor
FGF-2 Fibrobast growth factor-2
FGF-1 Fibroblast Growth Factor
FGF-2 Fibroblast Growth Factor
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 13
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, 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, 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, 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)
maturation-promoting factor <enzyme> A protein kinase that drives both the mitotic and meiotic cycles in all eukaryotic organisms.
In meiosis it induces immature oocytes to undergo meiotic maturation. In mitosis it has a role in the G2/M phase transition. Once activated by cyclins, maturation-promoting factor directly phosphorylates some of the proteins involved in nuclear envelope breakdown, chromosome condensation, spindle assembly, and the degradation of cyclins.
The catalytic subunit of maturation-promoting factor is protein p34cdc2.
Acronym: MPF
(12 Dec 1998)
reflection factor <microscopy> The ratio of reflected light from a surface to the incident light. This is sometimes called the coefficient of reflection. Unless especially stated it takes into account both specular and diffuse reflection.
(05 Aug 1998)
cattell personality factor questionnaire Self report questionnaire which yields 16 scores on personality traits, such as reserved vs. Outgoing, humble vs. Assertive, etc.
(12 Dec 1998)
glass factor <chemical> Stable blood coagulation factor activated by contact with the subendothelial surface of an injured vessel. Along with prekallikrein, it serves as the contact factor that initiates the intrinsic pathway of blood coagulation. Kallikrein activates factor xii to xiia. Deficiency of factor xii, also called the hageman trait, leads to increased incidence of thromboembolic disease.
Chemical name: Blood-coagulation factor XII
(12 Dec 1998)
relaxation factor Substance presumably involved in the return of muscle fibrils to the resting state after nervous stimulation ceases, postulated to act by withdrawing Calcium from myosin-ATPase sites.
(05 Mar 2000)
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