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  • ¿µ¹®
    ÇѱÛ
  • virus inhibitory factor
    ¹ÙÀÌ·¯½º¾ïÁ¦ÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • 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-
  • 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.
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  • 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)
  • thymidine factor
    ŸÀ̵̹ò ÀÎÀÚ (ì×í­)
  • thyrotropic hormone releasing factor
    °©»ó¼±ÀÚ±Ø(Ë£ßÒàÍí©Ð½) È£¸£¸ó À¯¸®ÀÎÀÚ(ë´×îì×í­)
  • time factor effect
    ½Ã°£ÀÎÀÚ È¿°ú (ãÁÊàì×í­üùÍý)
  • tissue factor
    Á¶Á÷ÀÎÀÚ (ðÚòÄì×í­)
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DRF Daily Rating Form; daily replacement factor; Deafness Research Foundation; dose reduction factor
EDF eosinophil differentiation factor; erythroid differentiation factor; extradural fluid
EIF erythrocyte initiation factor; eukaryotic initiation factor
FF degree of fineness of abrasive particles; fat-free; father factor; fecal frequency; fertility factor...
GF gastric fistula; gastric fluid; germ-free; glass factor; glomerular filtration; gluten-free; grandfa...
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LKM liver kidney microsomal
LM liver metastases
M.L.C. metastatic liver cancer
OLTX orthotopic liver transplant
RLE rat liver epithelial
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 12
macrophage colony-stimulating factor <growth factor> A glycoprotein growth factor that causes the committed cell line to proliferate and mature into macrophages.
A cytokine synthesised by mesenchymal cells that stimulates pluripotent stem cells of bone marrow into differentiating towards the production of monocytes (mononuclear phagocytes).
The compound stimulates the survival, proliferation, and differentiation of haematopoietic cells of the monocyte-macrophage series. It is a disulfide-bonded glycoprotein dimer with a mw of 70 kD and binds to a single class of high affinity receptor which is identical to the product of the c-fms proto-oncogene.
See: colony-stimulating factors.
Chemical name: Colony-stimulating factor 1
Acronym: M-CSF
(12 Dec 1998)
macrophage inhibition factor <cytokine> A group of lymphokines (including a 14 kD glycoprotein) produced by activated T lymphocytes that reduces macrophage mobility and probably increases macrophage macrophage adhesion.
(18 Nov 1997)
radiation weighting factor In radiation protection, a factor weighting the absorbed dose of radiation of a specific type and energy for its effect on tissue.
See: equivalent dose.
(05 Mar 2000)
maise factor <molecular biology, plant biology> A naturally occurring cytokinin, originally isolated from maize seeds. Its riboside is also a cytokinin.
(18 Nov 1997)
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)
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