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"erythrocyte maturation 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
  • factor VII
    Á¦7ÀÎÀÚ
  • factor VIII
    Á¦8ÀÎÀÚ
  • factor X
    Á¦10ÀÎÀÚ
  • factor XI
    Á¦11ÀÎÀÚ
  • factor XII
    Á¦12ÀÎÀÚ
  • factor XIII
    Á¦13ÀÎÀÚ
  • granulocyte colony-stimulating factor
    °ú¸³±¸Áý¶ôÀÚ±ØÀÎÀÚ
  • granulocyte-macrophage colony-stimulating factor
    °ú¸³±¸Å«Æ÷½Ä¼¼Æ÷Áý¶ôÀÚ±ØÀÎÀÚ, °ú¸³±¸´ë½Ä±¸Áý¶ôÀÚ±ØÀÎÀÚ
  • growth factor
    ¼ºÀåÀÎÀÚ
  • hyperglycemic-glycogenolytic factor
    °íÇ÷´ç±Û¸®ÄÚ°ÕºÐÇØÀÎÀÚ
  • hematopoietic growth factor
    Ç÷¾×Çü¼º¼ºÀåÀÎÀÚ, Á¶Ç÷¼ºÀåÀÎÀÚ
  • histamine sensitizing factor
    È÷½ºÅ¸¹Î¹Î°¨ÀÎÀÚ
  • host integration factor
    ¼÷ÁÖÅëÇÕÀÎÀÚ
  • human antihemophilic factor
    »ç¶÷Ç×Ç÷¿ìº´ÀÎÀÚ
  • intrinsic factor
    ³»ÀÎÀÎÀÚ, ³»ÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • fibrin stabilizing factor
    ¼¶À¯¼Ò¾ÈÁ¤ÀÎÀÚ
  • fibroblast growth factor
    ¼¶À¯¸ð¼¼Æ÷¼ºÀåÀÎÀÚ
  • granulocyte colony-stimulating factor
    °ú¸³±¸Áý¶ôÀÚ±ØÀÎÀÚ
  • granulocyte-macrophage colony-stimulating factor
    °ú¸³±¸Å«Æ÷½Ä¼¼Æ÷Áý¶ôÀÚ±ØÀÎÀÚ
  • growth factor
    ¼ºÀåÀÎÀÚ
  • hematopoietic growth factor
    Ç÷¾×Çü¼º¼ºÀåÀÎÀÚ, Á¶Ç÷¼ºÀåÀÎÀÚ
  • histamine sensitizing factor
    È÷½ºÅ¸¹Î¹Î°¨ÀÎÀÚ
  • host integration factor
    ¼÷ÁÖÅëÇÕÀÎÀÚ
  • hyperglycemic-glycogenolytic factor
    °íÇ÷´ç±Û¸®ÄÚ°ÕºÐÇØÀÎÀÚ
  • insulin-like growth factor
    Àν¶¸°À¯»ç¼ºÀåÀÎÀÚ
  • intrinsic factor
    ³»ÀÎÀÎÀÚ, ³»ÀÎÀÚ
  • ketogenic factor
    ÄÉÅæÇü¼ºÀÎÀÚ
  • labile factor
    ºÒ¾ÈÁ¤ÀÎÀÚ, ºÒ¾ÈÁ¤¿ä¼Ò
  • lactogenic factor
    Á¥ÃËÁøÀÎÀÚ
  • leukocyte inhibitory factor
    ¹éÇ÷±¸¾ïÁ¦ÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • alveolar dilution factor
    ÆóÆ÷Èñ¼®ÀÎÀÚ(¡­ýüà·ì×í­).
  • amplification factor
    ÁõÆøÀÎÀÚ
  • anisotropy factor
    ºñµî¹æ¼º°è¼ö
  • antigen, colonization factor
    Áý¶ôÇü¼ºÀÎÀÚÇ׿ø, ¼¼Æ÷±ºÇü¼ºÀÎÀÚÇ׿ø
  • antihemophilic A factor =AHA
    Ç×Ç÷¿ìº´ AÀÎÀÚ(?ËöËö).
  • antihemophilic factor =AHF
    Ç×Ç÷¿ìº´ÀÎÀÚ(¡­ì×í­)
  • antihemophilic factor =AHF
    Ç×Ç÷¿ìº´ÀÎÀÚ(?ËöËö).
  • 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.
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  • ¿µ¹®
    ÇѱÛ
  • intravascular erythrocyte aggregation =IEA
    Ç÷°ü³»ÀûÇ÷±¸ÀÀÁý(?ËøÌ´Ë´Ëô̤).
  • medial erythrocyte diameter =MED
    ÀûÇ÷±¸Á¤Áß°æ(îåúìϹïáñéÌÓ).
  • medial erythrocyte diameter =MED
    ÀûÇ÷±¸Á¤Áß°æ(ËøÌ´Ë´ËøÌ¡Ë­).
  • median erythrocyte diameter =MED
    ÀûÇ÷±¸Á¤Áß°æ(îåúìϹïáñéÌÓ).
  • median erythrocyte diameter =MED
    ÀûÇ÷±¸Á¤Áß°æ(ËøÌ´Ë´ËøÌ¡Ë­).
  • non-nucleated erythrocyte
    ¹«ÇÙ(Ùíú·)ÀûÇ÷±¸
  • normochromic erythrocyte
    Á¤¿°¼º(ïáæøàõ) ÀûÇ÷±¸
  • nucleated erythrocyte
    À¯ÇÙÀûÇ÷±¸
  • nucleated erythrocyte
    À¯ÇÙÀûÇ÷±¸(¡­îåúìϹ)
  • orthochromatic erythrocyte
    Á¤¿°¼º ÀûÇ÷±¸(?ËøÌ´Ë´).
  • orthochromatic erythrocyte
    Á¤¿°¼º ÀûÇ÷±¸(¡­îåúìϹ).
  • plasma membrane of erythrocyte
    ÀûÇ÷±¸ÇüÁú¸·
  • polychromatic erythrocyte
    ´Ù¿°¼ºÀûÇ÷±¸
  • polychromatophilic erythrocyte
    ¹µ»öµëÀûÇ÷±¸
  • sensitized erythrocyte agglutination test
    °¨ÀÛÀûÇ÷±¸ÀÀÁý½ÃÇè(ÊïíÂîåúìϹ ëêó¢ãËúÐ).
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  • ¿µ¹®
    ÇѱÛ
  • factor IF
    ÀÎÀÚ(ì×í­) IF
  • factor R
    ÀÎÀÚ(ì×í­) R
  • factor T
    ÀÎÀÚ(ì×í­) T
  • factor theory
    ÀÎÀÚ ÀÌ·Ð(ì×í­×âÖå)
  • factor X
    ÀÎÀÚ(ì×í­) X
  • factor Y
    ÀÎÀÚ(ì×í­) Y
  • fertility factor
    ¼öÁ¤ ÀÎÀÚ (áôïñì×í­)
  • F factor
    F ÀÎÀÚ(ì×í­)
  • F' factor
    F' ÀÎÀÚ(ì×í­)
  • fibrin-stabilizing factor
    ¼¶À¯¼Ò ¾ÈÁ¤È­ÀÎÀÚ(àéë«áÈäÌïÒûùì×í­)
  • Fitzgerald factor
    ÇÍÁ¦¶öµå ÀÎÀÚ(ì×í­)
  • g factor
    g ÀÎÀÚ(ì×í­)
  • G factor
    G ÀÎÀÚ(ì×í­)
  • glucose tolerance factor
    ±Û·çÄÚ½º ³»¼º ÀÎÀÚ(Ò±àõì×í­)
  • growth factor
    ¼ºÀåÀÎÀÚ (à÷íþì×í­)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 6
M4 myelocyte at the 4th stage of maturation
M6 band form in the 6th stage of myelocyte maturation
MAP malignant atrophic papulosis; mandibular angle plane; maturation-activated protein; maximal aerobic ...
MI first meiotic metaphase; maturation index; medical illustrator; medical informatics; medical inspect...
MICAM maturation index for colostrum and mature milk
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 6
ERFC erythrocyte Rosette-forming cells
E-GR erythrocyte glutathione reductase
EGR-AC erythrocyte glutathione reductase activity coefficient
MNE micronucleated erythrocyte
D factor Differentiation-stimulating factor
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • endogenous factor
    ³»Àμº ¿ä¼Ò
  • endothelium-derived relaxing factor
    ³»ÇÇ ¼¼Æ÷¼º ÀÌ¿Ï ÀÎÀÚ
  • endurance factor
    Áö¼Ó ÀÎÀÚ
  • environmental chemotactic factor
    ȯ°æ¼º È­ÇÐ ÁÖ¼º ÀÎÀÚ
  • eosinophil chemotactic factor
    È£»ê±¸ È­ÇÐ ÁÖ¼º ÀÎÀÚ
  • excess factor
    °úÀ× ÀÎÀÚ
  • F factor
    ¿¡ÇÁ ÀÎÀÚ
    ´ëÀå±Õ¿¡¼­ ¿õ¼ºÀ» ºÎ¿©ÇÏ´Â ÀÛ¿ëÀ» °¡Áø ¿¡ÇǼؼº ÀÎÀÚ. ÀÌ ÀÎÀÚ°¡ ÀÖ´Â ¼¼±ÕÀ» F¶ó ÇÏ¸ç ¿õ¼ºÀ» ³ªÅ¸³»°í, À̰ÍÀÌ ¾ø´Â °ÍÀ» F¶ó°í ÇÏ¿© ÀÚ¼ºÀ» ³ªÅ¸³½´Ù. µÎ ¼¼Æ÷¸¦ È¥ÇÕ ¹è¾çÇϸé Á¢ÇÕÀÌ ÀϾ F ¼¼Æ÷ÀÇ F ÀÎÀÚ´Â F ¼¼Æ÷·Î µé¾î°¡ ÀÚ¼ºÀ» ¿õ¼ºÀ¸·Î ¹Ù²Û´Ù. F ÀÎÀÚ¿¡ ¼¼±Õ ¿°»öüÀÇ ÀϺκÐÀÌ ºÎÂøµÇ¾î ÀÖ´Â »óŸ¦ F'¶ó Çϰí, F ÀÎÀÚ°¡ ¼¼±Õ ¿°»öü ¼ÓÀ¸·Î µé¾î°£ »óÅÂÀÇ °ÍÀ» Hfr
  • factor
    ÀÎÀÚ
    °á°ú »êÃâ¿¡ ÇÊ¿äÇÑ ÀÛ¿ëÀ̳ª ¹°Áú. ¿¹ÄÁ´ë ÀÀ°í ÀÎÀÚ. º¸Åë ÀÛ¿ë ±âÀüÀ̳ª È­ÇÐÀû ¼ºÁúÀÌ ¾Ë·ÁÁ® ÀÖÁö ¾ÊÀº ¹°ÁúÀ» °¡¸£Å°´Âµ¥ ¾²ÀÌ´Â ¿ë¾î·Î ³»ºÐºñ ¿µ¿ª¿¡¼­´Â ±× ÀÎÀÚÀÇ È­ÇÐÀû ¼ºÁúÀÌ ±Ô¸íµÈ ÈÄ¿¡´Â 'È£¸£¸ó'À̶ó°í °³ÄªÇÑ´Ù.
  • factor deficiency
    ÀÎÀÚ °áÇÌ, Á¦ÀÎÀÚ °áÇÌÁõ
  • factor IX deficiency
    Á¦ 9ÀÎÀÚ °áÇÌÁõ, Á¦9ÀÎÀÚ °áÇÌ
  • factor macrophage migration inhibition
    ´ë½Ä ¼¼Æ÷ À¯ÁÖ ÀúÁö ÀÎÀÚ
  • factor VII deficiency
    Á¦ 7ÀÎÀÚ °áÇÌÁõ
  • factor VIII deficiency
    Á¦ 8ÀÎÀÚ °áÇÌ
  • factor XI deficiency
    Á¦11ÀÎÀÚ °áÇÌ
    ÀÌ ÀÎÀÚ°¡ ºÎÁ·µÇ¸é Ç÷¿ìº´ C³ª Rosenthal ÁõÈıºÀ¸·Î ºÒ¸®´Â Àü½Å¼º Ç÷¾× ÀÀ°í Àå¾Ö¸¦ ÀÏÀ¸Å°´Âµ¥ °íÀüÀû Ç÷¿ìº´°ú À¯»çÇÏ´Ù.
  • follicle stimulating hormone releasing factor
    ³­Æ÷ ÀÚ±Ø È£¸£¸ó ¹æÃâ ÀÎÀÚ
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 6
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)
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)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
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    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
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    ±¸ºÐ/º¸Çè±Þ¿©
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