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"Receptors, Granulocyte Colony-Stimulating 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
  • carcinogenic factor
    ¹ß¾ÏÀÎÀÚ
  • corticotropin-releasing factor
    ºÎ½Å°ÑÁúÀÚ±ØÈ£¸£¸ó¹æÃâÀÎÀÚ
  • chemotactic factor
    È­Çнò¸²ÀÎÀÚ
  • drug resistance factor
    ¾àÁ¦ÀúÇ×ÀÎÀÚ
  • dermonecrotic factor
    ÇǺα«»çÀÎÀÚ
  • diabetogenic factor
    ´ç´¢º´À¯¹ßÀÎÀÚ
  • decay accelerating factor
    ºØ±«ÃËÁøÀÎÀÚ
  • dilution factor
    Èñ¼®ÀÎÀÚ
  • exclusion of confounding factor
    ±³¶õ¹èÁ¦ÀÎÀÚ
  • exogenous factor
    ¿ÜÀοä¼Ò
  • extrinsic factor
    ¿ÜÀÎÀÎÀÚ, ¿ÜÀÎÀÚ
  • elongation factor
    ´ÃÀÓÀÎÀÚ, ¿¬ÀåÀÎÀÚ
  • endothelium-derived contracting factor
    ³»ÇÇÀ¯·¡¼öÃàÀÎÀÚ
  • endothelium-derived relaxing factor
    ³»ÇÇÀ¯·¡ÀÌ¿ÏÀÎÀÚ
  • endurance factor
    °ßµõÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • 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
  • extrinsic factor
    ¿ÜÀÎÀÎÀÚ, ¿ÜÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • Kappa receptors
    Ä«ÆÄ¼ö¿ëü(áôé»ô÷)
  • Left ventricular receptors
    Á½ɽǼö¿ëü(ñ§ãýãøáôé»ô÷)
  • M1 muscarinic receptors
    M1 ¹«½ºÄ«¸°¼º ¼ö¿ëü(áôé»ô÷)
  • presynaptic receptors
    ½Å°æÁ¢ÇÕÀü ¼ö¿ëü
  • AHF=£¾antihemophilic factor
    Ç×Ç÷¿ìÀÎÀÚ.
  • B cell differentiation factor (BCDF)
    B¼¼Æ÷ ºÐÈ­À¯¹ßÀÎÀÚ
  • B cell growth factor
    B ¼¼Æ÷¼ºÀåÀÎÀÚ
  • B cell growth factor (BCGF)
    B¼¼Æ÷ Áõ½ÄÃËÁøÀÎÀÚ
  • B cell stimulating factor (BSF)
    B¼¼Æ÷ ÀÚ±ØÀÎÀÚ
  • Castles extrinsic factor
    Ĺ½½¿ÜÀÎÀÚ.
  • Castles intrinsic factor
    Ĺ½½³»ÀÎÀÚ.
  • Christmas factor
    Å©¸®½º¸¶½º ÀÎÀÚ(ì×í­)
  • Christmas factor.
    Å©¸®½º¸¶½ºÀÎÀÚ
  • D factor
    DÀÎÀÚ
  • Decay accelerating factor
    ºØ±«°¡¼Ó¿ä¼Ò(¿äÀÎ)
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • time, dose and fractionation factor, TDF factor
    ½Ã°£¼±·®ºÐÇÒÀÎÀÚ
  • absorbed dose conversion factor
    Èí¼ö¼±·®º¯È¯°è¼ö
  • age factor
    ¿¬·ÉÀÎÀÚ.
  • air kerma calibration factor
    °ø±âÄ¿¸¶ÃøÁ¤°è¼ö, -´«±Ý¸ÂÃã°è¼ö
  • 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.
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  • ¿µ¹®
    ÇѱÛ
  • calcium-activated factor
    Ä®½·ºÎȰ ÀÎÀÚ(Ý·üÀì×í­)
  • cell factor
    ¼¼Æ÷ÀÎÀÚ(á¬øàì×í­)
  • chloroplast coupling factor
    ¿±·Ïü(ç¨Öàô÷) ¦ÁöÀ½ÀÎÀÚ(ì×í­)
  • Christmas factor
    Å©¸®½º¸¶½º ÀÎÀÚ(ì×í­)
  • citrovorum factor
    "½ÃÆ®·Îº¸·ë ÀÎÀÚ,"
  • clearance factor
    ûÁ¤ÀÎÀÚ(ôèïäì×í­)
  • clot-promoting factor
    ÀÀ±«ÃËÁøÀÎÀÚ(ëêÎÕõµòäì×í­)
  • Col factor
    Col ÀÎÀÚ(ì×í­)
  • colicin factor
    Äݸ®½Å ÀÎÀÚ(ì×í­)
  • colicinogenic factor
    Äݸ®½Å »ý¼ºÀÎÀÚ(ßæà÷ì×í­)
  • colony-stimulating factor
    ÄݷδÏÀÚ±Ø ÀÎÀÚ(í©Ð½ì×í­)
  • contact factor
    "Á¢ÃËÀÎÀÚ(ïÈõºì×í­), (ÔÒ) Hageman factor"
  • conversion factor
    ÀüȯÀÎÀÚ(ï®üµì×í­)
  • cord factor
    ÄÚµå ÀÎÀÚ(ì×í­)
  • coupling factor
    ¦Áþ±â ÀÎÀÚ(ì×í­)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 3
GRF gastrin-releasing factor; genetically related macrophage factor; gonadotropin-releasing factor; grow...
HSF heat shock factor; hepatocyte stimulatory factor; histamine sensitizing factor; human serum esterase...
LPF leukocytosis-promoting factor; leukopenia factor; lipopolysaccharide factor; localized plaque format...
MIF macrophage inhibitory factor; melanocyte[-stimulating hormone]-inhibiting factor; maximum inspirator...
MRF Markov random field; medical record file; melanocyte-[stimulating hormone]-releasing factor; mesence...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 3
GM-CSF Granulocyte macrophage colony stimulator factor
GM-CSF Granulocyte--Monocyte Colony Stimulating Factor
GM-CSFr Granulocyte-macrophage colony-stimulating factor receptor
hG-CSF Human granulocyte colony stimulating factor
hGM CSF Human granulocyte-macrophage colony stimulating factor
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • clumping factor
    ÀÀ±« ÀÎÀÚ
  • coagulase-reacting factor
    Ç÷Àå ÀÀ°í È¿¼Ò ¹ÝÀÀ ÀÎÀÚ
  • coagulation factor
    ÀÀÇ÷ ÀÎÀÚ, ÀÀ°í ÀÎÀÚ
  • coagulation factor inhibitor
    ÀÀ°í ÀÎÀÚ ¾ïÁ¦Á¦
  • colicin factor
    Äݸ®½Å ÀÎÀÚ
  • colony stimulating factor
    ±ºÃ¼ ÀÚ±Ø ¿ä¼Ò, Áý¶ô ÀÚ±Ø ÀÎÀÚ
    ¹ß´Þ ´Ü°èÀÇ Àü±¸Àû ¼¼Æ÷°¡ Áý¶ôÀ» Çü¼ºÇÏ´Â °úÁ¤¿¡´Â À̰ÍÀÇ ÀÛ¿ëÀÌ ÇÊ¿äÇÏ´Ù´Â °ÍÀÌ ÀνĵǾú´Ù. ÀÌ ÀÎÀÚ´Â ¼¶À¯¾Æ¼¼Æ÷, ³»ÇǼ¼Æ÷, ´ë½Ä¼¼Æ÷ µî¿¡¼­ »ý»êµÇ¸ç ¼º¼÷ÇÑ ¸é¿ª°è ¼¼Æ÷ÀÇ ÀÛ¿ë¿¡µµ ¿µÇâÀ» ³¢Ä£´Ù.
  • competence inducing factor
    Àû°Ý À¯¹ß ÀÎÀÚ
  • complementary factor
    º¸Ãæ ÀÎÀÚ
  • complicating factor
    º¹ÇÕ ¿äÀÎ
  • constitutional factor
    ±¸¼º ¿ä¼Ò, üÁú ¿äÀÎ
  • contributing factor
    ±â¿© ¿äÀÎ
    ÁúȯÀ̳ª Àå¾Ö¸¦ À¯¹ßÇϰųª ¾ÇÈ­Çϴµ¥ ±â¿©ÇÏ´Â »óųª Çൿ.
  • conversion factor
    º¯È¯ °è¼ö
  • cooperative factor
    Çùµ¿ ÀÎÀÚ
  • coronary risk factor
    °ü»ó µ¿¸Æ Áúȯ À§Çè ¿äÀÎ
  • cothromboplastin factor VII
    ÄÚÆ®·Ò º¸ÇÃ¶ó½ºÆ¾
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
receptors, adrenergic, beta-1 A subclass of beta-adrenergic receptors (receptors, adrenergic, beta). Beta-1 adrenergic receptors are equally sensitive to epinephrine and norepinephrine and bind the agonist dobutamine and the antagonist metoprolol with high affinity. They are found in the heart, juxtaglomerular cells, and in the central and peripheral nervous systems.
(12 Dec 1998)
receptors, adrenergic, beta-2 A subclass of beta-adrenergic receptors (receptors, adrenergic, beta). Beta-2 adrenergic receptors are more sensitive to epinephrine than to norepinephrine and have a high affinity for the agonist terbutaline. They are widespread, with clinically important roles in skeletal muscle, liver, and vascular, bronchial, gastrointestinal, and genitourinary smooth muscle.
(12 Dec 1998)
receptors, albumin Cell surface proteins that bind albumin with high affinity and trigger intracellular changes influencing the behaviour of cells.
(12 Dec 1998)
receptors, aldosterone Cytoplasmic proteins that specifically bind aldosterone and mediate its cellular effects. The aldosterone-bound receptor acts in the nucleus to regulate the transcription of specific segments of DNA.
(12 Dec 1998)
receptors, amino acid Cell surface proteins that bind amino acids and trigger changes which influence the behaviour of cells. Glutamate receptors are the most common receptors for fast excitatory synaptic transmission in the vertebrate central nervous system, and gaba and glycine receptors are the most common receptors for fast inhibition.
(12 Dec 1998)
receptors, ampa Cell surface proteins that bind glutamate and directly gate ion channels in cell membranes. Ampa receptors were originally discriminated from other glutamate receptors by their affinity for the agonist ampa (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid). They are probably the most common mediators of fast excitatory synaptic transmission in the central nervous system. Several subtypes have been cloned, and for some types the traditional distinction from kainate receptors may not apply.
(12 Dec 1998)
receptors, androgen Proteins, generally found in the cytoplasm, that specifically bind androgens and mediate their cellular actions. The complex of the androgen and receptor migrates to the nucleus where it induces transcription of specific segments of DNA.
(12 Dec 1998)
receptors, angiotensin Cell surface proteins that bind angiotensins and trigger intracellular changes influencing the behaviour of cells.
(12 Dec 1998)
receptors, antigen Molecules on the surface of b- and T-lymphocytes that recognise and combine with specific antigens.
(12 Dec 1998)
receptors, antigen, B-cell Immunoglobulin molecules on the surface of B-lymphocytes that recognise and bind antigen.
(12 Dec 1998)
receptors, antigen, T-cell Molecules on the surface of T-lymphocytes that recognise and combine with antigens. The receptors are non-covalently associated with a complex of several polypeptides collectively called CD3 antigens (antigens, CD3). Recognition of foreign antigen and the major histocompatibility complex is accomplished by a single heterodimeric antigen-receptor structure, composed of either alpha-beta (receptors, antigen, T-cell, alpha-beta) or gamma-delta (receptors, antigen, T-cell, gamma-delta) chains.
(12 Dec 1998)
receptors, antigen, T-cell, alpha-beta T-cell receptors composed of CD3-associated alpha and beta polypeptide chains and expressed primarily in CD4+ or CD8+ T-cells. Unlike immunoglobulins, the alpha-beta T-cell receptors recognise antigens only when presented in association with major histocompatibility (MHC) molecules.
(12 Dec 1998)
receptors, antigen, T-cell, gamma-delta T-cell receptors composed of CD3-associated gamma and delta polypeptide chains and expressed primarily in CD4-/CD8- T-cells. The receptors appear to be preferentially located in epithelial sites and probably play a role in the recognition of bacterial antigens. The T-cell receptor gamma/delta chains are separate and not related to the gamma and delta chains which are subunits of CD3 (see antigens, CD3).
(12 Dec 1998)
receptors, aryl hydrocarbon Cytoplasmic proteins that bind certain aryl hydrocarbons, translocate to the nucleus, and activate transcription of particular DNA segments. Ah receptors are identified by their high-affinity binding to several carcinogenic or teratogenic environmental chemicals including polycyclic aromatic hydrocarbons found in cigarette smoke and smog, heterocyclic amines found in cooked foods, and halogenated hydrocarbons including dioxins and polychlorinated biphenyls. No endogenous ligand has been identified, but an unknown natural messenger with a role in cell differentiation and development is suspected.
(12 Dec 1998)
receptors, biogenic amine Cell surface proteins that bind biogenic amines with high affinity and regulate intracellular signals which influence the behaviour of cells. Biogenic amine is a chemically imprecise term which, by convention, includes the catecholamines epinephrine, norepinephrine, and dopamine, the indoleamine serotonin, the imidazolamine histamine, and compounds closely related to each of these.
(12 Dec 1998)
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