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  • ¿µ¹®
    ÇѱÛ
  • psychological factor
    ½É¸®¿äÀÎ
  • psychosocial factor
    ½É¸®»çȸ¿äÀÎ
  • phantom scatter factor
    ÆÒÅÒ»ê¶õ°è¼ö
  • quality factor
    1. Áú¿ä¼Ò 2. Á¤¼ºÀÎÀÚ
  • racial factor
    ÀÎÁ¾¿äÀÎ
  • realization factor
    ½ÇÇöÀÎÀÚ
  • recruitment factor
    µ¿¿øÀÎÀÚ
  • reducing factor
    ȯ¿øÀÎÀÚ
  • reinforcing factor
    °­È­¿äÀÎ
  • relaxing factor
    ÀÌ¿ÏÀÎÀÚ
  • 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
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  • ¿µ¹®
    ÇѱÛ
  • 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
  • thyrotrophin releasing factor
    ¹æÆÐ»ùÀÚ±ØÈ£¸£¸óÀ¯¸®ÀÎÀÚ, °©»ó»ùÀÚ±ØÈ£¸£¸óÀ¯¸®ÀÎÀÚ
  • time-dose factor
    ½Ã°£¼±·®ÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • 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
  • 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
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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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  • 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)
  • Reid factor
    ¶óÀ̵å ÀÎÀÚ(ì×í­)
  • relaxing factor
    ÀÌ¿Ï ÀÎÀÚ(ì¬èÐì×í­)
  • release factor
    À¯¸® ÀÎÀÚ(ë´×îì×í­)
  • resistance factor
    ÀúÇ× ÀÎÀÚ(ì×í­)
  • resistance-transfer factor
    ÀúÇ×ÀüÀÌ ÀÎÀÚ(ï®ì¹ì×í­)
  • R factor
    R ÀÎÀÚ(ì×í­)
  • Rhesus factor
    ·¹¼­½º ÀÎÀÚ(ì×í­)
  • rheumatoid factor
    ·ù¸¶ÅäÀ̵å ÀÎÀÚ
  • Rh factor
    Rh ÀÎÀÚ
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SPF skin protection factor; specific-pathogen free; spectrophotofluorometer; S-phase fraction; split pro...
CEF centrifugation extractable fluid; chick embryo fibroblast; constant electric field
CHEF Chinese hamster embryo fibroblast
CHF chick embryo fibroblast; chronic heart failure; congenital hepatic fibrosis; congestive heart failur...
FCFC fibroblast colony-forming cell
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RACK Receptors for activated C kinase
SARs Slowly adapting pulmonary stretch receptors
SAR Slowly adapting receptors
SR Steroid receptors
TR T(3) receptors
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • 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 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
  • wall correction factor
    º®±³Á¤ °è¼ö
  • wedge factor
    ½û±â ÀÎÀÚ
  • weighting factor
    °¡Áß°è¼ö
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receptors, cholinergic Cell surface proteins that bind acetylcholine with high affinity and trigger intracellular changes influencing the behaviour of cells. Cholinergic receptors are divided into two major classes, muscarinic and nicotinic, based originally on their affinity for nicotine and muscarine. Each group is further subdivided based on pharmacology, location, mode of action, and/or molecular biology.
(12 Dec 1998)
receptors, complement Molecules on the surface of some B-lymphocytes and macrophages, that recognise and combine with the c3b, c3d, c1q, and c4b components of complement.
(12 Dec 1998)
receptors, complement 3b Molecular sites on or in some B-lymphocytes and macrophages that recognise and combine with complement 3b. The primary structure of these receptors reveal that they contain transmembrane and cytoplasmic domains, with their extracellular portion composed entirely of thirty short consensus repeats each having 60 to 70 amino acids.
(12 Dec 1998)
receptors, complement 3d Molecular sites on or in B-lymphocytes, follicular dendritic cells, lymphoid cells, and epithelial cells that recognise and combine with complement 3d. Human cr2 serves as a receptor for both c3dg and the gp350/220 glycoprotein of herpes virus 4, human, and binds the monoclonal antibody okb7, which blocks binding of both ligands to the receptor.
(12 Dec 1998)
receptors, concanavalin a Glycoprotein moieties on the surfaces of cell membranes that bind concanavalin a selectively; the number and location of the sites depends on the type and condition of the cell.
(12 Dec 1998)
receptors, corticotropin Cell surface receptors that bind corticotropin (acth, adrenocorticotropic hormone) with high affinity and trigger intracellular changes. Pharmacology suggests there may be multiple acth receptors. An acth receptor has been cloned and belongs to a subfamily of g-protein-coupled receptors. In addition to the adrenal cortex, acth receptors are found in the brain and immune systems.
(12 Dec 1998)
receptors, corticotropin-releasing hormone Cell surface proteins that bind corticotropin-releasing hormone with high affinity and trigger intracellular changes which influence the behaviour of cells. The corticotropin releasing-hormone receptors on anterior pituitary cells mediate the stimulation of corticotropin release by hypothalamic corticotropin releasing factor. The physiological consequence of activating corticotropin-releasing hormone receptors on central neurons is not well understood.
(12 Dec 1998)
receptors, cxcr4 Seven-transmembrane G-protein-coupled receptors for alpha-chemokines. They also function as fusion cofactors for T-cell-tropic HIV-1 strains.
(12 Dec 1998)
receptors, cyclic AMP Cell surface proteins that bind cyclic AMP with high affinity and trigger intracellular changes which influence the behaviour of cells. The best characterised cyclic AMP receptors are those of the slime mold dictyostelium discoideum. The transcription regulator cyclic AMP receptor protein of prokaryotes is not included nor are the eukaryotic cytoplasmic cyclic AMP receptor proteins which are the regulatory subunits of cyclic AMP-dependent protein kinases.
(12 Dec 1998)
receptors, cytoadhesin A group of integrins that includes the platelet outer membrane glycoprotein gpiib-iiia (platelet glycoprotein gpiib-iiia complex) and the vitronectin receptor (receptors, vitronectin). They play a major role in cell adhesion and serve as receptors for fibronectin, von willebrand factor, and vitronectin.
(12 Dec 1998)
receptors, cytokine Cell surface proteins that bind cytokines and trigger intracellular changes influencing the behaviour of cells.
(12 Dec 1998)
receptors, cytoplasmic and nuclear Proteins in the cytoplasm or nucleus that specifically bind signalling molecules and trigger changes which influence the behaviour of cells. The major groups are the steroid hormone receptors, which usually are found in the cytoplasm, and the thyroid hormone receptors, which usually are found in the nucleus. Receptors, unlike enzymes, generally do not catalyze chemical changes in their ligands.
(12 Dec 1998)
receptors, dopamine Cell-surface proteins that bind dopamine with high affinity and trigger intracellular changes influencing the behaviour of cells.
(12 Dec 1998)
receptors, dopamine d1 A class of dopamine receptors identified by their binding profiles for synthetic ligands, their molecular biology, and, perhaps, by their mode of action.
(12 Dec 1998)
receptors, dopamine d2 A class of dopamine receptors identified by their binding profiles for synthetic ligands, their molecular biology, and, perhaps, their mode of action.
(12 Dec 1998)
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