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  • ¿µ¹®
    ÇѱÛ
  • plasma coagulation factor
    Ç÷ÀåÀÀ°íÀÎÀÚ
  • plasma thromboplastin factor
    Ç÷À寮·Òº¸ÇÃ¶ó½ºÆ¾ÀÎÀÚ
  • platelet activating factor
    Ç÷¼ÒÆÇȰ¼ºÀÎÀÚ
  • platelet factor 3
    Ç÷¼ÒÆÇÀÎÀÚ3
  • platelet factor 4
    Ç÷¼ÒÆÇÀÎÀÚ4
  • precipitation factor
    ħÀüÀÎÀÚ
  • predisposing factor
    ¼±Çà¿äÀÎ
  • prognostic factor
    ¿¹ÈÄÀÎÀÚ
  • prolactin inhibitory factor
    ÇÁ·Î¶ôƾºÐºñ¾ïÁ¦ÀÎÀÚ
  • prolactin releasing factor
    ÇÁ·Î¶ôƾºÐºñÀÎÀÚ
  • properdin factor B
    ÇÁ·ÎÆä¸£µòBÀÎÀÚ
  • properdin factor D
    ÇÁ·ÎÆä¸£µòDÀÎÀÚ
  • properdin factor E
    ÇÁ·ÎÆä¸£µòEÀÎÀÚ
  • protein synthesis factor
    ´Ü¹éÇÕ¼ºÀÎÀÚ
  • psychogenic factor
    Á¤½Å¼ºÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • psychogenic factor
    Á¤½Å¼º¿ä¼Ò
  • psychological factor
    ½É¸®¿ä¼Ò
  • psychosocial factor
    ½É¸®»çȸÀû¿äÀÎ
  • quality factor
    Áú¿ä¼Ò, Á¤¼ºÀÎÀÚ
  • racial factor
    ÀÎÁ¾¿äÀÎ
  • radiation weighting factor
    ¹æ»ç¼±°¡Áß°è¼ö
  • realization factor
    ½ÇÇöÀÎÀÚ
  • recruitment factor
    µ¿¿øÀÎÀÚ
  • reducing factor
    ȯ¿øÀÎÀÚ
  • reinforcing factor
    °­È­¿äÀÎ
  • relaxing factor
    ÀÌ¿ÏÀÎÀÚ
  • resistance factor
    ³»¼ºÀÎÀÚ, °ßµõÀÎÀÚ
  • resistancetransfer factor
    ³»¼ºÀü´ÞÀÎÀÚ
  • reticuloendothelial depressant factor
    ¼¼¸Á³»Çǰè¾ïÁ¦ÀÎÀÚ, ±×¹°³»Çǰè¾ïÁ¦ÀÎÀÚ
  • rheumatoid factor
    ·ù¸¶Æ¼½ºÀ¯»çÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • X factor
    X ÀÎÀÚ
  • X-factor
    XÀÎÀÚ, Ç츶ƾ
  • 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).
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  • ¿µ¹®
    ÇѱÛ
  • tumor growth
    Á¾¾ç¼ºÀå
  • tumor growth,cell aggreagation in
    ¡­¿¡¼­ ¼¼Æ÷ÀÀÁý(¼¼Æ÷ÀÀ±«)
  • tumor growth,cell cycle and
    ¼¼Æ÷ÁÖ±â¿Í ¡­
  • tumor growth,kinetics of
    ¡­ÀÇ ¼Óµµ·Ð(¿ªµ¿, µ¿ÅÂ)
  • tumor growth,latent period in
    ¡­Àẹ±â
  • 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).
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  • ¿µ¹®
    ÇѱÛ
  • multiple factor hypothesis
    ´ÙÀÎÀÚ¼³(Òýì×í­àã)
  • oligomycin-sensitivity-conferring factor
    ¿Ã¸®°í¸¶À̽а¨¼ö¼ººÎ¿©ÀÎÀÚ(Êïáôàõݾæ¨ì×í­)
  • particle scattering factor
    ÀÔÀÚ »ê¶õÀÎÀÚ(Ø£í­ß¤Õ¯ì×í­)
  • pellagra-preventaive factor
    Æç¶ó±×¶ó ¿¹¹æÀÎÀÚ(çãÛÁì×í­)
  • permeability factor
    Åõ°ú ÀÎÀÚ(÷âΦì×í­)
  • plasma factor
    Ç÷ÀåÀÎÀÚ(úìíìì×í­)
  • plasma thromboplastic factor
    Ç÷Àå Ç÷ÀüÇü¼ºÀÎÀÚ(úìíìúìîûû¡à÷ì×í­)
  • plasma thromboplastic factor B
    Ç÷Àå Ç÷ÀüÇü¼ºÀÎÀÚ B
  • platelet-activating factor
    Ç÷¼ÒÆÇȰ¼º ÀÎÀÚ(úìá³÷ùüÀàõì×í­)
  • PP factor
    PP ÀÎÀÚ(ì×í­)
  • preexponential factor
    Áö¼ö(ò¦â¦)¾ÕÀÚ¸® ÀÎÀÚ(ì×í­)
  • protein factor
    ´Ü¹éÁú ÀÎÀÚ(Ó±ÛÜòõì×í­)
  • protein release factor
    ´Ü¹éÁú ¹æÃâÀÎÀÚ(Ó±ÛÜòõÛ¯õóì×í­)
  • protein synthesis factor
    ´Ü¹éÁú ÇÕ¼ºÀÎÀÚ(Ó±ÛÜòõùêà÷ì×í­)
  • prothrombin factor
    ÇÁ·ÎÆ®·Òºó ÀÎÀÚ(ì×í­)
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LEF leukokinesis-enhancing factor; lupus erythematosus factor; lymphoid-enhanced binding factor
LIF laser-induced fluorescence; left iliac fossa; left index finger; leukemia-inhibiting factor; leukocy...
MF magnetic field; meat free; medium frequency; megafarad; membrane filler; merthiolate-formaldehyde [s...
MSF macrophage slowing factor; macrophage spreading factor; Medicins sans Frontieres [Doctors without Bo...
PIF paratoid isoelectric focusing variant protein; peak inspiratory flow; proinsulin-free; prolactin-inh...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 11
PBR Peripheral Benzodiazpine Receptors
PTBR Peripheral-type benzodiazepine receptors
PR Progestin receptors
PRL-R Prolactin receptors
PAR Protease activated receptors
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • resistance factor
    ³»¼º ÀÎÀÚ
  • Rh factor
    Rh ÀÎÀÚ
  • rheumsid factor
    ·ù¸¶Æ¼½º¾ç ÀÎÀÚ
  • risk factor
    À§Çè ¿äÀÎ, À§Çè ¿ä¼Ò, À§Çè ÀÎÀÚ
    °³ÀÎÀ̳ª ´Üü°¡ ÁúȯÀ̳ª Àå¾Ö¿¡ °É¸®±â ½±°Ô ÇÏ´Â ¿øÀÎÀÌ µÇ´Â ¿ä¼Ò·Î¼­ ¹Î°¨ÇÑ »ç¶÷µé¿¡¼­ ¹ß»ý ºóµµ¿Í Á¤µµ¸¦ Áõ°¡½ÃŲ´Ù.
  • safety factor
    ¾ÈÀü·ü
    ½Å°æ ¼¶À¯³ª ±Ù¼¶À¯ÀÇ ÈïºÐ Á¤µµ¿¡ À־ ÀÌ¹Ì ÈïºÐÇÑ °÷¿¡¼­, ¾ÆÁ÷ ÈïºÐÇϰí ÀÖÁö ¾ÊÀº ºÎºÐÀ¸·Î Àü·ù°¡ È帧À¸·Î½á ÈïºÐÀÌ ÀüµµÇϴµ¥, ÀÌ Àü·ù°¡ ½ÇÁ¦·Î ÈïºÐ½Ã۴µ¥ ÇÊ¿äÇÑ Àü·ù°ª.
  • self-associated rheumatoid factor complex

    self-care (ÀÚ°¡ Ä¡·á

  • sex factor
    ¼º ÀÎÀÚ
  • situational factor
    »óȲ ¿äÀÎ
  • socioeconomic factor
    »çȸ °æÁ¦Àû ¿äÀÎ
  • somatic factor
    ü¼º ¿äÀÎ
  • spreading factor
    È®»ê ÀÎÀÚ
  • stem cell factor
    °£ ¼¼Æ÷ ¿ä¼Ò
  • systemic etiologic factor
    Àü½ÅÀû ¿øÀÎ ¿ä¼Ò
  • transfer factor
    Àü´Þ ÀÎÀÚ, ÀüÀÌ ¿äÀÎ
  • tumor necrosis factor
    Á¾¾ç ±«»ç ÀÎÀÚ
    TNF. Á¾¾ç¿¡ °ü°èÇϰí ÀÖ´Â ¸é¿ª°èÀÇ ¼¼Æ÷ÀÎ Á¾¾ç ħÀ±¼º ¸²ÇÁ±¸
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 11
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)
receptors, bombesin Cell surface proteins that bind bombesin or closely related peptides with high affinity and trigger intracellular changes influencing the behaviour of cells. Gastrin- releasing peptide (grp), grp 18-27 (neuromedin c), and neuromedin b are endogenous ligands of bombesin receptors in mammals.
(12 Dec 1998)
receptors, bradykinin Cell surface receptors that bind bradykinin and related kinins with high affinity and trigger intracellular changes which influence the behaviour of cells. The identified receptor types (b-1 and b-2, or bk-1 and bk-2) recognise the endogenous kallidins, t-kinins, and certain bradykinin fragments as well as bradykinin itself.
(12 Dec 1998)
receptors, calcitonin Cell surface proteins that bind calcitonin and trigger intracellular changes which influence the behaviour of cells. Calcitonin receptors outside the nervous system mediate the role of calcitonin in calcium homeostasis. The role of calcitonin receptors in the brain is not well understood.
(12 Dec 1998)
receptors, calcitonin gene-related peptide Cell surface proteins that bind calcitonin gene-related peptide (cgrp) with high affinity and trigger intracellular changes which influence the behaviour of cells. Cgrp receptors are present in both the central nervous system and the periphery and are not the same as calcitonin receptors.
(12 Dec 1998)
receptors, calcitriol Proteins, usually found in the cytoplasm, that specifically bind calcitriol, migrate to the nucleus, and regulate transcription of specific segments of DNA. Vitamin d is converted in the liver and kidney to calcitriol and ultimately acts through these receptors.
(12 Dec 1998)
receptors, catecholamine Cell surface proteins that bind catecholamines with high affinity and trigger intracellular changes which influence the behaviour of cells. The catecholamine messengers epinephrine, norepinephrine, and dopamine are synthesised from tyrosine by a common biosynthetic pathway.
(12 Dec 1998)
receptors, ccr5 Seven-transmembrane G-protein-coupled receptors for beta-chemokines. They also function as fusion cofactors for macrophage-tropic HIV-1 strains.
(12 Dec 1998)
receptors, cell surface Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behaviour of the target cell. Cell surface receptors, unlike enzymes, do not chemically alter their ligands.
(12 Dec 1998)
receptors, chemokine Cell surface glycoproteins that bind to chemokines and thus mediate the migration of pro-inflammatory molecules. The receptors are members of the seven-transmembrane G-protein-coupled receptor family.
(12 Dec 1998)
receptors, cholecystokinin Cell surface proteins that bind cholecystokinin (cck) with high affinity and trigger intracellular changes influencing the behaviour of cells. Cholecystokinin receptors are activated by gastrin as well as by cck-4, cck-8, and cck-33. Activation of these receptors evokes secretion of amylase by pancreatic acinar cells, acid and pepsin by stomach mucosal cells, and contraction of the pylorus and gall bladder. The role of the widespread cck receptors in the central nervous system is not well understood.
(12 Dec 1998)
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