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  • ¿µ¹®
    ÇѱÛ
  • epidermal growth factor
    Ç¥ÇǼºÀåÀÎÀÚ
  • fermentation factor
    ¹ßÈ¿ÀÎÀÚ
  • fertility factor
    ¼öÅÂÀÎÀÚ
  • fibrin stabilizing factor
    ¼¶À¯¼Ò¾ÈÁ¤ÀÎÀÚ
  • fibroblast growth factor
    ¼¶À¯¸ð¼¼Æ÷¼ºÀåÀÎÀÚ
  • factor
    1. ÀÎÀÚ 2. ¿äÀÎ 3. °è¼ö
  • factor III
    Á¦3ÀÎÀÚ
  • factor IV
    Á¦4ÀÎÀÚ
  • factor IX
    Á¦9ÀÎÀÚ
  • factor IX complex
    Á¦9ÀÎÀÚº¹ÇÕü
  • factor V
    Á¦5ÀÎÀÚ
  • factor VI
    Á¦6ÀÎÀÚ
  • factor VII
    Á¦7ÀÎÀÚ
  • factor VIII
    Á¦8ÀÎÀÚ
  • factor X
    Á¦10ÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • factor
    ÀÎÀÚ, ¿äÀÎ, °è¼ö
  • factor theory
    ¿äÀÎÀÌ·Ð
  • fermentation factor
    ¹ßÈ¿ÀÎÀÚ
  • fertility factor
    ¼öÅÂÀÎÀÚ
  • fibrin stabilizing factor
    ¼¶À¯¼Ò¾ÈÁ¤ÀÎÀÚ
  • fibroblast growth factor
    ¼¶À¯¸ð¼¼Æ÷¼ºÀåÀÎÀÚ
  • 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
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  • ¿µ¹®
    ÇѱÛ
  • EDCF (endothlium-derived contracting factor)
    ³»ÇǼ¼Æ÷¼º(Ò®ù«á¬øààõ) ¼öÃàÀÎÀÚ(â¥õêì×í­)
  • EDRF (endothlium-derived relaxing factor)
    ³»ÇǼ¼Æ÷¼º(Ò®ù«á¬øààõ) ÀÌ¿ÏÀÎÀÚ(ì¬èÐì×í­)
  • EDRF=£¾endothelium derived relaxing factor
    ³»ÇǼ¼Æ÷¼ºÀÌ¿ÏÀÎÀÚ.
  • F factor
    FÀÎÀÚ
  • Factor IX
    IX ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor V
    V ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor VII
    VII ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor VIII
    VIII ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor X activated
    Ȱ¼ºÈ­(üÀàõûù)µÈ X ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor XI
    XI ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Factor XII
    XII ÀÀ°íÀÎÀÚ(ëêͳì×í­)
  • Fibrin-stabilizing factor
    ¼¶À¯¼Ò¾ÈÁ¤ÀÎÀÚ(¡­äÌïÒì×í­)
  • Fibroblast growth factor
    ¼¶À¯¸ð¼¼Æ÷(àéë«Ù½á¬øà)¼ºÀå¿äÀÎ(à÷íþé©ì×)
  • GH releasing factor
    ¼ºÀå(à÷íþ)È£¸£¸ó À¯¸®ÀÎÀÚ(ë´×îì×í­).
  • GH releasing factor
    ¼ºÀåÈ£¸£¸óÀ¯¸®ÀÎÀÚ.
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  • ¿µ¹®
    ÇѱÛ
  • 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
  • autocrine motility factor
    Autocrine motility factor
  • back scatter factor
    ÈĹæ»ê¶õ°è¼ö
  • beam scattering factor
    ºö»ê¶õÀÎÀÚ
  • biotic factor
    »ý¹°ÀÎÀÚ(¡­ì×í­), »ýȰ¿ä¼Ò(ßæüÀé©áÈ).
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  • ¿µ¹®
    ÇѱÛ
  • decay factor
    "ºØ±« ÀÎÀÚ(ÝÚÎÕì×í­), (ÔÒ) decay constant"
  • diffusing factor
    "È®»êÀÎÀÚ(üªß¤ì×í­), (ÔÒ) hyaluronidase"
  • dissociation factor
    ÇØ¸®ÀÎÀÚ(ú°×îì×í­)
  • egg white injury factor
    ÈØÀÚ ¼Õ»óÀÎÀÚ (áßß¿ì×í­)
  • elongation factor
    ¿¬ÀåÀÎÀÚ (æÅíþì×í­)
  • epidermal growth factor
    Ç¥ÇǼºÀåÀÎÀÚ (øúù«à÷íþì×í­)
  • epithelial growth factor
    »óÇǼºÀåÀÎÀÚ (ß¾ù«à÷íþì×í­)
  • erythrocyte maturation factor
    ÀûÇ÷±¸ ¼º¼÷ ÀÎÀÚ (îåúìϹà÷âÙì×í­)
  • extrinsic factor
    ¿ÜÀÎÀÚ(èâì×í­)
  • factor
    ÀÎÀÚ(ì×í­)
  • factor ¥°
    ÀÎÀÚ(ì×í­) I
  • factor ¥±
    ÀÎÀÚ(ì×í­) II
  • factor ¥²
    ÀÎÀÚ(ì×í­) III
  • factor ¥³
    ÀÎÀÚ(ì×í­) IV
  • factor ¥´
    ÀÎÀÚ(ì×í­) V
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NF nafcillin; National Formulary; nephritic factor; neurofibromatosis; neurofilament; neutral fraction;...
RF radial fiber; radio frequency; receptive field; regurgitant fraction; Reitland-Franklin [unit]; rela...
GM-CSF Granulocyte-Macrophage Colony Stimulating Factor
rGM-CSF recombinant Granulocyte-Macrophage Colony Stimulating Factor
G-CSF granulocyte colony-stimulating factor
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GM-CSF IFN)-gamma and granulocyte-macrophage colony-stimulating factor
rh GM-CSF Recombinant human granulocyte/macrophage colony stimulating factor
rG-CSF Recombinant granulocyte colony-stimulating factor
rhG-CSF Recombinant granulocyte colony-stimulating factor
rGM-CSF Recombinant granulocyte-macrophage colony-stimulating factor
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • coupling factor
    ¹è¿ì ÀÎÀÚ
  • covering factor
    ÇǺ¹ ÀÎÀÚ
  • cultural and ethnic factor
    ¹®È­ ¹ÎÁ·Àû ¿äÀÎ
  • cytotoxic factor
    ¼¼Æ÷ µ¶¼º ÀÎÀÚ
  • D and C ÀÚ±ÃÀÇ °æºÎ È®Àå°ú ³»¸· ¼ÒÆÄ.

    D factor

    D-ÀÎÀÚ
  • Decay accelerating factor
    ºØ±« °¡¼Ó ¿ä¼Ò
  • diabetogenic factor
    ´ç´¢ À¯¹ß ÀÎÀÚ
  • differentiation factor
    °¨º° ¿äÀÎ, °¨º° ¿ä¼Ò, °¨º° ÀÎÀÚ
  • diffusion factor
    È®»ê ÀÎÀÚ
  • dilution factor
    Èñ¼® ÀÎÀÚ
  • dose modifying factor
    ¼±·® ¼ö½Ä °è¼ö
  • drug resistance factor
    ¾àÁ¦ ³»¼º ÀÎÀÚ
  • drug resistance transfer factor
    ¾àÁ¦ ³»¼º Àü´Þ ÀÎÀÚ
  • EDA : electronic dental anesthesiaÀÇ ¾àÀÚ.

    edaphic factor

    ÅäÁö ÀÎÀÚ
  • effector-inhibitory factor
    È¿°ú±â ¾ïÁ¦ ÀÎÀÚ
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
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)
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)
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