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  • ¿µ¹®
    ÇѱÛ
  • 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
  • factor XI
    Á¦11ÀÎÀÚ
  • factor XII
    Á¦12ÀÎÀÚ
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  • ¿µ¹®
    ÇѱÛ
  • 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
  • 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
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  • ¿µ¹®
    ÇѱÛ
  • GH releasing factor
    ¼ºÀåÈ£¸£¸óÀ¯¸®ÀÎÀÚ.
  • Growth factor
    ¼ºÀåÀÎÀÚ(à÷íþì×í­)
  • Hageman factor
    ÇϰԸ¸ÀÎÀÚ
  • Hydrostatic factor
    Á¤¼öÀÎÀÚ(ð¡â©ì×í­)
  • IGF-I(insulin-like growth factor-I)
    Àν¶¸° À¯»ç ¼ºÀåÀÎÀÚ-1
  • Luteinization -inhibiting factor
    Ȳüȭ¾ïÁ¦¿äÀÎ(üÜô÷ûùåäð¤é©ì×)
  • Macrophage colony-stimulating factor
    ´ë½Ä¼¼Æ÷Áý¶ôÇü¼ºÃËÁøÀÎÀÚ(ÓÞãÝá¬øàó¢Õªû¡à÷õµòäì×í­)à÷õµòäì×?
  • NGF=>nerve growth factor
    ½Å°æ¼ºÀåÀÎÀÚ
  • PAF =platelet activating factor
    Ç÷¼ÒÆÇȰ¼ºÀÎÀÚ.
  • PAF= platelet activating factor
    Ç÷¼ÒÆÇ Ȱ¼ºÀÎÀÚ.
  • Q factor
    Å¥ ÀÎÀÚ
  • Q-factor
    Å¥-ÀÎÀÚ (ì×í­)
  • R factor
    ³»¼ºÀÎÀÚ.
  • R factor
    ³»¼ºÀÎÀÚ.
  • Rh factor
    RhÀÎÀÚ.
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  • ¿µ¹®
    ÇѱÛ
  • back scatter factor
    ÈĹæ»ê¶õ°è¼ö
  • beam scattering factor
    ºö»ê¶õÀÎÀÚ
  • biotic factor
    »ý¹°ÀÎÀÚ(¡­ì×í­), »ýȰ¿ä¼Ò(ßæüÀé©áÈ).
  • biotic factor
    »ý¹°ÀÎÀÚ(¡­ì×í­), »ýȰ¿ä¼Ò(ßæüÀé©áÈ).
  • blood factor
    Ç÷¾×ÀÎÀÚ(?ËöËö).
  • carcinogenic factor
    ¹ß¾ÏÀÎÀÚ(ËÑËâËöËö).
  • cavaliere blood factor
    Ä«¹ß¸®¿¡ Ç÷¾×ÀÎÀÚ.
  • cavity-gas calibration factor
    °­-±âü ±³Á¤°è¼ö, ºó±¸¸Û-
  • cell loss factor
    ¼¼Æ÷¼Ò½Ç°è¼ö
  • certainty factor
    È®½Ç¿äÀÎ
  • chamber calibration factor
    Àü¸®ÇÔ ÃøÁ¤°è¼ö, »óÀÚÃøÁ¤°è¼ö
  • chemotactic factor
    È­ÇÐÁÖ¼ºÀÎÀÚ(¡­ì×í­).
  • chemotactic factor
    (È­ÇÐ)ÁÖÈ­ÀÎÀÚ, È­ÇÐÁÖ¼ºÀÎÀÚ(¡­ì×í­).
  • chemotactic factor
    (È­ÇÐ)ÁÖÈ­ÀÎÀÚ, È­ÇÐÁÖ¼ºÀÎÀÚ(¡­ì×í­).
  • chemotactic factor
    (È­ÇÐ)ÁÖÈ­ÀÎÀÚ, È­ÇÐÁÖ¼ºÀÎÀÚ(¡­ì×í­)
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  • ¿µ¹®
    ÇѱÛ
  • coupling factor
    ¦Áþ±â ÀÎÀÚ(ì×í­)
  • 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
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RF radial fiber; radio frequency; receptive field; regurgitant fraction; Reitland-Franklin [unit]; rela...
ANF alpha-naphthoflavone; American Nurses' Foundation; antineuritic factor; antinuclear factor; atrial n...
APF acidulated phosphofluoride; American Psychological Foundation; anabolism-promoting factor; animal pr...
EPF early pregnancy factor; endocarditis parietalis fibroplastica; endothelial proliferating factor; est...
HF Hageman factor; haplotype frequency; hard filled [capsule]; hay fever; head of fetus; head forward; ...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 4
FcR Fc gamma Receptors
GRPR Gastrin-releasing peptide receptors
hPR Human progesterone receptors
IPR Imidazolines Preferring Receptors
IFN-gamma R Interferon gamma receptors
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • cothromboplastin factor VII
    ÄÚÆ®·Ò º¸ÇÃ¶ó½ºÆ¾
  • 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
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 4
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)
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)
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