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"Receptors, Mating 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
  • 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
  • risk factor
    À§ÇèÀÎÀÚ
  • roentgen-to-rad conversion factor
    ·ÛÆ®°Õ´ë·¡µåº¯È¯°è¼ö
  • somatotropin release inhibiting factor
    ¼ºÀåÈ£¸£¸óºÐºñ¾ïÁ¦ÀÎÀÚ
  • spreading factor
    È®»êÀÎÀÚ
  • stable factor
    ¾ÈÁ¤ÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • 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
  • tissue factor
    Á¶Á÷ÀÎÀÚ
  • transfer factor
    Àü´ÞÀÎÀÚ
  • transforming growth factor
    Àüȯ¼ºÀåÀÎÀÚ
  • transmission factor
    Åõ°ú°è¼ö
  • tumor angiogenesis factor
    Á¾¾çÇ÷°üÇü¼ºÀÎÀÚ
  • tumor necrosis factor
    Á¾¾ç±«»çÀÎÀÚ
  • vascular endothelial growth factor
    Ç÷°ü³»ÇǼºÀåÀÎÀÚ
  • vascular permeability factor
    Ç÷°üÅõ°úÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • hypothalamus releasing factor
    ½Ã»óÇϺÎÀ¯¸®ÀÎÀÚ.
  • inhibition(-tory) factor, macrophage migration
    ´ë½Ä¼¼Æ÷ À¯ÁÖÀúÁöÀÎÀÚ
  • intensity factor
    °­µµÀÎÀÚ
  • plasma coagulation factor
    Ç÷ÀåÀÀ°íÀÎÀÚ
  • plasma factor
    Ç÷ÀåÀÎÀÚ(úìíìì×í­), ÇöóÁÀÎÀÚ.
  • plasma factor
    Ç÷ÀåÀÎÀÚ(úìíìì×í­), ÇöóÁÀÎÀÚ(¡­ì×í­)
  • plasma thromboplastic factor
    Ç÷À寮·Òº¸ÇÃ¶ó½ºÆ¾ÀÎÀÚ.
  • plasma thromboplastin factor
    Ç÷À寮·Òº¸ÇÃ¶ó½ºÆ¾ÀÎÀÚ.
  • platelet activating factor
    Ç÷¼ÒÆÇ Ȱ¼º ÀÎÀÚ
  • platelet factor 4
    Ç÷¼ÒÆÇÀÎÀÚ(úìá³÷ùì×í­) 4
  • platelet factor 4=PF4
    Ç÷¼ÒÆÇÀÎÀÚ 4
  • platelet factor III
    Ç÷¼ÒÆÇÁ¦»ïÀÎÀÚ.
  • platelet-activating factor (PAF)
    Ç÷¼ÒÆÇ Ȱ¼ºÈ­ÀÎÀÚ
  • platelet-activating factor (paf)
    Ç÷¼ÒÆÇȰ¼ºÈ­ÀÎÀÚ(úìá³÷ùüÀàõûùì×í­)
  • platelet-derived growth factor
    Ç÷¼ÒÆÇÀ¯·¡ Áõ½ÄÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • endothelium-derived relaxing factor (EDRF)
    ³»ÇǼ¼Æ÷¼ºÀÌ¿ÏÀÎÀÚ
  • endurance factor =EF
    Áö¼ÓÀÎÀÚ(ò¥áÙì×í­).
  • environmental chemotactic factor
    ȯ°æ¼ºÈ­ÇÐÁÖ¼ºÀÎÀÚ(ü»ÌÑàõûùùÊñËàõì×í­)
  • environmental factor
    ȯ°æÀÎÀÚ.
  • eosinophil chemotactic factor
    È£»ê±¸ È­ÇÐÁÖ¼ºÀÎÀÚ
  • eosinophil chemotactic factor =ECF
    È£»ê±¸ È­ÇÐÁÖ¼ºÀÎÀÚ.
  • eosinophilic chemotactic factor
    È£»ê±¸¼º È­ÇÐÁÖ¼ºÀÎÀÚ
  • epidermal growth factor
    Ç¥ÇǼºÀåÀÎÀÚ
  • epidermal growth factor
    Ç¥ÇǼºÀåÀÎÀÚ(øúù«à÷íþì×í­)
  • epidermal growth factor
    Ç¥ÇǼºÀå ÀÎÀÚ(¡­à÷íþ ì×í­)
  • epidermal growth factor (EGF)
    ÇǺÎÁõ½ÄÀÎÀÚ
  • epidermal growth factor = EGF
    Ç¥ÇÇ ¼ºÀå ÀÎÀÚ
  • epidermoid growth factor
    Ç¥ÇÇ¾ç ¼ºÀåÀÎÀÚ(¡­à÷íþì×í­)
  • erythrocyte maturation factor
    ÀûÇ÷±¸¼º¼÷ÀÎÀÚ(?ËÛËàËöËö).
  • erythrocyte maturation factor
    ÀûÇ÷±¸¼º¼÷ÀÎÀÚ(¡­à÷âÙì×í­).
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • 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)
  • platelet-derived growth factor
    Ç÷¼ÒÆÇÀ¯·¡(úìá³÷ùë¦ÕÎ) ¼ºÀåÀÎÀÚ(à÷íþì×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)
  • Prower factor
    ÇÁ¶ó¿ö ÀÎÀÚ(ì×í­)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 9
BCF basophil chemotactic factor; bioconcentration factor; breast cyst fluid
BPF bradykinin-potentiating factor; bronchopulmonary fistula; burst-promoting factor
BSF back scatter factor; B-cell stimulatory factor; busulfan
CCF cancer coagulation factor; cardiolipin complement fixation; carotid-cavernous fistula; centrifuged c...
CMF calcium-magnesium free; catabolite modular factor; chondromyxoid fibroma; Christian Medical Fellowsh...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 9
D factor Differentiation-stimulating factor
TRAF Factor Receptor-associated factor
FVIII-vWF Factor VIII-von Willebrand Factor
Factor Xa Factor X
GM-CSF Granulocyte colony-stimulating factor , granulocyte-macrophage colony-stimulating factor
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • 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±¸
  • tumor necrotizing factor
    Á¾¾ç ±«»ç ÀÎÀÚ
  • turbo factor
    Åͺ¸ ÀÎÀÚ
  • V-factor
    V-ÀÎÀÚ
    Ç캸Çʷ罺¼ÓÀÇ ±ÕÀÇ ÀÌ¿­¼º ÀÎÀÚ.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
receptors, mitogen Glycoprotein molecules on the surface of b- and T-lymphocytes, that react with molecules of antilymphocyte sera, lectins, and other agents which induce blast transformation of lymphocytes.
(12 Dec 1998)
receptors, muscarinic One of the two major classes of cholinergic receptors. Muscarinic receptors were originally defined by their preference for muscarine over nicotine. There are several subtypes (usually m1, m2, m3...) that are characterised by their cellular actions, pharmacology, and molecular biology.
(12 Dec 1998)
receptors, neurokinin-1 A class of cell surface receptors for tachykinins with a preference for substance p. Neurokinin-1 (nk-1) receptors have been cloned and are members of the G-protein coupled receptor superfamily. They are found on many cell types including central and peripheral neurons, smooth muscle cells, acinar cells, endothelial cells, fibroblasts, and immune cells.
(12 Dec 1998)
receptors, neurokinin-2 A class of cell surface receptors for tachykinins that prefers neurokinin a (nka, substance k, neurokinin alpha, neuromedin l), neuropeptide k (npk), or neuropeptide gamma over other tachykinins. Neurokinin-2 (nk-2) receptors have been cloned and are similar to other g-protein coupled receptors.
(12 Dec 1998)
receptors, neurokinin-3 A class of cell surface receptors for tachykinins that prefers neurokinin b (neurokinin beta, neuromedin k) over other tachykinins. Neurokinin-3 (nk-3) receptors have been cloned and are members of the g-protein coupled receptor superfamily. They have been found in the central nervous system and in peripheral tissues.
(12 Dec 1998)
receptors, neuropeptide Cell surface receptors that bind specific neuropeptides with high affinity and trigger intracellular changes influencing the behaviour of cells. Many neuropeptides are also hormones outside of the nervous system.
(12 Dec 1998)
receptors, neuropeptide y Cell surface proteins that bind neuropeptide y with high affinity and trigger intracellular changes which influence the behaviour of cells.
(12 Dec 1998)
receptors, neurotensin Cell surface proteins that bind neurotensin with high affinity and trigger intracellular changes which influence the behaviour of cells. Neurotensin and neurotensin receptors are found in the central nervous system and in the periphery.
(12 Dec 1998)
receptors, neurotransmitter Cell surface receptors that bind signalling molecules released by neurons and convert these signals into intracellular changes influencing the behaviour of cells. Neurotransmitter is used here in its most general sense, including not only messengers that act to regulate ion channels, but also those which act on second messenger systems and those which may act at a distance from their release sites. Included are receptors for neuromodulators, neuroregulators, neuromediators, and neurohumors, whether or not located at synapses.
(12 Dec 1998)
receptors, nicotinic One of the two major classes of cholinergic receptors. Nicotinic receptors were originally distinguished by their preference for nicotine over muscarine. They are generally divided into muscle-type and neuronal-type (previously ganglionic) based on pharmacology, molecular biology, and biophysical properties of the channels.
(12 Dec 1998)
receptors, n-methyl-d-aspartate A class of ionotropic glutamate receptors characterised by affinity for n-methyl-d-aspartate. Nmda receptors have an allosteric binding site for glycine which must be occupied for the channel to open efficiently and a site within the channel itself to which magnesium ions bind in a voltage-dependent manner. The positive voltage dependence of channel conductance and the high permeability of the conducting channel to calcium ions (as well as to monovalent cations) are important in excitotoxicity and neuronal plasticity.
(12 Dec 1998)
receptors, odourant Proteins, usually projecting from the cilia of olfactory receptor neurons, that specifically bind odourant molecules and trigger responses in the neurons. The large number of different odourant receptors appears to arise from several gene families or subfamilies rather than from DNA rearrangement.
(12 Dec 1998)
receptors, opioid Cell membrane proteins that bind opioids and trigger intracellular changes which influence the behaviour of cells. The endogenous ligands for opioid receptors in mammals include three families of peptides, the enkephalins, endorphins, and dynorphins. The receptor classes include mu, delta, and kappa receptors. Sigma receptors bind several psychoactive substances, including certain opioids, but their endogenous ligands are not known.
(12 Dec 1998)
receptors, opioid, delta A class of opioid receptors recognised by its pharmacological profile. Delta opioid receptors bind endorphins and enkephalins with approximately equal affinity and have less affinity for dynorphins.
(12 Dec 1998)
receptors, opioid, kappa A class of opioid receptors recognised by its pharmacological profile. Kappa opioid receptors bind dynorphins with a higher affinity than endorphins which are themselves preferred to enkephalins.
(12 Dec 1998)
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    ±¸ºÐ/º¸Çè±Þ¿©
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