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"Receptors, Tumor Necrosis 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
  • mitogenic factor
    ºÐ¿­ÃËÁøÀÎÀÚ
  • myocardial depressant factor
    ½É(Àå)±Ù(À°)¾ïÁ¦ÀÎÀÚ
  • macrophage aggregating factor
    Å«Æ÷½Ä¼¼Æ÷ÀÀÁýÀÎÀÚ, ´ë½Ä¼¼Æ÷ÀÀÁýÀÎÀÚ
  • macrophage arming factor
    Å«Æ÷½Ä¼¼Æ÷¹«ÀåÀÎÀÚ, ´ë½Ä¼¼Æ÷¹«ÀåÀÎÀÚ
  • macrophage chemotactic factor
    Å«Æ÷½Ä¼¼Æ÷È­Çнò¸²ÀÎÀÚ, ´ë½Ä¼¼Æ÷È­Çнò¸²ÀÎÀÚ
  • macrophage colony-stimulating factor
    Å«Æ÷½Ä¼¼Æ÷Áý¶ôÀÚ±ØÀÎÀÚ, ´ë½Ä¼¼Æ÷Áý¶ôÀÚ±ØÀÎÀÚ
  • macrophage migration inhibitory factor
    Å«Æ÷½Ä¼¼Æ÷À̵¿ÀúÁöÀÎÀÚ, ´ë½Ä¼¼Æ÷À̵¿ÀúÁöÀÎÀÚ
  • macrophage-activating factor
    Å«Æ÷½Ä¼¼Æ÷Ȱ¼ºÀÎÀÚ, ´ë½Ä¼¼Æ÷Ȱ¼ºÀÎÀÚ
  • macrophage-derived growth factor
    Å«Æ÷½Ä¼¼Æ÷À¯·¡¼ºÀåÀÎÀÚ, ´ë½Ä¼¼Æ÷À¯·¡¼ºÀåÀÎÀÚ
  • nerve growth factor
    ½Å°æ¼ºÀåÀÎÀÚ
  • neutron kerma factor
    Áß¼ºÀÚÄ¿¸¶°è¼ö
  • neutrophil chemotactic factor
    Áß¼º±¸È­ÇÐÁÖ¼ºÀÎÀÚ, È£Áß±¸½ò¸²ÀÎÀÚ
  • occupancy factor
    °ÅÁÖ°è¼ö
  • obliquity factor
    ±â¿ï±â°è¼ö
  • output factor
    Ãâ·ÂÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 12
  • ¿µ¹®
    ÇѱÛ
  • migration inhibition factor
    Æ÷½Ä¼¼Æ÷À̵¿ÀúÇØÀÎÀÚ
  • mitogenic factor
    ºÐ¿­ÃËÁøÀÎÀÚ
  • myocardial depressant factor
    ½ÉÀå±Ù¾ïÁ¦ÀÎÀÚ
  • nerve growth factor
    ½Å°æ¼ºÀåÀÎÀÚ
  • neutron kerma factor
    Áß¼ºÀÚÄ¿¸¶°è¼ö
  • neutrophil chemotactic factor
    È£Áß±¸ÁÖ¼ºÀÎÀÚ, È£Áß±¸½ò¸²ÀÎÀÚ
  • obliquity factor
    ±â¿ï±â°è¼ö
  • occupancy factor
    °ÅÁÖ°è¼ö
  • output factor
    Ãâ·ÂÀÎÀÚ
  • oxygen gain factor
    »ê¼ÒÀ̵æ°è¼ö
  • phantom scatter factor
    ÆÒÅè»ê¶õ°è¼ö
  • plasma coagulation factor
    Ç÷ÀåÀÀ°íÀÎÀÚ
  • plasma thromboplastin factor
    Ç÷À寮·Òº¸ÇÃ¶ó½ºÆ¾ÀÎÀÚ
  • platelet activating factor
    Ç÷¼ÒÆÇȰ¼ºÀÎÀÚ
  • platelet-derived growth factor
    Ç÷¼ÒÆÇÀ¯·¡¼ºÀåÀÎÀÚ, Ç÷¼ÒÆÇ±â¿ø¼ºÀåÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 12
  • ¿µ¹®
    ÇѱÛ
  • 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).
  • 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.
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 12
  • ¿µ¹®
    ÇѱÛ
  • cooperative factor
    Çùµ¿ÀÎÀÚ.
  • cord factor
    ±Õ»öÀÎÀÚ
  • cord factor
    ÄÚ¿Àµå ÀÎÀÚ(¡­ì×í­)
  • cord factor
    ÄÚ¿ÀµåÀÎÀÚ(¡­ì×í­).
  • coronary risk factor
    °ü(»ó)(µ¿¸Æ)ÁúȯÀ§Çè¿äÀÎ.
  • corticotropin-releasing factor =CRF
    ºÎ½ÅÇÇÁú ÀÚ±ØÈ£¸£¸ó ¹æÃâÀÎÀÚ(Üù ãìù«òõô§Ð½¡­Û¯õóì×í­).
  • cothromboplastin factor VII
    ÄÚÆ®·Òº¸ÇÃ¶ó½ºÆ¾.
  • coupling factor
    ¹è¿ìÀÎÀÚ.
  • covering factor
    ÇǺ¹ÀÎÀÚ(¡­ì×í­).
  • cytotoxic factor
    ¼¼Æ÷ µ¶¼º ÀÎÀÚ
  • decay-accelerating factor
    ºÐÇØÃËÁøÀÎÀÚ
  • decay-accelerating factor (DAF)
    ºØ±«ÃËÁøÀÎÀÚ
  • decay-accelerating factor(daf)
    Decay-accelerating factor(DAF)
  • dermonecrotic factor
    ÇǺα«»çÀÎÀÚ
  • diabetogenic factor
    ´ç´¢À¯¹ßÀÎÀÚ.
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 12
  • ¿µ¹®
    ÇѱÛ
  • sex factor
    ¼ºÀÎÀÚ(àõì×í­)
  • shape factor
    ¸ð¾çÀÎÀÚ(Ù¼åÆì×í­)
  • sigma factor
    ½Ã±×¸¶ÀÎÀÚ(ì×í­)
  • SLR factor
    SLRÀÎÀÚ(ì×í­)
  • somatotropin factor
    ¼Ò¸¶Å䯮·ÎÇÉ ÀÎÀÚ(ì×í­)
  • specificity factor
    ƯÀ̼º ÀÎÀÚ(÷åì¶àõì×í­)
  • spreading factor
    ÆÛÁü ÀÎÀÚ(ì×í­)
  • stable factor
    ¾ÈÁ¤ÀÎÀÚ(äÌïÒì×í­)
  • steric factor
    ÀÔü ÀÎÀÚ(Ø¡ô÷ì×í­)
  • stringent factor
    ¾ö°Ý ÀÎÀÚ (åñÌ«ì×í­)
  • Stuart factor
    ½ºÆ©¾Æ¸£Æ® ÀÎÀÚ(ì×í­)
  • sulfation factor
    Ȳ»êÈ­ ÀÎÀÚ (üÜß«ûùì×í­)
  • surface factor
    Ç¥¸éÀÎÀÚ (øúØüì×í­)
  • T cell growth factor
    T ¼¼Æ÷¼ºÀåÀÎÀÚ (á¬øàà÷íþì×í­)
  • termination factor
    Á¾·áÀÎÀÚ (ðûÖõì×í­)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 12
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: 12
SAR Slowly adapting receptors
SR Steroid receptors
TR T(3) receptors
TNFRs TNF receptors
TR Thyroid Hormone Receptors
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 12
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • bone factor
    °ñ ÀÎÀÚ
    Ȱ¼ºÀ̳ª ÀÚÁï¿¡ ´ëÇÑ Ä¡Á¶°ñÀÇ »ó´ë ¹ÝÀÀ.
  • Castle factor
    ij½½ ÀÎÀÚ
    ½ÄǰÀ̳ª À§¾× ¼Ó¿¡ ÀÖ´Â Ç׺óÇ÷ ÀÎÀÚ. À̰ÍÀÌ °áÇÌµÇ¸é ¾Ç¼º ºóÇ÷ÀÌ µÈ´Ù. À§¾×¿¡ ÇÔÀ¯µÈ ij½½³» ÀÎÀÚ¿Í ½Äǰ¿¡ ÇÔÀ¯µÈ ij½½¿Ü ÀÎÀÚ°¡ ÀÖ´Ù. ³»ÀÎÀÚ°¡ °áÇÌµÇ¸é ½Äǰ ³»ÀÇ ¿ÜÀÎÀÚ°¡ Èí¼öµÇÁö ¾Ê°í ¾Ç¼º ºóÇ÷ÀÌ ÀϾ´Ù. À§ ¾Ï µîÀ¸·Î À§¸¦ ÀüºÎ Àß¶ó¹ö¸®¸é ºóÇ÷ÀÌ ÀϾ´Â °ÍÀº ³»ÀÎÀÚ°¡ ¾ø¾îÁö±â ¶§¹®ÀÌ´Ù. ³»ÀÎÀÚ´Â ºÐÀÚ·® ¾à 10¸¸ÀÎ ´Ü¹éÁú·Î À§º®ÀÇ ¹æ ¼¼Æ÷¿¡¼­ ºÐºñµÈ´Ù. ¿ÜÀÎÀڷμ­´Â ºñŸ¹Î D°¡ °ü°èÇÑ´Ù. 1927³â ¹Ì±¹ÀÇ W.B. ij½½ÀÌ Ã³À½À¸·Î ÀÌ·¯ÇÑ ±¸Á¶¸¦ Á¦Ã¢ÇÏ¿´´Ù.
  • Castles extrinsic factor
    ij½½ ¿ÜÀÎÀÚ
  • cavity-gas calibration factor
    °­-±âü ±³Á¤ °è¼ö
  • certainty factor
    È®½Ç ¿äÀÎ
  • chamber calibration factor
    Àü¸®ÇÔ ÃøÁ¤ °è¼ö, »óÀÚ ÃøÁ¤ °è¼ö
  • circumstance factor
    »óȲ ÀÎÀÚ
  • clotting factor
    ÀÀÇ÷ ÀÎÀÚ, ÀÀ°í ÀÎÀÚ
  • clumping factor
    ÀÀ±« ÀÎÀÚ
  • coagulase-reacting factor
    Ç÷Àå ÀÀ°í È¿¼Ò ¹ÝÀÀ ÀÎÀÚ
  • coagulation factor
    ÀÀÇ÷ ÀÎÀÚ, ÀÀ°í ÀÎÀÚ
  • coagulation factor inhibitor
    ÀÀ°í ÀÎÀÚ ¾ïÁ¦Á¦
  • colicin factor
    Äݸ®½Å ÀÎÀÚ
  • colony stimulating factor
    ±ºÃ¼ ÀÚ±Ø ¿ä¼Ò, Áý¶ô ÀÚ±Ø ÀÎÀÚ
    ¹ß´Þ ´Ü°èÀÇ Àü±¸Àû ¼¼Æ÷°¡ Áý¶ôÀ» Çü¼ºÇÏ´Â °úÁ¤¿¡´Â À̰ÍÀÇ ÀÛ¿ëÀÌ ÇÊ¿äÇÏ´Ù´Â °ÍÀÌ ÀνĵǾú´Ù. ÀÌ ÀÎÀÚ´Â ¼¶À¯¾Æ¼¼Æ÷, ³»ÇǼ¼Æ÷, ´ë½Ä¼¼Æ÷ µî¿¡¼­ »ý»êµÇ¸ç ¼º¼÷ÇÑ ¸é¿ª°è ¼¼Æ÷ÀÇ ÀÛ¿ë¿¡µµ ¿µÇâÀ» ³¢Ä£´Ù.
  • competence inducing factor
    Àû°Ý À¯¹ß ÀÎÀÚ
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 12
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)
receptors, opioid, mu A class of opioid receptors recognised by its pharmacological profile. Mu opioid receptors bind, in decreasing order of affinity, endorphins, dynorphins, met-enkephalin, and leu-enkephalin. They have also been shown to be molecular receptors for morphine.
(12 Dec 1998)
receptors, oxytocin Cell surface proteins that bind oxytocin with high affinity and trigger intracellular changes which influence the behaviour of cells. Oxytocin receptors in the uterus and the mammary glands mediate the hormone's stimulation of contraction and milk ejection. The presence of oxytocin and oxytocin receptors in neurons of the brain probably reflects an additional role as a neurotransmitter.
(12 Dec 1998)
receptors, pancreatic hormone Cell surface proteins that bind pancreatic hormones with high affinity and trigger intracellular changes which influence the behaviour of cells. These include receptors for glucagon (secreted by alpha cells), insulin (secreted by beta cells), somatostatin (secreted by delta cells), and pancreatic peptide (secreted by pp cells). Some of these hormones and receptors also support neurotransmission.
(12 Dec 1998)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 12
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
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    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
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  • ¿µ¹®
    ÇѱÛ
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    ÇѱÛ
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  • ¿µ¹®
    ÇѱÛ
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  • ¿µ¹®
    ÇѱÛ
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  • ¿µ¹®
    ÇѱÛ
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    ÇÑÀÚ
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    ÇÑÀÚ
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KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 12
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 12
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CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 12
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 12
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