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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
  • antiphagocytic factor
    Çׯ÷½ÄÀÎÀÚ, Ç׎½ÄÀÎÀÚ
  • antiplatelet factor
    Ç×Ç÷¼ÒÆÇÀÎÀÚ
  • antirachitic factor
    Ç×±¸·çº´ÀÎÀÚ
  • antiscorbutic factor
    Ç×±«Ç÷º´ÀÎÀÚ
  • antisterility factor
    Ç׺ÒÀÓÀÎÀÚ
  • atrial natriuretic factor
    ½É¹æ³ªÆ®·ýÀÌ´¢ÀÎÀÚ, ½É¹æ¼ÒµãÀÌ´¢ÀÎÀÚ
  • activation factor
    Ȱ¼ºÀÎÀÚ
  • absorbed dose conversion factor
    Èí¼ö¼±·®º¯È¯°è¼ö
  • alveolar dilution factor
    ÆóÆ÷Èñ¼®ÀÎÀÚ, ÇãÆÄ²Ê¸®Èñ¼®ÀÎÀÚ
  • amplification factor
    ÁõÆøÀÎÀÚ
  • behavioral risk factor
    ÇൿÀ§Çè¿äÀÎ
  • coagulation factor
    ÀÀ°íÀÎÀÚ
  • coagulation factor inhibitor
    ÀÀ°íÀÎÀÚ¾ïÁ¦Á¦
  • colony-stimulating factor
    Áý¶ôÀÚ±ØÀÎÀÚ
  • common factor
    °øÅëÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • trophoblastic tumor
    ¿µ¾ç¸·Á¾¾ç
  • virilizing tumor
    ³²¼ºÈ­Á¾¾ç
  • virus-induced tumor
    ¹ÙÀÌ·¯½ºÀ¯¹ßÁ¾¾ç
  • Wilms' tumor
    Àª¸§ÁîÁ¾¾ç
  • absorbed dose conversion factor
    Èí¼ö¼±·®º¯È¯°è¼ö
  • activation factor
    Ȱ¼ºÀÎÀÚ
  • alveolar dilution factor
    ÆóÆ÷Èñ¼®ÀÎÀÚ, ÇãÆÄ²Ê¸®Èñ¼®ÀÎÀÚ
  • amplification factor
    ÁõÆøÀÎÀÚ
  • antihemophlic factor
    Ç×Ç÷¿ìº´ÀÎÀÚ
  • antineuritic factor
    Ç׽Ű濰ÀÎÀÚ
  • antipellagra factor
    Çׯç¶ó±×¶óÀÎÀÚ
  • antiphagocytic factor
    Çׯ÷½ÄÀÛ¿ëÀÎÀÚ
  • antirachitic factor
    Ç×±¸·íº´ÀÎÀÚ
  • antiscorbutic factor
    Ç×±«Ç÷º´ÀÎÀÚ
  • antisterility factor
    Ç׺ÒÀÓÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • polipoid tumor
    Æú¸³¾çÁ¾¾ç(¡­åÆðþåË)
  • posterior fossa tumor
    ÈĵοÍÁ¾¾ç(ýªÔéèÀðþåË)
  • pregnancy tumor
    ÀÓ½ÅÁ¾¾ç(ìõããðþåË)
  • primary tumor
    ¿ø¹ßÁ¾¾ç(ê«Û¡ðþåË)
  • primitive neuroectodermal tumor
    ¿ø½Ã½Å°æ¿Ü¹è¿±Á¾¾ç(ê«ã·ãêÌèèâÛÏç¨ðþåË)
  • pulmonary sulcus tumor
    Æó±¸Á¾¾ç(øËÏ­ðþåË)
  • ranine tumor =ranulus
    µÎ²¨ºñÁ¾¾ç(¡­ðþåË). µÎ²¨ºñÁ¾(¡­ðþ), Çϸ¶Á¾(ùÁØ©ðþ)
  • recurrent tumor
    Àç¹ß¼º Á¾¾ç(î¢Û¡àõðþåË)
  • renal pelvic tumor
    ½Å¿ìÁ¾¾ç
  • renal pelvic tumor
    ½Å¿ìÁ¾¾ç(ãìéâðþåË)
  • renin-secreting juxtaglomerular tumor
    ·¹´ÑºÐºñ¼º¹æ»ç±¸Ã¼Á¾¾ç
  • AHF=£¾antihemophilic factor
    Ç×Ç÷¿ìÀÎÀÚ.
  • B cell differentiation factor (BCDF)
    B¼¼Æ÷ ºÐÈ­À¯¹ßÀÎÀÚ
  • B cell growth factor
    B ¼¼Æ÷¼ºÀåÀÎÀÚ
  • B cell growth factor (BCGF)
    B¼¼Æ÷ Áõ½ÄÃËÁøÀÎÀÚ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • simple necrosis
    ´Ü¼ø±«»ç
  • subacute hepatic necrosis
    ¾Æ±Þ¼º °£±«»ç(¡­ÊÜÎÕÞÝ)
  • subcutaneous fat necrosis
    ÇÇÇÏÁö¹æ±«»ç (¡­ò·Û¸ÎÕÞÝ).
  • subcutaneous fat necrosis
    ÇÇÇÏÁö¹æ±«»ç(¡­ò·Û¸ÎÕÞÝ)
  • subcutaneous fat necrosis of newborn
    ½Å»ý¾ÆÇÇÇÏÁö¹æ±«»ç.
  • subcutaneous fat necrosis of newborn
    ½Å»ý¾ÆÇÇÇÏÁö¹æ±«»ç(ãæßæä®ù«ù»ò·Û¸ÎÕÞÝ)
  • syphilitic necrosis
    ¸Åµ¶¼º ±«»ç
  • toxic necrosis
    Áßµ¶¼º±«»ç(¡­ÎÕÞÝ)
  • traumatic fat necrosis
    ¿Ü»ó¼º Áö¹æ±«»ç(¡­ò·Û¸ÎÕÞÝ)
  • tubular necrosis
    ¼¼´¢°ü±«»ç(¡­ÎÕÞÝ)
  • tubular necrosis, acute
    ¼¼´¢°ü±«»ç, ±Þ¼º
  • 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).
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  • ¿µ¹®
    ÇѱÛ
  • fibrin-stabilizing factor
    ¼¶À¯¼Ò ¾ÈÁ¤È­ÀÎÀÚ(àéë«áÈäÌïÒûùì×í­)
  • Fitzgerald factor
    ÇÍÁ¦¶öµå ÀÎÀÚ(ì×í­)
  • g factor
    g ÀÎÀÚ(ì×í­)
  • G factor
    G ÀÎÀÚ(ì×í­)
  • glucose tolerance factor
    ±Û·çÄÚ½º ³»¼º ÀÎÀÚ(Ò±àõì×í­)
  • growth factor
    ¼ºÀåÀÎÀÚ (à÷íþì×í­)
  • Hageman factor
    ÇØ±×¸Õ ÀÎÀÚ (ì×í­)
  • heat labile citrovorum factor
    ¿­ºÒ¾ÈÁ¤(æðÝÕäÌïÒ) ½ÃÆ®·Î¹ö·³ ÀÎÀÚ(ì×í­)
  • helper factor
    µµ¿òÀÌ ÀÎÀÚ(ì×í­)
  • hydration factor
    ¼öÈ­ ÀÎÀÚ(â©ûùì×í­)
  • hypercalcemic factor
    °ú(Φ)Ä®½·Ç÷Áõ(úìñø) ÀÎÀÚ(ì×í­)
  • hyperglycemic factor
    °úÇ÷´ç ÀÎÀÚ(ΦúìÓØì×í­)
  • hypocalcemic factor
    Àú(î¸)Ä®½·Ç÷Áõ(úìñø) ÀÎÀÚ(ì×í­)
  • hypoglycemic factor
    ÀúÇ÷´ç ÀÎÀÚ(î¸úìÓØì×í­)
  • initiation factor
    °³½ÃÀÎÀÚ(ËÒã·ì×í­)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 7
LPF leukocytosis-promoting factor; leukopenia factor; lipopolysaccharide factor; localized plaque format...
MIF macrophage inhibitory factor; melanocyte[-stimulating hormone]-inhibiting factor; maximum inspirator...
MRF Markov random field; medical record file; melanocyte-[stimulating hormone]-releasing factor; mesence...
NF nafcillin; National Formulary; nephritic factor; neurofibromatosis; neurofilament; neutral fraction;...
RF radial fiber; radio frequency; receptive field; regurgitant fraction; Reitland-Franklin [unit]; rela...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 7
TNFR1 tumour necrosis factor receptor 1
AR Alpha1-adrenergic receptors
alpha1-ARs Alpha1-adrenergic receptors
beta 2AR Beta 2-adrenergic receptors
CR1 C3b-C4b receptors
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  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • multiple vascular tumor
    ´Ù¹ß¼º Ç÷°ü Á¾¾ç
  • nasopharyngeal tumor
    ºñ ÀεΠÁ¾¾ç
  • nerve tumor
    ½Å°æ Á¾¾ç
  • neuroectodermal tumor
    ½Å°æ ¿Ü¹è¿± Á¾¾ç
  • neuroendocrine tumor
    ½Å°æ ³»ºÐºñÁ¾
  • neuroglial tumor
    ½Å°æ±³ Á¾¾ç
  • nevoid tumor
    ¸ð¹Ý¾ç Á¾¾ç
  • nonclassifed tumor
    ºÐ·ùµÇÁö ¾Ê´Â Á¾¾ç
  • nonodontogenic malignant tumor jaw
    ºñÄ¡¾Æ¼º ¾Ç¼º Á¾¾ç
  • odontogenic mixed tumor
    Ä¡¿ø È¥ÇÕ Á¾¾ç
  • ovarian tumor
    ³­¼Ò Á¾¾ç
    ³­¼Ò¿¡¼­ »ý±â´Â Á¾¾ç. ³­¼Ò´Â ÀÎüÀÇ Àå±â Áß¿¡¼­ °¡Àå ¸¹Àº Á¾·ùÀÇ Á¾¾çÀÌ ¹ß»ýÇÏ´Â ±â°üÀÌ¸ç ±× ºÐ·ù¹ýµµ ´Ù¾çÇØ, ¿©·¯ °¡Áö À̸§À¸·Î ºÒ¸°´Ù. ÀÓ»óÀûÀ¸·Î´Â ¾ç¼º, ¾Ç¼º, Áß°£¼ºÀÇ ¼¼ °¡Áö·Î ´ëº°µÇÁö¸¸ °¨º°ÀÌ °ï¶õÇÑ °æ¿ìµµ ÀÖ´Ù. ´ëü·Î Ãæ½ÇºÎ°¡ ÀüÇô ¾ø´Â ¼ø³¶Æ÷¼ºÀÇ °ÍÀ» ³¶Æ÷¼º Á¾¾çÀ̶ó ÇÏ¸ç ¾ç¼ºÀÌ´Ù. Ãæ½ÇºÎ·Î µÇ¾î ÀÖ´Â °æ¿ì¸¦ Ãæ½Ç¼º Á¾¾çÀ̶ó Çϸç, ³¶Æ÷ºÎ¿Í Ãæ½ÇºÎ°¡ ¼¯¿© ÀÖ´Â °æ¿ì¸¦ ¹ÝÃæ½Ç¼º Á¾¾çÀ̶ó Çϴµ¥ ÀÌ µÎ °¡Áö¸¦ ÇÕÃļ­ Ãæ½Ç¼º Á¾¾çÀ̶ó ÇÑ´Ù.
  • papillomatous tumor
    À¯µÎ¼º Á¾¾ç
  • paratesticular tumor
    °íȯ¹æ Á¾¾ç
  • pea-size tumor
    °­³²Äá Å©±âÀÇ Á¾¾ç
  • peripapillary tumor
    À¯µÎ ÁÖÀ§ Á¾¾ç
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
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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    ±¸ºÐ/º¸Çè±Þ¿©
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