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"B cell receptors"¿¡ ´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
  • ethmoidal air cell
    ¹úÁý, »ç°ñºÀ¼Ò
  • ethmoidal cell
    ¹úÁý, »ç°ñºÀ¼Ò
  • eukaryotic cell
    ÁøÇÙ¼¼Æ÷
  • fat cell
    Áö¹æ¼¼Æ÷
  • fat-storing cell
    Áö¹æÀúÀå¼¼Æ÷
  • flagellated cell
    Æí¸ð¼¼Æ÷
  • flame cell
    ºÒ²É¼¼Æ÷
  • fluorescence activated cell sorter
    Çü±¤Ç¥Áö¼¼Æ÷ºÐ·ù±â
  • foam cell
    °Åǰ¼¼Æ÷
  • follicle cell
    1. ¼ÒÆ÷¼¼Æ÷ 2. ³­Æ÷¼¼Æ÷
  • follicular cell
    1. ¼ÒÆ÷¼¼Æ÷ 2. ³­Æ÷¼¼Æ÷
  • foreign body giant cell
    À̹°°Å´ë¼¼Æ÷
  • fusiform cell
    ¹æÃß¼¼Æ÷
  • G cell
    G¼¼Æ÷
  • Gaucher cell
    °í½¦¼¼Æ÷
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  • ¿µ¹®
    ÇѱÛ
  • ethmoidal air cell
    ¹úÁý»À¹úÁý, »ç°ñ¹úÁý
  • eukaryotic cell
    ÁøÇÙ¼¼Æ÷
  • fat cell
    Áö¹æ¼¼Æ÷
  • fat-storing cell
    Áö¹æÀúÀå¼¼Æ÷
  • flagellated cell
    Æí¸ð¼¼Æ÷
  • foam cell
    °Åǰ¼¼Æ÷
  • follicle cell
    ¼ÒÆ÷¼¼Æ÷, ³­Æ÷¼¼Æ÷
  • follicular cell
    (¢¡follicle cell) ¼ÒÆ÷¼¼Æ÷, ³­Æ÷¼¼Æ÷
  • foreign body giant cell
    À̹°°Å´ë¼¼Æ÷
  • fusiform cell
    (¢¡spindle cell) ¹æÃß¼¼Æ÷
  • ganglion cell
    ½Å°æÀý¼¼Æ÷
  • germ cell
    Á¾ÀÚ¼¼Æ÷, ¹è¾Æ¼¼Æ÷, »ý½Ä¼¼Æ÷
  • germinal cell
    Á¾ÀÚ¼¼Æ÷
  • ghost cell
    ¼¼Æ÷ÂßÀïÀÌ, À¯·É¼¼Æ÷
  • giant cell
    °Å´ë¼¼Æ÷
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 10
  • ¿µ¹®
    ÇѱÛ
  • argyrophil(e) cell
    ÀºÄ£È­¼º ¼¼Æ÷(ëÞöÑûúàõá¬øà)
  • arsenical basal cell carcinoma
    ºñ¼Ò¼º(Ý÷áÈàõ) ±âÀú¼¼Æ÷¾Ï
  • arteritis,giant cell of aorta
    ´ëµ¿¸Æ(ÓÞÔÑØæ)ÀÇ °Å¼¼Æ÷¼º(ËÝá¬øààõ)
  • free cell
    ÀÚÀ¯¼¼Æ÷(í»ë¦á¬øà).
  • functional cell
    ±â´É¼¼Æ÷(ѦÒöá¬øà).
  • funicular cell
    ÁÙ¼¼Æ÷, »è¼¼Æ÷(ßãá¬øà).
  • fusiform cell
    ¹æÃß¼¼Æ÷
  • fusiform endothelial cell
    ¹æÃß³»ÇǼ¼Æ÷
  • fusiform myoepithelial cell
    ¹æÃßÇü ±Ù»óÇÇ ¼¼Æ÷
  • fusiform myoepithelial cell
    ¹æÃß±ÙÀ°»óÇǼ¼Æ÷
  • fusion, cell
    ¼¼Æ÷À¶ÇÕ
  • gangliocyte =ganglion cell
    ½Å°æÀý¼¼Æ÷(¡­á¬øà).
  • ganglion cell =gangliocyte
    ½Å°æÀý¼¼Æ÷(¡­á¬øà).
  • ganglion cell layer
    ½Å°æÀý¼¼Æ÷Ãþ(¡­öµ).
  • ganglion cell layer
    ½Å°æÀý¼¼Æ÷Ãþ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 10
  • ¿µ¹®
    ÇѱÛ
  • cardiac muscle cell
    ½ÉÀå±ÙÀ°¼¼Æ÷
  • caterpillar cell
    ¸ðÃæ ¼¼Æ÷(Ù¾õùá¬øà)
  • cell
    ¼¼Æ÷(á¬øà)
  • cell
    ¼¼Æ÷
  • cell adhesion molecular deficiency
    ¼¼Æ÷À¯ÂøºÐÀÚ°áÇÌ
  • cell adhesion molecule
    ¼¼Æ÷ºÎÂøºÐÀÚ
  • cell adhesive matrix assay
    ¼¼Æ÷Á¡Âø±âÁúºÐ¼®
  • cell age
    ¼¼Æ÷¿¬·É
  • cell associated antigen
    ¼¼Æ÷¿¬°üÇ׿ø
  • cell bank
    ¼¼Æ÷ÀºÇà
  • cell body
    ¼¼Æ÷ü(á¬øàô÷)
  • cell color ratio
    (Àû)Ç÷±¸»ö¼Òºñ.
  • cell cooperation, T-B
    T¼¼Æ÷-B¼¼Æ÷Çùµ¿
  • cell count
    ¼¼Æ÷¼ö
  • cell culture
    ¼¼Æ÷¹è¾ç(á¬øàÛÆå×).
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  • ¿µ¹®
    ÇѱÛ
  • Interdental cell
    û°¢Ä¡¾Æ»çÀ̼¼Æ÷
    [¿¾ ¿ë¾î] ûġ°£¼¼Æ÷
  • Merkel`s cell
    Ã˰¢¼¼Æ÷
    [¿¾ ¿ë¾î] MerkelÃ˰¢¼¼Æ÷
  • Macula densa cell
    Ä¡¹Ð¹ÝÁ¡¼¼Æ÷
    [¿¾ ¿ë¾î] Ä¡¹Ð¹Ý¼¼Æ÷
  • Chromaffin cell
    ģũ·Ò¼¼Æ÷
    [¿¾ ¿ë¾î] Å©·Òģȭ¼¼Æ÷
  • Golgi cell
    Å«º°¼¼Æ÷
    [¿¾ ¿ë¾î] °ñÁö¼¼Æ÷
  • Large cell part
    Å«¼¼Æ÷ºÎºÐ
    [¿¾ ¿ë¾î] ´ë¼¼Æ÷ºÎ
  • Decidual cell
    Å»¶ô¸·¼¼Æ÷
    [¿¾ ¿ë¾î] Å»¶ô¸·¼¼Æ÷
  • Cuticular cell
    Åв®Áú¼¼Æ÷
    [¿¾ ¿ë¾î] ¸ð¼ÒÇǼ¼Æ÷
  • Matrix cell
    ÅйÙÅÁÁú¼¼Æ÷
    [¿¾ ¿ë¾î] ¸ð±âÁú¼¼Æ÷
  • Hair cell
    Åм¼Æ÷
    [¿¾ ¿ë¾î] À¯¸ð°¨°¢¼¼Æ÷
  • Juxtaglomerular cell
    Å丮°ç¼¼Æ÷
    [¿¾ ¿ë¾î] »ç±¸Ã¼¹æ¼¼Æ÷
  • Flagellated epithelial cell
    Æí¸ð»óÇǼ¼Æ÷
    [¿¾ ¿ë¾î] Æí¸ð»óÇǼ¼Æ÷
  • Squamous epithelial cell
    ÆíÆò»óÇǼ¼Æ÷
    [¿¾ ¿ë¾î] ÆíÆò»óÇǼ¼Æ÷
  • Squamous cell
    ÆíÆò¼¼Æ÷
    [¿¾ ¿ë¾î] ÆíÆò¼¼Æ÷
  • Phagocytic synovial cell
    Æ÷½ÄÀ±È°¼¼Æ÷
    [¿¾ ¿ë¾î] Ȱ¸·½Ä¼¼Æ÷
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 10
JGCT juvenile granulosa cell tumor; juxtaglomerular cell tumor
K cell killer cell
LC Laennec cirrhosis; Langerhans cell; late clamped; large chromophobe; lecithin cholesterol acyltransf...
LCC lactose coliform count; left circumflex coronary (artery); left common carotid; left coronary cusp; ...
LCCSCT large-cell calcifying Sertoli cell tumor
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 10
VCAM-1 1/vascular cell adhesion molecule-1
PBSC Peripheral Blood Stem Cell
AC Accessory cell
ACC Acinic cell carcinoma
ALCAM Activated leukocyte cell adhesion molecule
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 10
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • ductule cell
    ¼Ò°ü ¼¼Æ÷
  • ealry squamous cell calcinoma
    ÃÊ±â ÆíÆò»óÇÇ ¼¼Æ÷¾Ï
    ±¸°­ ³» °¡Àå ÈçÇÑ ¾Ç¼º ÁúȯÀ̰í Ä¡°úÀǻ簡 Ä¡·áÇÏ´Â ¸î ¾È µÇ´Â Ä¡¸íÀû ÁúȯÀÇ ÇϳªÀÌ´Ù. Çǰ³ »óÇÇ ¼¼Æ÷ÀÇ ¾Ç¼º ¾ÏÁ¾¼º Áõ½ÄÀÌ´Ù. ¹é¹ÝÁõÀ̶ó°í ÇÏ´Â ÀÓ»ó ¿ë¾î·Îµµ ºÒ¸®´Â ¼Ò»ó »óÇÇ ºñÈÄ¿Í µ¿ÀÏÇÑ º´¼Ò¸¦ º¸¿©ÁØ´Ù. °¡Àå ÈçÇÑ ¿øÀÎÀ¸·Î »ý°¢µÇ´Â °ÍÀº ½À°üÀûÀÎ Èí¿¬°ú ¾ËÄÝÀÌ´Ù. ±¸°­ Á¡¸·¿¡ ¼Ò»ó ¹é»ö ¹ÝÁ¡À» ¸¸µå´Âµ¥ ÀÌ´Â »ý¸®Àû °ú°¢È­¿Í ºñ½ÁÇÏ°Ô º¸ÀδÙ. º´¼Ò¸¦ °ÇÁ¶½ÃŲ ÈÄ ÀÚ¼¼È÷ °üÂûÇϸé ÀÌÇü¼º º´¼ÒÀÇ Ç¥¸éÀÌ ÀϹÝÀûÀ¸·Î ´õ °ÅÄ¥°í ÂÞ±ÛÂÞ±ÛÇÑ °ÍÀ» º¼ ¼ö ÀÖ´Ù.
  • educated T cell
    Ç׿øÀ¸·Î °¨ÀÛµÈ T ¼¼Æ÷
    In vivo ¶Ç´Â in vitro¿¡¼­ Ç׿ø ÀÚ±ØÀ» ¹Þ¾Æ ¸é¿ª ±âÀüÀ» ¹ßÇöÇÒ ¼ö ÀÖ´Â »óŰ¡ µÈ T ¼¼Æ÷ÀÌ´Ù. In vivo¿¡¼­´Â ÀϹÝÀûÀ¸·Î Ä¡»ç·®ÀÇ ¹æ»ç¼±À» Á¶»çÇÑ Áã¿¡ ´Ù¸¥ µ¿¹°·ÎºÎÅÍÀÇ Èä¼± ¼¼Æ÷¸¦ ÀÌÀÔÇÔ°ú µ¿½Ã¿¡ Ç׿øÀÚ±ØÀ» ÇÏ´Â ¹æ¹ýÀÌ »ç¿ëµÈ´Ù.
  • endosteal cell
    °ñ³» ¼¼Æ÷
    À§Ä¡¿¡ ÀÇÇØ º¯°æµÇ°í, È®ÀεǴ ¸Á»ó ¼¼Æ÷. °ñ ³»¸·Àº °ñ¼ö ±âÁúÀÌ ³óÃàµÈ »óÅ´Ù.
  • endothelial cell
    ³»ÇÇ ¼¼Æ÷
  • enkephalinergic cell
    ¿£ÄÉÆÈ¸°¼º ¼¼Æ÷
  • eosinophilic cell
    È£»ê±¸
  • epidermoid type cell
    À¯Ç¥ÇÇ ¼¼Æ÷
  • epithelioid cell
    »óÇÇ¾ç ¼¼Æ÷, À¯»óÇÇ ¼¼Æ÷
    °áÇÙ µîÀÇ À°¾Æ¼º ¿°Áõ Áúȯ¿¡ À־ À°¾Æ ¼Ó¿¡¼­ È®ÀÎÇÒ ¼ö ÀÖ´Â Á¶Á÷±¸ÀÇ È£Äª.
  • ethmoid cell
    »ç°ñ ¹úÁý, »ç°ñ ºÀ¼Ò
  • eukaryotic cell
    ÁøÇÙ ¼¼Æ÷
  • excretory cell
    ¹è¼³ ¼¼Æ÷
  • fat cell
    Áö¹æ ¼¼Æ÷
  • fetal liver cell
    ÅÂ¾Æ °£ ¼¼Æ÷
    ÅÂ¾Æ °£ ¼¼Æ÷, Á¶Ç÷ stem ¼¼Æ÷°¡ µé¾î ÀÖ°í, µû¶ó¼­ °¢Á¾ ¸é¿ª ¼¼Æ÷ÀÇ Àü±¸ ¼¼Æ÷¸¦ Æ÷ÇÔÇÑ´Ù. ÃÖ±Ù ¸é¿ªºÎÀüÀÇ Áúȯ, ¿¹¸¦ µé¸é ÁßÁñ º¹ÇÕ ¸é¿ª ºÎÀüÁõ¿¡¼­´Â Á¶Á÷ ÀûÇÕ °ñ¼ö¸¦ ¾òÁö ¸øÇÏ´Â °æ¿ì, 8ÁÖ ÀÌÀüÀÇ ÅÂ¾Æ °£¼¼Æ÷ÀÇ À̽ÄÀÌ ÀÌ·ç¾îÁ® Àå±â°£ÀÇ »ýÁ¸ ¿¹¸¦ º¼ ¼ö ÀÖ´Ù.
  • fibroma-theca cell tumor
    ¼¶À¯Á¾-³­Æ÷¸· ¼¼Æ÷Á¾
    ¼¶À¯¾Æ¼¼Æ÷³ª ³­Æ÷¸· ¼¼Æ÷·Î ±¸¼ºµÈ´Ù. ±¸¼º ¼¼Æ÷°¡ ´ëºÎºÐ ³­Æ÷¸· ¼¼Æ÷ÀÎ ÀÌ Á¾¾çÀº È£¸£¸óÀ» »ý»êÇÒ ¼ö ÀÕ´Ù. ±×·¯³ª ¼ø¼öÇÑ ³­Æ÷¸· ¼¼Æ÷Á¾Àº µå¹°°í ´ëºÎºÐ Á¾¾çÀº ÁÖ·Î ¼¶À¯¸ð¼¼Æ÷·Î ±¸¼ºµÇ¾î ÀÖÀ¸¸ç È£¸£¸óÀ» »ý»êÇÏÁö ¾Ê´Â´Ù. 90%¿¡¼­ ÇÑÂÊ ³­¼Ò¿¡¼­¸¸ ¹ß»ýÇÑ´Ù. Á¾¾çÀº ȸ¹é»öÀÌ¸ç °íÇüÀÌ°í ±¸ÇüÀÌ¸ç ´Ü´ÜÇÏ´Ù. Á¶Á÷ÇÐÀûÀ¸·Î ¼¶À¯¸ð¼¼Æ÷¿Í ÄݶóÁ¨ °áü Á¶Á÷À¸·Î ±¸¼ºµÇ¾î ÀÖÀ¸¸ç ³­Æ÷¸· ¼¼Æ÷°¡ È¥ÀçÇÒ ¼ö ÀÖ´Ù. ȯÀÚ´Â °ñ¹ÝÅë°ú °ñ¹Ý Á¾±« µîÀÇ ºñƯÀÌÀû Áõ»óÀ» È£¼ÒÇϰųª º¹¼ö°¡ ³ªÅ¸³¯ ¼ö ÀÖ´Ù. ³­Æ÷¸· ¼¼Æ÷Á¾Àº ¾Ç¼ºÀÌ ¾ø´Ù.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 10
receptors, platelet-derived growth factor Specific molecular sites or structures on cell membranes that react with platelet-derived growth factor, its analogs, or antagonists, to elicit or to inhibit the specific response of the cell to this factor. Pdgf binds with different affinities and specificities to two structurally related receptors, the alpha-receptor and the beta-receptor. Both of these receptors are transmembrane proteins with an intracellular, ligand-stimulatable protein kinase domain.
(12 Dec 1998)
receptors, polymeric immunoglobulin Specialised fc receptors (receptors, fc) for polymeric immunoglobulins, which mediate transcytosis of polymeric IgA and IgM into external secretions. They are found on the surfaces of epithelial cells and hepatocytes. After binding to IgA, the receptor-ligand complex undergoes endocytosis, transport by vesicle, and secretion into the lumen by exocytosis. Before release, the part of the receptor (secretory component) that is bound to IgA is proteolytically cleaved from its transmembrane tail.
(12 Dec 1998)
receptors, presynaptic Neurotransmitter receptors located on or near presynaptic terminals or varicosities. Presynaptic receptors which bind transmitter molecules released by the terminal itself are termed autoreceptors.
(12 Dec 1998)
receptors, progesterone Specific proteins found in or on cells of progesterone target tissues that specifically combine with progesterone. The cytosol progesterone-receptor complex then associates with the nucleic acids to initiate protein synthesis. There are two kinds of progesterone receptors, a and b. Both are induced by oestrogen and have short half-lives.
(12 Dec 1998)
receptors, prolactin Labile proteins on or in prolactin-sensitive cells that bind prolactin initiating the cells' physiological response to that hormone. Mammary casein synthesis is one of the responses. The receptors are also found in placenta, liver, testes, kidneys, ovaries, and other organs and bind and respond to certain other hormones and their analogs and antagonists. This receptor is related to the growth hormone receptor.
(12 Dec 1998)
receptors, prostaglandin Cell surface receptors that bind prostaglandins with high affinity and trigger intracellular changes which influence the behaviour of cells. Prostaglandin receptor subtypes have been tentatively named according to their relative affinities for the endogenous prostaglandins. They include those which prefer prostaglandin d2 (dp receptors), prostaglandin e2 (ep1, ep2, and ep3 receptors), prostaglandin f2-alpha (fp receptors), and prostacyclin (ip receptors).
(12 Dec 1998)
receptors, prostaglandin e Cell surface receptors which bind prostaglandins with a high affinity and trigger intracellular changes which influence the behaviour of cells. Prostaglandin e receptors prefer prostaglandin e2 to other endogenous prostaglandins. They are subdivided into ep1, ep2, and ep3 types based on their effects and their pharmacology.
(12 Dec 1998)
receptors, purinergic Cell surface proteins that bind purines with high affinity and trigger intracellular changes which influence the behaviour of cells. The best characterised classes of purinergic receptors in mammals are the p1 receptors, which prefer adenosine, and the p2 receptors, which prefer ATP or ADP.
(12 Dec 1998)
receptors, purinergic p1 A class of cell surface receptors that prefers adenosine to other endogenous purines. Purinergic p1 receptors are widespread in the body including the cardiovascular, respiratory, immune, and nervous systems. There are at least two pharmacologically distinguishable types (a1 and a2, or ri and ra). The methylxanthines, e.g., caffeine, bind to these receptors, but also have other unrelated effects.
(12 Dec 1998)
receptors, purinergic p2 A class of cell surface receptors for purines that prefer ATP or ADP over adenosine. P2 purinergic receptors are widespread in the periphery and in the central and peripheral nervous system. Subtypes have been proposed, usually designated p2 x, y, z, and t. P2x receptors may mediate fast synaptic transmission by ATP. The ADP-preferring p2t receptors in platelets stimulate aggregation.
(12 Dec 1998)
receptors, retinoic acid Proteins in the nucleus or cytoplasm that specifically bind retinoic acid or retinol and trigger changes in the behaviour of cells. Retinoic acid receptors, like steroid receptors, are ligand-activated transcription regulators. Several types have been recognised.
(12 Dec 1998)
receptors, sensory Specialised neurons or parts of neurons which transduce sensory information and relay it centrally. Included are receptors for stimuli outside the body (exteroceptors) as well as receptors for stimuli from within the body itself (interoceptors and proprioceptors). Sensory receptors may include accessory structures which condition (e.g., filter) the input received by the receptor neurons themselves.
(12 Dec 1998)
receptors, serotonin Cell-surface proteins that bind serotonin and trigger intracellular changes which influence the behaviour of cells. Several types of serotonin receptors have been recognised which differ in their pharmacology, molecular biology, and mode of action.
(12 Dec 1998)
receptors, sigma A class of cell surface receptors recognised by its pharmacological profile. Sigma receptors were originally considered to be opioid receptors because they bind certain synthetic opioids. However they also interact with a variety of other psychoactive drugs, and their endogenous ligand is not known (although they can react to certain endogenous steroids). Sigma receptors are found in the immune, endocrine, and nervous systems, and in some peripheral tissues.
(12 Dec 1998)
receptors, somatomedin Cell surface receptors that bind somatomedins and trigger intracellular changes which influence the behaviour of cells. Studies have disclosed two types of receptors for this family of peptide hormones. The type I receptor is homologous to the insulin receptor and has tyrosine kinase activity. The type II receptor is identical to the mannose-6-phosphate receptor which is important in trafficking of lysosomal enzymes.
(12 Dec 1998)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
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    ±¸ºÐ/º¸Çè±Þ¿©
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    ±¸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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