¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"Bone Morphogenetic Protein 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.
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • bone marrow needle
    °ñ¼ö¹Ù´Ã
  • bone marrow transplantation
    °ñ¼öÀ̽Ä(¼ú)
  • bone marrow transplantation retinopathy
    °ñ¼öÀ̽ĸÁ¸·º´(Áõ)
  • bone marrow-derived cell
    °ñ¼öÀ¯·¡¼¼Æ÷
  • bone matrix
    »À¹ÙÅÁÁú, °ñ±âÁú
  • bone mineral metabolism
    »À±¤¹°´ë»ç, °ñ±¤¹°Áú´ë»ç
  • bone pain
    »ÀÅëÁõ
  • bone peg
    »À¸ø, °ñÁ¤
  • bone resorption
    »ÀÈí¼ö, °ñÈí¼ö
  • bone scan
    »À½ºÄµ, °ñ½ºÄµ
  • bone scissors
    »À°¡À§
  • bone screw
    »À³ª»ç, °ñ³ª»ç
  • bone shaft
    »À¸öÅë, °ñ°£
  • bone stump
    »ÀÀ߸°³¡, »À¹Øµ¿, °ñÀý´Ü´Ü
  • brittle bone
    Ãë¾à»À
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • bone marrow blood
    °ñ¼öÇ÷¾×
  • bone marrow depression
    °ñ¼ö±â´É¾ïÁ¦
  • bone marrow needle
    °ñ¼ö¹Ù´Ã
  • bone marrow transfusion
    °ñ¼ö¼öÇ÷
  • bone marrow transplantation
    °ñ¼öÀ̽Ä(¼ú)
  • bone marrow function test
    °ñ¼ö±â´É°Ë»ç
  • bone marrow transplantation retinopathy
    °ñ¼öÀ̽ĸÁ¸·º´Áõ
  • bone marrow-derived cell
    °ñ¼öÀ¯·¡¼¼Æ÷
  • bone mineral metabolism
    »À±¤¹°´ë»ç, °ñ±¤¹°Áú´ë»ç
  • brittle bone
    (¢¡osteogenesis imperfecta) ºÒ¿ÏÀü»À¹ß»ý, ºÒ¿ÏÀü°ñÇü¼ºÁõ
  • cancellous bone
    (¢¡spongy bone) °¹¼Ø»À, ÇØ¸é»À
  • capitate bone
    ¾Ë¸Ó¸®»À
  • carpal bone
    ¼Õ¸ñ»À
  • cartilage bone
    ¿¬°ñ»À
  • collar bone
    (¢¡clavicle) ºøÀå»À, ¼â°ñ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • Bence Jones protein
    º¥½º-Á¸½º´Ü¹é.
  • Bence-Jones protein
    º¥½º-Á¸½º ´Ü¹éÁú
  • C protein
    C´Ü¹éÁú
  • C-Fos protein
    ¾¾-Æ÷½º´Ü¹é(Ó±ÛÜ)
  • C-reative protein =CRP
    C¹ÝÀÀ¼º ´Ü¹é(Áú).
  • C-reative protein =CRP
    [¸é¿ª] [ÀÓº´]C¹ÝÀÀ¼º ´Ü¹éÁú.
  • DNA-binding protein
    DNA °áÇմܹéÁú
  • G protein
    G ´Ü¹é(Ó±ÛÜ)
  • G-myeloma protein
    ¸é¿ª±Û·ÎºÒ¸° G-°ñ¼öÁ¾´Ü¹éÁú
  • Heat shock protein
    ¿­¼ï´Ü¹éÁú
  • Integral membrane protein
    ÅëÇÕ(÷Öùê) ¸·´Ü¹é(Ø­Ó±ÛÜ)
  • M protein
    M´Ü¹éÁú
  • M protein
    M´Ü¹é.
  • NPN= non protein nitrogen
    ºñ´Ü¹éÁú¼Ò.
  • POMP (principal outer membrane protein)
    ÁÖ¿ä¿Ü¸·´Ü¹éÁú
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • muscle protein
    ±Ù´Ü¹é(ÐÉÓ±ÛÜ).
  • myelin basic protein
    ¼öÃÊ(âÐÃÊ)¿°±â¼º ´Ü¹é
  • myelin basic protein
    ¸¶ÀÌ¿¤¸° ¿°±â´Ü¹éÁú
  • myelin basic protein antigen
    ¼öÃʱâÃʴܹé(âËôþÐñõ¨Ó±ÛÜ)Ç׿ø(ù÷ê«)
  • myeloma protein
    °ñ¼öÁ¾´Ü¹éÁú
  • myotonin-protein kinase
    ¹Ì¿ÀÅä´Ñ-´Ü¹é(Ó±ÛÜ) Ű³ªÁ¦
  • non-protein nitrogenous compound
    ºñ´Ü¹é(Áú)Áú¼ÒÈ­ÇÕ¹°
  • nonspecific protein therapy
    ºñƯÀ̼º ´Ü¹é¿ä¹ý.
  • nonstructural protein
    ºñ±¸Á¶ ´Ü¹é
  • nuclear protein antigen
    Çٴܹé(Áú)Ç׿ø
  • oligomeric protein
    ¿Ã¸®°í¸Ó´Ü¹éÁú.
  • original endotoxin protein
    ±Õ³»µ¶¼Ò´Ü¹éÁú.
  • outer membrane protein
    ¿Ü¸·´Ü¹éÁú
  • p69 protein
    p69´Ü¹é(¡­Ó±ÛÜ)
  • pancreas,protein secertion pathway
    ´Ü¹éÁúºÐºñ°æ·Î(Ó±ÛÜòõÝÂÝôÌèÖØ)
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 12 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • Inferior body of hyoid bone
    ¸ñ»Ô»À¾Æ·¡¸öÅë
    [¿¾ ¿ë¾î] ¼³°ñÇÏü
  • Superior body of hyoid bone
    ¸ñ»Ô»ÀÀ§¸öÅë
    [¿¾ ¿ë¾î] ¼³°ñ»óü
  • Hip bone
    º¼±â»À [°ü°ñ]
    [¿¾ ¿ë¾î] °ü°ñ
  • Bone tissue
    »ÀÁ¶Á÷
    [¿¾ ¿ë¾î] °ñÁ¶Á÷
  • Histogenesis of bone
    »ÀÁ¶Á÷¹ß»ý
    [¿¾ ¿ë¾î] °ñ¹ß»ý
  • Reticulofibrous bone tissue
    ¼¼¸Á¼¶À¯»ÀÁ¶Á÷
    [¿¾ ¿ë¾î] ¼¼¸Á¼¶À¯¼º°ñÁ¶Á÷
  • Cuboid bone
    ÀÔ¹æ»À
    [¿¾ ¿ë¾î] ÀÔ¹æ°ñ
  • Tuberosity of cuboid bone
    ÀÔ¹æ»À°ÅÄ£¸é
    [¿¾ ¿ë¾î] ÀÔ¹æ°ñÁ¶¸é
  • Pisiform bone
    Äá¾Ë»À
    [¿¾ ¿ë¾î] µÎ»ó°ñ
  • Long bone
    ±ä»À
    [¿¾ ¿ë¾î] Àå°ñ
  • Short bone
    ªÀº»À
    [¿¾ ¿ë¾î] ´Ü°ñ
  • Sponge bone
    ÇØ¸é»À
    [¿¾ ¿ë¾î] ÇØ¸é°ñ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • I region-associated protein
    I ºÎÀ§¿¬°ü(Ý»êÈ֤μ) ´Ü¹éÁú(Ó±ÛÜòõ)
  • iron protein
    ö´Ü¹éÁú(ôÑÓ±ÛÜòõ)
  • iron-sulfur protein
    ö-À¯È² ´Ü¹éÁú(ôÑ×¼üÜÓ±ÛÜòõ)
  • isoelectric protein
    µîÀü´Ü¹éÁú(Ôõï³Ó±ÛÜòõ)
  • isoionic protein
    µî(Ôõ)À̿ ´Ü¹éÁú(Ó±ÛÜòõ)
  • late protein
    ¸¸±â´Ü¹éÁú(عѢӱÛÜòõ)
  • leader protein
    ¼±µµ´Ü¹éÁú(à»ÓôÓ±ÛÜòõ)
  • leaky protein
    ´©Ãâ´Ü¹éÁú(שõóÓ±ÛÜòõ)
  • LETS protein
    LETS ´Ü¹éÁú(Ó±ÛÜòõ)
  • light-harvesting Chl a/b protein
    Áý±¤¼º¿±·Ïü(ó¢ÎÃàõç¨Öàô÷) a/b ´Ü¹éÁú(Ó±ÛÜòõ)
  • link protein
    ¿¬°á´Ü¹éÁú(֧̿ӱÛÜòõ)
  • lipid-globular protein mosaic model
    "ÁöÁú-±¸»ó´Ü¹éÁú(ò·òõϹßÒÓ±ÛÜòõ) , ¸ðÀÚÀÌÅ©¸ðµ¨"
  • liquid protein diet
    ¾×ü´Ü¹éÁú½Ä(äûô÷Ó±ÛÜòõãÝ)
  • low-potential iron protein
    ÀúÀüÀ§ ö´Ü¹éÁú(î¸ï³êÈôÑÓ±ÛÜòõ)
  • low-quality protein
    ÀúÁú´Ü¹éÁú(î¸òõÓ±ÛÜòõ)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 7
AC/BC air conduction/bone conduction [time ratio]
ADR activation, depression, repetition [in bone remodeling]; adrenodoxin reductase; Adriamycin; adverse ...
ANB avascular necrosis of bone
BA Bachelor of Arts; backache; bacterial agglutination; basilar artery; basion; benzyladenine; best amp...
BC Bachelor of Surgery [Lat. Baccal-aureus Chirurgiae]; back care; bactericidal concentration; basal ce...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 7
PTBR Peripheral-type benzodiazepine receptors
PDGFR Platelet Derived Growth Factor Receptors
PR Progestin receptors
PRL-R Prolactin receptors
PAR Protease activated receptors
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • bone resorption
    °ñ Èí¼ö
  • bone saw
    °ñ Åé
  • bone scissors
    °ñ °¡À§
  • bone shaft
    °ñ°£
  • bone spicule
    °ñ ¼Ò±Ø
  • bone structure
    °ñ°Ý, »À ±¸Á¶, °ñ ±¸Á¶
    µ¿¹°ÀÇ ¸öÀ» ÁöÅÊÇϰí üÇüÀ» Çü¼ºÇÏ´Â ±â°ü. ü°Ý ¶Ç´Â ÀÚ¼¼¸¦ ÁöÅÊÇϸç, ¿îµ¿ÀÇ Åä´ë°¡ µÇ°í, ³»ÀåÀÇ ¸ðµç ±â°üÀ» º¸È£ÇÏ´Â ¿ªÇÒÀ» ÇÑ´Ù. ôÃßµ¿¹°¿¡¼­´Â ±âº»ÀûÀ¸·Î °ñ°Ý¿¡ °øÅëÁ¡ÀÌ Àִµ¥, µÎ°ñ°ú ôÃß°¡ Áß½ÉÀ» ÀÌ·ç¸ç, °Å±â¿¡ »çÁö°ñÀÌ À̾îÁø´Ù. µ¿¹°ÀÇ Á¾·ù¿¡ µû¶ó¼­ °ñ°ÝÀÇ Çü»óÀ̳ª ¼ö·® µî¿¡´Â Â÷À̰¡ ÀÖ´Ù. °ñ°ÝÀÇ °áÇÕ ¹æ¹ý¿¡´Â ´ÙÀ½ÀÇ 3Á¾·ù°¡ ÀÖ´Ù. ¨ç °üÀý °áÇÕ : °ñ°ÝÀÇ ´ëºÎºÐÀº °üÀý·Î¼­ ¿òÁ÷À̵µ·Ï µÇ¾î ÀÖ´Ù. ¨è ºÀÇÕ : µÎ°³°ñÀº °ñ°ÝÀÇ °áÇպκÐÀÌ Åé´Ïó·³ µÇ¾î ÀÖ¾î Åé´Ï¹ÙÄû¸¦ ¸ÂÃá µíÀÌ °áÇյǾî ÀÖ´Ù. ¨é ¿¬°ñ °áÇÕ : Á¿ìÀÇ Ä¡°ñÀ̳ª ôÃß°ñ »çÀÌ¿¡´Â ¿¬°ñ Á¶Á÷ÀÌ ÀÖ¾î ±×°ÍÀÌ °ñ°Ý°ú °ñ°ÝÀ» °áÇÕ½ÃŲ´Ù.
  • bone substance
    °ñÁú
  • bone swedging
    °ñ ¾ÐÀÎ
  • bone tissue
    »À Á¶Á÷, °ñ Á¶Á÷
  • bone tuberculosis
    °ñ °áÇÙ
    »À¿¡ ¹ß»ýÇÏ´Â °áÇÙÁõ. ÁÖ·Î Æó °áÇÙ¿¡¼­ 2Â÷ °¨¿°¿¡ ÀÇÇØ Ç÷Ç༺À¸·Î ¹ß»ýÇϰųª, ±ÙÁ¢ Àå±â·ÎºÎÅÍ ¿¬¼ÓÀûÀ¸·Î ħ¹üµÇ¾î ¹ß»ýÇÏ´Â °æ¿ì°¡ ¸¹°í, ¿ø¹ß¼ºÀÎ °ÍÀº µå¹°´Ù. °¡Àå ¸¹ÀÌ ¹ß»ýÇÏ´Â ºÎÀ§´Â Àå°ü »ó°ñÀÇ ´ÜºÎ¿Í Áß°£ºÎÀ̸ç û³â ¹× Àå³âÃþ¿¡ ¸¹´Ù. °ñ¼ö°¡ ħ¹üµÇ¸é °ñ¼ö ¼Ó¿¡ °áÇÙ º´¼Ò¸¦ Çü¼ºÇÏ¿© ÁÖÀ§ÀÇ °ñ Á¶Á÷À» ÆÄ±«ÇÏ°í ¸¶Ä§³»´Â ÇѼº ³ó¾çÀ» ÀÏÀ¸Å²´Ù. °ñ¸·ÀÌ Ä§¹üµÇ¸é °ñ¸éÀ» ħ½ÄÇÏ¿© Ä«¸®¿¡½º
  • bone tumor
    °ñ Á¾¾ç
    óÀ½¿¡ »À¿¡ ¹ß»ýÇÏ´Â Á¾¾ç. ´Ù¸¥ ºÎÀ§¿¡¼­ ¾ÏÀÌ ÀüÀÌÇÏ´Â Àϵµ ÀÖÀ¸³ª, ´ëºÎºÐÀº Á¶°ñ¼¼Æ÷³ª Á¶Á÷ÀÇ ÀÌ»ó Áõ½Ä¿¡ ÀÇÇÏ¿© »ý±ä´Ù. °ñ Á¶Á÷ ÀÚü¿¡¼­ ¹ß»ýÇÏ´Â Á¾¾çÀ¸·Î´Â °ñÁ¾, ¿¬°ñÁ¾ÀÌ ÀÖ°í, »À¿¡ Æ÷ÇÔµÈ °áÇÕÁ¶Á÷¿¡¼­ ¹ß»ýÇÏ´Â ¼¶À¯Á¾, Ç÷°ü¿¡¼­ ¹ß»ýÇÏ´Â Ç÷°üÁ¾, °ñ¼ö¿¡¼­ ¹ß»ýÇÏ´Â °ñ¼öÁ¾ÀÌ ÀÖ´Ù. °ñ¼öÁ¾À» Á¦¿ÜÇϰí´Â ¸ðµÎ ¾ç¼º Á¾¾çÀ¸·Î »ý¸íÀÇ À§ÇèÀÌ µû¸£´Â ÀÏÀº ¾ø°í °ÅÀÇ Å¸°¢ ¼Ò°ß
  • bone turnover
    °ñ ±³Ã¼
  • bone-marrow blood transfusion
    °ñ¼ö ¼öÇ÷
    °æ°ñ°ú Èä°ñÀÇ °ñ¼ö¿¡ Ç÷¾×À» ÁÖÀÔÇÏ´Â ¼öÇ÷ÀÇ º¯¹ý. Ç×»ó ¾²´Â Á¤¸Æ ³» ¼öÇ÷·Î´Â °¨¼ö¼ºÀÌ Áö³ªÄ¡°Ô °­Çϰųª ¸öÀÌ ºñ¸¸ÇÏ¿© Á¤¸ÆÀ» ã±â ¾î·Á¿î ȯÀÚ ¶Ç´Â À¯¾Æ¸¦ ´ë»óÀ¸·Î ÇÒ °æ¿ì ÀÌ ¹æ¹ýÀ¸·Î ¼öÇ÷ÇÒ ¶§°¡ ÀÖ´Ù. ¶Ç ¹éÇ÷º´À̳ª Àç»ýºÒ·®¼º ºóÇ÷ ȯÀÚ¿¡°Ô´Â ÀÌ ¹æ¹ýÀÌ Á¤¸Æ ¼öÇ÷º¸´Ù ¶Ù¾î³­ È¿°ú°¡ ÀÖ´Ù´Â °ßÇØµµ ÀÖ´Ù. ¹æ¹ýÀº °ñ¼ö õÀÚ¸¦ ÇÏ¿© Á¡Àû ÀåÄ¡ ¶Ç´Â ´ëÇü ÁÖ»ç±â·Î äÇ÷ÇÑ Ç÷¾×À» °ñ¼ö ³»¿¡ ÁÖÀÔÇÑ´Ù. ´Ù·® ¼öÇ÷ÀÌ °¡´ÉÇÏÁö¸¸, ±¹ºÎ ÇÇºÎ¿Í °ñ¸·¿¡ ±¹¼Ò¸¶Ã븦 ÇØ¾ß ÇÒ Çʿ䰡 ÀÖ´Ù. ±×¸®°í Á¤¸Æ ¼öÇ÷º¸´Ù ½Ã°£ÀÌ °É¸®°í ¼¼½ÉÇÑ ÁÖÀǰ¡ ÇÊ¿äÇϸç, ȯÀÚ¿¡°Ô °íÅëÀ» Áְųª, ³Ê¹« »¡¸® ÁÖÀÔÇÏ¸é ±¹¼Ò¿¡ ÅëÁõÀ» ÁÖ´Â µîÀÇ °áÁ¡ÀÌ ÀÖ´Ù.
  • bone-salt
    °ñ¿°
    °ñ³»ÀÇ ÁÖ¿ä È­ÇÕ¹°·Î¼­ ±³¿øÁúÀ» ÇÔÀ¯ÇÑ ±³¿ø¼¶À¯ÀÇ °ñ ±âÁú³»¿¡ ÀÛÀº °áÁ¤À¸·Î¼­ Ä§ÂøµÇ¾î ÀÖ´Ù. ÀÚ¿¬°è¿¡ Á¸ÀçÇÏ´Â ºÒ¼Ò ÀÎȸ¼®°ú À¯»çÇϳª, °ñ¿°Àº F°¡ OH·Î ġȯµÈ ¼ö»êÀÎȸ¼®À̶ó°í »ý°¢µÈ´Ù.
  • brush bone
    ¼âÀÚ¿¬
    ¼¼Æ÷ Ç¥¸éÀÌ ºÐÈ­µÈ °ÍÀ¸·Î¼­, Ç¥¸éÀûÀ» Å©°Ô Áõ´ë½ÃŰ´Â ¹Ì¼¼ÇÑ ¿øÅë»ó µ¹±â·Î ±¸¼ºµÇ¾î ÀÖ´Ù. ƯÈ÷ ôÃßµ¿¹° ¼¼´¢°üÀÇ ±ÙÀ§ ±¼°îºÎ »óÇǼ¼Æ÷³ª Àå°ü »óÇǼ¼Æ÷¿¡¼­ Àß ¹ß´ÞµÇ¾î ÀÖ´Ù.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
receptors, immunologic Cell surface molecules on cells of the immune system that specifically bind surface molecules or messenger molecules and trigger changes in the behaviour of cells. Although these receptors were first identified in the immune system, many have important functions elsewhere.
(12 Dec 1998)
receptors, insulin Cell surface proteins that bind insulin and trigger intracellular changes which influence the behaviour of cells. The best understood physiological consequence of insulin receptor activation is increased transport of glucose into most cells, which controls the rate of carbohydrate metabolism. The insulin receptor is a multifunctional protein complex that has intrinsic tyrosine kinase activity and is capable of autophosphorylation.
(12 Dec 1998)
receptors, insulin-like-growth factor I Specific proteins on or in cells to which insulin-like growth factor I (somatomedin c) binds and thereby modifies the function of the cells. These receptors contain transmembrane and cytosolic domains, bind igf-I preferentially, and have high-affinity sites for igf-II. The alpha-subunit has a mw of 130 kD and the beta subunit possesses tyrosine kinase activity.
(12 Dec 1998)
receptors, insulin-like-growth-factor II Specific proteins on or in cells to which insulin-like growth factor II and mannose-6-phosphate bind and thereby modify the function of the cells. These receptors have a mw of 250 kD and possess no tyrosine kinase activity.
(12 Dec 1998)
receptors, interferon Specific molecular sites or structures on or in cells with which interferons react or to which they bind in order to modify the function of the cells. Interferons exert their pleiotropic effects through two different receptors. Alpha- and beta-interferon crossreact with common receptors, while gamma-interferon initiates its biological effects through its own specific receptor system.
(12 Dec 1998)
receptors, interleukin Cell surface proteins that bind interleukins and trigger intracellular changes influencing the behaviour of cells.
(12 Dec 1998)
receptors, interleukin-1 Specific molecular sites or structures on cells with which interleukin-1 reacts or to which it binds to modify the function of the cells. The il-1 receptor on T-lymphocytes and fibroblasts is composed of a single polypeptide chain that binds both il-1 alpha and il-1 beta. The molecular weight of this high-affinity receptor is believed to be 80 kD.
(12 Dec 1998)
receptors, interleukin-2 Receptors present on activated t- and B-cells as a complex consisting of a 55 kD peptide, which reacts with the anti-tac monoclonal antibody, and a 75 kD non-tac interleukin-2-binding peptide. The receptor is present in two forms, one with a very high affinity and the other with low affinity for il-2. The high-affinity form appears to mediate exclusively the growth-promoting response to il-2. The receptor is present in large numbers on resting HTLV-I leukaemia cells, but not on normal resting cells.
(12 Dec 1998)
receptors, interleukin-3 Phosphotyrosine-containing proteins, mw 140 kD. They form a stable complex with interleukin-3 with an apparent mass of 170 kD. They are found on a variety of cells and activate interleukin-3.
(12 Dec 1998)
receptors, interleukin-4 Receptors present on a wide variety of haematopoietic and non-haematopoietic cell types and various human tumours. Two forms of the receptor have been described, soluble and membrane-bound. Low affinity and high affinity receptors for il-4 have been reported.
(12 Dec 1998)
receptors, interleukin-6 <chemical> Receptors present on t cells, mitogen-activated B-cells, peripheral monocytes, and some macrophage- and B-cell-derived tumour cell types. The receptor is a strongly glycosylated protein of 80 kD and a length of 468 amino acids.
Pharmacological action: growth inhibitors.
(12 Dec 1998)
receptors, invertebrate peptide Cell surface receptors for invertebrate peptide hormones or neuropeptides.
(12 Dec 1998)
receptors, kainic acid Cell surface proteins that bind glutamate and directly gate ion channels. Kainic acid receptors were originally discriminated from other glutamate receptors by their affinity for the agonist kainic acid. Activation of kainic acid receptors is generally excitatory to cells. Subtypes have been cloned, and for some the traditional distinction from ampa receptors may not apply.
(12 Dec 1998)
receptors, laminin Glycoprotein molecules on the surface of cells that react with or bind to laminin whose function allows the binding of epithelial cells to the basement membrane. The molecular weight of this high-affinity receptor is 67 kD.
(12 Dec 1998)
receptors, ldl Receptors on the plasma membrane of nonhepatic cells that specifically bind ldl. The receptors are localised in specialised regions called coated pits. Hypercholesteraemia is caused by an allelic genetic defect of three types: 1) receptors do not bind to ldl; 2) there is reduced binding of ldl; and 3) there is normal binding but no internalization of ldl. In consequence, entry of cholesterol esters into the cell is impaired and the intracellular feedback by cholesterol on 3-hydroxy-3-methylglutaryl CoA reductase is lacking.
(12 Dec 1998)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 7
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 7
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
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