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"bacterial cell protein"¿¡ ´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: 13
  • ¿µ¹®
    ÇѱÛ
  • chromophobic cell
    »ö¼Ò¾Èµê¼¼Æ÷
  • duct cell carcinoma
    °ü¼¼Æ÷¾ÏÁ¾
  • dust cell
    ¸ÕÁö¼¼Æ÷
  • delayed cell-mediated reaction
    Áö¿¬¼¼Æ÷¸Å°³¹ÝÀÀ
  • delta cell
    µ¨Å¸¼¼Æ÷
  • dendritic cell
    °¡Áö¼¼Æ÷, ¼öÁö»ó¼¼Æ÷
  • dark cell
    ¾îµÒ¼¼Æ÷
  • daughter cell
    µþ¼¼Æ÷
  • differentiated cell
    ºÐÈ­¼¼Æ÷
  • diffuse large B-cell lymphoma
    ±¤¹üÀ§Å«B¼¼Æ÷¸²ÇÁÁ¾
  • diploid cell
    µÎ¹è¼öü¼¼Æ÷
  • diploid cell line
    µÎ¹è¼öü¼¼Æ÷°è, À̹èü¼¼Æ÷°è
  • diploid cell strain
    µÎ¹è¼öü¼¼Æ÷ÁÖ
  • decoy cell
    µðÄÚÀ̼¼Æ÷
  • effector cell
    ÀÛµ¿¼¼Æ÷
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 13
  • ¿µ¹®
    ÇѱÛ
  • dark cell
    ¾îµÒ¼¼Æ÷
  • daughter cell
    µþ¼¼Æ÷
  • dendritic cell
    °¡Áö¼¼Æ÷
  • differentiated cell
    ºÐÈ­¼¼Æ÷
  • diploid cell
    µÎ¹è¼öü¼¼Æ÷
  • duct cell carcinoma
    °ü¼¼Æ÷¾ÏÁ¾
  • dust cell
    ¸ÕÁö¼¼Æ÷
  • effector cell
    ÀÛµ¿¼¼Æ÷
  • egg cell
    ³­¼¼Æ÷, ¾Ë¼¼Æ÷
  • endothelial cell
    ³»ÇǼ¼Æ÷
  • enterochromaffine cell
    âÀÚģũ·Ò¼¼Æ÷, âÀÚÅ©·Òģȭ¼¼Æ÷
  • eosinophilic cell
    È£»ê¼¼Æ÷
  • ependymal cell
    ³ú½Ç¸·¼¼Æ÷
  • epidermal cell
    Ç¥ÇǼ¼Æ÷
  • epithelial cell
    »óÇǼ¼Æ÷
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 13
  • ¿µ¹®
    ÇѱÛ
  • adamantinoid basal cell carcinoma
    ¹ý¶û Á¾¾ç(ÛöÕË ðþåÆ) ±âÀú¼¼Æ÷¾Ï(Ðñî¼á¬øàäß)
  • adcc(antibody dependent cell mediated cytotoxicity)
    Ç×üÀÇÁ¸¼¼Æ÷¸Å°³¼¼Æ÷µ¶¼º(ù÷ô÷ëîðíá¬øàØÚË¿á¬øàÔ¸àõ)
  • adenoid basal cell carcinoma
    ¼±»ó(àÍßÒ) ±âÀú¼¼Æ÷¾Ï(Ðñî¼á¬øàäß)
  • adenoid squamous cell carcinoma
    ¼±»ó ÆíÆò »óÇǼ¼Æ÷(àÍßÒ ø·øÁ ß¾ù«á¬øà) ¾Ï
  • adult T Cell leukemia virus
    ¼ºÀÎ T ¼¼Æ÷ ¹éÇ÷º´ ¹ÙÀÌ·¯½º
  • adult T cell leukemia virus (HTLV)
    ¼ºÀÎT¼¼Æ÷ ¹éÇ÷º´ ¹ÙÀÌ·¯½º
  • adult t-cell leukemia/lymphoma
    ¼º¼÷ T-¼¼Æ÷ ¹éÇ÷º´/¸²ÇÁÁ¾(à÷âÙ¡­á¬øà ÛÜúìÜ»/¡­ðþ)
  • alpha cell
    ¾ËÆÄ¼¼Æ÷
  • alpha cell
    ¾ËÆÄ¼¼Æ÷(¡­á¬øà)
  • alpha cell tumor
    ¾ËÆÄ ¼¼Æ÷Á¾(¡­á¬øàðþ)
  • amacrine cell
    ¾Æ¸¶Å©¸° ¼¼Æ÷
  • amacrine cell
    ¹«Ãà»è¼¼Æ÷
  • ameboid cell
    ¾Æ¸Þ¹Ù¸ð¾ç¼¼Æ÷
  • aneuploid cell
    À̼ö¼º¼¼Æ÷
  • anitschkow cell
    ¾Æ´ÏÄ¡ÄÚ¿ì¼¼Æ÷(¡­á¬øà)
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 13
  • ¿µ¹®
    ÇѱÛ
  • outer membrane protein
    ¿Ü¸·´Ü¹éÁú
  • p69 protein
    p69´Ü¹é(¡­Ó±ÛÜ)
  • pancreas,protein secertion pathway
    ´Ü¹éÁúºÐºñ°æ·Î(Ó±ÛÜòõÝÂÝôÌèÖØ)
  • penicillin binding protein (PBP)
    Æä´Ï½Ç¸° °áÇմܹéÁú
  • periplasmic binding protein
    ¿øÇüÁú¸· ÁÖÀ§°ø°£ °áÇմܹéÁú
  • perturbation of protein
    ´Ü¹éÁúº¯ÅÂ(Ó±ÛÜòõ ܨ÷¾).
  • pilus protein antigen
    ¼¶¸ð´Ü¹éÁúÇ׿ø
  • plasma protein
    Ç÷Àå´Ü¹é(Áú)
  • plasma protein
    Ç÷Àå´Ü¹éÁú(úìíìÓ±ÛÜòõ).
  • plasma protein binding
    Ç÷Àå´Ü¹é°áÇÕ.
  • plasma protein fraction =PCC
    Ç÷Àå´Ü¹éºÐȹ
  • principal outer membrane protein (POMP)
    ÁÖ¿ä¿Ü¸·´Ü¹éÁú
  • prosthetic protein
    ¹èÇÕ¼º ´Ü¹é(ÛÕùêàõÓ±ÛÜ).
  • protein
    ´Ü¹éÁú
  • protein
    ´Ü¹é(Ó±ÛÜ), ´Ü¹éÁú(Ó±ÛÜòõ)
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 13
  • ¿µ¹®
    ÇѱÛ
  • Intermitotic cell
    ºÐ¿­»çÀ̱⼼Æ÷
    [¿¾ ¿ë¾î] °£±â¼¼Æ÷
  • Epitheloid muscle cell
    »óÇǼº±ÙÀ°¼¼Æ÷
    [¿¾ ¿ë¾î] »óÇǾç±Ù¼¼Æ÷
  • Chromophilic cell
    »ö¼Òµë¼¼Æ÷
    [¿¾ ¿ë¾î] »ö¼ÒÈ£¼º¼¼Æ÷
  • Pigment cell
    »ö¼Ò¼¼Æ÷
    [¿¾ ¿ë¾î] »ö¼Ò¼¼Æ÷
  • Chromophobic cell
    »ö¼Ò¾Èµë¼¼Æ÷
    [¿¾ ¿ë¾î] »ö¼ÒÇø¼º¼¼Æ÷
  • Cell inclusions
    ¼¼Æ÷Æ÷ÇÔ¹°
    [¿¾ ¿ë¾î] ¼¼Æ÷Æ÷ÇÔ¹°
  • Purkinje cell
    ½ÉÀåÀüµµ±ÙÀ°¼¼Æ÷
    [¿¾ ¿ë¾î] ½ÉÀåÀÚ±ØÀüµµ¼¼Æ÷
  • Purkinje cell
    ½ÉÀåÀüµµ±ÙÀ°¼¼Æ÷
    [¿¾ ¿ë¾î] Ǫ¸£Å²¿¹¼¼Æ÷
  • Exocrine cell
    ¿ÜºÐºñ¼¼Æ÷
    [¿¾ ¿ë¾î] ¿ÜºÐºñ¼¼Æ÷
  • Villous muscle cell
    À¶¸ð±ÙÀ°¼¼Æ÷
    [¿¾ ¿ë¾î] À¶¸ð±Ù¼¼Æ÷
  • Chief cell
    À¸¶ä¼¼Æ÷
    [¿¾ ¿ë¾î] ÁÖ¼¼Æ÷
  • Milk secreting cell
    Á¥ºÐºñ¼¼Æ÷
    [¿¾ ¿ë¾î] À¯¼¼Æ÷
  • Purkinje cell
    Á¶·Õ¹Ú¼¼Æ÷
    [¿¾ ¿ë¾î] Purkinje¼¼Æ÷
  • Ovoid cell
    Ÿ¿ø¼¼Æ÷
    [¿¾ ¿ë¾î] ³­¿øÇü¼¼Æ÷
  • Oxyphilic cell
    È£»ê¼º¼¼Æ÷
    [¿¾ ¿ë¾î] »êÈ£¼º¼¼Æ÷
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 13
  • ¿µ¹®
    ÇѱÛ
  • heat shock protein
    ¿­(æð)
  • heat stable protein
    ¿­¾ÈÁ¤ ´Ü¹éÁú
  • helix-destabilizing protein
    ³ª¼± ºÒ¾ÈÁ¤È­ ´Ü¹éÁú(Õ¢àÁÝÕäÌïÒûùÓ±ÛÜòõ)
  • heme protein
    Èû´Ü¹éÁú(Ó±ÛÜòõ)
  • high-potential iron protein
    °íÀüÀ§(ÍÔï³êÈ) ö´Ü¹éÁú(ôÑÓ±ÛÜòõ)
  • homologous protein
    µ¿Á¾´Ü¹éÁú(ÔÒðúÓ±ÛÜòõ)
  • hybrid protein
    Æ¢±â´Ü¹éÁú(Ó±ÛÜòõ)
  • hypro-protein
    ÇÏÀÌÇÁ·Î´Ü¹éÁú(Ó±ÛÜòõ)
  • incomplete protein
    ºÒ¿ÏÀü ´Ü¹éÁú(ÝÕèÇîïÓ±ÛÜòõ)
  • inside-out protein
    ³»¿ÜÀüµµ ´Ü¹éÁú(Ò®èâï´ÓîÓ±ÛÜòõ)
  • internal protein
    ³»´Ü¹éÁú(Ò®Ó±ÛÜòõ)
  • intrinsic protein
    °íÀ¯ ´Ü¹éÁú(ͳêóÓ±ÛÜòõ)
  • in vitro protein synthesis
    ½ÃÇè°ü³» ´Ü¹éÁúÇÕ¼º(ãËúÐηҮ Ó±ÛÜòõùêà÷)
  • I protein
    I ´Ü¹éÁú(Ó±ÛÜòõ)
  • I region-associated protein
    I ºÎÀ§¿¬°ü(Ý»êÈ֤μ) ´Ü¹éÁú(Ó±ÛÜòõ)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 13
SC conditioned stimulus; sacrococcygeal; Sanitary Corps; scalenus [muscle]; scapula; Schwann cell; scia...
SCA self-care agency; severe congenital anomaly; sickle-cell anemia; single-camera autostereoscopic [ima...
SCC self-care center; sequential combination chemotherapy; services for crippled children; short-course ...
SCM Schwann cell membrane; sensation, circulation, and motion; Society of Computer Medicine; soluble cyt...
TCE T-cell enriched; tetrachlorodiphenyl ethane; trichloroethylene T-cell thymus-derived cell
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 13
AECA Anti-endothelial cell antibodies
RBC Anti-red blood cell
SRBC Anti-sheep red blood cell
ADCC Antibody Dependent Cell Cytotoxicity
ADCC Antibody Dependent Cell-Mediated Cytotoxicity
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 13
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • cutaneous B cell lymphoma
    ÇǺΠB ¼¼Æ÷ ¸²ÇÁÁ¾
  • cylindrical cell
    ¿øÁÖÇü ¼¼Æ÷, ¿øÁÖ»ó ¼¼Æ÷
  • daughter cell
    µþ ¼¼Æ÷, ³¶ ¼¼Æ÷
    1. ¸ð¼¼Æ÷°¡ ºÐ¿­ÇÏ¿© »ý±â´Â ¼¼Æ÷. 2. ¼¼Æ÷ ºÐ¿­ÀÇ °á°ú·Î »ý±ä 2°³ÀÇ »õ·Î¿î ¼¼Æ÷. ºÐ¿­ ÀüÀÇ ¸ð¼¼Æ÷¿¡ ´ëÇØ¼­ µþ ¼¼Æ÷¶ó°í ÇÏ¸ç ³¶ ¼¼Æ÷¶ó°íµµ ÇÑ´Ù. µþ ¼¼Æ÷ÀÇ ÇÙÀº 2°³°¡ ¼­·Î ³»¿ëÀÌ °°À¸¸ç, ¶Ç ¸ð¼¼Æ÷ÀÇ ÇÙ°úµµ ¶È°°Àºµ¥ ¼¼Æ÷ÁúÀº ¾à°£ ´Ù¸£´Ù. °¨¼öºÐ¿­ÀÇ Á¦1ºÐ¿­¿¡ ÀÇÇÏ¿© »ý±â´Â 2°³ÀÇ µþ¼¼Æ÷ÀÇ ¿°»öü ¼ö´Â ¸ð¼¼Æ÷ÀÇ ¹Ý¼ö·Î µÇ¾î ÀÖ´Â °ÍÀÌ º¸ÅëÀÌ´Ù.
  • Deiters cell
    ´ÙÀÌÅ׸£½º ¼¼Æ÷
    ³»ÀÌÀÇ ´ÞÆØÀ̰ü ³»ÀÇ ±âÀú¸· À§¿¡ ÀÖ´Â ÄÚ¸£Æ¼±â¸¦ ±¸¼ºÇÏ´Â ÀÏÁ¾ÀÇ ¼¼Æ÷. Á÷Á¢ ¼Ò¸® °¨°¢À» ¹Þ´Â ¿ÜÀ¯¸ð¼¼Æ÷ °£±ØÀ» ä¿ì°í ÀÖ´Â ÁöÁö¼¼Æ÷.
  • delta cell tumor
    µ¨Å¸ ¼¼Æ÷ Á¾¾ç
    ¼Ò¸¶Å佺ŸƾÀ» ºÐºñÇÏ´Â Á¾¾çÀ¸·Î ¼Ò¸¶Å佺ŸƾÁ¾
  • diploid cell
    2¹èü ¼¼Æ÷
    Á¤»óÀÇ 2¹è¼ºÀÇ ¿°»öü, ¶Ç´Â 2°³ÀÇ ÇÙÀ» °¡Áø ¼¼Æ÷. Á¤»óÀÎ Á¶Á÷ ¾È¿¡¼­´Â ¼öÁ¤¶õÀ̳ª ¼¶À¯¾Æ¼¼Æ÷¿¡¼­ º¼ ¼ö ÀÖ´Ù. ÀΰøÀûÀ¸·Î´Â HVJ³ª NDA µîÀÇ ¹ÙÀÌ·¯½º³ª
  • direct cell division
    Á÷Á¢ ¼¼Æ÷ ºÐ¿­
  • disintegrated cell
    ºØ±« ¼¼Æ÷
  • dorsal horn cell
    Èİ¢ ¼¼Æ÷, ¹è°¢ ¼¼Æ÷
  • dorsal horn pain transmission cell
    ¹è°¢ ÅëÁõ Àü´Þ ¼¼Æ÷, ¹è°¢ µ¿Åë Àü´Þ ¼¼Æ÷
  • ductal cell
    µµ°ü ¼¼Æ÷
  • 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.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 13
chemotactic protein methylesterase <enzyme> Demethylates methyl-accepting chemotaxis proteins
Registry number: EC 3.1.1.-
Synonym: chemotactic methylesterase, carboxymethylesterase of chemotaxis, cheb methylesterase
(26 Jun 1999)
peripheral membrane protein <protein> Membrane proteins that are bound to the surface of the membrane and not integrated into the hydrophobic region. Usually soluble and were originally thought to bind to integral proteins by ionic and other weak forces (and could therefore be removed by high ionic strength, for example). However, it is now clear that some peripheral membrane proteins are covalently linked to molecules that are part of the membrane bilayer (see acylated proteins and glypiation) and that there are others that fit the original definition but are perhps more appropriately considered proteins of the cytoskeleton (e.g. Band 4.1 and spectrin) or extracellular matrix (e.g. Fibronectin).
(18 Nov 1997)
peripheral protein <protein> A water-soluble protein that is loosely bound (by hydrogen bonds orelectrostatic forces) to a membrane.
(09 Oct 1997)
periplasmic protein disulfide oxidoreductase <enzyme> Isolated from haemophilus influenzae; may be required for assembly or folding of one or more disulfide-containing cell envelope proteins; ccmg isolated from paracoccus denitrificans
Registry number: EC 1.8.4.-
Synonym: por disulfide oxidoreductase, por gene product, periplasmic oxidoreductase, ccmg gene product
(26 Jun 1999)
ribose binding protein <protein> Periplasmic binding proteins of bacteria that interact either with the ribose transport system or with the methyl accepting chemotaxis protein MCP III (trg).
(18 Nov 1997)
ribosomal protein <protein> Proteins present within the ribosomal subunits. In prokaryotes there are 31 proteins in the large subunit and 21 in the small subunit. Eukaryotic subunits have 50 (large subunit) and 33 (small subunit) proteins.
(18 Nov 1997)
ribosomal protein s6 kinase <enzyme> A protein serine/threonine kinase which is involved in cell transformation by polyoma virus and is connected to the expression of igf2. The immunosuppressant rapamycin inhibits the activation of the kinase, leading to reduced translation of certain mRNAs and a decrease in protein synthesis.
Registry number: EC 2.7.10.-
(12 Dec 1998)
ribosomal protein S6 kinase kinase <enzyme> Isolated from unfertilised xenopus eggs; a 41 kD enzyme that is associated, in vivo, with phosphorylation on threonine and tyrosine residues and, in vitro, with phosphorylation on serine as well
Registry number: EC 2.7.1.-
Synonym: rsk kinase
(26 Jun 1999)
chk1 protein kinase <enzyme> A yeast protein kinase homolog, involved in cell-cycle arrest when DNA damage has occurred or when unligated DNA is present; named chk1 for checkpoint kinase; genbank af016582 (human), af016583 (murine)
Registry number: EC 2.7.1.-
Synonym: chk1 kinase, chk1 gene product, rad27 protein, rad27 gene product, hchk1 (human), mchk1 (murine), mammalian chk1
(26 Jun 1999)
green fluorescent protein <protein> A protein found in jellyfish which fluoresces, or glows green visible light when excited by UV light with a wavelength of 395 nanometres.
It can function as a biological marker when attached to other proteins. The structure of the protein is cylindrical with the glowing component, an amino acid complex called a fluorophore, in the middle of it.
(09 Oct 1997)
groel protein A chaperonin 60 heat-shock protein isolated from escherichia coli.
(12 Dec 1998)
groes protein A chaperonin 10 heat-shock protein isolated from escherichia coli.
(12 Dec 1998)
GTPase activating protein <molecular biology> Originally purified as a 125 kD protein from bovine brain (1044 amino acids), stimulates the GTPase activity of ras p21 and thereby switches it to the inactive state.
GAP may itself be regulated by phospholipids and by phosphorylation on a tyrosine residue by growth factor receptors (PDGF R, EGF R). The neurofibromatosis type 1 gene NF1) codes for a protein homologous to GAP. GAP has both SH2 and SH3 domains. Another example is sar 1 (from yeast).
(18 Nov 1997)
GTP-binding protein <molecular biology, protein> There are two main classes of G-proteins, the heterotrimeric G proteins that associate with receptors of the seven transmembrane domain superfamily and are involved in signal transduction and the small cytoplasmic G-proteins.
Regulatory proteins found in all cells. They are versatile molecular switches, involved in the control of a wide range of biological processes - protein synthesis, signal transduction pathways, growth and differentiation. They all act through a common molecular mechanism based on their ability to bind the guanine nucleotides GTP and GDP selectively and with high affinity.
Stimulatory G-proteins are permanently activated by cholera toxin, inhibitory ones by pertussis toxin. Transducin was one of the first of the heterotrimeric G-proteins to be identified.
The small G-proteins are a diverse group of monomeric GTPases that include ras, rab, rac and rho and that play an important part in regulating many intracellular processes including cytoskeletal organisation and secretion. Their GTPase activity is regulated by activators (GAPs) and inhibitors (GIPs) that determine the duration of the active state.
(12 Jul 2000)
RLK5-associated protein phosphatase <enzyme> Associated with serine-threonine receptor-like kinase, rlk5; from arabidopsis thaliana; composed of 3 domains, an amino-terminal signal anchor, a kinase interaction domain and a type 2c protein phosphatase catalytic domain; mw 65 kD; genbank u09505
Registry number: EC 3.1.3.-
Synonym: kapp, kinase-associated protein phosphatase
(26 Jun 1999)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 13
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 13
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 13
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 13
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 13
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