¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"single 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.
À̰ÍÀ» ¿øÇϼ̽À´Ï±î?
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • bipolar cell
    µÎ±Ø¼¼Æ÷
  • blast cell
    ¸ð¼¼Æ÷
  • blood cell
    Ç÷¾×¼¼Æ÷, Ç÷±¸
  • blood cell separator
    Ç÷±¸ºÐ¸®±â
  • bone marrow-derived cell
    °ñ¼öÀ¯·¡¼¼Æ÷
  • border cell
    °æ°è¼¼Æ÷, ¼Ó°æ°è¼¼Æ÷
  • balloon cell
    dz¼±¼¼Æ÷
  • balloon cell nevus
    dz¼±¼¼Æ÷¸ð¹Ý
  • bristle cell
    ¾ï¼¾Åм¼Æ÷, °­¸ð¼¼Æ÷
  • burr cell
    ¹«µòÅ鳯ÀûÇ÷±¸
  • ciliated cell
    ¼¶¸ð¼¼Æ÷
  • clear cell
    Åõ¸í¼¼Æ÷
  • clear cell acanthoma
    Åõ¸í¼¼Æ÷°¡½Ã¼¼Æ÷Á¾, Åõ¸í¼¼Æ÷±Ø¼¼Æ÷Á¾
  • clear cell adenocarcinoma
    Åõ¸í¼¼Æ÷»ù¾ÏÁ¾, Åõ¸í¼¼Æ÷¼±¾ÏÁ¾
  • clear cell carcinoma
    Åõ¸í¼¼Æ÷¾ÏÁ¾
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • beta cell
    º£Å¸¼¼Æ÷
  • bipolar cell
    µÎ±Ø¼¼Æ÷
  • blood cell
    Ç÷¾×¼¼Æ÷, Ç÷±¸
  • blood cell separator
    Ç÷±¸ºÐ¸®±â
  • bone marrow-derived cell
    °ñ¼öÀ¯·¡¼¼Æ÷
  • border cell
    °æ°è¼¼Æ÷, ¼Ó°æ°è¼¼Æ÷
  • bristle cell
    ¾ï¼¾Åм¼Æ÷, °­¸ð¼¼Æ÷
  • burr cell
    ¹«µòÅ鳯ÀûÇ÷±¸
  • cell bank
    ¼¼Æ÷ÀºÇà
  • nerve cell body
    ½Å°æ¼¼Æ÷ü
  • cell
    ¼¼Æ÷
  • cell culture
    ¼¼Æ÷¹è¾ç
  • cell cycle
    ¼¼Æ÷ÁÖ±â
  • cell death
    ¼¼Æ÷»ç
  • cell dedifferentiation
    ¼¼Æ÷¿ªºÐÈ­
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • Langerhans giant cell
    ¶û±×Çѽº°Å¼¼Æ÷
  • Langhans giant cell
    ¶û±×Çѽº°Å´ë¼¼Æ÷
  • Leydig cell
    ·¹À̵ðÈ÷ ¼¼Æ÷
  • Leydig cell adenoma
    ·¹À̵ðÈ÷¼¼Æ÷¼±Á¾
  • Leydig cell tumor
    ·¹À̵ðÈ÷¼¼Æ÷Á¾¾ç
  • Leydig s cell
    ¶óÀ̵ðÈ÷¼¼Æ÷.
  • MCH => mean cell hemoglobin
    Æò±ÕÀûÇ÷±¸Ç÷»ö¼Ò
  • MCHC => mean cell hemogiooln concentration
    Æò±ÕÀûÇ÷±¸Ç÷»ö¼Ò³óµµ
  • MCV => mean cell volume
    Æò±ÕÀûÇ÷±¸¿ëÀû
  • Merkel cell carcinoma
    ¸Þ¸£Ä̼¼Æ÷ ¾Ï(Á¾)
  • Mikulicz cell
    ¹ÌÄð¸®Áî ¼¼Æ÷
  • Muellers cell
    ¹Á·¯¼¼Æ÷, ºÎä»ì¾Æ±³¼¼Æ÷
  • NIH T cell
    NIH T¼¼Æ÷
  • Paget cell
    ÆÄÁ¬¼¼Æ÷
  • Purkinje s cell
    ǮŲ¿¹¼¼Æ÷.
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • iron porphyrin protein
    öÆ÷¸£ÇǸ°´Ü¹éÁú.
  • iron porphyrin protein
    ö(ôÑ)Æ÷¸£ÇǸ°´Ü¹éÁú(Ó±ÛÜòõ).
  • iron porphyrin protein enzymes
    öÆ÷¸£ÇǸ°´Ü¹éÈ¿¼Ò(¡­Ó±ÛÜý£áÈ).
  • iron-sulfur protein
    ÀüÀÚÀü´Þ ö-À¯È²´Ü¹éÁú
  • liver membrane protein
    °£¸·´Ü¹é
  • liver specific protein
    °£Æ¯À̴ܹé
  • low protein diet
    Àú´Ü¹é½Ä(î¸Ó±ÛÜãÝ).
  • maintenance protein
    À¯Áö´Ü¹éÁú(¡­Ó±ÛÜòõ).
  • major basic protein
    ÁÖ±âÀú´Ü¹é
  • major basic protein
    ÁÖ¿ä ±âÃʴܹé(ñ«é© Ðñõ¨Ó±ÛÜ)
  • matrix protein
    ±âÁú´Ü¹éÁú
  • membrane control protein
    ¸·Á¶Àý´Ü¹é
  • mitogen-activated protein kinase
    ¹ÌÅä°Õ Ȱ¼º ´Ü¹é ±Í³ªÁ¦(¡­ üÀàõ Ó±ÛÜ ¡­ )
  • monocyte chemotactant protein 1(mcp-1)
    ´Ü±¸È­ÇÐÁÖ¼º´Ü¹é(¡­ûùùÊñ«àõÓ±ÛÜ) 1 (MCP-1)
  • muscle protein
    ±Ù´Ü¹é(ÐÉÓ±ÛÜ).
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • Principal cell
    À¸¶ä¼¼Æ÷
    [¿¾ ¿ë¾î] ÁÖ¼¼Æ÷
  • Pancreatic endocrine cell
    ÀÌÀÚ³»ºÐºñ¼¼Æ÷
    [¿¾ ¿ë¾î] ÃéÀå³»ºÐºñ¼¼Æ÷
  • Pancreatic acinar cell
    ÀÌÀڿܺкñ¼¼Æ÷
    [¿¾ ¿ë¾î] ÃéÀå¼±¼¼Æ÷
  • Cuboidal epithelial cell
    ÀÔ¹æ»óÇǼ¼Æ÷
    [¿¾ ¿ë¾î] ÀÔ¹æ»óÇǼ¼Æ÷
  • Cuboidal cell
    ÀԹ漼Æ÷
    [¿¾ ¿ë¾î] ÀԹ漼Æ÷
  • Small cell part
    ÀÛÀº¼¼Æ÷ºÎºÐ
    [¿¾ ¿ë¾î] ¼Ò¼¼Æ÷ºÎ
  • Mucous cell
    Á¡¾×¼¼Æ÷
    [¿¾ ¿ë¾î] Á¡¾×¼¼Æ÷
  • Spermatogenic cell
    Á¤Àڹ߻ý¼¼Æ÷
    [¿¾ ¿ë¾î] Á¤Àڹ߻ý¼¼Æ÷
  • Purkinje cell layer
    Á¶·Õ¹ÚÃþ
    [¿¾ ¿ë¾î] Purkinje¼¼Æ÷Ãþ
  • Type I hair cell
    Á¶·Õ¹ÚÅм¼Æ÷
    [¿¾ ¿ë¾î] ¹è»ó¿¬Á¢¼¼Æ÷
  • Terminal glial cell
    Á¾¸»¾Æ±³¼¼Æ÷
    [¿¾ ¿ë¾î] Á¾¸»±³¼¼Æ÷
  • Central glial cell
    ÁßÃ߾Ʊ³¼¼Æ÷
    [¿¾ ¿ë¾î] Á߽ɽŰ汳¼¼Æ÷
  • Glial cell of central nervous system
    ÁßÃ߾Ʊ³¼¼Æ÷
    [¿¾ ¿ë¾î] ÁßÃß±³¼¼Æ÷
  • Mesothelial cell
    ÁßÇǼ¼Æ÷
    [¿¾ ¿ë¾î] ÁßÇǼ¼Æ÷
  • Cuticular cell
    Áý²®Áú¼¼Æ÷
    [¿¾ ¿ë¾î] ¼ÒÇǼ¼Æ÷
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
  • accelerator protein
    ÃËÁø´Ü¹éÁú (õµòäÓ±ÛÜòõ)
  • acyl-carrier protein
    ¾Æ½Ç¿î¹Ý ´Ü¹éÁú (ê¡ÚæÓ±ÛÜòõ)
  • ada protein
    ada ´Ü¹éÁú
  • adhesion protein
    ºÎÂø´Ü¹éÁú(ݾó·Ó±ÛÜòõ)
  • aldosterone-induced protein
    ¾Ëµµ½ºÅ×·ÐÀ¯µµ ´Ü¹éÁú(ë¯ÓôÓ±ÛÜòõ)
  • A myeloma protein
    °ñ¼öÁ¾´Ü¹éÁú(ÍéâÐðþÓ±ÛÜòõ) A
  • androgen-binding protein
    ¾Èµå·ÎÀü°áÇÕ(Ì¿ùê) ´Ü¹éÁú(Ó±ÛÜòõ)
  • animal protein factor
    µ¿¹°´Ü¹éÁúÀÎÀÚ(ÔÑÚªÓ±ÛÜòõì×í­)
  • anion-transport protein
    À½À̿¿î¹Ý(ê¡Úõ) ´Ü¹éÁú(Ó±ÛÜòõ)
  • antifreeze protein
    Ç×°áºù´Ü¹éÁú(ù÷̿޼ӱÛÜòõ)
  • antitumor protein
    Ç×Á¾¾ç ´Ü¹éÁú(ù÷ðþåËÓ±ÛÜòõ)
  • antiviral protein
    Ç×(ù÷) ¹ÙÀÌ·¯½º ´Ü¹éÁú(Ó±ÛÜòõ)
  • A protein
    A ´Ü¹éÁú(Ó±ÛÜòõ)
  • azo-dye protein
    ¾ÆÁ¶»ö¼Ò ´Ü¹éÁú(ßäáÈÓ±ÛÜòõ)
  • Bence-Jones protein
    º¥½º-Á¸½º ´Ü¹éÁú(Ó±ÛÜòõ)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 9
TCE T-cell enriched; tetrachlorodiphenyl ethane; trichloroethylene T-cell thymus-derived cell
TCR T-cell reactivity; T-cell receptor; T-cell rosette; thalamocortical relay; total cytoplasmic ribosom...
WBC well baby care/clinic; white blood cell; white blood cell count; whole blood cell count
WC ward clerk; water closet; Weber-Christian [syndrome]; wheel chair; white cell; white cell casts; whi...
ECG Electro-Cardio-Graphy(-Gram); ½ÉÀüµµ
   = EKG
  1. Conducting System Structu...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 9
SSCP Single Stranded Conformational Polymorphism
SSCP Single Stranded Conformational Polymorphism analysis
scFv Single chain Fv
scFvs Single chain Fv antibody fragments
scFv Single chain Fv fragments
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • cell culture biocompatibility test
    ¼¼Æ÷ ¹è¾ç »ýü ÀûÇÕ¼º °Ë»ç¹ý
  • cell cycle-non specific
    ¼¼Æ÷ Áֱ⠺ñƯÀ̼º Á¦Á¦
  • cell death
    ¼¼Æ÷»ç
    ¼¼Æ÷°¡ Á׾´Â °úÁ¤¿¡¼­ »ýü ÀÛ¿ëÀÌ ¼¼Æ÷ ¼öÁØ¿¡¼­ Áß´ÜµÈ ÁöÁ¡. ¼¼Æ÷»ç´Â Á¶Á÷À̳ª Àå±â¸¦ Àå±â ÀÌ½Ä °ø¿©Ã¼·Î »ç¿ëÇÏ´Â °Í¿¡ ¾Õ¼­ ÀϾ´Ù.
  • cell differentiation
    ¼¼Æ÷ ºÐÈ­
    ¼¼Æ÷µéÀÌ Á¶Á÷ÀÇ ´Ù¾çÇÑ ±âº» ¼¼Æ÷ ´ÜÀ§·Î ¼ºÀåÇÏ´Â °Í. »óÇǼ¼Æ÷, ½Å°æ¼¼Æ÷
  • cell division
    ¼¼Æ÷ ºÐ¿­
    ÇϳªÀÇ ¼¼Æ÷°¡ µÑ ÀÌ»óÀ¸·Î ³ª´©¾îÁö´Â ÀÏ. º¸Åë ÇÙ ºÐ¿­ÀÌ ¼¼Æ÷Áú ºÐ¿­º¸´Ù ¸ÕÀú ÀϾ´Ù. ÀÌ ÇÙ ºÐ¿­Àº ´ëºÎºÐÀÇ °æ¿ì À¯»çºÐ¿­À̸ç, À¯»çºÐ¿­Àº ¿°»öüÀÇ ºÐ¹è¿Í °°Àº Áß¿äÇÑ ÀÏÀ» ÇÑ´Ù. ü¼¼Æ÷ ºÐ¿­°ú °¨¼ö ºÐ¿­ ¾çÂÊ¿¡¼­ º¸ÀδÙ. ü¼¼Æ÷ ºÐ¿­ÀÇ ÇÙ ºÐ¿­Àº Àü±â, Áß±â, Èıâ, ¸»±â·Î ³ª´©¾îÁø´Ù. ºÐ¿­ °á°ú ¸¸µé¾îÁø µþ ¼¼Æ÷µéÀº ¸ð¼¼Æ÷¿Í µ¿ÀÏÇϸç, ÇÙ³»ÀÇ À¯Àü¹°ÁúÀº Á¤È®ÇÏ°Ô º¹Á¦µÇ¾î 2°³ÀÇ µþ ¼¼Æ÷·Î ³ª´©¾îÁ® µé¾î°£´Ù. °¨¼ö ºÐ¿­Àº »ý½Ä ¼¼Æ÷¸¦ Çü¼ºÇÒ ¶§ ÀϾ´Â ºÐ¿­·Î¼­, ±× °á°ú ¿°»öüÀÇ ¼ö°¡ ü¼¼Æ÷¿¡ ºñÇÏ¿© ¹ÝÀ¸·Î °¨¼ÒÇÑ´Ù. ±×¸®°í ü¼¼Æ÷ ºÐ¿­ÀÇ ÇÙ ºÐ¿­¿¡ ¾Õ¼­ ÀÌÇü ÇÙ ºÐ¿­ÀÎ Á¦1ºÐ¿­ÀÌ Á¸ÀçÇÑ´Ù. ¼¼Æ÷ ºÐ¿­ °úÁ¤À» »ìÆìº¸¸é, ºÐ¿­¿¡¼­ ´ÙÀ½ ºÐ¿­±îÁöÀÇ ½Ã±â¸¦ °£±â ¶Ç´Â ÈÞÁö±â¶ó°í ÇÑ´Ù. ÀÌ °£±â¿¡´Â ¼¼Æ÷³»ÀÇ ¹°Áú´ë»ç³ª °íºÐÀÚ ÇÕ¼ºÀÌ ÀϾ°í, DNA µîÀÇ ¿°»öü ¹°ÁúÀÇ º¹Á¦µµ ÀϾ´Ù. ºÐ¿­ Á÷ÈÄ Çü¼ºµÈ µþ ¼¼Æ÷´Â °£±â¿¡ Á¡Â÷ Ä¿Á® ÇÙµµ 2¹è·Î ÀÚ¶õ´Ù. °£±â ±â°£Àº µ¿¹°, ½Ä¹°, Á¾, ǰÁ¾, Á¶Á÷, ±â°üÀÇ Â÷ÀÌ, ¿Âµµ, ¿µ¾ç µî¿¡ µû¶ó ´Ù¸£¸ç, ¼ö ½Ã°£ ¶Ç´Â ¼ö½Ê ½Ã°£¿¡ À̸£´Â °æ¿ì°¡ ¸¹´Ù. °£±âÀÇ ÇÙÀº ÇÙ ºÐ¿­À» ¾È ÇÒ »Ó ¹°Áú´ë»ç´Â ¿Õ¼ºÇÏ´Ù. À¯»çºÐ¿­¿¡ ÀÇÇØ ¿°»öü°¡ 2°³ÀÇ ÇÙÀ¸·Î ³ª´©¾îÁø ÈÄ ¼¼Æ÷Áú ºÐ¿­ÀÌ ÀϾ´Ù. ºÐ¿­±â¿¡ µé¾î¼­¸é ¿ì¼± ÇÙÀÌ Àü±â, Áß±â, Èıâ, ¸»±â¸¦ °ÅÃÄ µþ ¼¼Æ÷°¡ Çü¼ºµÈ´Ù. ¨ç Àü±â : ÇÙ ¾ÈÀÇ ¿°»ö»ç°¡ ³ª¼±ÇüÀ¸·Î ²¿¿© µÎ²®°í ª¾ÆÁ® ²ö ¸ð¾çÀÇ ¿°»öü°¡ µÈ´Ù. ¿°»öü´Â 2°³ÀÇ ¿°»ö ºÐü°¡ ºÙ¾î ÀÖ´Â ¸ð¾çÀ¸·Î µÇ¾î ÀÖÀ¸¸ç, µ¿½Ã¿¡ ÇÙ¸·, ÀÎÀÌ ¼Ò½ÇµÈ´Ù. °íµî½Ä¹°À» Á¦¿ÜÇÑ ´ëºÎºÐÀÇ ¼¼Æ÷µéÀº ÇÑ ½ÖÀÇ Á߽ɸ³ÀÌ ÇÙ¸· ¹Ù±ùÂÊ¿¡ À§Ä¡ÇÑ´Ù. Á߽ɸ³Àº ¸ÕÀú ºÐ¿­ÇÑ ÈÄ À̵¿À» ½ÃÀÛÇÏ¿© ¾ç±Ø¿¡ µµ´ÞÇÑ´Ù. Áß½Éü°¡ ¾ø´Â ¼¼Æ÷¿¡¼­´Â ¾ç±ØÀ¸·ÎºÎÅÍ ¹æÃßü°¡ »ý±â±â ½ÃÀÛÇϴµ¥, À̸¦ ±Ø¸ð¶ó ÇÑ´Ù. µ¿½Ã¿¡ ¾ç±Ø ¶Ç´Â Áß½Éü¸¦ Áß½ÉÀ¸·Î ÇÏ¿© º°ºû ¸ð¾ç ¶Ç´Â ½Ç ¸ð¾ç ±¸Á¶¸¦ ÅëÆ²¾î ¼º»óü¶ó°í ÇÑ´Ù. À¯»çºÐ¿­ ±â°£ Áß Àü±â°¡ °¡Àå ±ä ½Ã°£À» Â÷ÁöÇÑ´Ù. ¨è Áß±â : ±¸ÇüÀÎ ÇÙÀÌ Å¸¿øÇüÀÌ µÇ¸ç ºñ¿°»öÁúÀº ¹æÃßÇüÀÇ ¹æÃßü¸¦ ÀÌ·ç¸é¼­ Àûµµ¸é
  • cell enclosure
    ¼¼Æ÷ ºÀÀÔü
    ¹ÙÀÌ·¯½º¿¡ °¨¿°µÈ ¼¼Æ÷³»¿¡ ±èÀÚ ¾× µî¿¡ ÀÇÇØ ¿°»öµÈ °ú¸³»ó ¶Ç´Â ±× ¹ÛÀÇ Æ¯Â¡ÀÌ ÀÖ´Â ÇüŸ¦ º¸ÀÌ´Â ¼Òü. °£´ÜÈ÷ ºÀÀÔü¶ó°íµµ ÇÑ´Ù. ±¤°ßº´ µî ¹ÙÀÌ·¯½º º´À» Áø´ÜÇÏ´Â µ¥ ÀÌ¿ëµÇ´Â ¼¼Æ÷ ºÀÀÔüÀÇ º»·¡ ÇüÅ¿¡ °üÇÑ ³íÀǰ¡ ¸¹¾ÒÀ¸³ª, Áö±ÝÀº ¹ÙÀÌ·¯½º º´ÀÇ º´¿øÃ¼ÀÓÀÌ È®ÀεǾú´Ù. ¼¼Æ÷ ºÀÀÔü¿¡´Â ¼¼Æ÷Áú³» ºÀÀÔü¿Í ¼¼Æ÷ÇÙ³» ºÀÀÔü°¡ ÀÖ´Ù. ¼¼Æ÷Áú³» ºÀÀÔü¿¡´Â õ¿¬µÎ, ¿ìµÎÀÇ °¡¸£´Ï¿¡¸® ¼Òü, ±¤°ßº´ÀÇ ³×±×¸® ¼Òü µîÀÌ ÀÖ´Ù. À̵éÀº È£»ê¼º, ¿øÇü, ±ÕÁú ¶Ç´Â °ú¸³»ó ±¸Á¶¸¦ °¡Áø °Í°ú Æ®¶óÄÚ¸¶ÀÇ ÇÁ·Î¹Ùüũ ¼Òü µî È£¿°±â¼ºÀ¸·Î º¹ÀâÇÑ ÇüÀ» °¡Áø °ÍÀÌ ÀÖ´Ù. ¼¼Æ÷ÇÙ³» ºÀÀÔü¿¡´Â Ç츣Æä½º À¯¹ß ¹ÙÀÌ·¯½º·Î Çü¼ºµÈ ºÀÀÔü°¡ ÀÖ´Ù. ¼¼Æ÷ ºÀÀÔü¸¦ ÇÔÀ¯ ³»¿ë¹°¿¡ µû¶ó ºÐ·ùÇϸé, ¹ÙÀÌ·¯½º°¡ ¸ðÀÎ °Í°ú ¹ÙÀÌ·¯½º ±¸¼º ¹°Áú·Î µÈ °ÍÀÌ ¸ðÀÎ °Í, ±×¸®°í ¹ÙÀÌ·¯½ºÀÇ ¼ººÐ°ú °ü·ÃÀÌ ¾ø´Â ƯÀ¯ÇÑ ´Ü¹éÁú·Î ÀÌ·ç¾îÁø °Í µî 3Á¾·ù·Î ³ª´¶´Ù. ¼¼Æ÷ ºÀÀÔüÀÇ Çü¼ºÀº ÁÖ·Î ¹ÙÀÌ·¯½ºÀÇ °¨¿°°ú °ü·ÃµÇ³ª À̿ܿ¡µµ Áß±Ý¼Ó µîÀÇ ¾àǰ Åõ¿©³ª ¼¼Æ÷´ë»ç Àå¾Ö¸¦ ÀÏÀ¸Å°´Â °Í¿¡ ÀÇÇÏ¿© ³ªÅ¸³ª±âµµ ÇÑ´Ù. ¿¹¸¦ µé¸é, ÁßÃ߽Űæ°èÀÇ ÁúȯÀÎ ÆÄŲ½¼ º´ÀÇ °æ¿ì ½Å°æ¼¼Æ÷³»¿¡¼­ ·¹ºß ¼Òü¶ó´Â ¼Òü¸¦, ¹Ì¿ÀŬ·Î´©½º °£Áú ȯÀÚÀÇ ³ú³ª ô¼öÀÇ ½Å°æ¼¼Æ÷³»¿¡¼­´Â ¹Ì¿ÀŬ·Î´©½º ¼Òü¸¦ º¼ ¼ö Àִµ¥ À̵éÀº ¸ðµÎ ¼¼Æ÷Áú³» ºÀÀÔüÀÌ´Ù.
  • cell fusion
    ¼¼Æ÷ ÀÀÇÕ, ¼¼Æ÷ À¶ÇÕ
    µÎ Á¾·ù ÀÌ»óÀÇ ¼¼Æ÷¸¦ ¹ÙÀÌ·¯½º,
  • cell harverter
    ¼¼Æ÷ ȸ¼ö±â
    ´Ù¼öÀÇ ¼¼Æ÷ ¹è¾ç ¿ë±â¿¡¼­ µ¿½Ã¿¡ ¹è¾çµÈ ´É·üÀÌ ÁÁÀº ¼¼Æ÷¸¦ äÃëÇÏ´Â ±â±âÀÇ ÃÑĪ.
  • cell hybridization
    ¼¼Æ÷ ÇÏÀ̺긮µå Çü¼º
  • cell injury
    ¼¼Æ÷ ¼Õ»ó
  • cell interface
    ¼¼Æ÷ »çÀÌ ¸é, ¼¼Æ÷ °£¸é
  • cell kinetics
    ¼¼Æ÷ ¿ªÇÐ
  • cell lethality
    ¼¼Æ÷ Ä¡»çÀ²
  • cell line
    ¼¼Æ÷°è
  • cell mass
    ¿ø±â ¼¼Æ÷±º
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 9
ceramide-activated protein kinase <enzyme> Mw 97 kD; stimulation of kinase takes place during sphingomyelin pathway; has membrane-bound activity capable of phosphorylating a peptide derived from the sequence surrounding thr(699) of the epidermal growth factor receptor; has role in signal transduction for tumour necrosis factor
Registry number: EC 2.7.10.-
Synonym: cap kinase
(26 Jun 1999)
ceramide-activated protein phosphatase <enzyme> Belongs to the heterotrimeric subfamily of the pp2a group of serine-threonine protein phosphatases; involved in ceramide-mediated signal transduction; inhibited by okadaic acid
Registry number: EC 3.1.3.-
Synonym: ceramide-stimulated phosphatase, capp (enzyme)
(26 Jun 1999)
Vps15 protein kinase <enzyme> Functions with vps34p as a membrane-associated complex which facilitates the delivery of proteins into the vacuole in yeast; amino acid sequence has been determined
Registry number: EC 2.7.10.-
Synonym: vps15 gene product, vps15p
(26 Jun 1999)
retinoblastoma protein <molecular biology, protein> Product of the retinoblastoma tumour suppressor gene.
It is a nuclear phosphoprotein hypothesised to normally act as an inhibitor of cell proliferation. Rb protein is absent in retinoblastoma cell lines. It also has been shown to form complexes with the adenovirus e1a protein, the sv40 t antigen, and the human papilloma virus e7 protein.
(03 Jul 1999)
retinol-binding protein <molecular biology> Proteins which bind with retinol.
The retinol-binding protein found in plasma has an alpha-1 mobility on electrophoresis and a molecular weight of 21,000-22,000. The protein has one binding site for retinol and is responsible for the transport of vitamin A.
The retinol- protein complex (molecular weight 80,000 to 90,000) circulates in plasma in the form of a protein-protein complex with prealbumin. The retinol-binding protein found in tissue has a molecular weight of 14,000 and carries retinol as a non-covalently-bound ligand.
(03 Jul 1999)
PEP protein tyrosine phosphatase <enzyme> Pest - pro, glu, ser and thr; an intracellular ptpase expressed primarily by cells of haematopoietic origin; involved in regulating nuclear tyrosine phosphorylation; amino acid sequence has been determined
Registry number: EC 3.1.3.-
Synonym: pep ptpase, pest-enriched phosphatase, ptp-pest
(26 Jun 1999)
membrane protein <protein> A protein with regions permanently attached to a membrane (peripheral membrane protein) or inserted into a membrane integral membrane protein). Insertion into a membrane implies hydrophobic domains in the protein. All transport proteins are integral membrane proteins.
(18 Nov 1997)
channel protein <chemistry, physiology> A protein that facilitates the diffusion of molecules/ions across lipid membranes by forming a hydrophilic pore. most frequently multimeric with the pore formed by subunit interactions.
(18 Nov 1997)
G-protein <cell biology, molecular biology> Intracellular membrane-associated proteins activated by several (e.g., beta adrenergic) receptors.
They serve as second messengers or transducers of the receptor-initiated response to intracellular elements such as enzymes to initiate an effect. They are also mediators of activated cell-surface receptors and their enzymes or of ion channels.
They are responsible for activating a chain of events that alters the concentration of intracellular signaling molecules such as cyclic AMP and calcium. In turn, these intracellular messengers alter the behaviour of other target proteins within the cell.
These proteins have a high affinity for guanine nucleotides and hence are named "G" proteins.
Synonym: G-protein, GTP-binding proteins.
(12 Jul 2000)
G-protein coupled receptor <cell biology> Cell surface receptors that are coupled to G-proteins (GTP-binding protein).
G-protein coupled receptors are thought to have seven membrane spanning domains and have been divided into 2 subclasses: those in which the binding site is in the extracellular domain for example receptors for glycoprotein hormones, such as thyroid stimulating hormone (TSH) and follicle-stimulating hormone (FSH) and those in which the ligand binding site is likely to be in the plane of the 7 transmembrane domains for example rhodopsin and receptors for small neurotransmitters and hormones for example muscarinic acetylcholine receptor.
(18 Nov 1997)
G-protein, inhibitory GI A g-protein that inhibits adenylyl cyclase and activates k+ channels.
(12 Dec 1998)
G-protein, stimulatory gs A G-protein that mediates the receptor activation of adenylyl cyclase.
(12 Dec 1998)
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)
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