¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"platelet endothelial cell activated protease"¿¡ ´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
  • committed cell
    ¾ô¸Ç¼¼Æ÷, ¼öÀÓ¼¼Æ÷
  • complex cell
    º¹ÇÕ¼¼Æ÷
  • cone cell
    ¿ø»Ô¼¼Æ÷
  • cone cell layer
    ¿ø»Ô¼¼Æ÷Ãþ, ¿øÃß¼¼Æ÷Ãþ
  • connective tissue cell
    °áÇÕÁ¶Á÷¼¼Æ÷
  • continuous cell line
    ¹«ÇÑÁõ½Ä¼¼Æ÷ÁÖ, ¿¬¼Ó°è´ë¼¼Æ÷ÁÖ
  • contractile fiber cell
    ¼öÃ༶À¯¼¼Æ÷
  • cover cell
    µ¤°³¼¼Æ÷
  • crenated cell
    Åé´ÏÀûÇ÷±¸
  • crescent cell anemia
    Ãʽ´ÞÀûÇ÷±¸ºóÇ÷
  • crypt cell
    âÀÚ»ù¼¼Æ÷, ¿ò¼¼Æ÷
  • cuboidal cell
    ÀԹ漼Æ÷, ÁÖ»çÀ§¼¼Æ÷
  • cylindrical cell
    ¿øÁÖ¼¼Æ÷
  • cytotoxic cell
    ¼¼Æ÷µ¶¼º¼¼Æ÷
  • cytotoxic cell protein
    ¼¼Æ÷µ¶¼º¼¼Æ÷´Ü¹éÁú
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • 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
  • cell division
    ¼¼Æ÷ºÐ¿­
  • cell envelope
    ¼¼Æ÷²®Áú
  • cell fusion
    ¼¼Æ÷À¶ÇÕ
  • cell hybridization
    ¼¼Æ÷ºÎÇÕÈ­, ¼¼Æ÷ÇÏÀ̺긮µåÈ­
  • cell inclusion
    ¼¼Æ÷Æ÷ÇÔ¹°
  • cell interaction
    ¼¼Æ÷»óÈ£ÀÛ¿ë
  • cell lethality
    ¼¼Æ÷Ä¡»çÀ²
  • cell line
    ¼¼Æ÷°è, ¼¼Æ÷ÁÖ
  • cell loss
    ¼¼Æ÷¼Ò½Ç
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • Graham cell
    ±×¶óÇÔ¼¼Æ÷
  • Granulosa cell
    °ú¸³¸·¼¼Æ÷(Î¨Ø£Ø¯á¬øà)
  • Granulosa cell tumor
    °ú¸³¸·¼¼Æ÷Á¾¾ç(Î¨Ø£Ø¯á¬øàðþåË)
  • H-9 cell line
    H-9 ¼¼Æ÷°è
  • HeLa cell
    Çï¶ó¼¼Æ÷.
  • HeLa cell
    Çï¶ó¼¼Æ÷
  • Heidenhain s cell
    ÇÏÀ̵§ÇÏÀμ¼Æ÷.
  • Henle s cell
    Çî·¯¼¼Æ÷.
  • Hfr cell
    °íºóµµÀçÁ¶ÇÕ¼¼Æ÷
  • Hulle cell
    ¿ÜÇǼ¼Æ÷
  • ICSH = interstitial cell stimulating hormone
    °£Áú¼¼Æ÷ÀÚ±Ø(Êàòõá¬øàí©Ð½)È£¸£¸ó.
  • ICSH=£¾interstitial cell stimulating hormone
    °£Áú¼¼Æ÷ÀÚ±ØÈ£¸£¸ó.
  • K cell
    K¼¼Æ÷, »ìÇØ¼¼Æ÷
  • LE cell
    LE¼¼Æ÷.
  • LE cell phenomenon
    LE¼¼Æ÷Çö»ó.
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • platelet sequestration
    Ç÷¼ÒÆÇ°Ý¸®(̰×î)
  • platelet survival measurement
    Ç÷¼ÒÆÇ»ýÁ¸´ÉÃøÁ¤
  • platelet transfusion
    Ç÷¼ÒÆÇ¼öÇ÷
  • platelet transfusion
    Ç÷¼ÒÆÇ¼öÇ÷(¡­âÃúì).
  • platelet,adhesion
    À¯Âø(ë¨ó·),ºÎÂø(ݾó·),Á¢Âø(ïÈó·)
  • platelet,aggregation
    ÀÀÁý(ëêó¢), ÀÀ±«(ëêÎÔ)
  • platelet-activating factor (PAF)
    Ç÷¼ÒÆÇ Ȱ¼ºÈ­ÀÎÀÚ
  • platelet-activating factor (paf)
    Ç÷¼ÒÆÇȰ¼ºÈ­ÀÎÀÚ(úìá³÷ùüÀàõûùì×í­)
  • platelet-derived growth factor
    Ç÷¼ÒÆÇÀ¯·¡ Áõ½ÄÀÎÀÚ
  • platelet-derived growth factor(PDGF)
    Ç÷¼ÒÆÇ À¯·¡ ¼ºÀå ÀÎÀÚ
  • platelet-derived growth factor(pdgf)
    ÆÇ-À¯µµ¼ºÀåÀÎÀÚ(úìá³÷ù-ë¯Óôà÷íþì×í­)
  • platelet-specific antigens
    Ç÷¼ÒÆÇƯÀÌÇ׿ø
  • platelet-type
    Ç÷¼ÒÆÇÇü(û¡)
  • therapeutic platelet-leukapheresis
    Ä¡·áÀû Ç÷¼ÒÆÇ¹éÇ÷±¸¼ººÐäÁý¼ú
  • thrombocyte [blood platelet]
    Ç÷¼ÒÆÇ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • Inner cell mass [Embryoblast]
    ¼Ó¼¼Æ÷µ¢ÀÌ [¹èÀÚ¸ðü]
    [¿¾ ¿ë¾î] ³»ºÎ¼¼Æ÷±«
  • Inner phalangeal cell
    ¼Ó¼Õ°¡¶ô¼¼Æ÷
    [¿¾ ¿ë¾î] ³»Áö»ó¼¼Æ÷
  • Medullary endocrine cell
    ¼ÓÁú³»ºÐºñ¼¼Æ÷
    [¿¾ ¿ë¾î] ¼öÁú³»ºÐºñ¼¼Æ÷
  • Inner hair cell
    ¼ÓÅм¼Æ÷
    [¿¾ ¿ë¾î] ³»À¯¸ð¼¼Æ÷
  • Internal nuclear layer [Bipolar cell layer]
    ¼ÓÇÙÃþ [µÎ±Ø¼¼Æ÷Ãþ]
    [¿¾ ¿ë¾î] ³»ÇÙÃþ(À̱ؼ¼Æ÷Ãþ)
  • Endocrine cell of pineal gland
    ¼Û°úü³»ºÐºñ¼¼Æ÷
    [¿¾ ¿ë¾î] ¼Û°úü³»ºÐºñ¼¼Æ÷
  • Pinealocyte [Clear cell]
    ¼Û°úü¼¼Æ÷
    [¿¾ ¿ë¾î] ¼Û°úü¼¼Æ÷
  • Horizontal cell
    ¼öÆò¼¼Æ÷
    [¿¾ ¿ë¾î] ¼öÆò¼¼Æ÷
  • Goblet cell
    ¼úÀܼ¼Æ÷
    [¿¾ ¿ë¾î] ¹è»ó¼¼Æ÷
  • Neurosensory epithelial cell
    ½Å°æ°¨°¢»óÇǼ¼Æ÷
    [¿¾ ¿ë¾î] ½Å°æ°¨°¢»óÇǼ¼Æ÷
  • Ganglion cell layer
    ½Å°æÀý¼¼Æ÷Ãþ
    [¿¾ ¿ë¾î] ½Å°æÀý¼¼Æ÷Ãþ
  • Satellite cell
    ½Å°æÀý¾Æ±³¼¼Æ÷
    [¿¾ ¿ë¾î] À§¼º¼¼Æ÷
  • Satellite cell
    ½Å°æÀý¾Æ±³¼¼Æ÷ [À§¼º¼¼Æ÷]
    [¿¾ ¿ë¾î] ½Å°æÀý±³¼¼Æ÷
  • Satellite cell
    ½Å°æÀý¾Æ±³¼¼Æ÷ [À§¼º¼¼Æ÷]
    [¿¾ ¿ë¾î] À§¼º¼¼Æ÷
  • Cardiac muscle cell
    ½ÉÀå±ÙÀ°¼¼Æ÷
    [¿¾ ¿ë¾î] ½É±Ù¼¼Æ÷
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
  • plasma cell
    ÇüÁú¼¼Æ÷(û¡òõá¬øà)
  • primed cell
    °¨ÀÛ¼¼Æ÷(ÊïíÂá¬øà)
  • productive cell
    »ý»ê ¼¼Æ÷(ßæß§á¬øà)
  • red cell agglutination
    ÀûÇ÷±¸ ÀÀÁý(îåúìϹëêó¢)
  • red cell lysis
    ÀûÇ÷±¸ ¿ëÇØ(îåúìϹéÁú°)
  • regulated secretory cell
    ÇÇÁ¶Àý(ù¬ðàï½) ºÐºñ¼¼Æ÷(ÝÂÝôá¬øà)
  • resting cell
    È޽O÷(ýÌãÓá¬øà)
  • restrictive cell
    Á¦ÇÑ ¼¼Æ÷(á¬øà)
  • sector cell
    ¼½ÅͽÇ(ãø)
  • separation cell
    ºÐ¸®½Ç(ÝÂ×îãø)
  • sickle cell
    ³´¼¼Æ÷(á¬øà)
  • sickle cell anemia
    ³´¼¼Æ÷(á¬øà)ºóÇ÷(Þ¸úì)
  • sickle cell disease
    ³´¼¼Æ÷(á¬øà)Áúȯ(òðü´)
  • sickle cell hemoglobin
    ³´¼¼Æ÷(á¬øà)È÷¸ð±Û·Îºó
  • sickle cell trait
    ³´¼¼Æ÷(á¬øà)¼ºÇâ(àõú¾)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 7
CDPS calcium-dependent protease small subunit
CTRL chymotrypsin-like [protease]
HFSP Hanukah factor serine protease
KPI kallikrein-protease inhibitor; karyopyknotic index
LMP large multifunctional protease; last menstrual period; latent membrane potential; left mentoposterio...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 7
ECGF Endothelial Cell Growth Factor
ECGS Endothelial Cell Growth Supplement
EC Endothelial cell
ECAM endothelial cell adhesion molecule
ECCM Endothelial cell conditioned medium
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • 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
  • cell mediated immunity
    ¼¼Æ÷ ¸Å°³ ¸é¿ª, ¼¼Æ÷ ¸Å°³¼º ¸é¿ª ÀÛ¿ë, ¼¼Æ÷¼º ¸é¿ª
    Ç׿øÀÌ T Àӯı¸¸¦ ÀÚ±ØÇÏ¸é ¸é¿ª ±Û·ÎºÒ¸°À» ÇÕ¼º ºÐºñÇÏ´Â °ÍÀÌ ¾Æ´Ï°í Àӯı¸ ÀÚ½ÅÀÌ Ç×ü·Î ÀÛ¿ëÇÏ´Â °¨ÀÛ Àӯı¸°¡ µÇ´Â °ÍÀÌ Ã¼¾×¼º ¸é¿ª°úÀÇ Â÷ÀÌ·Î, ü¾×¼º ¸é¿ªÀÌ ÁÖ·Î ±Þ¼º ¼¼±Õ¼º Áúȯ¿¡ ´ëÇÑ ¸é¿ª ±âÀüÀε¥ ºñÇØ¼­ ¼¼Æ÷¼º ¸é¿ªÀº ¸¸¼º ¼¼±Õ¼º Áúȯ, Á¶Á÷ À̽Ä, ¾Ï ¼¼Æ÷, °õÆÎÀÌ Áúȯ, ƯÈ÷ ¹ÙÀÌ·¯½º Áúȯ¿¡ ´ëÇÑ ¸é¿ª ±âÀüÀÌ´Ù.
  • cell mediated lympholysis
    ¼¼Æ÷ ¸Å°³ ¸²ÇÁ±¸ ¿ëÇØ
  • cell mediated reaction
    ¼¼Æ÷ ¸Å°³¼º ¹ÝÀÀ
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 7
B2 protease <enzyme> Isolated from benign strain of dichelobacter nodosus; differs from v2 protease by a single amino acid at position 219
Registry number: EC 3.4.21.-
Synonym: aprb2 gene product
(26 Jun 1999)
Bowman Birk protease inhibitors <pharmacology> Family of serine protease inhibitors found in seeds of leguminous plants and cereals.
(18 Nov 1997)
calcium dependent sulfhydryl protease <enzyme> Hydrolyzes actin binding protein; enzyme from platelets
Registry number: EC 3.4.22.-
Synonym: cdsp
(26 Jun 1999)
calcium-independent processing protease <enzyme> Converts hiv-1 gp160 precursor to gp120 and gp41
Registry number: EC 3.4.-
Synonym: viral envelope glycoprotein maturase, vem enzyme
(26 Jun 1999)
M4 protease <enzyme> Nonhemorrhagic fibrinolytic metalloprotease from crotalus molossus molossus venom (northern blacktail rattlesnake); mw 27,000
Pharmacological action: fibrinolytic agents
Registry number: EC 3.4.24.-
(26 Jun 1999)
V2 protease <enzyme> Isolated from virulent strain of dichelobacter nodosus; differs from b2 protease by a single amino acid at position 219; genbank l38395
Registry number: EC 3.4.21.-
Synonym: aprv2 gene product, dn aprv2 gene product
(26 Jun 1999)
V8 protease <enzyme> Protease from Staphylococcus aureus strain V8. Cleaves peptide bonds on the carboxyl side of aspartic and glutamic acid residues. Used experimentally for selective cleavage of proteins for amino acid sequence determination or peptide mapping.
(18 Nov 1997)
varicella-zoster virus protease <enzyme> Amino acid sequence given in first source
Registry number: EC 3.4.21.-
Synonym: vzv protease, gene 33 product, vzv
(26 Jun 1999)
VCP1 serine protease <enzyme> Isolated from verticillium chlamydosporium
Registry number: EC 3.4.21.-
(26 Jun 1999)
MASP-2 protease <enzyme> Masp = mannan-binding lectin (mbl)-associated serine proteinase.
Registry number: EC 3.4.21.-
(26 Jun 1999)
Vibrio alginolyticus alkaline protease <enzyme> Extracellular enzyme stimulated by histidine and urocanic acid
Registry number: EC 3.4.21.-
Synonym: vaa protease
(26 Jun 1999)
Vibrio vulnificus protease <enzyme> Forms haemorrhagic lesions and causes extensive dermonecrosis; enhances vascular permeability through histamine release and bradykinin generation by activation of the plasma kallikrein -kinin system; immediately inactivated by plasma protein
Registry number: EC 3.4.24.-
Synonym: vvp protease, vvp gene product
(26 Jun 1999)
MBP-associated serine protease <enzyme> Genbank d28593
Registry number: EC 3.4.21.-
Synonym: masp protease, mannose-binding protein-associated serine protease
(26 Jun 1999)
Mch4 protease <enzyme> An aspartate-specific cysteine protease containing two fadd-like domains.
Registry number: EC 3.4.22.-
(26 Jun 1999)
virus activating protease <enzyme> Endoprotease from chick embryo; activates para- and orthomyoxovirus fusion glycoproteins by cleaving them at a single arginine site; ca(2+) dependent; similar to blood clotting factor x
Registry number: EC 3.4.21.-
(26 Jun 1999)
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