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"Bone Morphogenetic Protein Receptors, Type II"¿¡ ´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
  • frontal bone
    À̸¶»À, ÀüµÎ°ñ
  • heel bone
    ¹ß²ÞÄ¡»À, Á¾°ñ
  • herring bone appearance
    û¾î»À¸ð¾ç
  • herring bone artifact
    û¾î»ÀÇã»ó, û¾î»ÀÀΰø¹°
  • hamate bone
    °¥°í¸®»À
  • hammer bone
    ¸ÁÄ¡»À
  • hip bone
    º¼±â»À, °ü°ñ
  • hyoid bone
    ¸ñ»Ô»À, ¼³°ñ
  • irregular bone
    ºÒ±ÔÄ¢»À
  • inlay bone graft
    ¼Ó³Ö±â»ÀÀ̽Ä, ºÀ¹ÚÀÌ»ÀÀ̽Ä, Àη¹À̰ñÀ̽Ä
  • innominate bone
    º¼±â»À, °ü°ñ
  • interwoven bone
    ¾ù°á»À
  • intramedullary bone graft
    ¼ÓÁú³»»ÀÀ̽Ä, °ñ¼ö³»°ñÀ̽Ä
  • lamellated bone
    ÃþÆÇ»À
  • lacrimal bone
    ´«¹°»À, ´©°ñ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 12
  • ¿µ¹®
    ÇѱÛ
  • cuneiform bone
    ½û±â»À
  • ethmoid bone
    ¹úÁý»À, »ç°ñ
  • flat bone
    ³³ÀÛ»À
  • frontal bone
    À̸¶»À
  • hamate bone
    °¥°í¸®»À
  • hammer bone
    (¢¡malleus) ¸ÁÄ¡»À
  • heel bone
    (¢¡calcaneus) ¹ß²ÞÄ¡»À
  • hip bone
    º¼±â»À, °ü°ñ
  • hyoid bone
    ¸ñ»Ô»À
  • innominate bone
    (¢¡hip bone) º¼±â»À, °ü°ñ
  • interwoven bone
    ¾ù°á»À
  • irregular bone
    ºÒ±ÔÄ¢»À
  • lacrimal bone
    ´«¹°»À
  • lamellated bone
    ÃþÆÇ»À
  • long bone
    ±ä»À
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 12
  • ¿µ¹®
    ÇѱÛ
  • 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
  • PPD (purified protein derivatives)
    ÇÇÇǵð, Á¤Á¦´Ü¹éÁú·ù(À¯µµÃ¼)
  • PPD(Purified protein derivative) test
    PPD °Ë»ç.
  • Reiters protein
    ¶óÀÌÅÍ ¸Åµ¶Áø´Ü¿ë´Ü¹éÁú
  • S100 protein
    S100 ´Ü¹éÁú
  • actin-binding protein
    ¾×ƾ °áÇմܹé(¡­Ì¿ùêÓ±ÛÜ)
  • activated protein C inhibitor
    Ȱ¼ºÈ­´Ü¹éÁú C ¾ïÁ¦Á¦
  • activated protein C resistance
    Ȱ¼ºÈ­C´Ü¹é³»¼º
  • acute phase protein
    ±Þ¼ºº´±â´Ü¹éÁú
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 12
  • ¿µ¹®
    ÇѱÛ
  • protein-losing enteropathy
    ´Ü¹é»ó½ÇÀ庴Áõ(Ó±ÛÜßÃã÷íóÜ»ñø)
  • purified protein derivative
    Á¤Á¦´Ü¹éÁúÀ¯µµÃ¼.
  • racemized protein
    ¶ó¼¼¹ÌÈ­´Ü¹éÁú(¡­ûùÓ±ÛÜòõ).
  • ras protein
    ras ´Ü¹é(¡­Ó±ÛÜ)
  • reserve protein
    ÀúÀå´Ü¹éÁú.
  • retinol-binding protein
    ·¹Æ¼³î°áÇմܹé(Áú)(·¹Æ¼³î Ì¿ùêÓ±ÛÜòõ)
  • serum protein
    Ç÷û´Ü¹é
  • serum protein
    Ç÷û´Ü¹éÁú(¡­Ó±ÛÜòõ).
  • serum protein bound iodine
    Ç÷û´Ü¹é°áÇÕ ¿äµå.
  • specific protein
    ƯÀ̴ܹéÁú(÷åì¶Ó±ÛÜòõ).
  • sphingolipid activator protein I deficiency
  • spindle protein
    ¹æÃßü´Ü¹éÁú(¡­ô÷Ó±ÛÜòõ).
  • stable plasma protein solution =SPPS
    ¾ÈÁ¤Ç÷Àå(´Ü¹é)¿ë¾×(¡­úìíìÓ±ÛÜéÁ äû).
  • structural protein
    ±¸Á¶ ´Ü¹éÁú
  • structural protein
    ±¸Á¶ ´Ü¹é
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 12
  • ¿µ¹®
    ÇѱÛ
  • protein conformation
    ´Ü¹éÁú(Ó±ÛÜòõ) ÀÔüÇüÅÂ(Ø¡ô÷û¡÷¾)
  • protein domain
    ´Ü¹éÁú ¿µ¿ª(Ó±ÛÜòõÖÅæ´)
  • protein efficiency ratio
    ´Ü¹éÁú(Ó±ÛÜòõ) È¿À²ºñ(üù×ËÝï)
  • protein efficiency ratio method
    ´Ü¹éÁú(Ó±ÛÜòõ) È¿À²ºñ¹ý(üù×ËÝïÛö)
  • protein engineering
    ´Ü¹éÁú °ø¹ý(Ó±ÛÜòõÍïÛö)
  • protein error
    ´Ü¹éÁú ¿ÀÂ÷(Ó±ÛÜòõè¦ó¬)
  • protein evolution
    ´Ü¹éÁú ÁøÈ­(Ó±ÛÜòõòäûù)
  • protein export
    ´Ü¹éÁú À¯Ãâ(Ó±ÛÜòõ×µõó)
  • protein factor
    ´Ü¹éÁú ÀÎÀÚ(Ó±ÛÜòõì×í­)
  • protein folding
    ´Ü¹éÁú(Ó±ÛÜòõ) Á¢±â
  • protein fractionation
    ´Ü¹éÁú ºÐȹȭ(Ó±ÛÜòõÝÂüñûù)
  • protein free filtrate
    Á¦(ð¶)´Ü¹éÁú ¿©°ú¾×(Ó±ÛÜòõÕëΦäû)
  • protein import
    ´Ü¹éÁú À¯ÀÔ(Ó±ÛÜòõ×µìý)
  • protein index
    ´Ü¹éÁú ÁöÇ¥(Ó±ÛÜòõò¦øö)
  • protein kinase
    "´Ü¹éÁú(Ó±ÛÜòõ) Ä«À̳×À̽º, ´Ü¹éÁú(Ó±ÛÜòõ) Ȱ¼ºÈ­È¿¼Ò(üÀàõûùý£áÈ)"
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 12
BMB biomedical belt; bone marrow biopsy
BMF bone marrow failure
BML bone marrow lymphocytosis
BMN bone marrow necrosis
BMT Bachelor of Medical Technology; basement membrane thickening; benign mesenchymal tumor; bone marrow ...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 12
PP2A Protein phosphatase type-2A
ABD Adynamic Bone Disease
AlloBMT Allogeneic Bone Marrow Transplantation
ABMT Allogeneic bone marrow transplantation
ABL Alveolar bone loss
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 12
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • 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.
  • bundle bone
    ¼Ó»ó°ñ
    Shar
  • calf's bone
    ºñ°ñ
    µ¿ÀǾî=fibula. ÇÏÅðÀÇ µÎ °³ÀÇ »À Áß¿¡¼­ ¹Ù±ùÂÊÀÇ ÀÛÀº °Í.
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 12
receptors, transforming growth factor beta Cell-surface proteins that bind transforming growth factor beta and trigger changes influencing the behaviour of cells. Two types of transforming growth factor receptors have been recognised. They differ in affinity for different members of the transforming growth factor beta family and in cellular mechanisms of action. Transforming growth factor alpha binds to the same receptors as epidermal growth factor (see receptors, epidermal growth factor-urogastrone).
(12 Dec 1998)
receptors, tumour necrosis factor Cell surface receptors that bind tumour necrosis factor and trigger changes which influence the behaviour of cells. The two recognised tumour necrosis factor receptors are designated alpha and beta receptors. Both receptors bind both alpha and beta tumour necrosis factors with high affinity, and both are members of the nerve growth factor receptor family.
(12 Dec 1998)
receptors, vasoactive intestinal peptide Cell surface proteins that bind vasoactive intestinal peptide (vip) with high affinity and trigger intracellular changes which influence the behaviour of cells.
(12 Dec 1998)
receptors, vasopressin Specific molecular sites or structures on or in cells that vasopressins react or to which they bind in order to modify the function of the cells. Two types of vasopressin receptor exist, the v1 receptor and the v2 receptor. The v1 receptor can be subdivided into v1a and v1b (formerly v3) receptors.
(12 Dec 1998)
receptors, very late antigen Members of the integrin family appearing late after T-cell activation. They are a family of proteins initially identified at the surface of stimulated T-cells, but now identified on a variety of cell types. At least six vla antigens have been identified as heterodimeric adhesion receptors consisting of a single common beta-subunit and different alpha-subunits.
(12 Dec 1998)
receptors, virus Specific molecular components of the cell capable of recognizing and interacting with a virus, and which, after binding it, are capable of generating some signal that initiates the chain of events leading to the biological response.
(12 Dec 1998)
receptors, vitronectin Alpha-v beta-3 integrins that bind vitronectin with high affinity and play a role in cell migration. They also bind fibrinogen, von willebrand factor, osteopontin, and thrombospondin. The highly homologous alpha-v beta-5 integrin also binds vitronectin, but mediates simple adhesion.
(12 Dec 1998)
cholinergic receptors Chemical sites in effector cells or at synapses through which acetylcholine exerts its action.
(05 Mar 2000)
muscarinic receptors Membrane-bound proteins whose extracellular domain contains a recognition site for acetylcholine (ACh); combination of Ach with the receptor initiates a physiologic change (slowing of heart rate, increased glandular secretory activity and stimulation of smooth muscle contractions); changes are observed after treatment with the mushroom alkaloid, muscarine. Muscarinic receptors are to be distinguished from nicotinic receptors.
(05 Mar 2000)
saturation of receptors Saturation, the state in which all receptors are effectively occupied all the time, can be said to occur in a simple binding equilibrium when the concentration of ligand is more than 5 times the Kd value, although strictly this will only be true at infinite ligand concentration.
(18 Nov 1997)
pulmonary stretch receptors Stretch receptors found in the bronchi and bronchioles. Pulmonary stretch receptors are sensors for a reflex which stops inspiration. In humans, the reflex is protective and is probably not activated during normal respiration.
(12 Dec 1998)
sensory receptors Peripheral endings of afferent neurons.
(05 Mar 2000)
stretch receptors Receptor's that are sensitive to elongation, especially those in Golgi tendon organs and muscle spindles, but also those found in visceral organs such as the stomach, small intestine, and urinary bladder; these receptor's have the function of detecting elongation, and this distinguishes them from baroreceptors, which actually are activated by stretching of the wall of the blood vessel but whose function is to elicit central reflex mechanism reducing the arterial blood pressure.
(05 Mar 2000)
nicotinic receptors A class of cholinergic receptors on skeletal muscle cells that are linked to ion channels in the cell membrane.
(05 Mar 2000)
opiate receptors Regions of the brain which have the capacity to bind morphine; some, along the aqueduct of Sylvius and in the centre median, are in areas related to pain, but others, as in the striatum, are not related.
(05 Mar 2000)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
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  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
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    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
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  • ¿µ¹®
    ÇѱÛ
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  • ¿µ¹®
    ÇѱÛ
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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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  • ¿µ¹®
    ÇѱÛ
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    ÇѱÛ
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  • ¿µ¹®
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