¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"alpha,alpha-trehalose phosphorylase"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • alpha chain disease
    ¾ËÆÄ¼âÁúȯ
  • alpha cradle
    ¾ËÆÄ¹Þħ´ë
  • alpha decay
    ¾ËÆÄºØ±«
  • alpha emitter
    ¾ËÆÄ¹æ»çü, ¾ËÆÄ¹æÃâü
  • alpha fetoprotein =AFP
    ¾ËÆÄžƴܹé(¡­÷Ãä®Ó±ÛÜ).
  • alpha fiber
    ¾ËÆÄ(½Å°æ)¼¶À¯
  • alpha granule
    ¾ËÆÄ °ú¸³(¡­Î¨Ø£)
  • alpha hemolysis
    ¾ËÆÄ¿ëÇ÷(¡­éÁúì).
  • alpha hemolysis
    ¾ËÆÄ¿ëÇ÷(¡­éÁúì).
  • alpha hydroxy acids
    ¾ËÆÄÈ÷µå·Ï½Ã»ê
  • alpha motoneuron
    ¾ËÆÄ¿îµ¿´º¿ì·Ð
  • alpha particle
    ¾ËÆÄÀÔÀÚ
  • alpha ray
    ¾ËÆÄ¼±
  • alpha rhythm
    ¾ËÆÄ¸®µë ³úÆÄ(Òà÷î)ÀÇ .
  • alpha thalassemia
    ¾ËÆÄÅ»¶ó¼¼¹Ì¾Æ.
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • alpha blocking
    ¾ËÆÄÂ÷´Ü
  • alpha cell
    ¾ËÆÄ¼¼Æ÷
  • alpha cell
    ¾ËÆÄ¼¼Æ÷(¡­á¬øà)
  • alpha cell glucagon cell
    ¾ËÆÄ¼¼Æ÷ ±Û·çÄ«°ï¼¼Æ÷
  • alpha cell tumor
    ¾ËÆÄ ¼¼Æ÷Á¾(¡­á¬øàðþ)
  • alpha chain disease
    ¾ËÆÄ¼âº´(¡­áðÜ»).
  • alpha chain disease
    ¾ËÆÄ¼âÁúȯ
  • alpha cradle
    ¾ËÆÄ¹Þħ´ë
  • alpha decay
    ¾ËÆÄºØ±«
  • alpha emitter
    ¾ËÆÄ¹æ»çü, ¾ËÆÄ¹æÃâü
  • alpha fetoprotein =AFP
    ¾ËÆÄžƴܹé(¡­÷Ãä®Ó±ÛÜ).
  • alpha fiber
    ¾ËÆÄ(½Å°æ)¼¶À¯
  • alpha granule
    ¾ËÆÄ °ú¸³(¡­Î¨Ø£)
  • alpha hemolysis
    ¾ËÆÄ¿ëÇ÷(¡­éÁúì).
  • alpha hemolysis
    ¾ËÆÄ¿ëÇ÷(¡­éÁúì).
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 3 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
  • polysaccharide phosphorylase
    ´Ù´çÁú(ÒýÓØòõ) Æ÷½ºÆ÷¸±·¹À̽º
  • starch phosphorylase
    ³ì¸» Æ÷½ºÆ÷¸±·¹À̽º
  • synthase-phosphorylase kinase
    ½ÅÅ×À̽º-Æ÷½ºÆ÷¸±·¹À̽º Ä«À̳×À̽º
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 2
IP icterus praecox; imaging plate; immune precipitate; immunoblastic plasma; immunoperoxidase technique...
MTAP methylthioadenosine phosphorylase
NP nasopharynx, nasopharyngeal; near point; necrotizing pancreatitis; neonatal-perinatal; neuritic plag...
PBK phosphorylase B kinase
PHK phosphohexokinase; phosphorylase kinase; postmortem human kidney
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 2
PD-ECGF/TP Platelet-derived endothelial cell growth factor/thymidine phosphorylase
PNPase Polynucleotide phosphorylase
PNP Purine nucleoside phosphorylase
PyNPase Pyrimidine nucleoside phosphorylase
TP Thymidine phosphorylase
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 10 ÆäÀÌÁö: 2
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • alpha streptococus
    ¾ËÆÄÇü ¿¬¼â ±¸±Õ
  • alpha toxin
    ¾ËÆÄ µ¶¼Ò
  • alpha-adrenergic receptor
    ¾ËÆÄ-¾Æµå·¹³¯¸° ¼ö¿ëü
  • alpha-amylase
    ¾ËÆÄ-¾Æ¹Ð¶óÁ¦
  • alpha-fetoprotein
    ¾ËÆÄ-ÆäÅäÇÁ·ÎÅ×ÀÎ, ¾ËÆÄ ÅÂ¾Æ ´Ü¹éÁú
    Àü±â ¿µµ¿»ó ¾ËÆÄ 1 ´ë·Î ¿òÁ÷ÀÌ´Â ºÐÀÚ·® 70,000ÀÇ Ç÷Àå ´Ü¹é. žÆÀÇ °£, ³­È² ¶õ ¹× ¼ÒÈ­±â°ü¿¡¼­ »ý¼ºµÇ¸ç »ýÈÄ 1³â Á¤µµ¿¡ Ç÷ÀåÄ¡°¡ Å©°Ô °¨¼Ò. ±×·¯³ª ´ëºÎºÐÀÇ °£¾Ï°ú ±âÇü ¾ÏÁ¾, °íȯ ³­¼Ò ¹× »ý½Ä¼±ÀÇ Àå±â¿¡ ¹ß»ýÇÏ´Â Å»ý ¾ÏÀÌ ÀÖÀ» ¶§ Ç÷ÁßÄ¡°¡ Áõ°¡. ÀÌ ´Ü¹é ÇÔ·® ÃøÁ¤Àº °£¾ÏÀ̳ª ¹è¼¼Æ÷ Á¾¾çÀÇ Ä¡·á ÃøÁ¤¿¡ ÀÌ¿ëÇÑ´Ù.
  • alpha-galactosidase
    ¾ËÆÄ-°¥¶ôÅä½Ã´Ù¾ÆÁ¦
  • alpha-l-iduronidase
    a-L-Iduronidase
  • alpha-oxynaphthoic acid
    ¾ËÆÄ-¿Á½Ã³ªÇÁÅä»ê
    °áÁ¤¼ºÀÇ »ê,OHC10H6COOH.°ú°Å¿¡´Â ¹æºÎÁ¦, ¹æÃëÁ¦·Î »ç¿ëµÇ¾ú´Ù.
  • { alpha }`_{2 } ^{A } { gamma }`_{ 2} ^{F }

    ¶ó°í ±âÀçµÈ´Ù. Çì¸ð±Û·Îºó A(¼ºÀÎ Çì¸ð±Û·Îºó)´Â º¸Åë ¼ºÀÎÀÇ ´ëºÎºÐÀÌ µÇ¸ç,
    ¿ëÇ÷¼º
    Çì¸ð±Û·ÎºóÀÌ ÀûÇ÷±¸¿¡¼­ À¯¸®ÇÏ¿© Ç÷ÀåÁß¿¡ ³ªÅ¸³ª´Â ¼ºÁú.
  • myelinated A alpha mechanoreceptor
    À¯¼öÃÊ A-¾ËÆÄ ±â°è ¼ö¿ëü, À¯¼öÃÊ A-¾ËÆÄ ±â°è ¼ö¿ë±â
  • CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 2
    5 alpha-dihydroprogesterone 3 alpha-hydroxysteroid oxidoreductase <enzyme> Catalyses conversion of 5 alpha-dihydroprogesterone to 3 alpha -hydroxy-5 alpha-pregnane-20-one
    Registry number: EC 1.1.1.-
    Synonym: 5-dp-3 alpha-hso, NADPH-5 alpha-dihydroprogesterone 3 alpha-hydroxysteroid oxidoreductase, alpha-hsor
    (26 Jun 1999)
    5 beta-cholestane-3 alpha,7 alpha-diol 26-hydroxylase <enzyme> Nadp-dependent
    Registry number: EC 1.14.13.-
    (26 Jun 1999)
    7 alpha-hydroxy-4-cholesten-3-one-12 alpha monooxygenase <enzyme> Liver microsomal enzyme active in conversion of cholesterol to cholic acid; introduces a 12 alpha-hydroxyl group into the steroid nucleus of cholesterol
    Registry number: EC 1.14.99.-
    Synonym: 7-hco-monooxygenase, hco 12 alpha-hydroxylase
    (26 Jun 1999)
    maltodextrin phosphorylase <enzyme> From E coli
    Registry number: EC 2.4.1.-
    Synonym: e350a
    (26 Jun 1999)
    GDPmannose phosphorylase <enzyme> A transferase that catalyses the transfer of GDP to the mannose of mannose-1-phosphate.
    Consider also the bifunctional enzyme, phosphomannose isomerase-guanosine diphospho-d-mannose pyrophosphorylase; rfbm has similarity to long-chain, iron-containing alcohol dehydrogenases
    Registry number: EC 2.7.7.13
    Synonym: GDPmannose phosphorylase, GDP mannose pyrophosphorylase, GTP-alpha-d-mannose-1-phosphate guanylyltransferase, GDP-mannose pyrophosphorylase, rfbm gene product, rfbm protein
    (26 Jun 1999)
    cellodextrin phosphorylase <enzyme> Reverse reaction is used to synthesise cellodextrins
    Registry number: EC 2.4.1.49
    (26 Jun 1999)
    glycogen phosphorylase <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase).
    (21 Jun 2000)
    phosphorylase <enzyme> Enzyme that catalyses the sequential removal of glycosyl residues from glycogen to yield one glucose-1-phosphate per reaction. Its activity is controlled by phosphorylation (by phosphorylase kinase).
    (21 Jun 2000)
    phosphorylase a <enzyme> The phosphorylated and more active form of phosphorylase that functions as a regulatory enzyme during glycogen breakdown. The phosphate groups are hydrolytically removed by phosphorylase phosphatase to form phosphorylase b and orthophosphate.
    Registry number: EC 2.4.1.-
    (12 Dec 1998)
    phosphorylase b <enzyme> The relatively inactive form of phosphorylase that is reactivated to form phosphorylase a by phosphorylase kinase, which catalyses the enzymatic phosphorylation of the serine residues at the expense of ATP.
    Registry number: EC 2.4.1.-
    (12 Dec 1998)
    phosphorylase kinase <enzyme> The enzyme that regulates the activity of phosphorylase and glycogen synthetase by addition of phosphate groups. A large and complex enzyme, itself regulated by phosphorylation. Integrates the hormonal and calcium signals in muscle.
    (18 Nov 1997)
    phosphorylase kinase phosphatase <enzyme> Aspect of phosphoprotein phosphatase EC 3.1.3.16
    Registry number: EC 3.1.3.-
    (26 Jun 1999)
    phosphorylase phosphatase <enzyme> An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form.
    Chemical name: (Phosphorylase a) phosphohydrolase
    Registry number: EC 3.1.3.17
    (12 Dec 1998)
    phosphorylase-rupturing enzyme <enzyme> An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form.
    Chemical name: (Phosphorylase a) phosphohydrolase
    Registry number: EC 3.1.3.17
    (12 Dec 1998)
    muscle phosphorylase deficiency Type V glycogen storage disease, affecting muscle, caused by deficiency of muscle phosphorylase.
    (05 Mar 2000)
    ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
    KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • Á¦Ç°¸í
      ¼ººÐ/ÇÔ·®
      ±¸ºÐ/º¸Çè±Þ¿©
    KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • 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: 2
    ¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    ´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    ´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    ¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    ¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    ¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    ¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    ´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    ´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    ´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
      ÇÑÀÚ
    ´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
      ÇÑÀÚ
    ´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    ´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    ´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ÄÚµå
      ¿µ¹®
      ÇѱÛ
    Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ÄÚµå
      ¿µ¹®
      ÇѱÛ
    °æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
      ¼³¸í
    CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 2
    MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 2
    ¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 2
    ¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 2
    ¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
    ¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
    ¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
    ¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 2
    ¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 2
    Á¦Ç°¸í
    ÆÇ¸Å»ç
    º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
    ¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ À¯»ç °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 2
    Á¦Ç°¸í
    ÆÇ¸Å»ç
    º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
    ¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference ¸ÂÃã °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 2
    ¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 2
    ¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 2
    ¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 2
    KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    • ¿µ¹®
      ÇѱÛ
    WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 2
    ¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 2
    ¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 2
    ÅëÇÕ°Ë»ö ¿Ï·á