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"Matrix Metalloproteinase 3"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
¿µ¹® matrix ÇÑ±Û ¹ÙÅÁÁú, ±âÁú
¼³¸í   
  1. °áÇÕ Á¶Á÷ÀÇ ±âº»¹°Áú. Á ¹°Ã¼¸¦ ÁÖÁ¶Çϴ ±âÃÊ ¶Ç´Â ¹°Ã¼°¡ ¹ß»ýµÇ´Â Á¶Á÷. 2. È¿¼Ò¿Í ÀÛ¿ëÇÏ¿© È­ÇР¹ÝÀÀÀ» ÀÏÀ¸Å°´Â ¹°Áú. ¿¹¸¦ µé¸é, ³ì¸»Àº ±× È¿¼ÒÀΠ¾Æ¹Ð¶ó¾ÆÁ¦ÀÇ ±âÁúÀÌ´Ù. 2. È£Èí¿¡ ¾²À̴ ¹°Áú. ´ç·ù³ª Áö¹æ µûÀ§°¡ ÀÖ´Ù. 4. ÁÖÇüÀ̳ª ÁÖÁ¶¿¡ »ç¿ëµÇ´Â Æ².
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • metalloproteinase
    ±Ý¼Ó´Ü¹éºÐÇØÈ¿¼Ò
  • acquisition matrix number
    ȹµæÇà·Ä¼ö
  • amalgam matrix
    ¾Æ¸»°¨¶ì
  • bone matrix
    »À¹ÙÅÁÁú, °ñ±âÁú
  • cytoplasmic matrix
    ¼¼Æ÷Áú¹ÙÅÁÁú, ¼¼Æ÷Áú±âÁú
  • cartilage matrix
    ¿¬°ñ¹ÙÅÁÁú, ¿¬°ñ±âÁú
  • extracellular matrix
    ¼¼Æ÷¹Ù±ù¹ÙÅÁÁú, ¼¼Æ÷¿Ü±âÁú
  • extracellular matrix protein
    ¼¼Æ÷¹Ù±ù¹ÙÅÁÁú´Ü¹éÁú, ¼¼Æ÷¿Ü±âÁú´Ü¹éÁú
  • hair matrix
    ÅйÙÅÁÁú, ÅбâÁú
  • interterritorial matrix
    ¿µ¿ª»çÀ̹ÙÅÁÁú, ¿µ¿ª°£±âÁú
  • mitochondrial matrix
    »ç¸³Ã¼¹ÙÅÁÁú, ¹ÌÅäÄܵ帮¾Æ±âÁú
  • matrix
    ¹ÙÅÁÁú, ±âÁú
  • matrix adaptor
    ¸ÅÆ®¸¯½ºÀûÇÕ±â
  • matrix band
    ¹ÙÅÁ¶ì, ´ë»ó°Ýº®
  • matrix calculus
    ¹ÙÅÁÁúµ¹, ±âÁú°á¼®
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 3 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • metalloproteinase
    ±Ý¼Ó´Ü¹éºÐÇØÈ¿¼Ò
  • matrix
    ¹ÙÅÁÁú, ±âÁú
  • bone matrix
    »À¹ÙÅÁÁú
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • metalloproteinase
    ±Ý¼Ó´Ü¹éºÐÇØÈ¿¼Ò
  • acquisition matrix number
    ȹµæÇà·Ä¼ö
  • amalgam matrix
    (¢¡matrix band) ¶ì¹ÙÅÁ, ´ë»ó°Ýº®
  • matrix adaptor
    ¸ÅÆ®¸¯½ºÀûÇÕ±â
  • bone matrix
    »À¹ÙÅÁÁú
  • matrix band
    ¶ì¹ÙÅÁ, ´ë»ó°Ýº®
  • cartilage matrix
    ¿¬°ñ¹ÙÅÁÁú
  • chromosome matrix
    ¿°»öü¹ÙÅÁÁú
  • cytoplasmic matrix
    ¼¼Æ÷Áú¹ÙÅÁÁú
  • matrix calculus
    ¹ÙÅÁÁúµ¹
  • matrix cell
    ±âÁú¼¼Æ÷, ÅйÙÅÁÁú¼¼Æ÷
  • extracellular matrix
    ¼¼Æ÷¿Ü¹ÙÅÁÁú
  • extracellular matrix protein
    ¼¼Æ÷¿Ü°£Áú´Ü¹é
  • functional matrix theory
    ±â´É¼º±âÁú¼³
  • hair matrix
    ÅйÙÅÁÁú
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 6 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • Interteritorial matrix
    ¿µ¿ª»çÀ̹ÙÅÁÁú
  • acquisition matrix number
    ȹµæ Çà·Ä ¼ö, ȹµæ ¸ÅÆ®¸¯½º ¼ö
  • amalgam matrix
    ÇÕ±ÝÁÖÇü(ùêÐÝñÑúþ).
  • groove of matrix
    ¹ÙÅÁÁú°í¶û
  • hair matrix
    ÅбâÁú, ¸ð±âÁú(Ù¾Ðñòõ).
  • hair matrix
    ÅйÙÅÁÁú
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • metalloproteinase
    ±Ý¼Ó´Ü¹éºÐÇØÈ¿¼Ò(ÐÝáÕÓ±ÛÜÝÂú°ý£áÈ)
  • tissue inhibitor of metalloproteinase
    ±Ý¼Ó´Ü¹éºÐÇØÈ¿¼Ò
  • acquisition matrix number
    ȹµæ Çà·Ä ¼ö, ȹµæ ¸ÅÆ®¸¯½º ¼ö
  • amalgam matrix
    ÇÕ±ÝÁÖÇü(ùêÐÝñÑúþ).
  • band matrix
    ´ë»ó°Ýº®(ÓáßÒ̰Ûú).
  • bone matrix
    »À ±âÁú, °ñ ±âÁú(ÍéÐñòõ).
  • bone matrix
    »À±âÁú, °ñ±âÁú(ÍéÐñòõ).
  • bone matrix
    »À¹ÙÅÁÁú
  • cartilage matrix
    ¿¬°ñ¹ÙÅÁÁú
  • cell adhesive matrix assay
    ¼¼Æ÷Á¡Âø±âÁúºÐ¼®
  • cell matrix
    ¼¼Æ÷±âÁú
  • chromosome matrix
    ¿°»öü±âÁú(¡­Ñ¨òõ).
  • crest of matrix
    ¹ÙÅÁÁú´É¼±
  • cytoplasmic matrix
    ¼¼Æ÷Áú±âÁú(¡­Ðñòõ).
  • extracellular matrix
    ¼¼Æ÷¿Ü±âÁú
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • Matrix
    ¹ÙÅÁÁú
    [¿¾ ¿ë¾î] Á¶±âÁú
  • Groove of matrix
    ¹ÙÅÁÁú°í¶û
    [¿¾ ¿ë¾î] Á¶±âÁú±¸
  • Crest of matrix
    ¹ÙÅÁÁú´É¼±
    [¿¾ ¿ë¾î] Á¶±âÁú¸ª
  • Matrix fiber
    ¹ÙÅÁÁú¼¶À¯
    [¿¾ ¿ë¾î] ±âÁú¼¶À¯
  • Nail matrix
    ¹ßÅé¹ÙÅÁÁú
    [¿¾ ¿ë¾î] Á¶±âÁú
  • Bone matrix
    »À¹ÙÅÁÁú
    [¿¾ ¿ë¾î] °ñ±âÁú
  • Mitochondrial matrix
    »ç¸³Ã¼¹ÙÅÁÁú
    [¿¾ ¿ë¾î] »ç¸³Ã¼±âÁú
  • Nail matrix
    ¼ÕÅé¹ÙÅÁÁú
    [¿¾ ¿ë¾î] Á¶±âÁú
  • Nail matrix
    ¼ÕÅé¹ÙÅÁÁú
    [¿¾ ¿ë¾î] Á¶»ó
  • Cartilage matrix
    ¿¬°ñ¹ÙÅÁÁú
    [¿¾ ¿ë¾î] ¿¬°ñ±âÁú
  • Matrix of chromosome
    ¿°»öü¹ÙÅÁÁú
    [¿¾ ¿ë¾î] ¿°»öü±âÁú
  • Territorial matrix
    ¿µ¿ª¹ÙÅÁÁú
    [¿¾ ¿ë¾î] ±¸¿ª±âÁú
  • Interterritorial matrix
    ¿µ¿ª»çÀ̹ÙÅÁÁú
    [¿¾ ¿ë¾î] ±¸¿ª°£±âÁú
  • Hair matrix
    ÅйÙÅÁÁú
    [¿¾ ¿ë¾î] ¸ð±âÁú
  • Matrix cell
    ÅйÙÅÁÁú¼¼Æ÷
    [¿¾ ¿ë¾î] ¸ð±âÁú¼¼Æ÷
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 4 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • matrix
    ±âÁú(Ðñòõ)
  • matrix interference
    ¸ÅÆ®¸¯½º ¹æÇØ(Ûªúª)
  • matrix method
    ¸ÅÆ®¸¯½º¹ý(Ûö)
  • matrix protein
    ±âÁú´Ü¹éÁú(ѨòõÓ±ÛÜòõ)
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • acquisition matrix number
    ȹµæÇà·Ä¼ö, ȹµæ¸ÅÆ®¸¯½º¼ö
  • bone matrix
    »À±âÁú, °ñ±âÁú
  • germinal matrix
    ¹è¾Æ±âÁú
  • matrix
    ±âÁú, ¼¼Æ÷°£Áú, ¸ðÇü, ÁÖÇü, Çà·Ä, ¸ÞÆ®¸¯½º
  • matrix number
    Çà·Ä¼ö
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
MMP matrix metalloproteinase; muscle mechanical power
MMPI matrix metalloproteinase specific for collagen type I; Minnesota Multiphasic Personality Inventory
PUMP putative metalloproteinase
CMAR cell matrix adhesion regulator
CMD campomelic dysplasia; camptomelic dwarfism; cartilage matrix deficiency; chief medical director; chi...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
MMP-9 B/matrix metalloproteinase-9
EMMPRIN Extracellular matrix metalloproteinase inducer
MMP-3 MATRIX METALLOPROTEINASE-3
MMP-2 Matrix Metalloproteinase-2
MMP-1 Matrix metalloproteinase 1
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • metalloproteinase
    ±Ý¼Ó ´Ü¹é ºÐÇØ È¿¼Ò
  • acquisition matrix number
    ȹµæ Çà·Ä¼ö, ȹµæ ¸ÅÆ®¸¯½º ¼ö
  • cartilage matrix
    ¿¬°ñ ¹ÙÅÁÁú
    ¹«Á¤ÇüÀÇ ±âÁú¿¡ ºÀ¸ÅµÈ ¼¼Æ÷ ¹× ¼¼Æ÷¿Ü ¼¶À¯·Î ÀÌ·ç¾îÁø ¿¬°ñÀÇ ¼¼Æ÷°£ ¹°Áú.
  • cell adhesive matrix assay
    ¼¼Æ÷ Á¡Âø ±âÁú ºÐ¼®
  • crest of matrix
    ¹ÙÅÁÁú ´É¼±
  • cytoplasmic matrix
    ¼¼Æ÷ ±âÁú
  • dentin matrix
    »ó¾Æ ±âÁú
    À¯±âÁú°ú ¹°·Î ±¸¼ºµÇ¾î »ó¾ÆÁú¿¡ ź·Â¼ºÀ» Á¦°øÇÏ°í ¹«±âÁúÀ» Àâ¾ÆÁÖ´Â ¿ªÇÒÀ» ÇÏ´Â Ä¡¾Æ ±¸Á¶¹°.
  • extracellular matrix
    ¼¼Æ÷¿Ü ±âÁú
  • mail matrix
    ¼ÕÅé ±âÁú, ¹ßÅé ±âÁú, Á¶»ó
  • matrix adaptor
    ¸ÅÆ®¸¯½º ÀûÇÕ±â
  • matrix band
    °Ýº® ¹êµå, ȯ»ó °Ýº®
    1. 2±Þ ¿Íµ¿ ÃæÀü ½Ã »ó½ÇµÈ ÀÎÁ¢ ¸é¸¦ ´ë½ÅÇϱâ À§ÇØ ÃæÀü¹° ÃæÀü¿¡ »ç¿ëÇÏ´Â ¹êµå. 2. ¿Íµ¿ Áß¿¡ ¾Æ¸»°¨À» ÃæºÐÈ÷ Àü»öÇϱâ À§ÇÏ¿©, ¶Ç´Â º¹À⠿͵¿ÀÇ °á¼Õ º®À» ä¿ì±â À§ÇÏ¿© Ä¡¾Æ µÑ·¹¿¡ ºÙÀÎ ¾ãÀº ±Ý¼Ó Æí.
  • matrix crown
    ¸ÞÆ®¸¯½º ÁÖÁ¶°ü
    ±Ý¼Ó°üÀÇ ÀÏÁ¾À¸·Î¼­ Áö´ëÄ¡ À§¿¡ 34¹øÀÇ ¼ø±Ý ÆÇÀ» ¾ÐÁ¢ÇÏ¿© ¸ÞÆ®¸¯½º¸¦ Á¦ÀÛÇϰí, ÀÌ À§¿¡ ¼ºÇüÀ» ÇÏ¿© ÁÖÁ¶ ÈÄ ¸ÞÆ®¸¯½º¿Í ÁÖÁ¶ºÎ¸¦ ÇÕÁ¢ÇÏ¿© ¿Ï¼ºÇÑ´Ù. ±Ý¼ÓÀÇ ÁÖÁ¶ ¼öÃàÀ» ¹æÁöÇϹǷΠÀûÇÕÀÌ ÁÁ´Ù.
  • matrix granule
    ±âÁú °ú¸³
  • matrix mechanics
    Çà·Ä ¿ªÇÐ
  • matrix of chromosome
    ¿°»öü ¹ÙÅÁÁú
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
membrane-type 3 matrix metalloproteinase <enzyme> Sm3 is a soluble form of mt3-mmp, probably an alternatively sliced variant.
Registry number: EC 3.4.24.-
Synonym: mt3-mmp, sm3-mmp
(26 Jun 1999)
membrane-type 4 matrix metalloproteinase <enzyme> Cloned from breast carcinoma.
Registry number: EC 3.4.24.-
Synonym: mt4-mmp, mmp-17 gene product, mmp-17
(26 Jun 1999)
membrane-type matrix metalloproteinase <enzyme> Activates gelatinase a; isolated from a human placenta cdna gene library; contains a transmembrane domain; do not use for any other numbered matrix metalloproteinases; genbank d26512
Registry number: EC 3.4.24.-
Synonym: mt-mmp, mmp-x1 protein, matrix metalloproteinase, membrane-type, mmp14 gene product, mmp-14 gene product, mt1-mmp, matrix metalloproteinase 14, mt2-mmp, mmp15 gene product, mmp16 gene product
(26 Jun 1999)
Aspergillus fumigatus metalloproteinase <enzyme> Mol mass 82 kD; pi 5.6; hydrolyzes phenylazobenzyloxycarbonyl-pro-leu-gly-pro-arg and cleaves native rat type I collagen
Registry number: EC 3.4.24.-
Synonym: a. Fumigatus metalloproteinase, af-mep
(26 Jun 1999)
BaP1 metalloproteinase <enzyme> From bothrops asper venom; causes haemorrhage at site of venom injection and systemically in different organs
Registry number: EC 3.4.24.-
(26 Jun 1999)
haemorrhagic metalloproteinase <enzyme> Extracted from vipera berus berus venom; hydrolyzes casein, fibrinogen and splits the insulin b chain at positions ala(14)-leu(15), tyr(16)-leu(17), his(10)-leu(11); digests alpha chain of fibrinogen
Registry number: EC 3.4.24.-
(26 Jun 1999)
Xolloid metalloproteinase <enzyme> Tolloid-like protein from xenopus with development-regulating activity; acts as a ventralizing agent that mimics low doses of bone morphogenetic protein-4
Registry number: EC 3.4.24.-
Synonym: xolloid gene product
(26 Jun 1999)
S. marcescens minor metalloproteinase <enzyme> Precursor protein consists of 352 amino acids, mw 38.479 kD from serratia marcescens; mature protein consists of 300 amino acids mw 32.515 kD with optimal activity at pH 8.0 and 50c; do not confuse with smp protein, a membrane protein from E coli
Registry number: EC 3.4.24.-
Synonym: smp proteinase
(26 Jun 1999)
Streptococcus faecalis metalloproteinase <enzyme> Bacterial metalloproteinase from streptococcus faecalis
Registry number: EC 3.4.24.-
Synonym: streptococcus faecalis metalloendopeptidase, metalloproteinase (streptococcus faecalis), sf-metalloproteinase
(26 Jun 1999)
tissue-inhibitor of metalloproteinase-1 <chemical> A member of the family of tissue inhibitor of metalloproteinases. It is a n-glycosylated protein, molecular weight 28 kD, produced by a vast range of cell types and found in a variety of tissues and body fluids. It has been shown to suppress metastasis and inhibit tumour invasion in vitro.
Pharmacological action: antineoplastic agent, protease inhibitors.
(12 Dec 1998)
tissue inhibitor-of metalloproteinase-2 <chemical> A member of the family of tissue inhibitor of metalloproteinases. It is a 21 kD nonglycosylated protein found in tissue fluid and is secreted as a complex with progelatinase a by human fibroblast and uncomplexed from alveolar macrophages. An overexpression of timp-2 has been shown to inhibit invasive and metastatic activity of tumour cells and decrease tumour growth in vivo.
Pharmacological action: antineoplastic agent, protease inhibitors.
(12 Dec 1998)
tissue inhibitor of-metalloproteinase-3 <chemical> A member of the family of tissue inhibitor of metalloproteinases. It is a 21 kD, nonglycosylated protein. Timp-3 does not show a high degree of structural similarity unlike timp-1 and timp-2 which are structurally similar. However, it does possess a high degree of structural similarity with that of chicken timp-3 (chimp-3). Human timp-3 is of particular concern because of its potential role in cancer, arthritis, and eye diseases.
Pharmacological action: antineoplastic agent, protease inhibitors.
(12 Dec 1998)
tissue inhibitors of metalloproteinase <cell biology> Family of proteins of around 200 residues that can inhibit metalloproteinases, for example collagenase, by binding to them.
(18 Nov 1997)
amalgam matrix A device used during placement of the amalgam mass within a compound cavity preparation, facilitating proper condensation and contour thereof by providing a confining wall.
(05 Mar 2000)
bone matrix The intercellular substance of bone tissue consisting of collagen fibres, ground substance, and inorganic bone salts.
(05 Mar 2000)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 1 ÆäÀÌÁö: 1
  • Matrix Metalloproteinase 3 - »õâ An extracellular endopeptidase of vertebrate tissues similar to MATRIX METALLOPROTEINASE 1. It digests PROTEOGLYCAN; FIBRONECTIN; COLLAGEN types III, IV, V, and IX, and activates procollagenase. (Enzyme Nomenclature, 1992)
    Synonyms : MMP-3 Metalloproteinase, MMP3 Metalloproteinase, Stromelysin, MMP 3 Metalloproteinase, Metalloproteinase 3, Matrix, Metalloproteinase, MMP-3, Metalloproteinase, MMP3
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 6 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • dot matrix printer
    Àμâ ÀåÄ¡
  • matrix
    ÁÖÇü; ¸ðÇü
  • matrix
    ÀÚ±Ã;¸ðü;(»ý) ¼¼Æ÷ °£Áú;ÀÚ¸ð;ÁöÇü;(ÄÄÇ»ÅÍÀÇ)Çà·Ä
  • matrix management
    ¸ÅÆ®¸¯½º ¸Å´ÏÁö¸ÕÆ®(Àü¹® ½ºÅÂÇÁ¸¦ ÇöÁöÀÇ ÀÏ»ó ¾÷¹« Á¶¾ðÀÚ°â Áß¾Ó ½ºÅÂÇÁ°¡ µÇ°Ô ÇÏ´Â Á¶Á÷ ÇüÅÂ
  • matrix sentence
    ¸ðÇü¹® (º¸±â,The book that I want is gone.ÀÇ the book is gone)
  • matrix system
    ¸ÅÆ®¸¯½º ½Ã½ºÅÛ (Á¾Àû Á¶Á÷ »Ó ¾Æ´Ï¶ó ȾÀû ÇÁ·ÎÁ§Æ® ÆÀÀÇ ÀÏ¿øµµ µÇ°Ô ÇÏ´Â °æ¿µ ½Ã½ºÅÛ)
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • 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: 1
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
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