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"protein domain"¿¡ ´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® protein ÇÑ±Û ´Ü¹éÁú
¼³¸í   
  Åº¼Ò, ¼ö¼Ò, »ê¼Ò, Áú¼Ò, È²À» ÇÔÀ¯Çϰí Àִ À¯±âÈ­ÇÕ¹°·Î, ¸ðµç ¼¼Æ÷ÀÇ ¿øÇüÁúÀ» ÀÌ·ç°í Àִ ±âº» ±¸¼º¹°ÁúÀÌ´Ù. ´Ü¹éÁúÀº ±× ´ÜÀ§ÀΠ¾Æ¹Ì³ë»êµéÀÌ ÆéƼµå°áÇÕ¿¡ ÀÇÇØ °áÇյǾî ÀÖÀ¸¸ç, º¸Åë 20°³ÀÇ ¾Æ¹Ì³ë»êµéÀÌ ´Ù¸¥ ¼ø¼­¿Í Á¶¼ºÀ» °¡Áö°í ¹è¿­µÇ¾î, µ¶Æ¯ÇÑ ÇϳªÀÇ ´Ü¹éÁúÀ» Çü¼ºÇϰԠµÈ´Ù.
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • domain
    1. ¿µ¿ª, Á¤ÀÇ¿ª, ±¸¿ª 2. µµ¸ÞÀÎ
  • immunoglobulin domain
    ¸é¿ª±Û·ÎºÒ¸°¿µ¿ª
  • magnetic domain
    Àڱⱸ¿ª
  • antifreeze protein
    Ç×µ¿°á´Ü¹éÁú
  • antiviral protein
    Ç×¹ÙÀÌ·¯½º´Ü¹éÁú
  • adherence protein
    ºÎÂø´Ü¹éÁú
  • androgen binding protein
    ¾Èµå·Î°Õ°áÇմܹéÁú
  • Bence Jones protein
    º¥½º-Á¸½º´Ü¹éÁú
  • coat protein
    ¿ÜÇǴܹéÁú
  • competitive protein binding radioassay
    °æÇմܹéÁú°áÇÕ¹æ»çÃøÁ¤(¹ý)
  • conjugated protein
    Á¢ÇմܹéÁú, °áÇմܹéÁú
  • contractile protein
    ¼öÃà´Ü¹éÁú
  • core protein
    ÇٽɴܹéÁú
  • C-reactive protein
    C-¹ÝÀÀ´Ü¹éÁú
  • cytotoxic cell protein
    ¼¼Æ÷µ¶¼º¼¼Æ÷´Ü¹éÁú
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 8 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • domain
    ¿µ¿ª
  • protein binding
    ´Ü¹é°áÇÕ
  • protein-losing enteropathy
    ´Ü¹é¼Ò½ÇâÀÚº´Áõ
  • protein
    ´Ü¹é, ´Ü¹éÁú
  • adherence protein
    ºÎÂø´Ü¹é
  • reserve protein
    ÀúÀå´Ü¹é
  • split-timed urine protein
    ½Ã°£´ëº°¿ä´Ü¹éÁ¤·®
  • structural protein
    ±¸Á¶´Ü¹é, ±¸Á¶´Ü¹éÁú
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • domain
    µµ¸ÞÀÎ, Á¤ÀDZ¸¿ª, ¿µ¿ª
  • immunoglobulin domain
    ¸é¿ª±Û·ÎºÒ¸°¿µ¿ª
  • magnetic domain
    Àڱ⿵¿ª, ÀÚ¼º¿µ¿ª
  • adherence protein
    ºÎÂø´Ü¹é
  • antifreeze protein
    Ç×µ¿°á´Ü¹éÁú
  • protein binding
    ´Ü¹é°áÇÕ
  • carrier protein
    ¿î¹Ý´Ü¹é, ¿î¹Ý´Ü¹éÁú
  • catabolite activating protein
    ÀÌÈ­»ê¹°È°¼ºÈ­´Ü¹é
  • coat protein
    ¿ÜÇǴܹé
  • competitive protein binding radioassay
    °æÇմܹé°áÇÕ¹æ»çÃøÁ¤(¹ý)
  • conjugated protein
    º¹Çմܹé, Á¢ÇմܹéÁú
  • contractile protein
    ¼öÃà´Ü¹éÁú
  • core protein
    Çٽɴܹé
  • cytotoxic cell protein
    ¼¼Æ÷µ¶¼º¼¼Æ÷´Ü¹é
  • denatured protein
    º¯¼º´Ü¹é
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • immunoglobulin domain
    ¸é¿ª±Û·ÎºÒ¸°¿µ¿ª.
  • AA protein
    ¾Æ¹Ð·ÎÀ̵åA´Ü¹é(¡­Ó±ÛÜ)
  • ABP=> androgen-binding protein
    ¾Èµå·ÎÁ¨°áÇմܹé
  • Bence Jones protein
    º¥½º-Á¸½º´Ü¹é.
  • Bence-Jones protein
    º¥½º-Á¸½º ´Ü¹éÁú
  • C protein
    C´Ü¹éÁú
  • C-Fos protein
    ¾¾-Æ÷½º´Ü¹é(Ó±ÛÜ)
  • C-reative protein =CRP
    C¹ÝÀÀ¼º ´Ü¹é(Áú).
  • C-reative protein =CRP
    [¸é¿ª] [ÀÓº´]C¹ÝÀÀ¼º ´Ü¹éÁú.
  • DNA-binding protein
    DNA °áÇմܹéÁú
  • G protein
    G ´Ü¹é(Ó±ÛÜ)
  • 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
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • domain
    µµ¸ÞÀÎ, Á¤ÀDZ¸¿ª
  • domain
    ¿µ¿ª(ÖÅæ´)
  • domain
    ¿µ¿ª(ËçËç).
  • domain
    ¿µ¿ª(çÐæ´).
  • domain structure
    ¿µ¿ª±¸Á¶
  • immunoglobulin domain
    ¸é¿ª±Û·ÎºÒ¸°¿µ¿ª.
  • magnetic domain
    ÀÚ±â(ÀÚ¼º) ¿µ¿ª
  • 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
  • acute phase reactive protein
    ±Þ¼º±â ¹ÝÀÀ¼º ´Ü¹é.
  • al protein
    AL ´Ü¹é(¡­Ó±ÛÜ)
  • amyloid precurssor protein
    ¾Æ¹Ð·ÎÀ̵å Àü±¸ ´Ü¹éÁú
  • androgen- binding protein
    ¸¸¼ºÈ£¸£¸ó °áÇմܹé
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • Protein granule
    ´Ü¹éÁú°ú¸³
    [¿¾ ¿ë¾î] ´Ü¹éÁú°ú¸³
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 4 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • adherence protein
    ºÎÂø´Ü¹éÁú
  • circumsporozoite protein (CSP)
    Æ÷ÀÚ¼Òü¸·´Ü¹éÁú
  • protein layer
    ´Ü¹éÁúÃþ
  • stage-specific protein
    ¹ßÀ°´Ü°èƯÀ̴ܹéÁú
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • protein domain
    ´Ü¹éÁú ¿µ¿ª(Ó±ÛÜòõÖÅæ´)
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • domain
    ¿µ¿ª(ÖÅæ´)
  • mononucleotide binding domain
    ¸ð³ë´©Å¬·¹¿ÀŸÀÌµå °áÇÕ¿µ¿ª(Ì¿ùêÖÅæ´)
  • nucleotide-binding domain
    ´©Å¬¸®¿ÀŸÀÌµå °áÇÕ¿µ¿ª(Ì¿ùêÖÅæ´)
  • 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)
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 11 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • domain
    ¿µ¿ª, µµ¸ÞÀÎ, Á¤ÀDZ¸¿ª
  • magnetic domain
    Àڱ⿵¿ª
  • Bence-Jones protein
    º¥½º-Á¸½º´Ü¹é
  • C-reactive protein
    C-¹ÝÀÀ¼º´Ü¹éÁú
  • high protein diet
    °í´Ü¹é½ÄÀÌ
  • plasma protein
    Ç÷Àå´Ü¹éÁú
  • protein
    ´Ü¹é(Áú)
  • protein metabolism
    ´Ü¹é(Áú)´ë»ç
  • protein-losing enteropathy
    ´Ü¹é»ó½Ç¼ºÀ庴Áõ
  • protein-losing gastroenteropathy
    ´Ü¹é»ó½Ç¼ºÀ§ÀåÁõ
  • serum protein
    Ç÷û´Ü¹é
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
MAP malignant atrophic papulosis; mandibular angle plane; maturation-activated protein; maximal aerobic ...
MBP major basic protein; maltose-binding protein; management by policy; mannose-binding protein; mean bl...
RP radial pulse; radiopharmaceutical; rapid processing [of film]; Raynaud phenomenon; reactive protein;...
DNS Domain Name System
FQDN Fully Qualified Domain Name
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
FADD FAS-associated death domain protein
AD activation domain
CTD C-terminal domain
CTD COOH-terminal domain
CRD Carbohydrate recognition domain
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • domain structure
    ¿µ¿ª ±¸Á¶
  • salivary domain
    Ÿ¾× ¿µ¿ª
  • abnormal protein
    ºñÁ¤»ó ´Ü¹éÁú
  • activated protein C resistance
    Ȱ¼ºÈ­ C ´Ü¹é ³»¼º
  • acute phase protein
    ±Þ¼º±â ´Ü¹éÁú
    °¨¿°À̳ª Á¶Á÷ ¼Õ»óÀÌ ÀÖÀ» ¶§ Á¤»óº¸´Ù 2-100¹è Á¤µµ Áõ°¡ÇÏ´Â Ç÷Àå ´Ü¹éÁúÀ» ÃÑĪÇÏ¿© APP¶ó°í ÇÏ¸ç ¼±Ãµ¼º ¸é¿ª¿¡ °ü¿©ÇÑ´Ù.
  • androgen binding protein
    ³²¼º È£¸£¸ó °áÇÕ ´Ü¹é
  • bacterio protein
    ¼¼±Õ ´Ü¹éÁú
  • body protein
    ü´Ü¹é, ü´Ü¹éÁú
  • C-reactive protein
    C-¹ÝÀÀ ´Ü¹é, C-¹ÝÀÀ¼º ´Ü¹éÁú
  • cellular retinoid acid-binding protein
    ¼¼Æ÷³» ·¹Æ¼³ëÀ̵å»ê °áÇÕ ´Ü¹é
  • chromatographic protein separation
    Å©·Î¸¶Åä±×·¡Çǹý ´Ü¹é ºÐ¸®
  • D-myeloma protein
    D-°ñ¼öÁ¾ ´Ü¹é
    ¸é¿ª ±Û·ÎºÎ¸°ÀÇ ÇÑ ºÎ·ùÀÎ IgD¸¦ »ý»êÇÏ´Â °ñ¼öÁ¾¿¡¼­ ¸¸µé¾îÁø ´Ü¹éÁú.
  • eosinophil protein X
    È£»ê±¸ ´Ü¹é X
  • estrogen receptor protein
    ¿¡½ºÆ®·Î°Õ ¼ö¿ëü ´Ü¹éÁú
  • hapten-protein conjugate
    ÇÕÅÙ ´Ü¹é °áÇÕ¹°
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
apple domain <molecular biology> A consensus sequence, composed of 90 amino acids including 6 cysteines, that forms a characteristic, vaguely apple shaped, pattern via disulphide bridges. Shared by plasma kallikrein and coagulation factor XI, both serine proteases.
(18 Nov 1997)
carboxy-terminal domain kinase <enzyme> Protein kinase that phosphorylates the c-terminal repeat domain of the largest subunit of RNA polymerase II at serine residues
Registry number: EC 2.7.1.-
Synonym: ctd kinase, hs-ctd kinase, tfiih-associated ctd kinase
(26 Jun 1999)
paired box domain <molecular biology> Conserved domain of 128 amino acids, found in several developmentally regulated proteins in Drosophila (for example paired, gooseberry, Pox), mouse and human (for example Pax, HuP1, HuP48).
(18 Nov 1997)
POU domain <molecular biology> A conserved protein domain of around 150 amino acids, composed of a 20 amino acid homeobox domain and a larger POU specific domain and so is the target of some transcription factors.
Named POU (Pit Oct Unc) after 3 such proteins: Pit 1 regulates expression of certain pituitary genes, Oct 1 and 2, that bind an octamer sequence in the promoters of histone H2A and some immunoglobulin genes and Unc 86, involved in nematode sensory neuron development.
(31 Dec 1997)
SH3 domain-containing proline-rich kinase <enzyme> A protein kinase which both phosphorylates ser and thr residues and has an sh3 domain; contains 847 amino acid residues; mol mass 92,688 da; genbank u07747
Registry number: EC 2.7.10.-
Synonym: src-homology 3 domain-containing proline-rich kinase, sprk protein, sprk gene product
(26 Jun 1999)
dinucleotide domain A structural domain in certain proteins that binds NAD+ or NADP+.
Synonym: dinucleotide domain.
(05 Mar 2000)
domain <molecular biology> Used to describe a part of a molecule or structure that shares common physico chemical features, for example hydrophobic, polar, globular, helical domains or properties for example DNA binding domain, ATP binding domain.
(18 Nov 1997)
EGF like domain Region of 30-40 amino acids containing 6 cysteines found originally in EGF and also in a range of proteins involved in cell signalling.
Examples: TGF _, amphiregulin, urokinase, tissue plasminogen activator, complement C6 C9, fibronectin, laminin (each subunit at least 13 times), nidogen, selectins. It is also found in the Drosophila gene products: Notch (36 times) Delta, Slit, Crumbs, Serrate.
(18 Nov 1997)
exit domain <molecular biology> One of the two main binding sites on the ribosome molecule. The finished portion of the polypeptide being translated is attached to this site and leaves the ribosome from this site when the entire polypeptide is finished.
(09 Oct 1997)
frequency domain The expression of a function by its amplitude and phase at each component frequency, usually as determined by Fourier analysis.
(05 Mar 2000)
LIM domain Domain found in proteins required for developmental decisions. Contain 60 residue conserved, cysteine rich, repeats. Named after first 3 genes in group: Lin 11 (C. Elegans required for asymmetric division of blast cells), IsI 1 (mammalian insulin gene binding enhancer protein), mec 3 (C. Elegans required for differentiation of a set of sensory neurons).
(18 Nov 1997)
acetoacetyl-acyl carrier protein synthase <enzyme> E coli enzyme, that catalyses condensation of malonyl-acyl carrier protein plus acetyl-acyl carrier protein; not inhibited by cerulenin
Registry number: EC 2.3.1.-
Synonym: acetoacetyl-acp synthase
(26 Jun 1999)
acid soluble spore protein <molecular biology> A DNA binding protein in the spores of some bacteria, thought to stabilise the DNA in an A configuration, so protecting it from cleavage by enzymes or UV light.
(18 Nov 1997)
acute-phase protein <haematology> These plasma proteins (in addition to fibrinogen) increase 25% or more in response to inflammation and injury are under direct control of interleukin-6 (IL-6) (hepatocyte-stimulating factor).
Other proteins which increase are ceruloplasmin, C3 and C4 which increase 50% or more; alpha-1 acid glycoprotein, alpha-1 antitrypsin, haptoglobin and fibrinogen (the major determinant of viscosity 1 ) which increase two- to fourfold; C-reactive protein (CRP) and serum amyloid A which increase several hundred-fold.
Despite long-held clinical opinion to the contrary, available data indicate that neither ESR nor measurement of specific acute-phase reactants are useful in excluding underlying infection or inflammation regardless of the pretest probability.
These proteins are secreted into the blood in increased or decreased quantities by hepatocytes in response to trauma, inflammation, or disease. They can serve as inhibitors or mediators of the inflammatory processes. Certain acute-phase proteins have been used to diagnose and follow the course of diseases or as tumour markers.
See also: amyloid, c-reactive protein, erythrocyte sedimentation rate, viscosity.
(25 Jun 1999)
acyl-(acyl-carrier-protein)-phospholipid acyltransferase <enzyme> Catalyses the formation of phosphatidylethanolamine from acyl-acyl carrier protein and 2-acyl-sn-glycero-3-phosphoethanolamine
Registry number: EC 2.3.1.40
Synonym: 2-acyl-gpe acyltransferase, 2-acylglycerophosphoethanolamine acyltransferase
(26 Jun 1999)
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 12 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • domain
    ¿µÅä;¿µ¿ª;ÅäÁö;°³ÀÎ ¼ÒÀ¯Áö;¹üÀ§;º¯¿ª;¿µ¿ª;ÀÚ±¸
  • eminent domain
    (¹ý)ÅäÁö ¼ö¿ë±Ç
  • magnetic domain
    (°­ÀÚ¼ºÃ¼ÀÇ) ÀÚ±¸
  • public domain
    (ÁÖ³ª Á¤ºÎÀÇ)°øÀ¯Áö(in the public domain(ÀúÀÛ±Ç Æ¯Çã±Ç ¼Ò¸ê¿¡ ÀÇÇØ)ÀÚÀ¯·Î »ç¿ëÇÒ ¼ö ÀÖ´Â)
  • public domain
    °øÀ¯Áö;ÀÚÀ¯·Î »ç¿ëÇÒ ¼ö ÀÖ´Â
  • protein
    ´Ü¹éÁú
  • coat protein
    ÇǸ· ´Ü¹é
  • conjugated protein
    º¹ÇÕ ´Ü¹éÁú
  • fish protein concentrate
    ¾îÀ° ³óÃà ´Ü¹é
  • protein
    ´Ü¹éÁú;´Ü¹éÁúÀÇ(À» ÇÔÀ¯ÇÏ´Â). proteinic a.
  • protein clock
    ´Ü¹éÁú ½Ã°è(´Ü¹éÁú ÁøÈ­ ¼Óµµ¸¦ Á¶ÀýÇÏ´Â °¡¼³Àû ü³» ±â±¸)
  • repressor protein
    ¾ïÁ¦ ´Ü¹é(Á¦¾î À¯ÀüÀÚ¿¡ ÀÇÇÏ¿© ¸¸µé¾îÁö´Â ´Ü¹é)
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®
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