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"protein modification"¿¡ ´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.
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  • ¿µ¹®
    ÇѱÛ
  • antigen modification
    Ç׿øº¯È­, Ç׿ø¼ö½Ä
  • allotropic modification
    µ¿¼Òüº¯Çü
  • behavioral modification
    Çൿ¼öÁ¤
  • host-controlled modification
    ¼÷ÁÖÁ¶Àý¼ö½Ä
  • modification
    º¯Çü, º¯È­, º¯°æ, ¼ö½Ä, ¼öÁ¤
  • phenotypic modification
    Ç¥ÇöÇüº¯È­
  • 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
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 9 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • modification
    º¯È­, ¼ö½Ä
  • behavioral modification
    Çൿ¼öÁ¤
  • 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
  • allotropic modification
    µ¿¼Òüº¯Çü
  • antigen modification
    Ç׿øº¯È­, Ç׿ø¼ö½Ä
  • behavioral modification
    Çൿ¼öÁ¤
  • host-controlled modification
    ¼÷ÁÖÁ¶Àý¼ö½Ä
  • modification
    º¯È­, ¼ö½Ä
  • phenotypic modification
    Ç¥ÇöÇüº¯È­
  • 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
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • allotropic modification
    µ¿¼Òüº¯Çü(ÔÒáÈô÷ܨû¡).
  • antigen modification
    Ç׿øº¯Çü.
  • phenotypic modification
    Ç¥ÇöÇü ¼ö½Ä, Ç¥ÇöÇü º¯È­
  • 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
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • allotropic modification
    µ¿¼Òüº¯Çü(ÔÒáÈô÷ܨû¡).
  • antigen modification
    Ç׿øº¯Çü.
  • behavior modification technique
    Çൿ(ÇàÅÂ)¼öÁ¤±â¹ý
  • behavioral modification
    Çൿ¼öÁ¤
  • host-controlled modification
    ¼÷ÁÖÁ¶Àý¼ö½Ä
  • modification of karyotype
    ÇÙÇüº¯ÀÌ
  • modification, behavioral
  • phenotypic modification
    Ç¥ÇöÇü ¼ö½Ä, Ç¥ÇöÇü º¯È­
  • 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
´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 modification
    ´Ü¹éÁú ¼ö½Ä(Ó±ÛÜòõáóãÞ)
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • covalently modification
    °øÀ¯°áÇÕ ¼ö½Ä(ÍìêóÌ¿ùêáóãÞ)
  • DNA modification
    "DNA ¼ö½Ä(áóãÞ), (ÔÒ) postreplicative modification"
  • host-controlled modification
    ¼÷ÁÖÁ¦¾î ¼ö½Ä(âÖñ«ð¤åÙáóãÞ)
  • host-induced modification
    ¼÷ÁÖÀ¯µµ ¼ö½Ä(âÖñ«ë¯ÓôáóãÞ)
  • modification
    ¼ö½Ä(áóãÞ)
  • modification allele
    ¼ö½Ä´ë¸³À¯ÀüÀÚ(áóãÞÓߨ¡ë¶îîí­)
  • modification and restriction
    ¼ö½Ä(áóãÞ)°ú Á¦ÇÑ(ð¤ùÚ)
  • modification enzyme
    ¼ö½ÄÈ¿¼Ò(áóãÞý£áÈ)
  • modification gene
    ¼ö½ÄÈ¿¼Ò À¯ÀüÀÚ(áóãÞý£áÈë¶îîí­)
  • modification methylase
    ¼ö½Ä(áóãÞ)¸ÞÆ¿·¹À̽º
  • postreplicative modification
    º¹Á¦ÈÄ ¼ö½Ä(áóãÞ)
  • post-trancriptional modification
    Àü»çÈÄ ¼ö½Ä(ï®ÞÐý­áóãÞ)
  • post-translational modification
    ¹ø¿ªÈÄ ¼ö½Ä(Ûèæ»ý­áóãÞ)
  • restriction-modification system
    Á¦ÇÑ ¼ö½Ä(áóãÞ) ½Ã½ºÅÛ
  • RNA modification
    RNA ¼ö½Ä(áóãÞ)
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 10 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • modification
    ¼öÁ¤
  • 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
Bmod behavior modification
CM California mastitis [test]; calmodulin; capreomycin; carboxymethyl; cardiac murmur; cardiac muscle; ...
CMS children's medical services; Christian Medical Society; chronic myelodysplastic syndrome; chromosome...
EBM electrophysiologic behavior modification; epidermal basement membrane; evidence-based medicine; expr...
ICD-9-CM International Classification of Diseases-ninth revision-Clinical Modification
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
DMF Dose modification factors
ICD9CM International Classification of Diseases 9th Revision Clinical Modification
ICD-9 CM International Classification of Diseases, Ninth Revision, Clinical Modification
MDRD Modification of Diet in Renal Disease
R-M Restriction and modification
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • behavior modification
    Çൿ º¯Çü, Çൿ Á¶Àý, Çൿ º¯¿ë¹ý, Çൿ ¼öÁ¤
    ÁÖ¾îÁø Àڱؿ¡ ´ëÇØ »õ·Î¿î ¹ÝÀÀÀ¸·Î ´ëÄ¡ÇÔÀ¸·Î¼­ °üÂû °¡´ÉÇÑ ÇൿÀÇ ÇüŸ¦ º¯È­½ÃŰ·Á°í ½ÃµµÇÏ´Â Á¤½Å Ä¡·á¹ý.
  • behavioral modification
    Çൿ º¯Çü, Çൿ ¼öÁ¤
  • clinical modification code
    ÀÓ»ó ¼öÁ¤ ºÎÈ£
  • function modification
    ±â´É º¯Çü
  • modification of karyotype
    ÇÙÇü º¯ÀÌ
  • speech aid prosthesis modification
    ¹ßÀ½ º¸Á¶ º¸Ã¶¹° º¯Çü
  • 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¸®
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
modification 1. A nonhereditary change in an organism; e.g., one that is acquired from its own activity or environment.
2. A chemical or structural alteration in a molecule.
Behaviour modification, the systematic use of principles of conditioning and learning, especially operant or instrumental conditioning, to teach certain skills or to extinguish undesirable behaviours, attitudes, or phobias.
Chemical modification, alteration in the structure of a molecule, typically a macromolecule such as a protein, by chemical means; often, the covalent addition by some reagent.
Covalent modification, alteration in the structure of a macromolecule by enzymatic means, resulting in a change in the properties of that macromolecule; frequently, this type of modification is physiologically relevant.
(05 Mar 2000)
modification enzyme <enzyme, molecular biology> An enzyme that introduces minor bases into DNA or RNA or that alters bases already incorporated. Serves to alter the sequence so that restriction enzymes will not damage the strand.
(18 Nov 1997)
post-translational modification The enzymatic processing of a polypeptide chain after translation from messenger RNA and after peptide bond formation has occurred.
Examples include glycosylation, acylation, limited proteolysis, phosphorylation, isoprenylation.
(10 Oct 1997)
ScrFI modification methylase <enzyme> From lactococcus lactis subsp. Cremoris uc503; recognises sequence ccngg and forms m(5)ccngg; see also DNA modification methylase dsav and DNA modification methylase ssoii
Registry number: EC 2.1.1.-
Synonym: scrfi methylase
(26 Jun 1999)
host restriction-modification A bacterial system where the bacterium is able to destroy invading DNA from a bacteriophage (virus which infects bacteria) while at the same time preventing the destruction of their own DNA. The phage DNA is cleaved by a restriction enzyme made by the bacterium, the bacterial DNA is modified (usually with methylation) so that the enzyme will not destroy it.
(09 Oct 1997)
Stirling's modification of Gram's stain <technique> A stable aniline-crystal violet stain.
(05 Mar 2000)
DNA modification <molecular biology> A variety of chemical changes made to a DNA molecule just after it has been replicated. An example is DNA methylation.
(09 Oct 1997)
DNA modification methylases <enzyme> Enzymes that are part of the restriction-modification systems. They are responsible for producing a species-characteristic methylation pattern, on either adenine or cytosine residues, in a specific short base sequence in the host cell's own DNA. This methylated sequence will occur many times in the hosT-cell DNA and remain intact for the lifetime of the cell. Any DNA from another species which gains entry into a living cell and lacks the characteristic methylation pattern will be recognised by the restriction endonucleases of similar specificity and destroyed by cleavage. most have been studied in bacterial systems, but a few have been found in eukaryotic organisms.
Registry number: EC 2.1.1.-
(12 Dec 1998)
DNA restriction-modification enzymes Systems consisting of two enzymes, a modification methylase and a restriction endonuclease. They are closely related in their specificity and protect the DNA of a given bacterial species. The methylase adds methyl groups to adenine or cytosine residues in the same target sequence that constitutes the restriction enzyme binding site. The methylation renders the target site resistant to restriction, thereby protecting DNA against cleavage.
(12 Dec 1998)
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)
acyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine acyltransferase <enzyme> E coli enzyme involved in lipid a biosynthesis; uses beta-hydroxymyristoyl-acyl carrier protein to form udp-3-monoacyl-n-acetylglucosamine; amino acid sequence given in second source
Registry number: EC 2.3.1.129
Synonym: udp-aguatransferase, lpxa protein, udp-n-acetylglucosamine-3-acyltransferase, udp-n-acetylglucosamine 3-o-acyltransferase, udp-3-o-(r-3-hydroxymyristoyl)glucosamine-n-acyltransferase, lpxd protein, fira gene product, fira protein
(26 Jun 1999)
acyl carrier protein <protein> A small (77 peptides long) protein which binds six other enzymes involved in fatty acid synthesis. It was first isolated in E. Coli bacteria.
(09 Oct 1997)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 1 ÆäÀÌÁö: 1
  • Protein Modification, Translational - »õâ Any of the enzymatically catalyzed modifications of the individual AMINO ACIDS of PROTEINS, and enzymatic cleavage or crosslinking of peptide chains that occur pre-translationally (on the amino acid component of AMINO ACYL TRNA), co-translationally (during the process of GENETIC TRANSLATION), or after translation is completed (POST-TRANSLATIONAL PROTEIN PROCESSING).
    Synonyms : Amino Acid Modification, Pre-Translational, Amino Acid Modification, Pretranslational, Amino Acid Modification, Translational, Co-Translational Amino Acid Modification, Co-Translational Protein Modification, Co-Translational Protein Processing
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 8 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • modification
    °¡°¨;¼öÁ¤;¼ö½Ä
  • 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¿©
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  • ¿µ¹®
    ÇѱÛ
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  • ¿µ¹®
    ÇѱÛ
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  • ¿µ¹®
    ÇѱÛ
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  • ¿µ¹®
    ÇѱÛ
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