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"periplasmic protein disulfide oxidoreductase"¿¡ ´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
  • oxidoreductase
    »êȭȯ¿øÈ¿¼Ò
  • periplasmic enzyme
    ¿øÇüÁú¸·ÁÖÀ§È¿¼Ò
  • periplasmic space
    ¿øÇüÁú¸·ÁÖÀ§°ø°£
  • carbon disulfide
    ÀÌȲȭź¼Ò
  • disulfide
    ÀÌȲȭ¹°
  • disulfide bond
    ÀÌȲ°áÇÕ
  • hydrogen disulfide
    ÀÌȲȭ¼ö¼Ò
  • 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
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 7 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • 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
  • oxidoreductase
    »êȭȯ¿øÈ¿¼Ò
  • periplasmic enzyme
    ¿øÇüÁú¸·ÁÖÀ§È¿¼Ò
  • periplasmic space
    ¿øÇüÁú¸·ÁÖÀ§°ø°£
  • disulfide bond
    µð¼³Çǵå°áÇÕ
  • carbon disulfide
    ÀÌȲȭź¼Ò
  • disulfide
    ÀÌȲȭ¹°
  • hydrogen disulfide
    ÀÌȲȭ¼ö¼Ò
  • 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
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • hydrogen disulfide
    ÀÌȲȭ¼ö¼Ò.
  • 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
  • periplasmic binding protein
    ¿øÇüÁú¸· ÁÖÀ§°ø°£ °áÇմܹéÁú
  • oxidoreducase =oxidoreductase
    »êȭȯ ¿øÈ¿¼Ò(¡­ü½êªý£áÈ), ¿Á½Ãµµ¸®´ÚÅ×À̽º.
  • periplasmic enzyme
    ¿øÇüÁú¸· ÁÖÀ§°ø°£ È¿¼Ò
  • periplasmic space
    ¿øÇüÁú¸· ÁÖÀ§°ø°£
  • carbon disulfide
    ÀÌȲȭ(ì£üÜûù)ź¼Ò.
  • carbon disulfide poisoning
    ÀÌȲȭź¼ÒÁßµ¶(¡­ñéÔ¸).
  • disulfide
    ÀÌȲȭ¹°(ì£üÜûùÚª).
  • disulfide bond
    µð¼³Çǵå<ÀÌȲȭ>°áÇÕ
  • disulfide bond
    µð¼³Çǵå<ÀÌȲȭ>°áÇÕ (¡­Ì¿ùê).
  • hydrogen disulfide
    ÀÌȲȭ¼ö¼Ò.
  • nickel disulfide
    ÀÌȲȭ(ì£üÜûù)´ÏÄÌ.
  • 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
´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 À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • periplasmic component
    ÁÖº¯¼¼Æ÷Áú ¼ººÐ(ñ²Ü«á¬øàòõà÷ÝÂ)
  • periplasmic enzyme
    ÁÖº¯ ¼¼Æ÷Áú È¿¼Ò(ñ²Ü«á¬øàòõý£áÈ)
  • periplasmic permease
    ¼¼Æ÷ÁÖ°­¼ººÐ(á¬øàñ²Ë·à÷ÝÂ) ÆÛ¹Ì¿¡À̽º
  • periplasmic space
    ¼¼Æ÷ÁÖ°­(á¬øàñ²Ë·)
  • cytochrome c : oxygen oxidoreductase
    »çÀÌÅäÅ©·Ò c »ê¼Ò(ß«áÈ) ¿Á½Ãµµ¸®´öÅ×À̽º (ÔÒ) complex IV
  • disulfide
    ÀÌȲȭ¹°(ì£üÜûùÚª)
  • disulfide bond
    ÀÌȲ°áÇÕ(ì£üÜÌ¿ùê)
  • disulfide bridge
    "ÀÌȲ °¡±³(ì£üÜÊ­Îé), (ÔÒ) disulfide bond"
  • disulfide interchange
    ÀÌȲȭ¹°±³È¯(ì£üÜü§ÚªÎßüµ)
  • disulfide link
    "ÀÌȲ ¿¬°á(ì£üÜÖ§Ì¿), (ÔÒ) disulfide bond"
  • ferredoxin-NADP-oxidoreductase
    Æä¸®µ¶½Å-NADP-¿Á½Ãµµ¸®´ÚÅ×À̽º
  • NADH : ubiquinone oxidoreductase
    NADH À¯ºñÅ¥³í ¿Á½Ãµµ¸®´ÚÅ×À̽º
  • oxidoreductase
    "¿Á½Ãµµ¸®´ÚÅ×À̽º, »êȭȯ¿øÈ¿¼Ò(ß«ûùü½êªý£áÈ)"
  • succinate:ubiquinone oxidoreductase
    ¼÷½Å»ê(ß«):À¯ºñÄû³í ¿Á½Ãµµ¸®´ÚÅ×À̽º
  • accelerator protein
    ÃËÁø´Ü¹éÁú (õµòäÓ±ÛÜòõ)
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 9 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • 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
DDD AV universal [pacemaker]; defined daily dose; degenerative disc disease; dehydroxydinaphthyl disulfi...
NMOR nemadione oxidoreductase; N-nitrosomorpholine
NQO NAD(P)H:quinone oxidoreductase
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...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
PDI Protein disulfide isomerase
CS2 Carbon Disulfide
DADS Diallyl disulfide
DMDS Dimethyl disulfide
dsFv Disulfide-stabilized Fv
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • carbon disulfide poisoning
    ÀÌȲȭ ź¼Ò Áßµ¶
    ÀÌȲȭ ź¼Ò¿¡ ³ëÃâµÇ¾î »ý±â´Â Àü½Å ¼è¾à, ºÒ¸é, ½Ã·Â Àå¾Ö¸¦ Ư¡À¸·Î ÇÏ´Â Áßµ¶ Áõ¼¼.
  • hydrogen disulfide
    ÀÌȲȭ ¼ö¼Ò
  • periplasmic
    ¼¼Æ÷ ÇüÁúÀÇ
  • periplasmic enzyme
    ¿øÇüÁú¸· ÁÖÀ§ °ø°£ È¿¼Ò
  • 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
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
periplasmic protein disulfide oxidoreductase <enzyme> Isolated from haemophilus influenzae; may be required for assembly or folding of one or more disulfide-containing cell envelope proteins; ccmg isolated from paracoccus denitrificans
Registry number: EC 1.8.4.-
Synonym: por disulfide oxidoreductase, por gene product, periplasmic oxidoreductase, ccmg gene product
(26 Jun 1999)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
protein disulfide-isomerase <enzyme> An enzyme that catalyses the rearrangement of disulfide bonds within proteins during folding. It is a monomer identical to one of the subunits of procollagen-proline dioxygenase.
Chemical name: Protein disulfide-isomerase
Registry number: EC 5.3.4.1
(12 Dec 1998)
protein disulfide reductase (glutathione) <enzyme> An enzyme that catalyses the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates.
Chemical name: Glutathione:protein-disulfide oxidoreductase
Registry number: EC 1.8.4.2
(12 Dec 1998)
periplasmic binding proteins Transport proteins located within the periplasmic space. Some act as receptors for bacterial chemotaxis, interacting with MCPs. Their mode of action is unclear.
(18 Nov 1997)
periplasmic space Structureless region between the plasma membrane and the cell wall of gram-negative bacteria.
(18 Nov 1997)
Escherichia coli periplasmic proteinase <enzyme> Included in group of microbial serine proteinases, EC 3.4.21.14
Registry number: EC 3.4.21.-
Synonym: E coli protease I, proteinase i
(26 Jun 1999)
molybdenum-iron protein aldehyde oxidoreductase <enzyme> Related to xanthine oxidase; isolated from desulfovibrio gigas
Registry number: EC 1.2.7.-
Synonym: mop protein
(26 Jun 1999)
asymmetric disulfide <chemistry> Disulfide which is not symmetric on both sides of the -s-s- linkage; e.g., the disulfide formed between coenzyme A and glutathione or between cysteine and coenzyme A or glutathione.
Synonym: asymmetric disulfide.
(05 Mar 2000)
carbon disulfide <chemical> Carbon disulfide (cs2). A colourless, flammable, poisonous liquid, cs2. It is used as a solvent, and is a counterirritant and has local anaesthetic properties but is not used as such. It is highly toxic with pronounced CNS, haematologic, and dermatologic effects.
Chemical name: Carbon disulfide
(12 Dec 1998)
carbon disulfide poisoning Acute or chronic intoxication by CS2, an industrial condition encountered among rubber workers and makers of artificial silk (rayon) by the viscose process; characterised by insomnia, listlessness, and irritability, followed by paralyses, impaired vision, peptic ulcer, and psychoses.
(05 Mar 2000)
carbon monoxide dehydrogenase disulfide reductase <enzyme> Catalyses a reversible exchange of coash with acetyl-CoA in combination with carbon monoxide dehydrogenase (EC 1.2.99.2)
Registry number: EC 1.8.-
Synonym: co dehydrogenase disulfide reductase, co-dd-reductase
(26 Jun 1999)
glutathione disulfide <chemical> A glutathione derivative that forms when the sulfhydryl side chains of the cysteine residues of two glutathione molecules form a disulfide bond during the course of being oxidised with various oxides and peroxides in cells. Glutathione reductase, with the coupled oxidation of NADPH, reduces gssg to two moles of glutathione.
Chemical name: Bis(gamma-Glutamyl-L-cysteinylglycine) Disulfide
(12 Dec 1998)
mixed disulfide <chemistry> Disulfide which is not symmetric on both sides of the -s-s- linkage; e.g., the disulfide formed between coenzyme A and glutathione or between cysteine and coenzyme A or glutathione.
Synonym: asymmetric disulfide.
(05 Mar 2000)
symmetric disulfide Disulfide that is symmetric on both sides of the -s-s- linkage; i.e., disulfide formed from identical thiol-containing compounds; e.g., cystine, glutathione disulfide.
(05 Mar 2000)
disulfide 1. A molecule containing two atoms of sulfur to one of the reference element, e.g., CS2, carbon disulfide.
2. A compound containing the -S-S-group, e.g., cystine.
(05 Mar 2000)
disulfide bond A single bond between two sulfurs; specifically, the -S-S- link binding two peptide chains (or different parts of one peptide chain); also occurs as part of the molecule of the amino acid, cystine, and is important as a structural determinant in many protein molecules, notably keratin, insulin, and oxytocin. A symmetric disulfide is R-S-S-R; R'-S-S-R is a mixed disulfide.
(05 Mar 2000)
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 9 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • disulfide
    ÀÌȲȭ¹°
  • disulfide
    (È­)2Ȳȭ¹°
  • 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®
    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
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