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"isonicotinic acid hydroxylase"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • acid-fast bacillus
    Ç׻긷´ë±Õ, Ç×»ê±Õ
  • acid-fast bacterium
    Ç×»ê±Õ
  • acid-fast organism
    Ç×»ê±Õ
  • acid-fast stain
    Ç׻꿰»ö
  • acid-fastness
    Ç׻꼺
  • adenylic acid
    ¾Æµ¥´Ò»ê
  • aliphatic amino acid
    Áö¹æÁ·¾Æ¹Ì³ë»ê
  • allokainic acid
    ¾Ë·ÎÄ«Àλê
  • amino acid
    ¾Æ¹Ì³ë»ê
  • amino acid sequence
    ¾Æ¹Ì³ë»ê¼ø¼­
  • aminohippuric acid
    ¾Æ¹Ì³ëÈ÷Ǫ¸£»ê
  • benzoic acid
    º¥Á¶»ê
  • bile acid
    ´ãÁó»ê
  • boric acid
    ºØ»ê
  • boric acid ointment
    ºØ»ê¿¬°í
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 13 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • uric acid
    ¿ä»ê
  • valproic acid
    ¹ßÇÁ·ÎÀÌÅ©»ê
  • vanillylmandelic acid
    ¹Ù´Ò¸¸µ¨»ê
  • gamma aminobutyric acid
    °¨¸¶¾Æ¹Ì³ëºÎƼ¸£»ê
  • acid burn
    »êÈ­»ó
  • acid-fast bacterium
    Ç×»ê±Õ
  • acid-fast bacillus
    Ç׻긷´ë±Õ, Ç×»ê±Õ
  • uric acid nephropathy
    (¢¡ urate nephropathy) ¿ä»ê¿°ÄáÆÏº´Áõ
  • acid fast organism
    Ç×»ê±Õ
  • acid radical
    »ê±â
  • acid salt
    »ê¼º¿°
  • acid-fast stain
    Ç׻꿰»ö
  • acetylsalycylic acid antiplatelet therapy
    Ç×Ç÷¼ÒÆÇ¿ä¹ý
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • arachidonic acid
    ¾Æ¶ó۵·»ê
  • arsenic acid
    ºñ»ê
  • ascorbic acid
    ¾Æ½ºÄÚ¸£ºó»ê
  • benzoic acid
    º¥Á¶»ê
  • bile acid
    ´ãÁó»ê
  • boric acid
    ºØ»ê
  • butyric acid
    ºÎƼ¸£»ê
  • cacodylic acid
    Ä«ÄÚµô»ê
  • caffeic acid
    Ä«ÆäÀλê
  • carbolic acid
    (¢¡phenol) Æä³î, ¼®Åº»ê
  • carbonic acid
    ź»ê
  • chamber acid
    ¿¬½ÇȲ»ê
  • chitonic acid
    Űſ»ê
  • cholic acid
    ´ãÁó»ê
  • citric acid
    ±¸¿¬»ê, ½ÃÆ®¸£»ê
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • Gamma-aminobutyric acid
    °¨¸¶¾Æ¹Ì³ëºÎƼ¸£»ê(ß«)
  • Glycogen-lactic acid system
    ±Û¸®ÄÚ°Õ-¶ôÆ®»ê°è
  • Growth folic acid in
    ¼ºÀå(à÷íþ)¿°»ê(ç¤ß«)¿°
  • HIAA = 5-hydroxyindoleacetic acid
    5-ÇÏÀ̵å·ÎÀε¹ÃÊ»ê
  • Hydrochloric acid
    ÇÏÀ̵å·ÎÅ©·Ð»ê
  • Hydroxybutyric acid
    ÇÏÀ̵å·ÎºÎÆ¿»ê
  • Kainate amino acid receptor
    Ä«À̳×ÀÌÆ® ¾Æ¹Ì³ë»ê ¼ö¿ëü(áôé»ô÷)
  • Lactic acid = lactate
    ¶ôÆ®»ê(¡­ß«),Á¥»ê(¡­ß«)
  • Lactic acid dehydrogenase
    ¶ôÆ® »êÅ»¼ö¼ÒÈ¿¼Ò(¡­ß«÷­â©áÈý£áÈ)
  • N-Benzol-L-tyrosyl-p-aminobenzoic acid
    N-º¥Á¹-L-Ƽ·Î½Ç-p- ¾Æ¹Ì³ë¾È½ÄÇâ»ê
  • N-Formiminoglutamic acid
    N-Æ÷¸§À̹̳ë±Û·çŽ»ê
  • RNA =>ribonucleic acid
    ¸®º¸ÇÙ»ê
  • RNA=£¾ribonucleic acid
    ¸®º¸ÇÙ»ê.
  • VMA =>vanillymandelic acid
    ¹Ù´Ò¸¸µ¥¸¯»ê
  • Van Slyke amino acid procedure
    ¹Ý½½¶óÀÌÅ©¾Æ¹Ì³ë»ê¹æ¹ý
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • acid fast
    Ç×»ê(¼º)(ù÷ß«àõ)ÀÇ.
  • acid fast bacillus (AFB)
    Ç×»ê±Õ, Ç׻긷´ë±Õ
  • acid fast bacterium
    Ç×»ê(¼º) ¼¼±Õ.
  • acid fast bacterium
    Ç×»ê(¼º) ¼¼±Õ.
  • acid fast organism
    Ç×»ê±Õ
  • acid fast stain
    Ç×»ê(¼º) ¿°»ö(¡­æøßä).
  • acid fastness
    Ç׻꼺
  • acid food
    »ê¼º½Äǰ.
  • acid forming
    »ê¹ß»ý(ß«Û¡ßæ)ÀÇ.
  • acid free diet
    ¹«»ê½ÄÀÌ.
  • acid hematin method
    »êÇ츶ƾ¹ý(¡­Ûö).
  • acid intoxication
    »êÁßµ¶(Áõ)(ß«ñéÔ¸ñø).
  • acid lipase deficiency
    »ê¼º ¸®ÆÄÁ¦ °áÇÌÁõ(ß«àõ¡­ÌÀù¹ñø)
  • acid mucopolysaccharide(s)
    »ê¼ºÁ¡´Ù´çÁú(ïÄÒýÓØòõ)
  • acid perfusion
    »ê°ü·ù(߫δêü), »êȯ·ù.
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • amino acid accepting RNA
    ¾Æ¹Ì³ë»ê(ß«) ¼ö³³(áôÒ¡)RNA
  • amino acid activating enzyme
    ¾Æ¹Ì³ë»ê(ß«) Ȱ¼ºÈ­(üÀàõûù) È¿¼Ò(ý£áÈ)
  • amino acid activation
    ¾Æ¹Ì³ë»ê(ß«) Ȱ¼ºÈ­(üÀàõûù)
  • amino acid analysis
    ¾Æ¹Ì³ë»ê(ß«) ºÐ¼®(ÝÂà°)
  • amino acid analyzer
    ¾Æ¹Ì³ë»ê(ß«) ºÐ¼®±â(ÝÂà°Ðï)
  • amino acid arm
    ¾Æ¹Ì³ë»ê ÆÈ
  • amino acid attachement site
    ¾Æ¹Ì³ë»ê(ß«) ºÎÂø(ݾó·)ÀÚ¸®
  • amino acid composition
    ¾Æ¹Ì³ë»ê Á¶¼º(ðÚà÷)
  • amino acid incorporation
    ¾Æ¹Ì³ë»ê(ß«) ÆíÀÔ(øºìý)
  • amino acid nitrogen
    ¾Æ¹Ì³ë»ê(ß«) Áú¼Ò(òòáÈ)
  • amino acid oxidase
    ¾Æ¹Ì³ë»ê(ß«) ¿Á½Ãµ¥À̽º
  • amino acid replacement
    ¾Æ¹Ì³ë»ê(ß«) ´ëü(ÓÛôð)
  • amino acid residue
    ¾Æ¹Ì³ë»ê(ß«) Àܱâ(íÑÐñ)
  • amino acid sequence
    ¾Æ¹Ì³ë»ê(ß«) ¼­¿­(ßíæê)
  • amino acid sequencer
    ¾Æ¹Ì³ë»ê(ß«) ¼­¿­°áÁ¤±â(ßíæê̽ïÒÐï)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 3
OA obstructive apnea; occipital artery; occipito-anterior; occiput anterior; octanoic acid; ocular albi...
PAA partial agonist activity; phenylacetic acid; phosphonoacetic acid; physical abilities analysis; plas...
ASA acetylsalicylic acid; active systemic anaphylaxis; Adams-Stokes attack; American Society of Anesthes...
CA anterior commissure [Lat. commissura anterior]; calcium antagonist; California [rabbit]; cancer; Can...
DHA dehydroacetic acid; dehydroascorbic acid; dehydroepiandrosterone; dihydroacetic acid; dihydroxyaceto...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 3
LH Lysyl hydroxylase
P-450c17 P-450 17alpha-hydroxylase-C17,20 lyase
PNPH P-nitrophenol hydroxylase
PAH Phenylalanine hydroxylase
PH Phenylalanine hydroxylase
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • acid-base compensation
    »ê ¿°±â º¸»ó
  • acid-base indicator
    »ê ¿°±â Áö½Ã¾à
  • acid-fast nonmotile rod
    Ç׻꼺 ºñ¿îµ¿¼º °£±Õ
  • acid-gel application
    °ÖÇü »ê Àû¿ë
  • adenylic acid deaminase
    ¾Æµ¥´Ò»ê Å»¾Æ¹Ì³ë È¿¼Ò
  • aldobionic acid
    ¾Ëµµºñ¿Â»ê
    C11H19O10COOH. ±× ¼ººÐ´çÀÇ Çϳª·Î¼­ ¿ì·Ð»êÀ» ÇÔÀ¯Çϰí ÀÖ´Â ÀÌ´ç·ùÀ̸ç, ¿©·¯ Á¾·ùÀÇ ½Ä¹°¼º °í¹«¿Í ƯÁ¤ÇÑ º´¿øÃ¼ Áß¿¡ Á¸ÀçÇÑ´Ù. Æó·Å±Õ 3ÇüÀÇ Æ¯¼ö ´Ù´ç·ùÀÇ °¡¼öºÐÇØ¿¡ ÀÇÇØ¼­ ¾òÀ» ¼ö ÀÖ´Ù.
  • allokainic acid
    ¾Ë·ÎÄ«ÀÎ »ê
  • alloxyproteic acid
    ¾Ë·Ï½Ã ´Ü¹é»ê
    ¶§¶§·Î ´¢ Áß¿¡ ¹è¼³µÇ´Â À¯È² ÇÔÀ¯ È­ÇÕ¹°.
  • alpha-oxynaphthoic acid
    ¾ËÆÄ-¿Á½Ã³ªÇÁÅä»ê
    °áÁ¤¼ºÀÇ »ê,OHC10H6COOH.°ú°Å¿¡´Â ¹æºÎÁ¦, ¹æÃëÁ¦·Î »ç¿ëµÇ¾ú´Ù.
  • amino acid L-tryptophan
    ¾Æ¹Ì³ë»ê L-Æ®¸³ÅäÆÇ
  • aminoacetic acid
    ¾Æ¹Ì³ë¾Æ¼¼Æ®»ê, ¾Æ¹Ì³ëÃÊ»ê
    ºñÇʼö ¾Æ¹Ì³ë»ê, NH2CH2COOH. ¸¹Àº ´Ü¹éÁúÀÇ ±¸¼º ¼ººÐÀ¸·Î Á¸ÀçÇÑ´Ù. ÇÕ¼ºµÇ°í ÀÖÀ¸¸ç À§ Á¦»êÁ¦¿Í º¸Ãæ½ÄǰÀ¸·Î »ç¿ëµÇ¾îÁø´Ù. ¶ÇÇÑ ¿©·¯ °¡Áö ±ÙÀ°º´ ¹× ¸»ÃÊÇ÷°ü ºÎÀüÁõÀÇ Ä¡·á¿¡µµ »ç¿ëµÈ´Ù.
  • aminobenzoic acid
    ¾Æ¹Ì³ë ¾È½ÄÇâ »ê
    C7H7NO2. ½Ä¹°°ú µ¿¹°Á¶Á÷¿¡ ³Î¸® ºÐÆ÷Çϸç, ºñŸ¹Î B±ºÀÇ ±¸¼º ¼ººÐ¿¡ °ü°èµÈ´Ù. ¼³ÆÄÁ¦ÀÇ Á¤±ÕÀÛ¿ëÀ» ¹«È¿È­½ÃŲ´Ù.
  • arachidonic acid
    ¾Æ¶ó۵·»ê
    1. °íµµÀÇ ºÒÆ÷È­ Çʼö Áö¹æ»ê. CH3
  • arachidonic acid metabolism
    ¾Æ¶ó۵·»ê ´ë»ç¹°Áú
  • aromatic amino acid
    ¹æÇâÁ· ¾Æ¹Ì³ë»ê
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
retinol 4-hydroxylase <enzyme> Converts retinol to 4-hydroxyretinol in presence of NADPH
Registry number: EC 1.14.13.-
(26 Jun 1999)
chlorsulfuron-5-hydroxylase <enzyme> Hydroxylates the herbicide chlorsulfuron; 5-hydroxychlorsulfuron is not observed intact in plants but is transformed immediately to a glucose conjugate
Registry number: EC 1.14.99.-
(26 Jun 1999)
cholesterol 26-hydroxylase <enzyme> Cyt p-450 dependent, ferredoxin involved
Registry number: EC 1.14.15.-
(26 Jun 1999)
mevastatin hydroxylase <enzyme> Hydroxylates ml-236b (mevastatin) to pravastatin; requires NADH-cytochrome p-450 reductase
Registry number: EC 1.14.13.-
Synonym: cytochrome p-450sca monoxygenase, cytochrome p-450(sca)
(26 Jun 1999)
phenylalanine 4-hydroxylase <enzyme> An enzyme that catalyses the oxidation of l-phenylalanine to l-tyrosine with O2 and tetrahydrobiopterin (the latter forming the dihydro derivative) which is reduced by NADPH and a reductase to the active form; a deficiency of either of these enzymes will result in phenylketonuria.
Synonym: phenylalanine 4-hydroxylase.
(05 Mar 2000)
phenylalanine hydroxylase <enzyme> An enzyme of the oxidoreductase class that catalyses the reaction l-phenylalanine, tetrahydrobiopterin, and oxygen to yield l-tyrosine, dihydrobiopterin, and water, the reaction synthesizing tyrosine from phenylalanine.
Chemical name: L-Phenylalanine,tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating)
Registry number: EC 1.14.16.1
(12 Dec 1998)
phenylalanine hydroxylase phosphatase <enzyme> Catalyses dephosphorylation of phosphorylated phenylalanine hydroxylase
Registry number: EC 3.1.3.-
Synonym: phe hydroxylase phosphatase
(26 Jun 1999)
phytanoyl-coenzyme A hydroxylase <enzyme> Mutations in gene pahx result in refsum disease; amino acid sequence given in second source; genbank af023462-3
Registry number: EC 1.14.-
Synonym: phytanoyl-CoA hydroxylase, pahx protein, pahx gene product
(26 Jun 1999)
warfarin-7-hydroxylase <enzyme> Hydroxylates warfarin in presence of cytochrome p-450 and NADPH
Registry number: EC 1.14.13.-
(26 Jun 1999)
corticosterone 15alpha-hydroxylase <enzyme> Use of cytochrome p-450coh in which phe209 is replaced by asn gives the cytochrome p-450coh a high corticosterone 15alpha hydroxylase activity instead of a coumarin hydroxylase activity
Registry number: EC 1.14.99.-
Synonym: co 15-hydroxylase
(26 Jun 1999)
coumarin hydroxylase <enzyme> Different preparations hydroxylate at position 3 and position 7; if cytochrome p-450coh is mutated at position 209, its substrate specificity is changed from coumarin hydroxylation to steroid hydroxylation
Registry number: EC 1.14.99.-
Synonym: cytochrome p-450coh, cytochrome p-4502a-5, cyp2a-5 gene product, coumarin 7-hydroxylase, cytochrome p-450 2a6, cyp2a6, cytochrome p-450 2a3, cyp2a3, p450 2a5, dhea hydroxylase, cyp2a5
(26 Jun 1999)
cymA hydroxylase reductase <enzyme> Flavoprotein electron transport reductase from pseudomonas aureofaciens; genbank u86603
Registry number: EC 1.-
Synonym: p-cymene methyl hydroxylase reductase, cyma gene product
(26 Jun 1999)
cytochrome P-450-dependent digitoxin 12beta-hydroxylase <enzyme> Isolated from digitalis lantata cell cultures
Registry number: EC 1.14.99.-
Synonym: digitoxin 12beta-hydroxylase
(26 Jun 1999)
progesterone-6-hydroxylase <enzyme> Cytochrome p-450 2c3 with valine at position 364 which confers 6beta-hydroxylase activity; see also record for cyp2c3 gene product
Registry number: EC 1.14.99.-
Synonym: progesterone 6beta-hydroxylase, cytochrome p450 2c3v
(26 Jun 1999)
prolyl hydroxylase Specific proline residues on the amino side of a glycine residue in collagen become hydroxylated at C4, before the polypeptides become helical, by the activity of prolyl hydroxylase. This enzyme has a ferrous ion at the active site and a reducing agent such as ascorbate is necessary to maintain the iron in the ferrous state. The presence of hydroxyproline is essential to produce stable triple helical tropocollagen, hence the problems caused by ascorbate deficiency in scurvy. This unusual amino acid is also present in considerable amounts in the major glycoprotein of primary plant cell walls (see HRGP).
(18 Nov 1997)
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • fulminic acid
    ³ú»ê
  • fumaric acid
    Ǫ¸¶¸£»ê
  • gallic acid
    °¥»ê
  • glacial acetic acid
    ºùÃÊ»ê
  • glutamic acid
    ±Û·çŸ¹Î»ê
  • hyaluronic acid
    È÷¾Ë·ç·Ð»ê (»ê¼º´ç·ù)
  • hydriodic acid
    ¿ÁÈ­ ¼ö¼Ò»ê
  • hydrochloric acid
    ¿°»ê
  • hydrocyanic acid
    ½Ã¾ÈÈ­ ¼ö¼Ò»ê;û»ê
  • hydrofluoric acid
    ºÒÈ­ ¼ö¼Ò»ê
  • hypochlorous acid
    Â÷¾Æ¿°¼Ò»ê
  • hypophosphoric acid
    Â÷Àλê
  • hypophosphorous acid
    Â÷¾ÆÀλê
  • indoleacetic acid
    Àε¹ÃÊ»ê(½Ä¹°ÀÇ ¼ºÀå È£¸£¸ó)
  • inosinic acid
    À̳ë½Å»ê
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ¾àǰ/ÀǾàǰ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
KMLE ¾àǰ/ÀǾàǰ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • 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: 3
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
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    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
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    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
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    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
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´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
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´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ÄÚµå
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Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
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