¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"DNA ligase"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 12 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • DNA, infectious(-tive)
    °¨¿°¼º DNA
  • DNA, recombinant
    ÀçÁ¶ÇÕ DNA
  • DNA-RNA hybridization
    DNA-RNA ¦Áö¿ì±â, DNA-RNA ºÎÇÕ°Ë»ç¹ý(ݬùê~)
  • DNA-binding protein
    DNA °áÇմܹéÁú
  • DNA-containing virus
    DNA(Æ÷ÇÔ)¹ÙÀÌ·¯½º.
  • DNA-dependent RNA polymerase
    DNA-ÀÇÁ¸ DNA ÁßÇÕÈ¿¼Ò
  • DNA-dependent RNA polymerase
    DNA-ÀÇÁ¸ RNA ÁßÇÕÈ¿¼Ò
  • RNA-dependent DNA polymerase
    RNA-ÀÇÁ¸ DNA ÁßÇÕÈ¿¼Ò
  • antidouble stranded dna antibody
    Ç×ÀÌÁß¼â DNAÇ×ü(¡­ì£ñìáð¡­ù÷ô÷)
  • hybridization, DNA-RNA
    DNA-RNA ¦Áö¿ì±â, DNA-RNA ºÎÇÕÈ­(~ݬùêûù)
  • infectious (-tive) DNA
    °¨¿°¼º DNA
  • recombinant DNA
    ÀçÁ¶ÇÕ DNA
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
  • DNA-delay mutant
    DNAÁöü º¯ÀÌü(òÀôòܨì¶ô÷)
  • DNA-dependent RNA polymerase
    DNAÀÇÁ¸ RNA Æú¸®¸Ó·¹À̽º
  • DNA dot blot
    DNA Á¡(ïÃ)ºí·Ô
  • DNA-driven hybridization
    DNAÃßÁø(õÏòä) Æ¢±âÇü¼º(û¡à÷)
  • DNA duplex
    DNA µÎ°¡´Ú
  • DNA duplicase
    "DNA µÎÇø®ÄÉÀ̽º, (ÔÒ) DNA polymerase"
  • DNA glycosylase
    DNA ±Û¶óÀÌÄڽǷ¹À̽º
  • dna G protein
    dna G ´Ü¹éÁú(Ó±ÛÜòõ)
  • DNA groove
    DNA Ȩ
  • DNA gyrase
    DNA ÀÚÀÌ·¹À̽º
  • DNA helicase
    DNA Ç︮ÄÉÀ̽º
  • DNA library
    "DNA ¶óÀ̺귯¸®, (ÔÒ) gene library"
  • DNA-like RNA
    DNAÀ¯»ç(×¾ÞÄ) RNA
  • DNA-melting protein
    "DNAÀ¶ÇØ ´Ü¹éÁú(ë×ú°Ó±ÛÜòõ), (ÔÒ) single-strand binding protein"
  • DNA methylase
    DNA ¸ÞÆ¿·¹À̽º
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 4 ÆäÀÌÁö: 3
recon the smallest unit of DNA capable of recombination [recombination + Gr. on quantum]
ss(c)DNA single-stranded circular deoxyribonucleic acid
ssDNA single-stranded DNA
Z-DNA zig-zag (left-handed helical) deoxyribonucleic acid
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 3
DNA-PK DNA-activated protein kinase
DNA-PK(CS) DNA-dependent protein kinase
DNA-PKCS DNA-dependent protein kinase catalytic subunit
HBV DNA Hepatitis B virus DNA
mt DNA Mitochondrial DNA
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 3
threonine-trna ligase <enzyme> An enzyme that activates threonine with its specific transfer RNA.
Chemical name: L-Threonine:tRNA(Thr) ligase (AMP-forming)
Registry number: EC 6.1.1.3
(12 Dec 1998)
tRNA excision ligase <enzyme> Processes pre-trna-tyr into mature trna-tyr
Registry number: EC 6.5.1.-
(26 Jun 1999)
tRNA splicing ligase <enzyme> One of two enzymes involved in trna splicing in archaea
Registry number: EC 6.5.1.-
(26 Jun 1999)
tryptophan-trna ligase <enzyme> An enzyme that activates tryptophan with its specific transfer RNA.
Chemical name: L-Tryptophan:tRNA(Trp) ligase (AMP-forming)
Registry number: EC 6.1.1.2
(12 Dec 1998)
tubulin-tyrosine ligase <enzyme> An enzyme that covalently links a tyrosine to the C-terminal glutamyl residue of tubulin, coupled with the hydrolysis of ATP to ADP and Pi; this is a unique posttranslational modification that may have a significant role in cytoskeletal traffic and design.
(05 Mar 2000)
tyrosine-trna ligase <enzyme> An enzyme that activates tyrosine with its specific transfer RNA.
Chemical name: L-Tyrosine:tRNA-(Tyr) ligase (AMP-forming)
Registry number: EC 6.1.1.1
(12 Dec 1998)
tyrosyltubulin ligase <enzyme> Catalyses reversible, post-translational addition of tyrosine, phenylalanine or dopa to carboxyl terminal of alpha-chain of tubulin
Registry number: EC 6.3.2.-
Synonym: tubulin-tyrosine ligase, tyrosyl tubulin ligase
(26 Jun 1999)
ubiquitin-calmodulin ligase <enzyme> Covalentyl links ubiquitin to bovine calmodulin in an ATP-dependent manner
Registry number: EC 6.3.2.21
Synonym: ubiquityl-calmodulin synthetase
(26 Jun 1999)
ubiquitin-protein ligase <enzyme> Consists of 3 enzymes; e1 is ubiquitin activating enzyme; e2 transfers activated ubiquitin as an enzyme-ubiquitin thiol ester to e3, which transfers ubiquitin to an intracellular protein; e1 forms both an enzyme-bound cooh-terminal ubiquitin thiolester and a cooh-terminal ubiquitin-adenylatte; ube1y is putative y function in spermatogonial proliferation; ube1x and ube1y encode the e1 enzyme
Registry number: EC 6.3.2.19
Synonym: ubiquitin-protein ligase system, ubiquitin-protein-lysine n-omega-ligase, ubiquitin-activating enzyme, ubiquitin-activating enzyme e1, ubiquitination activating enzyme e1, ube1 gene product, rsp5 ubiquitin-protein ligase, npi1 protein, ube1y gene product, ube1x gene product, ikappab-ubiquitin ligase
(26 Jun 1999)
UDP-N-acetylmuramoylalanine-D-glutamate ligase <enzyme> From E coli; catalyses the synthesis of udp-n-acetylmuramoyl-l-alanyl-d-glutamate from ATP and udp-n-acetylmuramoyl-l-alanine and d-glutamate
Registry number: EC 6.3.2.9
Synonym: d-glu-adding enzyme, d-glutamic acid adding enzyme, murd gene product
(26 Jun 1999)
UDP-N-acetylmuramoylalanyl-glutamyl-2,6-diaminopimelate-alanyl-alanine ligase <enzyme> Reaction: ATP + udp-n-acetylmuramoyl-l-ala-d-glu-2,6 -diaminoheptanedioate d-ala-d-ala = ADP + orthophosphate + udp-n-acetylmuramoyl-l-ala-d-glu-6-carboxy-l-lys-d-ala-d-ala; 454 amino acids, mw 48 kD; from bacteria; final step in synthesis of udp-n-acetylmuramoyl pentapeptide; genbank x62437
Registry number: EC 6.3.2.15
Synonym: udp-n-acetylmuramoyl-alanyl-d-glutamyl-meso-2,6-diaminopimeloyl-d-alanyl-d-alanine synthetase, murf gene product, udp-n-acetylmuramoyl-l-ala-glu-meso-2,6-diaminopimeloyl-ala-ala synthetase
(26 Jun 1999)
2,3-dihydroxybenzoate-AMP ligase <enzyme> Catalyses the conversion of 2,3-dihydroxybenzoate and ATP to form (2,3-dihydroxybenzoyl)adenylate, this acyladenylate remains bound to the enzyme for further reactions in the overall biosynthesis of enterobactin
Registry number: EC 6.5.-
Synonym: 2,3dhb-AMP ligase, ente gene product
(26 Jun 1999)
2,3-dihydroxybenzoate - serine ligase <enzyme> From E coli; ATP and 2,3-dihydroxybenzoate and serine yields the products of ATP breakdown and n-(2,3-dihydroxybenzoyl)-l-serine; involved in biosynthesis of enterobactin
Registry number: EC 6.3.2.14
Synonym: enterochelin synthetase, entf gene product, 2,3-dihydroxybenzoylserine synthetase
(26 Jun 1999)
2-aminobenzoate coenzyme A ligase <enzyme> From a denitrifying pseudomonas sp.; catalyses the formation of CoA thioester of 2-aminobenzoate with the formation of AMP and pyrophosphate from ATP
Registry number: EC 6.2.1.-
Synonym: 2-ab CoA ligase
(26 Jun 1999)
3-hydroxypicolinic acid-AMP ligase <enzyme> From cell extracts of streptomyces pristinaespiralis; activates the first pristinamycin 1 residue 3-hydroxypicolinic acid; shows 58% nh2-terminal amino acid sequence identity with s. Griseoviridus 3-hpa-activating enzyme; amino acid sequence given in first source (page 709)
Registry number: EC 6.3.2.-
Synonym: pi synthetase 1, snba protein, pristinamycin I synthetase 1,3-hpa-AMP ligase
(26 Jun 1999)
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 3
DNA ligase An enzyme capable of repairing breaks in the DNA backbone by forming the phosphodiesterbond that is placed between the 5' phosphate and the 3'OH group of ribose.
Ãâó: www.cwu.edu/~chem/courses/chem388488f00/mcclung/mc...
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 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °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
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °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 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °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
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    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
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѽŰæ¿Ü°úÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
    ÇÑÀÚ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
´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
    ¿µ¹®
    ÇѱÛ
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 3
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 3
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 3
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 3
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 3
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 3
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 3
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 3
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 3
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ À¯»ç °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 3
Á¦Ç°¸í
ÆÇ¸Å»ç
º¸ÇèÄÚµå ¼ººÐ/ÇÔ·®
±¸ºÐ/º¸Çè±Þ¿©
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference ¸ÂÃã °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 3
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 3
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 3
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 3
KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
  • ¿µ¹®
    ÇѱÛ
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 3
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 3
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 3
ÅëÇÕ°Ë»ö ¿Ï·á