¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"GTP"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 3 ÆäÀÌÁö: 1
GTP Guanosine Tri-Phosphate
GTP glutamyl transpeptidase; guanosine triphosphate
GTPase guanosine triphosphatase
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 6 ÆäÀÌÁö: 1
GTP Green tea polyphenols
GTP Guanosine 5'-triphosphate
GTP green tea
GTP-CH GTP cyclohydrolase I
GTPase Guanosine triphosphatase
GTP[S] 5'(-)[gamma-thio]triphosphate
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
GEF GDP/GTP exchange factor
GEP GDP/GTP exchange protein
GCH GTP cyclohydrolase I
G-proteins GTP)-binding regulatory proteins
GAP GTP-ase-activating protein
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • GTP (guanosine triphosphate)
    »ïÀλ걸¾Æ³ë½Å
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • Guanosine triphosphate (GTP)
    »ïÀλ걸¾Æ³ë½Å
  • guanosine triphosphate(gtp)-bindting proteins
    »ïÀλ걸¾Æ³ë½Å°áÇմܹéÁú
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • guanosine triphosphate(gtp)-bindting proteins
    »ïÀλ걸¾Æ³ë½Å°áÇմܹéÁú
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 3 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • GTP
    "(å²) guanosine triphosphate, guanosine-5'-triphosphate"
  • GTP-binding protein
    GTP°áÇÕ ´Ü¹éÁú(Ì¿ùêÓ±ÛÜòõ)
  • GTPase
    (å²) guanosine triphosphatase
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 7 ÆäÀÌÁö: 1
GTP An immediate precursor of guanine nucleotides in RNA; similar to ATP; has a crucial role in microtubule formation.
GTP cyclohydrolase, an enzyme that catalyses the reaction of GTP and H2O forming formate and a precursor of tetrahydrobiopterin; a deficiency of this enzyme will result in one form of malignant hyperphenylalaninaemia.
Acronym: GTP
(05 Mar 2000)
GTP cyclohydrolase <enzyme> (GTP cyclohydrolase I) or GTP 7,8-8,9-dihydrolase (pyrophosphate-forming) (GTP cyclohydrolase II). An enzyme group that hydrolyzes the imidazole ring of GTP, releasing carbon-8 as formate. Two c-n bonds are hydrolyzed and the pentase unit is isomerised. This is the first step in the synthesis of folic acid from GTP.6 (GTP cyclohydrolase I) and GTP cyclohydrolase II.
Chemical name: GTP 7,8-8,9-dihydrolase
Registry number: EC 3.5.4.16
(12 Dec 1998)
GTP phosphohydrolase <enzyme> An enzyme that hydrolyzes GTP to GDP and provides energy for peptide chain elongation.
Registry number: EC 3.6.1.-
(12 Dec 1998)
GTP pyrophosphokinase <enzyme> An enzyme that catalyses reversibly the transfer of a pyrophosphate group from ATP to the 3'-oh group of GDP or GTP with the formation of guanosine 3'-diphosphate 5'-diphosphate or guanosine 3'-diphosphate 5'-triphosphate and AMP. The enzyme, also called stringent factor, is located in the rela gene in stringent strains of bacteria. The above synthesis is induced by mRNA and uncharged trna which is bound to the aminoacyl-t-RNA binding site of the ribosome by a codon-specific association.
Chemical name: ATP:GTP 3'-pyrophosphotransferase
Registry number: EC 2.7.6.5
(12 Dec 1998)
GTP-binding protein <molecular biology, protein> There are two main classes of G-proteins, the heterotrimeric G proteins that associate with receptors of the seven transmembrane domain superfamily and are involved in signal transduction and the small cytoplasmic G-proteins.
Regulatory proteins found in all cells. They are versatile molecular switches, involved in the control of a wide range of biological processes - protein synthesis, signal transduction pathways, growth and differentiation. They all act through a common molecular mechanism based on their ability to bind the guanine nucleotides GTP and GDP selectively and with high affinity.
Stimulatory G-proteins are permanently activated by cholera toxin, inhibitory ones by pertussis toxin. Transducin was one of the first of the heterotrimeric G-proteins to be identified.
The small G-proteins are a diverse group of monomeric GTPases that include ras, rab, rac and rho and that play an important part in regulating many intracellular processes including cytoskeletal organisation and secretion. Their GTPase activity is regulated by activators (GAPs) and inhibitors (GIPs) that determine the duration of the active state.
(12 Jul 2000)
GTP-RNA guanylyltransferase <enzyme> Catalyses addition of GMP residue to 3'-ends of oligonucleotide primers
Registry number: EC 2.7.7.-
Synonym: terminal guanylyltransferase
(26 Jun 1999)
GTPase activating protein <molecular biology> Originally purified as a 125 kD protein from bovine brain (1044 amino acids), stimulates the GTPase activity of ras p21 and thereby switches it to the inactive state.
GAP may itself be regulated by phospholipids and by phosphorylation on a tyrosine residue by growth factor receptors (PDGF R, EGF R). The neurofibromatosis type 1 gene NF1) codes for a protein homologous to GAP. GAP has both SH2 and SH3 domains. Another example is sar 1 (from yeast).
(18 Nov 1997)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
phosphoenolpyruvate carboxykinase (GTP) <enzyme> An enzyme of the lyase class that catalyses the conversion of GTP and oxaloacetate to GDP, phosphoenolpyruvate, and carbon dioxide. This reaction is part of gluconeogenesis in the liver. The enzyme occurs in both the mitochondria and cytosol of mammalian liver.
Chemical name: GTP:oxaloacetate carboxy-lyase (transphosphorylating)
Registry number: EC 4.1.1.32
(12 Dec 1998)
transducin GTP phosphohydrolase <enzyme> Stimulated by bovine rhodopsin mutants (asp63 to asn) and (glu134 to gln) with slightly lowered efficiency
Registry number: EC 3.6.1.-
Synonym: transducin GTPase
(26 Jun 1999)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 5 ÆäÀÌÁö: 1
  • GTP Cyclohydrolase - »õâ (GTP cyclohydrolase I) or GTP 7,8-8,9-dihydrolase (pyrophosphate-forming) (GTP cyclohydrolase II). An enzyme group that hydrolyzes the imidazole ring of GTP, releasing carbon-8 as formate. Two C-N bonds are hydrolyzed and the pentase unit is isomerized. This is the first step in the synthesis of folic acid from GTP. EC 3.5.4.16 (GTP cyclohydrolase I) and EC 3.5.4.25 (GTP cyclohydrolase II).
    Synonyms : 7, 8-Dihydroneopterintriphosphate Synthetase, GTP Cyclohydrolase I, GTP Cyclohydrolase II, 7, 8 Dihydroneopterintriphosphate Synthetase, 8-Formylhydrolase, GTP, Cyclohydrolase I, GTP, Cyclohydrolase II, GTP, Cyclohydrolase, GTP, Dihydrolase, GTP
  • GTP Phosphohydrolase Activators - »õâ Agents and factors that activate GTP phosphohydrolase activity.
    Synonyms : Small GTPase Activators, Activators, GTP Phosphohydrolase, Activators, GTPase, Activators, Small GTPase
  • GTP Phosphohydrolase-Linked Elongation Factors - »õâ Factors that utilize energy from the hydrolysis of GTP to GDP for peptide chain elongation. EC 3.6.1.-.
    Synonyms : Elongation Factors, GTPase-Linked, Elongation Factors, Guanosinetriphosphatase-Linked, Factors, GTPase-Linked Elongation, Factors, Guanosinetriphosphatase-Linked Elongation, GTP Phosphohydrolase Linked Elongation Factors, GTPase Linked Elongation Factors
  • GTP Phosphohydrolases - »õâ Enzymes that hydrolyze GTP to GDP. EC 3.6.1.-.
    Synonyms : GTP Phosphohydrolase, Phosphohydrolase, GTP, Phosphohydrolases, GTP, Phosphohydrolases, Guanosine Triphosphate, Triphosphate Phosphohydrolases, Guanosine
  • GTP Pyrophosphokinase - »õâ An enzyme that catalyzes reversibly the transfer of a pyrophosphate group from ATP to the 3'-OH group of GDP or GTP with the formation of guanosine 3'-diphosphate 5'-diphosphate or guanosine 3'-diphosphate 5'-triphosphate and AMP. The enzyme, also called stringent factor, is located in the relA gene in stringent strains of bacteria. The above synthesis is induced by mRNA and uncharged tRNA which is bound to the aminoacyl-t-RNA binding site of the ribosome by a codon-specific association. EC 2.7.6.5.
    Synonyms : ATP Guanosine Phosphate Pyrophosphotransferase, Factor, Stringent, Pyrophosphokinase, GTP, Pyrophosphotransferase, ATP-Guanosine Phosphate
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 2 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition ¸ÂÃã °Ë»ö (http://www.drugs.com) °á°ú: 1 ÆäÀÌÁö: 1
KMLE À¥ ¿ë¾î ¸ÂÃã °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
GTP-binding protein any of a number of regulatory proteins, including the G proteins and the monomeric small GTP-binding proteins, in which the exchange of GDP for GTP induces a conformational change to produce an active state, while the hydrolysis of GTP to GDP produces an inactive state. GTP-binding proteins act as switches that couple cell-surface receptor activation with intracellular processes such as protein synthesis.
Ãâó: www.mercksource.com/pp/us/cns/cns_hl_dorlands.jspz...
GTPase-activating protein a protein that stimulates the GTPase activity of a GTP-binding protein, resulting in the conversion of the protein to its inactive form.
Ãâó: www.mercksource.com/pp/us/cns/cns_hl_dorlands.jspz...
GTPase GTPases are a large family of enzymes that can bind and hydrolyze GTP. The GTP binding and hydrolysis takes place in the highly conserved G domain common to all GTPases. GTPases play an important role in: * Signal transduction at the intracellular domain of transmembrane receptors, including recognition of taste, smell and light. * Protein biosynthesis (aka translation) at the ribosome. * Control and differentiation during cell division. * Translocation of proteins through membranes. ...
Ãâó: en.wikipedia.org/wiki/GTPase
GTP guanosine triposphate. A high energy molecule, required for a number of biochemical reactions, including nucleic acid and protein synthesis (formation).
Ãâó: www.nutrabio.com/Definitions/definitions_g.htm
GTP A popular road racing car in 1 to 1 scale. A sports car coupe body style popular with the racers who like to race scale appearing bodies.
Ãâó: www.scaleautoracing.com/slotfaqs/gg.html
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °á°ú: 2 ÆäÀÌÁö: 1
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
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¿©
ÀÇÇÐ³í¹® ¾àÀÚ(Pubmed/Entrez) °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
Çѱ¹Ç¥ÁØÁúº´»çÀκзù ¾àÀÚ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ÄÚµå
    ¿µ¹®
    ÇѱÛ
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
¾Ë±â½¬¿î ÀÇÇпë¾îÇ®ÀÌÁý, ¼­¿ïÀÇ´ë ±³¼ö ÁöÁ¦±Ù, °í·ÁÀÇÇÐ ÃâÆÇ À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °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
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °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 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °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
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °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
  • ¿µ¹®
    ÇѱÛ
´ëÇѱâ»ýÃæÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü À¯»ç °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - A.D.A.M. Medical Encyclopedia À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - MedlinePlus Health Topics À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - µå·¯±×ÀÎÆ÷ ¾àÇÐ Á¤º¸ ¸ÂÃã °Ë»ö (http://www.druginfo.co.kr) °á°ú: 0 ÆäÀÌÁö: 1
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: 1
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: 1
¿ÜºÎ ¸µÅ© - WebMD.com Drug Reference À¯»ç °Ë»ö (http://www.webmd.com) °á°ú: 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Drug.com Drugs by Medical Condition À¯»ç °Ë»ö (http://www.drugs.com) °á°ú: 0 ÆäÀÌÁö: 1
KMLE À¥ ¿ë¾î À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
ÇÑ¿µ/¿µÇÑ »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü À¯»ç °Ë»ö (https://www.ahdictionary.com) °á°ú: 0 ÆäÀÌÁö: 1
ÅëÇÕ°Ë»ö ¿Ï·á