¼±Åà - È­»ìǥŰ/¿£ÅÍŰ ´Ý±â - ESC

 
"hypoxanthine guanine phospho ribosyl"¿¡ ´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® guanine ÇÑ±Û ±¸¾Æ´Ñ
¼³¸í   
  DNA³ª RNAÀÇ ±¸¼º¿ä¼Ò·Î ¿°±â ÁßÀÇ Çϳª.
´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • guanine
    ±¸¾Æ´Ñ
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • guanine
    ±¸¾Æ´Ñ
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • guanine
    ±¸¾Æ´Ñ
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • hypoxanthine guanine phosphoribosyl transferase(hgprt)
    hypoxanthine guanine phospho ribosyl
  • hypoxanthine-guanine phosphoribosyl transferse
    ÇÏÀÌÆ÷ÀÜÆ¾¾Æ´Ñ Æ÷½ºÆ÷¸®º¸½ÇÆ®¶õ½ºÆä¶óÁ¦
  • hypoxanthine-aminopterin-thymidine medium
    HAT¹èÁö
  • Guanine
    ±¸¾Æ´Ñ
  • guanine gout
    ±¸¾Æ´ÑÅëdz(¡­÷Ôù¦).
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • hypoxanthine guanine phosphoribosyl transferase(hgprt)
    hypoxanthine guanine phospho ribosyl
  • hypoxanthine-guanine phosphoribosyl transferse
    ÇÏÀÌÆ÷ÀÜÆ¾¾Æ´Ñ Æ÷½ºÆ÷¸®º¸½ÇÆ®¶õ½ºÆä¶óÁ¦
  • hypoxanthine-aminopterin-thymidine medium
    HAT¹èÁö
  • guanine gout
    ±¸¾Æ´ÑÅëdz(¡­÷Ôù¦).
  • hypoxamthine guanine
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 3 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • hypoxanthine
    ÇÏÀÌÆ÷À鯾
  • guanine
    ±¸¾Æ´Ñ
  • guanine-nucleotide-binding protein
    ±¸¾Æ´Ñ´©Å¬·¹¿ÀŸÀÌµå °áÇÕ ´Ü¹éÁú(Ì¿ùêÓ±ÛÜòõ)
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
HGPRT Hypoxanthine-Guanine Phospho-Ribosyl Transferase
HPRT Hypoxanthine Phospho-Ribosyl-Transferase
amidoPRT amido-Phospho-Ribosyl-Transferase
APRT Adenine Phospho-Ribosyl-Transferase
PRA   1) Plasma Renin Activity
  2) Phospho-Ribosyl-Amine
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
CHO/HGPRT Chinese hamster ovary cell hypoxanthine guanine phosphoribosyl transferase
HGPRT Hypoxanthine Guanine Phosphoribosyl Transferase
HPRT Hypoxanthine guanine phosphoribosyltransferase
HGPRTase Hypoxanthine-guanine phosphoribosyl transferase
HGXPRTase Hypoxanthine-guanine-xanthine phosphoribosyl transferase
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • dihydroxy-propoxy-methyl guanine
    ´ÙÀÌÇÏÀ̵å·Ï½Ã-ÇÁ·ÎÆø½Ã-¸ÞÆ¿ ±¸¾Æ´Ñ
  • hypoxanthine-aminopterin-thymidine medium
    HAT ¹èÁö
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
5-phospho-alpha-d-ribosyl 1-pyrophosphate 5-Phosphoribosyl 1-diphosphate;d-Ribose carrying a phosphate group on ribose carbon-5 and a pyrophosphate group on ribose carbon-1; an intermediate in the formation of the pyrimidine and purine nucleotides as well as NAD+.
Synonym: 5-phosphoribose 1-diphosphate.
Acronym: PRPP
(05 Mar 2000)
hypoxanthine-guanine phosphoribosyl tranferase marker The gene which codes for the enzyme hypoxanthine-guanine phosphoribosyl transferase. It is a selectable marker because cells which have a defective version of this gene are resistant to poisoning by toxic purine derivatives which result from the metabolic pathway that the HGPRT enzyme catalyses. (The purine derivatives are toxic because they incorporate into DNA as a result of the HGPRT enzyme's actions). Because the defective gene cannot produce the enzyme, no toxic purine derivatives are produced, the gene can therefore be selected for.
(09 Oct 1997)
hypoxanthine guanine phosphoribosyltransferase <enzyme> An enzyme that catalyses the conversion of 5-phosphoribosyl-1-pyrophosphate and hypoxanthine, guanine, or 6-mercaptopurine to the corresponding 5'-mononucleotides and pyrophosphate. The enzyme is important in purine biosynthesis as well as central nervous system functions. Complete lack of enzyme activity is associated with the lesch-nyhan syndrome, while partial deficiency results in overproduction of uric acid.
Chemical name: IMP:pyrophosphate phospho-D-ribosyltransferase
Registry number: EC 2.4.2.8
(12 Dec 1998)
hypoxanthine-guanine phosphoribosyl transferase <enzyme> An enzyme which plays an important role in the making of ATP and GTP from guanine -- the only way guanine, adenine, or other purine molecules are able to become part of nucleic acids. Biologists study gene action via the incorporation of modified nitrogenous bases into DNA by manipulating the metabolic role which this enzyme plays. Similarly, the enzyme thymidine kinase is used for the same purpose by biologists because it fills the same important and unique role for the pyrimidines (thymine, cytosine, uracil, etc.).
Acronym: HGPRT
(09 Oct 1997)
hypoxanthine guanine phosphoribosyltransferase deficiency A sex-linked inherited metabolic disorder; complete deficiency results in Lesch-Nyhan syndrome; incomplete deficiency is associated with acute gouty arthritis and renal stones.
(05 Mar 2000)
hypoxanthine-guanine-xanthine phosphoribosyltransferase <enzyme> From tritrichomonas foetus; in contrast to EC 2.4.2.8, this enzyme also uses xanthine as substrate; mw 24 kD
Registry number: EC 2.4.2.-
Synonym: hgxprtase
(26 Jun 1999)
GDP-ribosyl cyclase <enzyme> Catalyses the conversion of ngd+ (the guanine analog of nad) to cyclic GDP-ribose
Registry number: EC 3.2.2.-
(26 Jun 1999)
ribosyl The radical formed by loss of the hemiacetal OH group from either of the two cyclic forms of ribose (yielding ribofuranosyl and ribopyranosyl compounds), by combination with an H of an -NH-or a -CH-group; the natural nucleosides are ribosyl compounds, not ribosides, as the bond between ribose and aglycon is C-N or C-C, not -C-O-X-.
(05 Mar 2000)
N-(5-amino-1-ribosyl-4-imidazolylcarbonyl)-L-aspartic acid 5'-phosphate synthetase <enzyme> 5-amino-1-ribosyl-4-imidazole carboxylic acid 5'-phosphate (carboxy-air), ATP and aspartate yield n(5-amino-4-imidazolylcarbonyl)-l-aspartic acid 5'-phosphate(succino-aicar), ADP and p
Registry number: EC 6.3.4.-
(26 Jun 1999)
hypoxanthine Purine base present in inosine monophosphate (IMP) from which adenosine monophosphate (AMP) and guanosine monophosphate (GMP) are made. The product of deamination of adenine, 6 hydroxy purine.
(18 Nov 1997)
hypoxanthine-aminopterin-thymine medium A type of agar growth medium (a selective medium) which is used to select for cells that are able to make their nucleic acids out of hypoxanthine and/or thymine. All cells are prevented from making nucleotides by any other means (due to the presence of aminopterin or other drugs in the medium), so cells which are unable to use hypoxanthine and/or thymine to do this will not grow, multiply, and become visible colonies. This leaves the cells which are being selected for.
(09 Oct 1997)
hypoxanthine oxidase <enzyme> Dehydrogenases involved in conversion of hypoxanthine to xanthine and xanthine to uric acid, as the final catabolism of purines. Deficient in the human disease xanthinuria.
(18 Nov 1997)
hypoxanthine phosphoribosyltransferase <enzyme> An enzyme that catalyses the conversion of 5-phosphoribosyl-1-pyrophosphate and hypoxanthine, guanine, or 6-mercaptopurine to the corresponding 5'-mononucleotides and pyrophosphate. The enzyme is important in purine biosynthesis as well as central nervous system functions. Complete lack of enzyme activity is associated with the lesch-nyhan syndrome, while partial deficiency results in overproduction of uric acid.
Chemical name: IMP:pyrophosphate phospho-D-ribosyltransferase
Registry number: EC 2.4.2.8
(12 Dec 1998)
tRNA-hypoxanthine ribosyltransferase <enzyme> Incorporates hypoxanthine into mature trna molecules
Registry number: EC 2.4.2.-
Synonym: trna-hpx ribosyltransferase
(26 Jun 1999)
glucose-1-phospho-D-mannosylglycoprotein phosphodiesterase <enzyme> Removes the glucose-1-phosphate from glc-alpha-1-p-6-mannose residues in glycoproteins as a unit; pH optimum 7.5
Registry number: EC 3.1.4.51
Synonym: ag1p phosphodiesterase, alpha-glucose-1-phosphate phosphodiesterase
(26 Jun 1999)
ÇÑ¿µ/¿µÇÑ »çÀü À¯»ç °Ë»ö °á°ú : 3 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • guanine
    ±¸¾Æ´Ñ(DAN,RNA¸¦ ±¸¼ºÇϴ Ǫ¸° ¿°±âÀÇ Çϳª)
  • phospho
    'ÀÎ'ÀÇ ¶æÀÇ °áÇÕ»ç
  • phospho
    'ÀÎ'À̶õ ¶æÀÇ °áÇÕ»ç
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
´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 ¸ÂÃã °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
KMLE ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
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
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 1
MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °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 ¸ÂÃã °Ë»ö (http://www.drugs.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 ¸ÂÃã °Ë»ö °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
WordNet ÀÏ¹Ý ¿µ¿µ »çÀü °Ë»ö °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - American Heritage Dictionary ¿µ¿µ»çÀü ¸ÂÃã °Ë»ö (https://www.ahdictionary.com) °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