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Volumn 234, Issue , 2015, Pages 178-187

Molecular and biochemical characterisation of human short-chain dehydrogenase/reductase member 3 (DHRS3)

Author keywords

[No Author keywords available]

Indexed keywords

ANDROSTENEDIONE; DEHYDROGENASE REDUCTASE MEMBER 3; ESTRONE; GLYCERALDEHYDE; MESSENGER RNA; OXIDOREDUCTASE; PROTEINASE K; UNCLASSIFIED DRUG; ALCOHOL DEHYDROGENASE; FATTY ACID SYNTHASE; MEMBRANE PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RETINOIC ACID; SHORT CHAIN TRANS-2-ENOYL-COA REDUCTASE;

EID: 84928404033     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2014.10.018     Document Type: Article
Times cited : (14)

References (50)
  • 1
    • 84875232324 scopus 로고    scopus 로고
    • Classification and nomenclature of the superfamily of short-chain dehydrogenases/reductases (SDRs)
    • B. Persson, and Y. Kallberg Classification and nomenclature of the superfamily of short-chain dehydrogenases/reductases (SDRs) Chem. Biol. Interact. 202 2013 111 115 10.1016/j.cbi.2012.11.009
    • (2013) Chem. Biol. Interact. , vol.202 , pp. 111-115
    • Persson, B.1    Kallberg, Y.2
  • 2
    • 59149107301 scopus 로고    scopus 로고
    • The human short-chain dehydrogenase/reductase (SDR) superfamily: A bioinformatics summary
    • J.E. Bray, B.D. Marsden, and U. Oppermann The human short-chain dehydrogenase/reductase (SDR) superfamily: a bioinformatics summary Chem. Biol. Interact. 178 2009 99 109 10.1016/j.cbi.2008.10.058
    • (2009) Chem. Biol. Interact. , vol.178 , pp. 99-109
    • Bray, J.E.1    Marsden, B.D.2    Oppermann, U.3
  • 3
    • 0032555517 scopus 로고    scopus 로고
    • Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal
    • F. Haeseleer, J. Huang, L. Lebioda, J.C. Saari, and K. Palczewski Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal J. Biol. Chem. 273 1998 21790 21799
    • (1998) J. Biol. Chem. , vol.273 , pp. 21790-21799
    • Haeseleer, F.1    Huang, J.2    Lebioda, L.3    Saari, J.C.4    Palczewski, K.5
  • 4
    • 84878986448 scopus 로고    scopus 로고
    • Enzymology of retinoic acid biosynthesis and degradation
    • N.Y. Kedishvili Enzymology of retinoic acid biosynthesis and degradation J. Lipid Res. 54 2013 1744 1760 10.1194/jlr.R037028
    • (2013) J. Lipid Res. , vol.54 , pp. 1744-1760
    • Kedishvili, N.Y.1
  • 5
    • 0036174012 scopus 로고    scopus 로고
    • RetSDR1, a short-chain retinol dehydrogenase/reductase, is retinoic acid-inducible and frequently deleted in human neuroblastoma cell lines
    • F. Cerignoli, X. Guo, B. Cardinali, C. Rinaldi, J. Casaletto, and L. Frati retSDR1, a short-chain retinol dehydrogenase/reductase, is retinoic acid-inducible and frequently deleted in human neuroblastoma cell lines Cancer Res. 62 2002 1196 1204
    • (2002) Cancer Res. , vol.62 , pp. 1196-1204
    • Cerignoli, F.1    Guo, X.2    Cardinali, B.3    Rinaldi, C.4    Casaletto, J.5    Frati, L.6
  • 6
    • 80051517670 scopus 로고    scopus 로고
    • P53-Inducible DHRS3 is an endoplasmic reticulum protein associated with lipid droplet accumulation
    • C. Deisenroth, Y. Itahana, L. Tollini, A. Jin, and Y. Zhang P53-Inducible DHRS3 is an endoplasmic reticulum protein associated with lipid droplet accumulation J. Biol. Chem. 286 2011 28343 28356 10.1074/jbc.M111.254227
    • (2011) J. Biol. Chem. , vol.286 , pp. 28343-28356
    • Deisenroth, C.1    Itahana, Y.2    Tollini, L.3    Jin, A.4    Zhang, Y.5
  • 7
    • 84865765909 scopus 로고    scopus 로고
    • DHRS3, a retinal reductase, is differentially regulated by retinoic acid and lipopolysaccharide-induced inflammation in THP-1 cells and rat liver
    • R. Zolfaghari, Q. Chen, and A.C. Ross DHRS3, a retinal reductase, is differentially regulated by retinoic acid and lipopolysaccharide-induced inflammation in THP-1 cells and rat liver Am. J. Physiol. Gastrointest. Liver Physiol. 303 2012 G578 88 10.1152/ajpgi.00234.2012
    • (2012) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.303 , pp. G578-G588
    • Zolfaghari, R.1    Chen, Q.2    Ross, A.C.3
  • 8
    • 33745387612 scopus 로고    scopus 로고
    • Overview of retinoid metabolism and function
    • R. Blomhoff, and H.K. Blomhoff Overview of retinoid metabolism and function J. Neurobiol. 66 2006 606 630 10.1002/neu.20242
    • (2006) J. Neurobiol. , vol.66 , pp. 606-630
    • Blomhoff, R.1    Blomhoff, H.K.2
  • 9
    • 77953601542 scopus 로고    scopus 로고
    • The retinal dehydrogenase/reductase retSDR1/DHRS3 gene is activated by p53 and p63 but not by mutants derived from tumors or EEC/ADULT malformation syndromes
    • R.D. Kirschner, K. Rother, G.A. Müller, and K. Engeland The retinal dehydrogenase/reductase retSDR1/DHRS3 gene is activated by p53 and p63 but not by mutants derived from tumors or EEC/ADULT malformation syndromes Cell Cycle 9 2010 2177 2188 10.4161/cc.9.11.11844
    • (2010) Cell Cycle , vol.9 , pp. 2177-2188
    • Kirschner, R.D.1    Rother, K.2    Müller, G.A.3    Engeland, K.4
  • 10
    • 84890507119 scopus 로고    scopus 로고
    • The retinaldehyde reductase DHRS3 is essential for preventing the formation of excess retinoic acid during embryonic development
    • S.E. Billings, K. Pierzchalski, N.E. Butler Tjaden, X.-Y. Pang, P.A. Trainor, and M.A. Kane The retinaldehyde reductase DHRS3 is essential for preventing the formation of excess retinoic acid during embryonic development FASEB J. 27 2013 4877 4889 10.1096/fj.13-227967
    • (2013) FASEB J. , vol.27 , pp. 4877-4889
    • Billings, S.E.1    Pierzchalski, K.2    Butler Tjaden, N.E.3    Pang, X.-Y.4    Trainor, P.A.5    Kane, M.A.6
  • 11
    • 84887089596 scopus 로고    scopus 로고
    • Dhrs3 protein attenuates retinoic acid signaling and is required for early embryonic patterning
    • R.K.T. Kam, W. Shi, S.O. Chan, Y. Chen, G. Xu, and C.B.-S. Lau Dhrs3 protein attenuates retinoic acid signaling and is required for early embryonic patterning J. Biol. Chem. 288 2013 31477 31487 10.1074/jbc.M113.514984
    • (2013) J. Biol. Chem. , vol.288 , pp. 31477-31487
    • Kam, R.K.T.1    Shi, W.2    Chan, S.O.3    Chen, Y.4    Xu, G.5    Lau, C.B.-S.6
  • 12
    • 84888584531 scopus 로고    scopus 로고
    • Biochemical properties of human dehydrogenase/reductase (SDR family) member 7
    • H. Štambergová, L. Škarydová, J.E. Dunford, and V. Wsól Biochemical properties of human dehydrogenase/reductase (SDR family) member 7 Chem. Biol. Interact. 207 2014 52 57 10.1016/j.cbi.2013.11.003
    • (2014) Chem. Biol. Interact. , vol.207 , pp. 52-57
    • Štambergová, H.1    Škarydová, L.2    Dunford, J.E.3    Wsól, V.4
  • 13
    • 0031826040 scopus 로고    scopus 로고
    • SOSUI: Classification and secondary structure prediction system for membrane proteins
    • T. Hirokawa, S. Boon-Chieng, and S. Mitaku SOSUI: classification and secondary structure prediction system for membrane proteins Bioinformatics 14 1998 378 379 10.1093/bioinformatics/14.4.378
    • (1998) Bioinformatics , vol.14 , pp. 378-379
    • Hirokawa, T.1    Boon-Chieng, S.2    Mitaku, S.3
  • 14
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane-spanning proteins
    • E. Hartmann, T.A. Rapoport, and H.F. Lodish Predicting the orientation of eukaryotic membrane-spanning proteins Proc. Natl. Acad. Sci. U.S.A. 86 1989 5786 5790
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 5786-5790
    • Hartmann, E.1    Rapoport, T.A.2    Lodish, H.F.3
  • 15
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • G.E. Tusnády, and I. Simon The HMMTOP transmembrane topology prediction server Bioinformatics 17 2001 849 850
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnády, G.E.1    Simon, I.2
  • 16
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning protein segments
    • K. Hofmann, and W. Stoffel TMbase - a database of membrane spanning protein segments Biol. Chem. Hoppe-Seyler 374 1993 166
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 19
    • 0037469145 scopus 로고    scopus 로고
    • Differential recognition of the free versus bound retinol by human microsomal retinol/sterol dehydrogenases: Characterization of the holo-CRBP dehydrogenase activity of RoDH-4
    • E.A. Lapshina, O.V. Belyaeva, O.V. Chumakova, and N.Y. Kedishvili Differential recognition of the free versus bound retinol by human microsomal retinol/sterol dehydrogenases: characterization of the holo-CRBP dehydrogenase activity of RoDH-4 Biochemistry 42 2003 776 784 10.1021/bi026836r
    • (2003) Biochemistry , vol.42 , pp. 776-784
    • Lapshina, E.A.1    Belyaeva, O.V.2    Chumakova, O.V.3    Kedishvili, N.Y.4
  • 20
    • 0346365098 scopus 로고    scopus 로고
    • Properties of short-chain dehydrogenase/reductase RalR1: Characterization of purified enzyme, its orientation in the microsomal membrane, and distribution in human tissues and cell lines
    • O.V. Belyaeva, A.V. Stetsenko, P. Nelson, and N.Y. Kedishvili Properties of short-chain dehydrogenase/reductase RalR1: characterization of purified enzyme, its orientation in the microsomal membrane, and distribution in human tissues and cell lines Biochemistry 42 2003 14838 14845 10.1021/bi035288u
    • (2003) Biochemistry , vol.42 , pp. 14838-14845
    • Belyaeva, O.V.1    Stetsenko, A.V.2    Nelson, P.3    Kedishvili, N.Y.4
  • 21
    • 84890933715 scopus 로고    scopus 로고
    • Purification and reconstitution of human membrane-bound DHRS7 (SDR34C1) from Sf9 cells
    • A. Skarka, L. Škarydová, H. Štambergová, and V. Wsól Purification and reconstitution of human membrane-bound DHRS7 (SDR34C1) from Sf9 cells Protein Expr. Purif. 95 2014 44 49 10.1016/j.pep.2013.11.013
    • (2014) Protein Expr. Purif. , vol.95 , pp. 44-49
    • Skarka, A.1    Škarydová, L.2    Štambergová, H.3    Wsól, V.4
  • 22
    • 3042665732 scopus 로고    scopus 로고
    • Blue silver: A very sensitive colloidal Coomassie G-250 staining for proteome analysis
    • G. Candiano, M. Bruschi, L. Musante, L. Santucci, G.M. Ghiggeri, and B. Carnemolla Blue silver: a very sensitive colloidal Coomassie G-250 staining for proteome analysis Electrophoresis 25 2004 1327 1333 10.1002/elps.200305844
    • (2004) Electrophoresis , vol.25 , pp. 1327-1333
    • Candiano, G.1    Bruschi, M.2    Musante, L.3    Santucci, L.4    Ghiggeri, G.M.5    Carnemolla, B.6
  • 23
    • 33645293441 scopus 로고    scopus 로고
    • SPUD: A quantitative PCR assay for the detection of inhibitors in nucleic acid preparations
    • T. Nolan, R.E. Hands, W. Ogunkolade, and S.A. Bustin SPUD: a quantitative PCR assay for the detection of inhibitors in nucleic acid preparations Anal. Biochem. 351 2006 308 310 10.1016/j.ab.2006.01.051
    • (2006) Anal. Biochem. , vol.351 , pp. 308-310
    • Nolan, T.1    Hands, R.E.2    Ogunkolade, W.3    Bustin, S.A.4
  • 24
    • 33749408808 scopus 로고    scopus 로고
    • Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases and aldo-keto reductases with retinoids
    • O. Gallego, O.V. Belyaeva, S. Porté, F.X. Ruiz, A.V. Stetsenko, and E.V. Shabrova Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases and aldo-keto reductases with retinoids Biochem. J. 399 2006 101 109 10.1042/BJ20051988
    • (2006) Biochem. J. , vol.399 , pp. 101-109
    • Gallego, O.1    Belyaeva, O.V.2    Porté, S.3    Ruiz, F.X.4    Stetsenko, A.V.5    Shabrova, E.V.6
  • 25
    • 79957572955 scopus 로고    scopus 로고
    • Anthracyclines and their metabolism in human liver microsomes and the participation of the new microsomal carbonyl reductase
    • A. Skarka, L. Škarydová, H. Štambergová, and V. Wsól Anthracyclines and their metabolism in human liver microsomes and the participation of the new microsomal carbonyl reductase Chem. Biol. Interact. 191 2011 66 74 10.1016/j.cbi.2010.12.016
    • (2011) Chem. Biol. Interact. , vol.191 , pp. 66-74
    • Skarka, A.1    Škarydová, L.2    Štambergová, H.3    Wsól, V.4
  • 26
    • 0032570959 scopus 로고    scopus 로고
    • High-performance liquid chromatography study of stereospecific microsomal enzymes catalysing the reduction of a potential cytostatic drug, oracin. Interspecies comparison
    • V. Wsól, B. Szotáková, E. Kvasničková, and A.F. Fell High-performance liquid chromatography study of stereospecific microsomal enzymes catalysing the reduction of a potential cytostatic drug, oracin. Interspecies comparison J. Chromatogr. A 797 1998 197 201
    • (1998) J. Chromatogr. A , vol.797 , pp. 197-201
    • Wsól, V.1    Szotáková, B.2    Kvasničková, E.3    Fell, A.F.4
  • 27
    • 84876743972 scopus 로고    scopus 로고
    • A simple identification of novel carbonyl reducing enzymes in the metabolism of the tobacco specific carcinogen NNK
    • L. Škarydová, M. Zvěřinová, H. Štambergová, and V. Wsól A simple identification of novel carbonyl reducing enzymes in the metabolism of the tobacco specific carcinogen NNK Drug Metab. Lett. 6 2012 174 181 10.2174/1872312811206030004
    • (2012) Drug Metab. Lett. , vol.6 , pp. 174-181
    • Škarydová, L.1    Zvěřinová, M.2    Štambergová, H.3    Wsól, V.4
  • 30
    • 0036385378 scopus 로고    scopus 로고
    • Short-chain dehydrogenases/reductases (SDRs)
    • Y. Kallberg, U. Oppermann, H. Jörnvall, and B. Persson Short-chain dehydrogenases/reductases (SDRs) Eur. J. Biochem. 269 2002 4409 4417 10.1046/j.1432-1033.2002.03130.x
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4409-4417
    • Kallberg, Y.1    Oppermann, U.2    Jörnvall, H.3    Persson, B.4
  • 31
    • 45549097780 scopus 로고    scopus 로고
    • Overview of the physical state of proteins within cells
    • H.R. Petty Overview of the physical state of proteins within cells Curr. Protoc. Protein Sci. 2003 10.1002/0471140864.ps0105s31 Chapter 1, Unit 1.5
    • (2003) Curr. Protoc. Protein Sci.
    • Petty, H.R.1
  • 32
    • 84901414605 scopus 로고    scopus 로고
    • The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis
    • M.K. Adams, O.V. Belyaeva, L. Wu, and N.Y. Kedishvili The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis J. Biol. Chem. 289 2014 14868 14880 10.1074/jbc.M114.552257
    • (2014) J. Biol. Chem. , vol.289 , pp. 14868-14880
    • Adams, M.K.1    Belyaeva, O.V.2    Wu, L.3    Kedishvili, N.Y.4
  • 34
    • 18244398944 scopus 로고    scopus 로고
    • Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): Catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type i (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxi
    • O.V. Belyaeva, O.V. Korkina, A.V. Stetsenko, T. Kim, P.S. Nelson, and N.Y. Kedishvili Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxi Biochemistry 44 2005 7035 7047 10.1021/bi050226k
    • (2005) Biochemistry , vol.44 , pp. 7035-7047
    • Belyaeva, O.V.1    Korkina, O.V.2    Stetsenko, A.V.3    Kim, T.4    Nelson, P.S.5    Kedishvili, N.Y.6
  • 35
    • 0014621744 scopus 로고
    • The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver
    • R.L. Veech, L.V. Eggleston, and H.A. Krebs The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver Biochem. J. 115 1969 609 619
    • (1969) Biochem. J. , vol.115 , pp. 609-619
    • Veech, R.L.1    Eggleston, L.V.2    Krebs, H.A.3
  • 36
    • 84863338797 scopus 로고    scopus 로고
    • Short chain dehydrogenase/reductase rdhe2 is a novel retinol dehydrogenase essential for frog embryonic development
    • O.V. Belyaeva, S.-A. Lee, M.K. Adams, C. Chang, and N.Y. Kedishvili Short chain dehydrogenase/reductase rdhe2 is a novel retinol dehydrogenase essential for frog embryonic development J. Biol. Chem. 287 2012 9061 9071 10.1074/jbc.M111.336727
    • (2012) J. Biol. Chem. , vol.287 , pp. 9061-9071
    • Belyaeva, O.V.1    Lee, S.-A.2    Adams, M.K.3    Chang, C.4    Kedishvili, N.Y.5
  • 39
    • 6944248900 scopus 로고    scopus 로고
    • Identification of RDH10, an all-trans retinol dehydrogenase, in retinal muller cells
    • B.X. Wu, G. Moiseyev, Y. Chen, B. Rohrer, R.K. Crouch, and J.-X. Ma Identification of RDH10, an all-trans retinol dehydrogenase, in retinal muller cells Invest. Ophthalmol. Vis. Sci. 45 2004 3857 3862 10.1167/iovs.03-1302
    • (2004) Invest. Ophthalmol. Vis. Sci. , vol.45 , pp. 3857-3862
    • Wu, B.X.1    Moiseyev, G.2    Chen, Y.3    Rohrer, B.4    Crouch, R.K.5    Ma, J.-X.6
  • 40
    • 0038070588 scopus 로고    scopus 로고
    • 17 beta-hydroxysteroid dehydrogenase type XI localizes to human steroidogenic cells
    • Z. Chai, P. Brereton, T. Suzuki, H. Sasano, V. Obeyesekere, and G. Escher 17 beta-hydroxysteroid dehydrogenase type XI localizes to human steroidogenic cells Endocrinology 144 2003 2084 2091 10.1210/en.2002-221030
    • (2003) Endocrinology , vol.144 , pp. 2084-2091
    • Chai, Z.1    Brereton, P.2    Suzuki, T.3    Sasano, H.4    Obeyesekere, V.5    Escher, G.6
  • 41
    • 84859758143 scopus 로고    scopus 로고
    • Human microsomal carbonyl reducing enzymes in the metabolism of xenobiotics: Well-known and promising members of the SDR superfamily
    • L. Škarydová, and V. Wsól Human microsomal carbonyl reducing enzymes in the metabolism of xenobiotics: well-known and promising members of the SDR superfamily Drug Metab. Rev. 44 2012 173 191 10.3109/03602532.2011.638304
    • (2012) Drug Metab. Rev. , vol.44 , pp. 173-191
    • Škarydová, L.1    Wsól, V.2
  • 42
    • 33846945701 scopus 로고    scopus 로고
    • Carbonyl reductases: The complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology
    • U. Oppermann Carbonyl reductases: the complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology Annu. Rev. Pharmacol. Toxicol. 47 2007 293 322 10.1146/annurev.pharmtox.47.120505.105316
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 293-322
    • Oppermann, U.1
  • 44
    • 0033852886 scopus 로고    scopus 로고
    • Purification and characterization of oxidoreductases-catalyzing carbonyl reduction of the tobacco-specific nitrosamine 4-methylnitrosamino-1-(3-pyridyl)-1-butanone (NNK) in human liver cytosol
    • A. Atalla, U. Breyer-Pfaff, and E. Maser Purification and characterization of oxidoreductases-catalyzing carbonyl reduction of the tobacco-specific nitrosamine 4-methylnitrosamino-1-(3-pyridyl)-1-butanone (NNK) in human liver cytosol Xenobiotica 30 2000 755 769 10.1080/00498250050119826
    • (2000) Xenobiotica , vol.30 , pp. 755-769
    • Atalla, A.1    Breyer-Pfaff, U.2    Maser, E.3
  • 45
    • 0037325532 scopus 로고    scopus 로고
    • Purification, characterization and NNK carbonyl reductase activities of 11β-hydroxysteroid dehydrogenase type 1 from human liver: Enzyme cooperativity and significance in the detoxification of a tobacco-derived carcinogen
    • E. Maser, J. Friebertshäuser, and B. Völker Purification, characterization and NNK carbonyl reductase activities of 11β-hydroxysteroid dehydrogenase type 1 from human liver: enzyme cooperativity and significance in the detoxification of a tobacco-derived carcinogen Chem. Biol. Interact. 143-144 2003 435 448 10.1016/S0009-2797(02)00180-1
    • (2003) Chem. Biol. Interact. , vol.143-144 , pp. 435-448
    • Maser, E.1    Friebertshäuser, J.2    Völker, B.3
  • 46
    • 0020120634 scopus 로고
    • The lipid composition of human liver microsomes
    • L. Waskell, D. Koblin, and E. Canova-Davis The lipid composition of human liver microsomes Lipids 17 1982 317 320 10.1007/BF02534948
    • (1982) Lipids , vol.17 , pp. 317-320
    • Waskell, L.1    Koblin, D.2    Canova-Davis, E.3
  • 47
    • 59049101287 scopus 로고    scopus 로고
    • Biochemical characterization of human epidermal retinol dehydrogenase 2
    • S.-A. Lee, O.V. Belyaeva, and N.Y. Kedishvili Biochemical characterization of human epidermal retinol dehydrogenase 2 Chem. Biol. Interact. 178 2009 182 187 10.1016/j.cbi.2008.09.019
    • (2009) Chem. Biol. Interact. , vol.178 , pp. 182-187
    • Lee, S.-A.1    Belyaeva, O.V.2    Kedishvili, N.Y.3
  • 48
    • 21244499405 scopus 로고    scopus 로고
    • GAPDH as a housekeeping gene: Analysis of GAPDH mRNA expression in a panel of 72 human tissues
    • R.D. Barber, D.W. Harmer, R.A. Coleman, and B.J. Clark GAPDH as a housekeeping gene: analysis of GAPDH mRNA expression in a panel of 72 human tissues Physiol. Genomics. 21 2005 389 395 10.1152/physiolgenomics.00025.2005
    • (2005) Physiol. Genomics. , vol.21 , pp. 389-395
    • Barber, R.D.1    Harmer, D.W.2    Coleman, R.A.3    Clark, B.J.4
  • 49
    • 68949205722 scopus 로고    scopus 로고
    • Correlations between RNA and protein expression profiles in 23 human cell lines
    • M. Gry, R. Rimini, S. Strömberg, A. Asplund, F. Pontén, and M. Uhlén Correlations between RNA and protein expression profiles in 23 human cell lines BMC Genomics 10 2009 10.1186/1471-2164-10-365
    • (2009) BMC Genomics , vol.10
    • Gry, M.1    Rimini, R.2    Strömberg, S.3    Asplund, A.4    Pontén, F.5    Uhlén, M.6
  • 50
    • 77956261738 scopus 로고    scopus 로고
    • Sequence signatures and mRNA concentration can explain two-thirds of protein abundance variation in a human cell line
    • C. Vogel, R.D.S. Abreu, D. Ko, S.-Y. Le, B.A. Shapiro, and S.C. Burns Sequence signatures and mRNA concentration can explain two-thirds of protein abundance variation in a human cell line Mol. Syst. Biol. 6 2010 1 9 10.1038/msb.2010.59
    • (2010) Mol. Syst. Biol. , vol.6 , pp. 1-9
    • Vogel, C.1    Abreu, R.D.S.2    Ko, D.3    Le, S.-Y.4    Shapiro, B.A.5    Burns, S.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.