메뉴 건너뛰기




Volumn 25, Issue 6-7, 2008, Pages 557-566

Isolation, characterization and molecular 3D model of human GDE4, a novel membrane protein containing glycerophosphodiester phosphodiesterase domain

Author keywords

3 D model; Cytoplasm; GDE domain; Glycerophosphodiester phosphodiesterase 4; Homo sapiens

Indexed keywords

AMINO ACID; COMPLEMENTARY DNA; GLYCEROPHOSPHATE; GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE 4; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; PHOSPHODIESTERASE; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG;

EID: 56849095532     PISSN: 09687688     EISSN: 14645203     Source Type: Journal    
DOI: 10.1080/09687680802537605     Document Type: Article
Times cited : (15)

References (33)
  • 1
    • 33947241907 scopus 로고    scopus 로고
    • Transport and metabolism of glycerophosphodiesters produced through phospholipid deacylation
    • Patton-Vogt J. 2007. Transport and metabolism of glycerophosphodiesters produced through phospholipid deacylation. Biochim Biophys Acta 1771:337-342.
    • (2007) Biochim Biophys Acta , vol.1771 , pp. 337-342
    • Patton-Vogt, J.1
  • 2
    • 0024563256 scopus 로고
    • Nucleotide sequence of the ugpQ gene encoding glycerophosphoryl diester phosphodiesterase of Escherichia coli K-12
    • Kasahara M, Makino K, Amemura M, Nakata A. 1989. Nucleotide sequence of the ugpQ gene encoding glycerophosphoryl diester phosphodiesterase of Escherichia coli K-12. Nucleic Acids Res 17:2854-2866.
    • (1989) Nucleic Acids Res , vol.17 , pp. 2854-2866
    • Kasahara, M.1    Makino, K.2    Amemura, M.3    Nakata, A.4
  • 3
    • 0025775076 scopus 로고
    • Characterization of two genes, glpQ and ugpQ, encoding glycerophosphoryl diester phosphodiesterases of Escherichia coli
    • Tommassen J, Eiglmeier K, Cole ST, Overduin P, Larson TJ, Boos W. 1991. Characterization of two genes, glpQ and ugpQ, encoding glycerophosphoryl diester phosphodiesterases of Escherichia coli. Mol Gen Genet 226:321-327.
    • (1991) Mol Gen Genet , vol.226 , pp. 321-327
    • Tommassen, J.1    Eiglmeier, K.2    Cole, S.T.3    Overduin, P.4    Larson, T.J.5    Boos, W.6
  • 4
    • 0020641705 scopus 로고
    • Periplasmic glycerophosphodiester phosphodiesterase of Escherichia coli, a new enzyme of the glp regulon
    • Larson TJ, Ehrmann M, Boos W. 1983. Periplasmic glycerophosphodiester phosphodiesterase of Escherichia coli, a new enzyme of the glp regulon. J Biol Chem 258:5428-5432.
    • (1983) J Biol Chem , vol.258 , pp. 5428-5432
    • Larson, T.J.1    Ehrmann, M.2    Boos, W.3
  • 5
    • 0028258204 scopus 로고
    • The glpT and glpQ genes of the glycerol regulon in Bacillus subtilis
    • Nilsson RP, Beijer L, Rutberg B. 1994. The glpT and glpQ genes of the glycerol regulon in Bacillus subtilis. Microbiology140:723-730
    • (1994) Microbiology140 , pp. 723-730
    • Nilsson, R.P.1    Beijer, L.2    Rutberg, B.3
  • 6
    • 0030821179 scopus 로고    scopus 로고
    • Identification of homologs for thioredoxin, peptidyl prolyl cis-trans isomerase, and glycerophosphodiester phosphodiesterase in outer membrane fractions from Treponema pallidum, the syphilis spirochete
    • Shevchenko DV, Akins DR, Robinson EJ, Li M, Shevchenko OV, Radolf JD. 1997. Identification of homologs for thioredoxin, peptidyl prolyl cis-trans isomerase, and glycerophosphodiester phosphodiesterase in outer membrane fractions from Treponema pallidum, the syphilis spirochete. Infect Immun 65:4179-4189.
    • (1997) Infect Immun , vol.65 , pp. 4179-4189
    • Shevchenko, D.V.1    Akins, D.R.2    Robinson, E.J.3    Li, M.4    Shevchenko, O.V.5    Radolf, J.D.6
  • 8
    • 31944439123 scopus 로고    scopus 로고
    • Glycerophosphocholine catabolism as a new route for choline formation for phosphatidylcholine synthesis by the kennedy pathway
    • Fernandez-Murray JP, McMaster CR. 2005. Glycerophosphocholine catabolism as a new route for choline formation for phosphatidylcholine synthesis by the kennedy pathway. J Biol Chem 280:38290-38296.
    • (2005) J Biol Chem , vol.280 , pp. 38290-38296
    • Fernandez-Murray, J.P.1    McMaster, C.R.2
  • 9
    • 27744505616 scopus 로고    scopus 로고
    • Glycerophosphocholine-dependent growth requires gde1p (ypl110c) and git1p in Saccharomyces cerevisiae
    • Fisher E, Almaguer C, Holic R, Griac P, Patton-Vogt J. 2005. Glycerophosphocholine-dependent growth requires gde1p (ypl110c) and git1p in Saccharomyces cerevisiae. J Biol Chem 280:36110-36117.
    • (2005) J Biol Chem , vol.280 , pp. 36110-36117
    • Fisher, E.1    Almaguer, C.2    Holic, R.3    Griac, P.4    Patton-Vogt, J.5
  • 10
    • 47749139636 scopus 로고    scopus 로고
    • Yeast Pgc1p (YPL206c) controls the amount of phosphatidylglycerol via a phospholipase C-type degradation mechanism
    • Simocková M, Holic R, Tahotná D, Patton-Vogt J, Griac P. 2008. Yeast Pgc1p (YPL206c) controls the amount of phosphatidylglycerol via a phospholipase C-type degradation mechanism. J Biol Chem 283:17107-17115.
    • (2008) J Biol Chem , vol.283 , pp. 17107-17115
    • Simocková, M.1    Holic, R.2    Tahotná, D.3    Patton-Vogt, J.4    Griac, P.5
  • 11
    • 0034635962 scopus 로고    scopus 로고
    • MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16
    • Zheng B, Chen D, Farquhar MG. 2000. MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16. Proc Natl Acad Sci USA 97:3999-4004.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3999-4004
    • Zheng, B.1    Chen, D.2    Farquhar, M.G.3
  • 12
    • 0037452765 scopus 로고    scopus 로고
    • GDE1/MIR16 is a glycerophosphoinositol phosphodiesterase regulated by stimulation of G protein-coupled receptors
    • Zheng B, Berrie CP, Corda D, Farquhar MG. 2003. GDE1/MIR16 is a glycerophosphoinositol phosphodiesterase regulated by stimulation of G protein-coupled receptors. Proc Natl Acad Sci USA 100:1745-1750.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1745-1750
    • Zheng, B.1    Berrie, C.P.2    Corda, D.3    Farquhar, M.G.4
  • 13
    • 44049087532 scopus 로고    scopus 로고
    • Anandamide biosynthesis catalyzed by the phosphodiesterase GDE1 and detection of glycerophospho-N-acyl ethanolamine precursors in mouse brain
    • Simon GM, Cravatt BF. 2008. Anandamide biosynthesis catalyzed by the phosphodiesterase GDE1 and detection of glycerophospho-N-acyl ethanolamine precursors in mouse brain. J Biol Chem 283:9341-9349.
    • (2008) J Biol Chem , vol.283 , pp. 9341-9349
    • Simon, G.M.1    Cravatt, B.F.2
  • 14
  • 15
    • 3242812875 scopus 로고    scopus 로고
    • Isolation and characterization of two serpentine membrane proteins containing glycerophosphodiester phosphodiesterase, GDE2 and GDE6
    • Nogusa Y, Fujioka Y, Komatsu R, Kato N, Yanaka N. 2004. Isolation and characterization of two serpentine membrane proteins containing glycerophosphodiester phosphodiesterase, GDE2 and GDE6. Gene 337:173-179.
    • (2004) Gene , vol.337 , pp. 173-179
    • Nogusa, Y.1    Fujioka, Y.2    Komatsu, R.3    Kato, N.4    Yanaka, N.5
  • 16
    • 33846844866 scopus 로고    scopus 로고
    • Involvement of membrane protein GDE2 in retinoic acid-induced neurite formation in Neuro2A cells
    • Yanaka N, Nogusa Y, Fujioka Y, Yamashita Y, Kato N. 2007. Involvement of membrane protein GDE2 in retinoic acid-induced neurite formation in Neuro2A cells. FEBS Lett 581:712-718.
    • (2007) FEBS Lett , vol.581 , pp. 712-718
    • Yanaka, N.1    Nogusa, Y.2    Fujioka, Y.3    Yamashita, Y.4    Kato, N.5
  • 17
    • 49449085894 scopus 로고    scopus 로고
    • GDPD5 is a glycerophosphocholine phosphodiesterase that osmotically regulates the osmoprotective organic osmolyte GPC.Proc
    • Gallazzini M, Ferraris JD, Burg MB. 2008. GDPD5 is a glycerophosphocholine phosphodiesterase that osmotically regulates the osmoprotective organic osmolyte GPC.Proc Natl Acad Sci USA 105:11026-1031.
    • (2008) Natl Acad Sci USA , vol.105 , pp. 11026-11031
    • Gallazzini, M.1    Ferraris, J.D.2    Burg, M.B.3
  • 18
    • 36148963665 scopus 로고    scopus 로고
    • Mammalian glycerophosphodiester phosphodiesterases
    • Yanaka N. 2007. Mammalian glycerophosphodiester phosphodiesterases. Biosci Biotechnol Biochem 71:1811-1818.
    • (2007) Biosci Biotechnol Biochem , vol.71 , pp. 1811-1818
    • Yanaka, N.1
  • 19
    • 33751527380 scopus 로고    scopus 로고
    • Rolipram: A specific phosphodiesterase 4 inhibitor with potential antipsychotic activity
    • Kanes SJ, Tokarczyk J, Siegel SJ, Bilker W, Abel T, Kelly MP. 2007. Rolipram: a specific phosphodiesterase 4 inhibitor with potential antipsychotic activity. Neuroscience 144:239-246.
    • (2007) Neuroscience , vol.144 , pp. 239-246
    • Kanes, S.J.1    Tokarczyk, J.2    Siegel, S.J.3    Bilker, W.4    Abel, T.5    Kelly, M.P.6
  • 22
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S, Tamura K, Nei M. 2004. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinform 5:150-163.
    • (2004) Brief Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 23
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J, Schwede T. 2006. The SWISS-MODEL Workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 25
    • 44949103270 scopus 로고    scopus 로고
    • Crystal structure of glycerophosphodiester phosphodiesterase (GDPD) from Thermoanaerobacter tengcongensis, a metal ion-dependent enzyme: Insight into the catalytic mechanism
    • Shi L, Liu JF, An XM, Liang DC. 2008. Crystal structure of glycerophosphodiester phosphodiesterase (GDPD) from Thermoanaerobacter tengcongensis, a metal ion-dependent enzyme: insight into the catalytic mechanism. Proteins 72:280-288.
    • (2008) Proteins , vol.72 , pp. 280-288
    • Shi, L.1    Liu, J.F.2    An, X.M.3    Liang, D.C.4
  • 27
    • 0023651307 scopus 로고
    • RNA splice junctions of different classes of eukaryotes: Sequence statistics and functional implications in gene expression
    • Shapiro MB, Senapathy P. 1987. RNA splice junctions of different classes of eukaryotes: sequence statistics and functional implications in gene expression. Nucleic Acids Res 15:7155-7174
    • (1987) Nucleic Acids Res , vol.15 , pp. 7155-7174
    • Shapiro, M.B.1    Senapathy, P.2
  • 28
    • 33645228201 scopus 로고    scopus 로고
    • Genomic organization, characterization, and molecular 3D model of GDE1, a novel mammalian glycerophosphoinositol phosphodiesterase
    • Bachmann AS, Duennebier FF, Mocz G. 2006. Genomic organization, characterization, and molecular 3D model of GDE1, a novel mammalian glycerophosphoinositol phosphodiesterase. Gene 371:144-153.
    • (2006) Gene , vol.371 , pp. 144-153
    • Bachmann, A.S.1    Duennebier, F.F.2    Mocz, G.3
  • 29
    • 48249109179 scopus 로고    scopus 로고
    • Cloning and characterization of a human GDPD domain-containing protein GDPD5
    • Lang Q, Zhang H, Li J, Yin H, Zhang Y, Tang W, Wan B, Yu L. 2008. Cloning and characterization of a human GDPD domain-containing protein GDPD5. Mol Biol Rep 35:351-359.
    • (2008) Mol Biol Rep , vol.35 , pp. 351-359
    • Lang, Q.1    Zhang, H.2    Li, J.3    Yin, H.4    Zhang, Y.5    Tang, W.6    Wan, B.7    Yu, L.8
  • 30
    • 25844477017 scopus 로고    scopus 로고
    • Transmembrane protein GDE2 induces motor neuron differentiation in vivo
    • Rao M, Sockanathan S. 2005. Transmembrane protein GDE2 induces motor neuron differentiation in vivo. Science 309:2212-2215.
    • (2005) Science , vol.309 , pp. 2212-2215
    • Rao, M.1    Sockanathan, S.2
  • 33
    • 38049187056 scopus 로고    scopus 로고
    • Primary antioxidant free radical scavenging and redox signaling pathways in higher plant cells
    • Shao HB, Chu LY, Lu ZH, Kang CM.2008.Primary antioxidant free radical scavenging and redox signaling pathways in higher plant cells. Int J Biol Sci 4:8-14.
    • (2008) Int J Biol Sci , vol.4 , pp. 8-14
    • Shao, H.B.1    Chu, L.Y.2    Lu, Z.H.3    Kang, C.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.