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Volumn 62, Issue 1, 2008, Pages 36-43

Expression and purification of the active variant of recombinant murine Golli-interacting protein (GIP)-characterization of its phosphatase activity and interaction with Golli-BG21

Author keywords

BG21; Circular dichroism; Cross linking; Genes of oligodendrocyte lineage (Golli); Golli interacting protein (GIP); Intrinsically disordered protein; Phosphatase

Indexed keywords

GOLLI INTERACTING PROTEIN, MOUSE; GOLLI-INTERACTING PROTEIN, MOUSE; MBP PROTEIN, MOUSE; NERVE PROTEIN; NUCLEAR PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; RECOMBINANT PROTEIN; TRANSCRIPTION FACTOR;

EID: 52949110958     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.06.004     Document Type: Article
Times cited : (4)

References (27)
  • 2
    • 3042567344 scopus 로고    scopus 로고
    • The golli-myelin basic protein negatively regulates signal transduction in T lymphocytes
    • Feng J.M., Fernandes A.O., Campagnoni C.W., Hu Y.H., and Campagnoni A.T. The golli-myelin basic protein negatively regulates signal transduction in T lymphocytes. J. Neuroimmunol. 152 (2004) 57-66
    • (2004) J. Neuroimmunol. , vol.152 , pp. 57-66
    • Feng, J.M.1    Fernandes, A.O.2    Campagnoni, C.W.3    Hu, Y.H.4    Campagnoni, A.T.5
  • 3
    • 0034669882 scopus 로고    scopus 로고
    • Why are natively unfolded proteins unstructured under physiologic conditions?
    • Uversky V.N., Gillespie J.R., and Fink A.L. Why are natively unfolded proteins unstructured under physiologic conditions?. Proteins 41 (2000) 415-427
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 4
    • 3042553626 scopus 로고    scopus 로고
    • Myelin basic protein-diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis
    • Harauz G., Ishiyama N., Hill C.M., Bates I.R., Libich D.S., and Farès C. Myelin basic protein-diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis. Micron 35 (2004) 503-542
    • (2004) Micron , vol.35 , pp. 503-542
    • Harauz, G.1    Ishiyama, N.2    Hill, C.M.3    Bates, I.R.4    Libich, D.S.5    Farès, C.6
  • 6
    • 0038168110 scopus 로고    scopus 로고
    • A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5
    • Yeo M., Lin P.S., Dahmus M.E., and Gill G.N. A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5. J. Biol. Chem. 278 (2003) 26078-26085
    • (2003) J. Biol. Chem. , vol.278 , pp. 26078-26085
    • Yeo, M.1    Lin, P.S.2    Dahmus, M.E.3    Gill, G.N.4
  • 7
    • 0033858096 scopus 로고    scopus 로고
    • Complete nucleotide sequence and genomic structure of the human NRAMP1 gene region on chromosome region 2q35
    • Marquet S., Lepage P., Hudson T.J., Musser J.M., and Schurr E. Complete nucleotide sequence and genomic structure of the human NRAMP1 gene region on chromosome region 2q35. Mamm. Genome 11 (2000) 755-762
    • (2000) Mamm. Genome , vol.11 , pp. 755-762
    • Marquet, S.1    Lepage, P.2    Hudson, T.J.3    Musser, J.M.4    Schurr, E.5
  • 8
    • 0028053812 scopus 로고
    • Purification and characterization of a phosphatase from HeLa cells which dephosphorylates the C terminal domain of RNA polymerase II
    • Chambers R.S., and Dahmus M.E. Purification and characterization of a phosphatase from HeLa cells which dephosphorylates the C terminal domain of RNA polymerase II. J. Biol. Chem. 269 (1994) 26243-26248
    • (1994) J. Biol. Chem. , vol.269 , pp. 26243-26248
    • Chambers, R.S.1    Dahmus, M.E.2
  • 9
    • 2242454131 scopus 로고    scopus 로고
    • TFIIF-associating carboxyl-terminal domain phosphatase dephosphorylates phosphor-serines 2 and 5 of RNA polymerase II
    • Lin P.S., Dubois M.F., and Dahmus M.E. TFIIF-associating carboxyl-terminal domain phosphatase dephosphorylates phosphor-serines 2 and 5 of RNA polymerase II. J. Biol. Chem. 277 (2002) 45949-45956
    • (2002) J. Biol. Chem. , vol.277 , pp. 45949-45956
    • Lin, P.S.1    Dubois, M.F.2    Dahmus, M.E.3
  • 10
    • 4143117908 scopus 로고    scopus 로고
    • Structure and mechanism of RNA polymerase II CTD phosphatase
    • Kamenski T., Heilmeier S., Meinhart A., and Cramer P. Structure and mechanism of RNA polymerase II CTD phosphatase. Mol. Cell 15 (2004) 399-407
    • (2004) Mol. Cell , vol.15 , pp. 399-407
    • Kamenski, T.1    Heilmeier, S.2    Meinhart, A.3    Cramer, P.4
  • 11
    • 18844431580 scopus 로고    scopus 로고
    • Cloning and characterization of a novel RNA polymerase II C-terminal domain phosphatase
    • Zheng H.R., Ji C.N., Gu S.H., Shi B., Wang J., Xie Y., and Mao Y. Cloning and characterization of a novel RNA polymerase II C-terminal domain phosphatase. Biochem. Biophys. Res. Commun. 331 (2005) 1401-1407
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 1401-1407
    • Zheng, H.R.1    Ji, C.N.2    Gu, S.H.3    Shi, B.4    Wang, J.5    Xie, Y.6    Mao, Y.7
  • 12
    • 33751538328 scopus 로고    scopus 로고
    • Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1
    • Zhang Y., Kim Y., Genoud N., Gao J., Kelly J.W., Pfaff S.L., Gill G.N., and Noel J.P. Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1. Mol. Cell 24 (2006) 759-770
    • (2006) Mol. Cell , vol.24 , pp. 759-770
    • Zhang, Y.1    Kim, Y.2    Genoud, N.3    Gao, J.4    Kelly, J.W.5    Pfaff, S.L.6    Gill, G.N.7    Noel, J.P.8
  • 14
    • 4344585269 scopus 로고    scopus 로고
    • Phosphoryl group transfer: evolution of a catalytic scaffold
    • Allen K.N., and Dunaway-Mariano D. Phosphoryl group transfer: evolution of a catalytic scaffold. Trends Biochem. Sci. 29 (2004) 495-503
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 495-503
    • Allen, K.N.1    Dunaway-Mariano, D.2
  • 15
    • 13944254436 scopus 로고    scopus 로고
    • New vision from eyes absent: transcription factors as enzymes
    • Rebay I., Silver S.J., and Tootle T.L. New vision from eyes absent: transcription factors as enzymes. Trends Genet. 21 (2005) 163-171
    • (2005) Trends Genet. , vol.21 , pp. 163-171
    • Rebay, I.1    Silver, S.J.2    Tootle, T.L.3
  • 16
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • Gohla A., Birkenfeld J., and Bokoch G.M. Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat. Cell Biol. 7 (2005) 21-29
    • (2005) Nat. Cell Biol. , vol.7 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 18
    • 33846871687 scopus 로고    scopus 로고
    • Purification and spectroscopic characterization of the recombinant BG21 isoform of murine golli myelin basic protein
    • Bamm V.V., Ahmed M.A., Ladizhansky V., and Harauz G. Purification and spectroscopic characterization of the recombinant BG21 isoform of murine golli myelin basic protein. J. Neurosci. Res. 85 (2007) 272-284
    • (2007) J. Neurosci. Res. , vol.85 , pp. 272-284
    • Bamm, V.V.1    Ahmed, M.A.2    Ladizhansky, V.3    Harauz, G.4
  • 19
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: an interactive website for analysis of protein secondary structure from circular dichroism data
    • Lobley A., Whitmore L., and Wallace B.A. DICHROWEB: an interactive website for analysis of protein secondary structure from circular dichroism data. Bioinformatics 18 (2002) 211-212
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 20
    • 33747855587 scopus 로고    scopus 로고
    • A reference database for circular dichroism spectroscopy covering fold and secondary structure space
    • Lees J.G., Miles A.J., Wien F., and Wallace B.A. A reference database for circular dichroism spectroscopy covering fold and secondary structure space. Bioinformatics 22 (2006) 1955-1962
    • (2006) Bioinformatics , vol.22 , pp. 1955-1962
    • Lees, J.G.1    Miles, A.J.2    Wien, F.3    Wallace, B.A.4
  • 21
    • 0036893088 scopus 로고    scopus 로고
    • 2+-calmodulin: in vitro studies using gel shift assays
    • 2+-calmodulin: in vitro studies using gel shift assays. Mol. Cell Biochem. 241 (2002) 45-52
    • (2002) Mol. Cell Biochem. , vol.241 , pp. 45-52
    • Libich, D.S.1    Harauz, G.2
  • 23
    • 0032486282 scopus 로고    scopus 로고
    • A new class of phosphotranspherase phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif
    • Collet J.F., Stroobant V., Pirard M., Delpierre G., and Van Schaftingen E. A new class of phosphotranspherase phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif. J. Biol. Chem. 273 (1998) 14107-14112
    • (1998) J. Biol. Chem. , vol.273 , pp. 14107-14112
    • Collet, J.F.1    Stroobant, V.2    Pirard, M.3    Delpierre, G.4    Van Schaftingen, E.5
  • 24
    • 36248949702 scopus 로고    scopus 로고
    • Increased expression of golli myelin basic proteins enhances calcium influx into oligodendroglial cells
    • Paez P.M., Spreuer V., Handley V., Feng J.M., Campagnoni C., and Campagnoni A.T. Increased expression of golli myelin basic proteins enhances calcium influx into oligodendroglial cells. J. Neurosci. 27 (2007) 12690-12699
    • (2007) J. Neurosci. , vol.27 , pp. 12690-12699
    • Paez, P.M.1    Spreuer, V.2    Handley, V.3    Feng, J.M.4    Campagnoni, C.5    Campagnoni, A.T.6
  • 26
    • 34548261730 scopus 로고    scopus 로고
    • The BG21 isoform of Golli myelin basic protein is intrinsically disordered with a highly flexible amino-terminal domain
    • Ahmed M.A.M., Bamm V.V., Harauz G., and Ladizhansky V. The BG21 isoform of Golli myelin basic protein is intrinsically disordered with a highly flexible amino-terminal domain. Biochemistry 46 (2007) 9700-9712
    • (2007) Biochemistry , vol.46 , pp. 9700-9712
    • Ahmed, M.A.M.1    Bamm, V.V.2    Harauz, G.3    Ladizhansky, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.