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Volumn 1652, Issue 2, 2003, Pages 83-90

Expression, purification and spectroscopic studies of full-length Kir3.1 channel C-terminus

Author keywords

Circular dichroism spectroscopy; Kir3.1; Protein expression; Secondary structure

Indexed keywords

BINDING PROTEIN; CARBOXYL GROUP; DIMER; GUANINE NUCLEOTIDE BINDING PROTEIN; HISTIDINE; POLYPEPTIDE; POTASSIUM CHANNEL; RECOMBINANT DNA; RECOMBINANT PROTEIN; RESIN;

EID: 1242328704     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2003.07.001     Document Type: Article
Times cited : (3)

References (28)
  • 1
    • 0020575547 scopus 로고
    • + channels in isolated pacemaker cells of the mammalian heart
    • + channels in isolated pacemaker cells of the mammalian heart. Nature. 303:1983;250-253.
    • (1983) Nature , vol.303 , pp. 250-253
    • Sakmann, B.1    Noma, A.2    Trautwein, W.3
  • 7
    • 0028792376 scopus 로고
    • Identification of structural elements involved in G-protein gating of the GIRK1 potassium channel
    • Slesinger P.A., Reuveny E., Jan Y.N., Jan L.Y. Identification of structural elements involved in G-protein gating of the GIRK1 potassium channel. Neuron. 15:1995;1145-1156.
    • (1995) Neuron , vol.15 , pp. 1145-1156
    • Slesinger, P.A.1    Reuveny, E.2    Jan, Y.N.3    Jan, L.Y.4
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0028068336 scopus 로고
    • Purification of Tβγ subunit of transducin
    • Bigay J., Chabre M. Purification of Tβγ subunit of transducin. Methods Enzymol. 237:1994;449-451.
    • (1994) Methods Enzymol. , vol.237 , pp. 449-451
    • Bigay, J.1    Chabre, M.2
  • 13
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher S.W., Glöckner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry. 20:1981;33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glöckner, J.2
  • 14
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular-dichroism spectra using an unsupervised learning neural-network
    • Andrade M.A., Chacón P., Merelo J.J., Morán F. Evaluation of secondary structure of proteins from UV circular-dichroism spectra using an unsupervised learning neural-network. Protein Eng. 6:1993;383-390.
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Merelo, J.J.3    Morán, F.4
  • 15
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama N., Venyaminov S.Y., Woody R.W. Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8:1999;370-380.
    • (1999) Protein Sci. , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 16
    • 0023652252 scopus 로고
    • Differential absorption flattening optical effects are significant in the circular-dichroism spectra of large membrane-fragments
    • Wallace B.A., Teeters C.L. Differential absorption flattening optical effects are significant in the circular-dichroism spectra of large membrane-fragments. Biochemistry. 26:1987;65-70.
    • (1987) Biochemistry , vol.26 , pp. 65-70
    • Wallace, B.A.1    Teeters, C.L.2
  • 17
    • 0028181528 scopus 로고
    • Protein classification by stochastic modeling and optimal filtering of amino acid sequences
    • White J.V., Stultz C.M., Smith T.F. Protein classification by stochastic modeling and optimal filtering of amino acid sequences. Math. Biosci. 119:1994;35-75.
    • (1994) Math. Biosci. , vol.119 , pp. 35-75
    • White, J.V.1    Stultz, C.M.2    Smith, T.F.3
  • 18
    • 77956716177 scopus 로고    scopus 로고
    • Predicting protein structure with probabilistic models in protein structural biology in bio-medical research
    • N. Allewell, & C. Woodward. Greenwich: JAI Press
    • Stultz C.M., Nambudripad R., Lathrop R.H., White J.V. Predicting protein structure with probabilistic models in protein structural biology in bio-medical research. Allewell N., Woodward C. Advances in Molecular and Cell Biology. vol. 22B:1997;447-506 JAI Press, Greenwich.
    • (1997) Advances in Molecular and Cell Biology , vol.22 , pp. 447-506
    • Stultz, C.M.1    Nambudripad, R.2    Lathrop, R.H.3    White, J.V.4
  • 19
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile based neural networks
    • Rost B. PHD: predicting one-dimensional protein structure by profile based neural networks. Methods Enzymol. 266:1996;525-539.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 20
    • 0026540796 scopus 로고
    • Involvement of the chaperonin DnaK in the rapid degradation of a mutant protein in Escherichia coli
    • Sherman M.Y., Goldberg A.L. Involvement of the chaperonin DnaK in the rapid degradation of a mutant protein in Escherichia coli. EMBO J. 11:1992;71-77.
    • (1992) EMBO J. , vol.11 , pp. 71-77
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 22
    • 0032538623 scopus 로고    scopus 로고
    • + (GIRK4) channel homomultimers
    • + (GIRK4) channel homomultimers. J. Biol. Chem. 273:1998;27499-27504.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27499-27504
    • Corey, S.1    Clapham, D.E.2
  • 26
    • 0037737799 scopus 로고    scopus 로고
    • Binding of the anticonvulsant drug lamotrigine and the neurotoxin batrachotoxin to voltage-gated sodium channels induces conformational changes associated with block and steady-state activation
    • Cronin N.B., O'Reilly A., Duclohier H., Wallace B.A. Binding of the anticonvulsant drug lamotrigine and the neurotoxin batrachotoxin to voltage-gated sodium channels induces conformational changes associated with block and steady-state activation. J. Biol. Chem. 278:2003;10675-10682.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10675-10682
    • Cronin, N.B.1    O'Reilly, A.2    Duclohier, H.3    Wallace, B.A.4
  • 27
    • 0037184996 scopus 로고    scopus 로고
    • Structural basis of inward rectification: Cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 resolution
    • Nishida M., MacKinnon R. Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 resolution. Cell. 111:2002;957-965.
    • (2002) Cell , vol.111 , pp. 957-965
    • Nishida, M.1    MacKinnon, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.