메뉴 건너뛰기




Volumn 1, Issue SUPPL.67, 2012, Pages

Introduction to membrane proteins

Author keywords

Membrane protein; Protein stabilization; Purification and detergent solubilization

Indexed keywords

MEMBRANE PROTEIN; DETERGENT; LIPID;

EID: 84861123284     PISSN: 19343655     EISSN: 19343663     Source Type: Journal    
DOI: 10.1002/0471140864.ps2901s67     Document Type: Article
Times cited : (7)

References (69)
  • 2
    • 70350038016 scopus 로고    scopus 로고
    • Mapping the human membrane proteome: A majority of the human membrane proteins can be classified according to function and evolutionary origin
    • Almen, M.S., Nordstrom, K.J., Fredriksson, R., and Schioth, H.B. 2009. Mapping the human membrane proteome: A majority of the human membrane proteins can be classified according to function and evolutionary origin. BMC Biol. 7:50.
    • (2009) BMC Biol , vol.7 , pp. 50
    • Almen, M.S.1    Nordstrom, K.J.2    Fredriksson, R.3    Schioth, H.B.4
  • 3
    • 60149096311 scopus 로고    scopus 로고
    • Properties and identification of human protein drug targets
    • Bakheet, T.M. and Doig, A.J. 2009. Properties and identification of human protein drug targets. Bioinformatics 25:451-457.
    • (2009) Bioinformatics , vol.25 , pp. 451-457
    • Bakheet, T.M.1    Doig, A.J.2
  • 4
    • 0037007480 scopus 로고    scopus 로고
    • In vitro folding, functional characterization, and disulfide pattern of the extracellular domain of human GLP-1 receptor
    • Bazarsuren, A., Grauschopf, U., Wozny, M., Reusch, D., Hoffmann, E., Schaefer, W., Panzner, S., and Rudolph, R. 2002. In vitro folding, functional characterization, and disulfide pattern of the extracellular domain of human GLP-1 receptor. Biophys. Chem. 96:305-318.
    • (2002) Biophys. Chem. , vol.96 , pp. 305-318
    • Bazarsuren, A.1    Grauschopf, U.2    Wozny, M.3    Reusch, D.4    Hoffmann, E.5    Schaefer, W.6    Panzner, S.7    Rudolph, R.8
  • 8
    • 0003884063 scopus 로고    scopus 로고
    • Wiley-Liss, New York
    • Brown, T.A. 1999. Genomes. Wiley-Liss, New York.
    • (1999) Genomes
    • Brown, T.A.1
  • 9
    • 0037827862 scopus 로고    scopus 로고
    • Wiley-Liss, New York
    • Brown, T.A. 2002. Genomes. Wiley-Liss, New York.
    • (2002) Genomes
    • Brown, T.A.1
  • 10
    • 56049094738 scopus 로고    scopus 로고
    • Garland Science, New York
    • Brown, T.A. 2007. Genomes 3. Garland Science, New York.
    • (2007) Genomes 3
    • Brown, T.A.1
  • 11
    • 11244255332 scopus 로고    scopus 로고
    • Location and nature of the residues important for ligand recognition in Gprotein coupled receptors
    • Bywater, R.P. 2005. Location and nature of the residues important for ligand recognition in Gprotein coupled receptors. J. Mol. Recognit. 18:60-72.
    • (2005) J. Mol. Recognit. , vol.18 , pp. 60-72
    • Bywater, R.P.1
  • 12
    • 0028110277 scopus 로고
    • On allosteric mechanisms and acetylcholine receptors
    • Changeux, J.P. and Edelstein, S.J. 1994. On allosteric mechanisms and acetylcholine receptors. Trends Biochem. Sci. 19:399-400.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 399-400
    • Changeux, J.P.1    Edelstein, S.J.2
  • 13
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • Changeux, J.P. and Edelstein, S.J. 2005. Allosteric mechanisms of signal transduction. Science 308:1424-1428.
    • (2005) Science , vol.308 , pp. 1424-1428
    • Changeux, J.P.1    Edelstein, S.J.2
  • 14
    • 80053539881 scopus 로고    scopus 로고
    • Conformational selection or induced fit? 50 years of debate resolved
    • Changeux, J.P. and Edelstein, S. 2011. Conformational selection or induced fit? 50 years of debate resolved. F1000 Biol. Rep. 3:19.
    • (2011) F1000 Biol. Rep. , vol.3 , pp. 19
    • Changeux, J.P.1    Edelstein, S.2
  • 15
    • 47049130746 scopus 로고    scopus 로고
    • Over-expression, solubilization, and purification of G proteincoupled receptors for structural biology
    • Chiu, M.L., Tsang, C., Grihalde, N., and MacWilliams, M.P. 2008. Over-expression, solubilization, and purification of G proteincoupled receptors for structural biology. Comb. Chem. High Throughput Screen. 11:439-462.
    • (2008) Comb. Chem. High Throughput Screen. , vol.11 , pp. 439-462
    • Chiu, M.L.1    Tsang, C.2    Grihalde, N.3    MacWilliams, M.P.4
  • 16
    • 0033430142 scopus 로고    scopus 로고
    • Orphan receptors, novel neuropeptides and reverse pharmaceutical research
    • Civelli, O., Reinscheid, R.K, and Nothacker, H.P. 1999. Orphan receptors, novel neuropeptides and reverse pharmaceutical research. Brain Res. 848:63-65.
    • (1999) Brain Res , vol.848 , pp. 63-65
    • Civelli, O.1    Reinscheid, R.K.2    Nothacker, H.P.3
  • 17
    • 3142567042 scopus 로고    scopus 로고
    • Advances in membrane receptor screening and analysis
    • Cooper, M.A. 2004. Advances in membrane receptor screening and analysis. J. Mol. Recognit. 17:286-315.
    • (2004) J. Mol. Recognit. , vol.17 , pp. 286-315
    • Cooper, M.A.1
  • 18
    • 1542743648 scopus 로고    scopus 로고
    • Plasmon-waveguide resonance studies of ligand binding to the human beta 2-adrenergic receptor
    • Devanathan, S., Yao, Z., Salamon, Z., Kobilka, B., and Tollin, G. 2004. Plasmon-waveguide resonance studies of ligand binding to the human beta 2-adrenergic receptor. Biochemistry 43:3280-3288.
    • (2004) Biochemistry , vol.43 , pp. 3280-3288
    • Devanathan, S.1    Yao, Z.2    Salamon, Z.3    Kobilka, B.4    Tollin, G.5
  • 19
    • 0025081330 scopus 로고
    • Refolding of an integral membrane protein OmpA of Escherichia coli
    • Dornmair, K., Kiefer, H., and Jahnig, F. 1990. Refolding of an integral membrane protein. OmpA of Escherichia coli. J. Biol. Chem. 265:18907-18911.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18907-18911
    • Dornmair, K.1    Kiefer, H.2    Jahnig, F.3
  • 20
    • 0033959340 scopus 로고    scopus 로고
    • Drug discovery today and tomorrow
    • Drews, I.I. 2000. Drug discovery today and tomorrow. Drug Discov. Today 5:2-4.
    • (2000) Drug Discov. Today , vol.5 , pp. 2-4
    • Drews, I.I.1
  • 21
    • 0034677966 scopus 로고    scopus 로고
    • Drug discovery: A historical perspective
    • Drews, J. 2000. Drug discovery: A historical perspective. Science 287:1960-1964.
    • (2000) Science , vol.287 , pp. 1960-1964
    • Drews, J.1
  • 23
    • 77952682080 scopus 로고    scopus 로고
    • Relationships between structural dynamics and functional kinetics in oligomeric membrane receptors
    • Edelstein, S.J. and Changeux, J.P. 2010. Relationships between structural dynamics and functional kinetics in oligomeric membrane receptors. Biophys. J. 98:2045-2052.
    • (2010) Biophys. J. , vol.98 , pp. 2045-2052
    • Edelstein, S.J.1    Changeux, J.P.2
  • 26
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • Grisshammer, R. and Tate, C.G. 1995. Overexpression of integral membrane proteins for structural studies. Q. Rev. Biophys. 28:315-422.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 315-422
    • Grisshammer, R.1    Tate, C.G.2
  • 28
    • 0142039027 scopus 로고    scopus 로고
    • Global analysis of G-protein-coupled receptor signaling in human tissues
    • Hakak, Y., Shrestha, D., Goegel, M.C., Behan, D.P., and Chalmers, D.T. 2003. Global analysis of G-protein-coupled receptor signaling in human tissues. FEBS Lett. 550:11-17.
    • (2003) FEBS Lett , vol.550 , pp. 11-17
    • Hakak, Y.1    Shrestha, D.2    Goegel, M.C.3    Behan, D.P.4    Chalmers, D.T.5
  • 29
    • 0028815284 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • Haltia, T. and Freire, E. 1995. Forces and factors that contribute to the structural stability of membrane proteins. Biochim. Biophys. Acta 1228:1-27.
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 1-27
    • Haltia, T.1    Freire, E.2
  • 30
    • 33750970320 scopus 로고    scopus 로고
    • Recovering motifs from biased genomes: Application of signal correction
    • Hasan, S. and Schreiber, M. 2006. Recovering motifs from biased genomes: Application of signal correction. Nucleic Acids Res. 34:5124-5132.
    • (2006) Nucleic Acids Res , vol.34 , pp. 5124-5132
    • Hasan, S.1    Schreiber, M.2
  • 31
    • 33745607880 scopus 로고    scopus 로고
    • Prioritizing genomic drug targets in pathogens: Application to Mycobacterium tuberculosis
    • Hasan, S., Daugelat, S., Rao, P.S., and Schreiber, M. 2006. Prioritizing genomic drug targets in pathogens: Application to Mycobacterium tuberculosis. PLoS Comput. Biol. 2:e61.
    • (2006) PLoS Comput. Biol. , vol.2
    • Hasan, S.1    Daugelat, S.2    Rao, P.S.3    Schreiber, M.4
  • 32
    • 0015236357 scopus 로고
    • Removal of lipids from human plasma low-density lipoprotein by detergents
    • Helenius, A. and Simons, K. 1971. Removal of lipids from human plasma low-density lipoprotein by detergents. Biochemistry 10:2542-2547.
    • (1971) Biochemistry , vol.10 , pp. 2542-2547
    • Helenius, A.1    Simons, K.2
  • 33
    • 0016657917 scopus 로고
    • Solubilization of membranes by detergents
    • Helenius, A. and Simons, K. 1975. Solubilization of membranes by detergents. Biochim. Biophys. Acta 415:29-79.
    • (1975) Biochim. Biophys. Acta , vol.415 , pp. 29-79
    • Helenius, A.1    Simons, K.2
  • 38
    • 0037450517 scopus 로고    scopus 로고
    • In vitro folding of alpha-helical membrane proteins
    • Kiefer, H. 2003. In vitro folding of alpha-helical membrane proteins. Biochim. Biophys. Acta 1610:57-62.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 57-62
    • Kiefer, H.1
  • 39
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R.F. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 40
    • 3543074650 scopus 로고    scopus 로고
    • Towards higher-throughput membrane protein production for structural genomics initiatives
    • Laible, P.D., Scott, H.N., Henry, L., and Hanson, D.K. 2004. Towards higher-throughput membrane protein production for structural genomics initiatives. J. Struct. Funct. Genomics 5:167-172.
    • (2004) J. Struct. Funct. Genomics , vol.5 , pp. 167-172
    • Laible, P.D.1    Scott, H.N.2    Henry, L.3    Hanson, D.K.4
  • 43
    • 84858287267 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: Detecting and interpreting the mobility of transmembrane proteins in vivo
    • 2.19.1-2.19.16
    • Malchus, N. 2011. Fluorescence correlation spectroscopy: Detecting and interpreting the mobility of transmembrane proteins in vivo. Curr. Protoc. Toxicol. 48:2.19.1-2.19.16.
    • (2011) Curr. Protoc. Toxicol. , vol.48
    • Malchus, N.1
  • 44
    • 77956191678 scopus 로고    scopus 로고
    • High-throughput expression and purification of membrane proteins
    • Mancia, F. and Love, J. 2010. High-throughput expression and purification of membrane proteins. J. Struct. Biol. 172:85-93.
    • (2010) J. Struct. Biol. , vol.172 , pp. 85-93
    • Mancia, F.1    Love, J.2
  • 45
    • 80052089904 scopus 로고    scopus 로고
    • High throughput platforms for structural genomics of integral membrane proteins
    • Mancia, F. and Love, J. 2011. High throughput platforms for structural genomics of integral membrane proteins. Curr. Opin. Struct. Biol. 21:517-522.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 517-522
    • Mancia, F.1    Love, J.2
  • 47
    • 80054687050 scopus 로고    scopus 로고
    • Toward rational design of protein detergent complexes: Determinants of mixed micelles that are critical for the in vitro stabilization of a G-protein coupled receptor
    • O'Malley, M.A., Helgeson, M.E., Wagner, N.J., and Robinson, A.S. 2011. Toward rational design of protein detergent complexes: Determinants of mixed micelles that are critical for the in vitro stabilization of a G-protein coupled receptor. Biophys. J. 101:1938-1948.
    • (2011) Biophys. J. , vol.101 , pp. 1938-1948
    • O'Malley, M.A.1    Helgeson, M.E.2    Wagner, N.J.3    Robinson, A.S.4
  • 49
    • 0942298112 scopus 로고    scopus 로고
    • The 5- hydroxytryptamine(1A) receptor is stably palmitoylated, and acylation is critical for communication of receptor with Gi protein
    • Papoucheva, E., Dumuis, A., Sebben, M., Richter, D.W., and Ponimaskin, E.G. 2004. The 5-hydroxytryptamine(1A) receptor is stably palmitoylated, and acylation is critical for communication of receptor with Gi protein. J. Biol. Chem. 279:3280-3291.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3280-3291
    • Papoucheva, E.1    Dumuis, A.2    Sebben, M.3    Richter, D.W.4    Ponimaskin, E.G.5
  • 50
    • 0035227924 scopus 로고    scopus 로고
    • Functional genomics Comprehensive interference
    • Patterson, M. 2001. Functional genomics. Comprehensive interference. Nat. Rev. Genet. 2:6.
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 6
    • Patterson, M.1
  • 54
    • 0036514182 scopus 로고    scopus 로고
    • Optimizing functional versus total expression of the human mu-opioid receptor in Pichia pastoris
    • Sarramegna, V., Demange, P., Milon, A., and Talmont, F. 2002. Optimizing functional versus total expression of the human mu-opioid receptor in Pichia pastoris. Protein Expr. Purif. 24:212-220.
    • (2002) Protein Expr. Purif. , vol.24 , pp. 212-220
    • Sarramegna, V.1    Demange, P.2    Milon, A.3    Talmont, F.4
  • 55
    • 0041876269 scopus 로고    scopus 로고
    • Heterologous expression of Gprotein-coupled receptors: Comparison of expression systems from the standpoint of largescale production and purification
    • Sarramegna, V., Talmont, F., Demange, P., and Milon, A. 2003. Heterologous expression of Gprotein-coupled receptors: Comparison of expression systems from the standpoint of largescale production and purification.Cell.Mol. Life Sci. 60:1529-1546.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1529-1546
    • Sarramegna, V.1    Talmont, F.2    Demange, P.3    Milon, A.4
  • 56
    • 0033850756 scopus 로고    scopus 로고
    • Molecularmanipulation of G-protein-coupled receptors: A new avenue into drug discovery
    • Sautel, M. and Milligan, G. 2000. Molecularmanipulation of G-protein-coupled receptors: A new avenue into drug discovery. Curr. Med. Chem. 7:889-896.
    • (2000) Curr. Med. Chem. , vol.7 , pp. 889-896
    • Sautel, M.1    Milligan, G.2
  • 57
    • 43149099684 scopus 로고    scopus 로고
    • Protein expression in Drosophila Schneider 2 cell system
    • 4.16.1-4.16.15
    • Schetz, J.A and Shankar, E.P.N. 2004. Protein expression in Drosophila Schneider 2 cell system. Curr. Protoc. Neurosci. 27:4.16.1-4.16.15.
    • (2004) Curr. Protoc. Neurosci. , vol.27
    • Schetz, J.A.1    Shankar, E.P.N.2
  • 58
    • 84868156593 scopus 로고    scopus 로고
    • Overview of membrane protein solubilization
    • Schimerlik, M.I. 1998. Overview of membrane protein solubilization. Curr. Protoc. Neurosci. 2:5.9.1-5.9.5.
    • (1998) Curr. Protoc. Neurosci. , vol.2
    • Schimerlik, M.I.1
  • 59
    • 0037690722 scopus 로고    scopus 로고
    • World's best selling drugs
    • Scussa, F. 2002. World's best selling drugs. Med. Ad. News 21:1-46.
    • (2002) Med. Ad. News , vol.21 , pp. 1-46
    • Scussa, F.1
  • 60
    • 0015858252 scopus 로고
    • Solubilization of the membrane proteins from Semliki Forest virus with Triton X100
    • Simons, K., Helenius, A., and Garoff, H. 1973. Solubilization of the membrane proteins from Semliki Forest virus with Triton X100. J. Mol. Biol. 80:119-133.
    • (1973) J. Mol. Biol. , vol.80 , pp. 119-133
    • Simons, K.1    Helenius, A.2    Garoff, H.3
  • 62
    • 0030298385 scopus 로고    scopus 로고
    • Heterologous expression of G-protein-coupled receptors
    • Tate, C.G. and Grisshammer, R. 1996. Heterologous expression of G-protein-coupled receptors. Trends Biotechnol. 14:426-430.
    • (1996) Trends Biotechnol , vol.14 , pp. 426-430
    • Tate, C.G.1    Grisshammer, R.2
  • 65
    • 3042621274 scopus 로고    scopus 로고
    • The progress of membrane protein structure determination
    • White, S.H. 2004. The progress of membrane protein structure determination. Protein Sci. 13:1948-1949.
    • (2004) Protein Sci , vol.13 , pp. 1948-1949
    • White, S.H.1
  • 66
    • 77949521932 scopus 로고    scopus 로고
    • Advances and hold-ups in the study of structure, function and regulation of Cys-loop ligand-gated ion channels and receptors
    • Yakel, J. 2010. Advances and hold-ups in the study of structure, function and regulation of Cys-loop ligand-gated ion channels and receptors. J. Physiol. 588:555-556.
    • (2010) J. Physiol. , vol.588 , pp. 555-556
    • Yakel, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.