메뉴 건너뛰기




Volumn 106, Issue 6, 2009, Pages 1760-1765

Detergent binding explains anomalous SDS-PAGE migration of membrane proteins

Author keywords

Detergent binding; Gel shifting; Membrane proteins; SDS PAGE; Sodium dodecyl sulfate

Indexed keywords

DETERGENT; DODECYL SULFATE SODIUM; HELIX LOOP HELIX PROTEIN; MEMBRANE PROTEIN; MUTANT PROTEIN; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 60549094781     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0813167106     Document Type: Article
Times cited : (629)

References (57)
  • 2
    • 0016366728 scopus 로고
    • Free-boundary electrophoresis of sodium dodecyl sulfate-protein polypeptide complexes with special reference to SDSpolyacrylamide gel electrophoresis
    • Shirahama K, Tsujii K, Takagi T (1974) Free-boundary electrophoresis of sodium dodecyl sulfate-protein polypeptide complexes with special reference to SDSpolyacrylamide gel electrophoresis. J Biochem (Tokyo) 75:309-319.
    • (1974) J Biochem (Tokyo) , vol.75 , pp. 309-319
    • Shirahama, K.1    Tsujii, K.2    Takagi, T.3
  • 3
    • 0025314149 scopus 로고
    • Protein-decorated micelle structure of sodium-dodecyl-sulfate-protein complexes as determined by neutron scattering
    • Ibel K, et al. (1990) Protein-decorated micelle structure of sodium-dodecyl-sulfate-protein complexes as determined by neutron scattering. Eur J Biochem 190:311-318.
    • (1990) Eur J Biochem , vol.190 , pp. 311-318
    • Ibel, K.1
  • 4
    • 0014816360 scopus 로고
    • Binding of dodecyl sulfate to proteins at high binding ratios: Possible implications for the state of proteins in biological membranes
    • Reynolds JA, Tanford C (1970) Binding of dodecyl sulfate to proteins at high binding ratios: Possible implications for the state of proteins in biological membranes. Proc Natl Acad Sci USA 66:1002-1007.
    • (1970) Proc Natl Acad Sci USA , vol.66 , pp. 1002-1007
    • Reynolds, J.A.1    Tanford, C.2
  • 6
    • 0001076494 scopus 로고
    • The molecular weight of the major glycoprotein from the human erythrocyte membrane
    • Grefrath SP, Reynolds JA (1974) The molecular weight of the major glycoprotein from the human erythrocyte membrane. Proc Natl Acad Sci USA 71:3913-3916.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 3913-3916
    • Grefrath, S.P.1    Reynolds, J.A.2
  • 7
    • 0017882604 scopus 로고
    • Isolation of a membrane protein from R rubrum chromatophores and its abnormal behavior in SDS-polyacrylamide gel electrophoresis due to a high binding capacity for SDS
    • Miyake J, Ochiai-Yanagi S, Kasumi T, Takagi T (1978) Isolation of a membrane protein from R rubrum chromatophores and its abnormal behavior in SDS-polyacrylamide gel electrophoresis due to a high binding capacity for SDS. J Biochem 83:1679-1686.
    • (1978) J Biochem , vol.83 , pp. 1679-1686
    • Miyake, J.1    Ochiai-Yanagi, S.2    Kasumi, T.3    Takagi, T.4
  • 8
    • 0016424433 scopus 로고
    • The binding of deoxycholate, Triton X-100, sodium dodecyl sulfate, and phosphatidylcholine vesicles to cytochrome b5
    • Robinson NC, Tanford C (1975) The binding of deoxycholate, Triton X-100, sodium dodecyl sulfate, and phosphatidylcholine vesicles to cytochrome b5. Biochemistry 14:369-378.
    • (1975) Biochemistry , vol.14 , pp. 369-378
    • Robinson, N.C.1    Tanford, C.2
  • 9
    • 33645504750 scopus 로고    scopus 로고
    • NMR study of the tetrameric KcsA potassium channel in detergent micelles
    • Chill JH, Louis JM, Miller C, Bax A (2006) NMR study of the tetrameric KcsA potassium channel in detergent micelles. Protein Sci 15:684-698.
    • (2006) Protein Sci , vol.15 , pp. 684-698
    • Chill, J.H.1    Louis, J.M.2    Miller, C.3    Bax, A.4
  • 10
    • 0025359489 scopus 로고
    • Binding of sodium dodecyl sulphate to an integral membrane protein and to a water-soluble enzyme: Determination by molecular-sieve chromatography with flow scintillation detection
    • Wallsten M, Lundahl P (1990) Binding of sodium dodecyl sulphate to an integral membrane protein and to a water-soluble enzyme: Determination by molecular-sieve chromatography with flow scintillation detection. J Chrom 512:3-12.
    • (1990) J Chrom , vol.512 , pp. 3-12
    • Wallsten, M.1    Lundahl, P.2
  • 11
    • 0014342404 scopus 로고
    • The binding of sodium dodecyl sulphate to various proteins
    • Pitt-Rivers R, Impiombato FS (1968) The binding of sodium dodecyl sulphate to various proteins. Biochem J 109:825-830.
    • (1968) Biochem J , vol.109 , pp. 825-830
    • Pitt-Rivers, R.1    Impiombato, F.S.2
  • 12
    • 0017232611 scopus 로고
    • Mobility of sodium dodecyl sulphate - protein complexes
    • Dunker AK, Kenyon AJ (1976) Mobility of sodium dodecyl sulphate - protein complexes. Biochem J 153:191-197.
    • (1976) Biochem J , vol.153 , pp. 191-197
    • Dunker, A.K.1    Kenyon, A.J.2
  • 13
    • 0034952420 scopus 로고    scopus 로고
    • Interhelical hydrogen bonds in the CFTR membrane domain
    • Therien AG, Grant FE, Deber CM (2001) Interhelical hydrogen bonds in the CFTR membrane domain. Nat Struct Biol 8:597-601.
    • (2001) Nat Struct Biol , vol.8 , pp. 597-601
    • Therien, A.G.1    Grant, F.E.2    Deber, C.M.3
  • 14
    • 0025081330 scopus 로고
    • Refolding of an integral membrane protein. OmpA of Escherichia coli
    • Dornmair K, Kiefer H, 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
  • 15
    • 0032532698 scopus 로고    scopus 로고
    • Characterization of a heat modifiable protein, Escherichia coli outer membrane protein OmpA in binary surfactant system of sodium dodecyl sulfate and octylglucoside
    • Ohnishi S, Kameyama K, Takagi T (1998) Characterization of a heat modifiable protein, Escherichia coli outer membrane protein OmpA in binary surfactant system of sodium dodecyl sulfate and octylglucoside. Biochim Biophys Acta 1375:101-109.
    • (1998) Biochim Biophys Acta , vol.1375 , pp. 101-109
    • Ohnishi, S.1    Kameyama, K.2    Takagi, T.3
  • 16
    • 0032832765 scopus 로고    scopus 로고
    • Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent
    • Kleinschmidt JH, Wiener MC, Tamm LK (1999) Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent. Protein Sci 8:2065-2071.
    • (1999) Protein Sci , vol.8 , pp. 2065-2071
    • Kleinschmidt, J.H.1    Wiener, M.C.2    Tamm, L.K.3
  • 17
    • 33845428343 scopus 로고    scopus 로고
    • An unfolding story of helical transmembrane proteins
    • Renthal R (2006) An unfolding story of helical transmembrane proteins. Biochemistry 45:14559-14566.
    • (2006) Biochemistry , vol.45 , pp. 14559-14566
    • Renthal, R.1
  • 18
    • 3042517378 scopus 로고    scopus 로고
    • Non-native interhelical hydrogen bonds in the cystic fibrosis transmembrane conductance regulator domain modulated by polar mutations
    • Choi MY, Cardarelli L, Therien AG, Deber CM (2004) Non-native interhelical hydrogen bonds in the cystic fibrosis transmembrane conductance regulator domain modulated by polar mutations. Biochemistry 43:8077-8083.
    • (2004) Biochemistry , vol.43 , pp. 8077-8083
    • Choi, M.Y.1    Cardarelli, L.2    Therien, A.G.3    Deber, C.M.4
  • 19
    • 0036925967 scopus 로고    scopus 로고
    • Expression and purification of two hydrophobic double-spanning membrane proteins derived from the cystic fibrosis transmembrane conductance regulator
    • Therien AG, Glibowicka M, Deber CM (2002) Expression and purification of two hydrophobic double-spanning membrane proteins derived from the cystic fibrosis transmembrane conductance regulator. Protein Expr Purif 25:81-86.
    • (2002) Protein Expr Purif , vol.25 , pp. 81-86
    • Therien, A.G.1    Glibowicka, M.2    Deber, C.M.3
  • 20
    • 34250873336 scopus 로고    scopus 로고
    • Role of the extracellular loop in the folding of a CFTR transmembrane helical hairpin
    • Wehbi H, Rath A, Glibowicka M, Deber CM (2007) Role of the extracellular loop in the folding of a CFTR transmembrane helical hairpin. Biochemistry 46:7099-7106.
    • (2007) Biochemistry , vol.46 , pp. 7099-7106
    • Wehbi, H.1    Rath, A.2    Glibowicka, M.3    Deber, C.M.4
  • 21
    • 0027283560 scopus 로고
    • Detergent binding as a measure of hydrophobic surface area of integral membrane proteins
    • Moller JV, le Maire M (1993) Detergent binding as a measure of hydrophobic surface area of integral membrane proteins. J Biol Chem 268:18659-18672.
    • (1993) J Biol Chem , vol.268 , pp. 18659-18672
    • Moller, J.V.1    le Maire, M.2
  • 22
    • 58749084475 scopus 로고    scopus 로고
    • Gel chromatography and analytical ultracentrifugation to determine the extent of detergent binding and aggregation, and Stokes radius of membrane proteins using sarcoplasmic reticulum Ca2+-ATPase as an example
    • le Maire M, et al. (2008) Gel chromatography and analytical ultracentrifugation to determine the extent of detergent binding and aggregation, and Stokes radius of membrane proteins using sarcoplasmic reticulum Ca2+-ATPase as an example. Nat Protoc 3:1782-1795.
    • (2008) Nat Protoc , vol.3 , pp. 1782-1795
    • le Maire, M.1
  • 23
    • 0018382749 scopus 로고
    • Conformation of human erythrocyte glycophorin A and its constituent peptides
    • Schulte TH, Marchesi VT (1979) Conformation of human erythrocyte glycophorin A and its constituent peptides. Biochemistry 18:275-280.
    • (1979) Biochemistry , vol.18 , pp. 275-280
    • Schulte, T.H.1    Marchesi, V.T.2
  • 24
    • 0017819024 scopus 로고
    • Influence of single amino acid substitutions on electrophoretic mobility of sodium dodecyl sulfate-protein complexes
    • de Jong WW, Zweers A, Cohen LH (1978) Influence of single amino acid substitutions on electrophoretic mobility of sodium dodecyl sulfate-protein complexes. Biochem Biophys Res Commun 82:532-539.
    • (1978) Biochem Biophys Res Commun , vol.82 , pp. 532-539
    • de Jong, W.W.1    Zweers, A.2    Cohen, L.H.3
  • 25
    • 0017251379 scopus 로고
    • Subunit structure of human erythrocyte glycophorin A
    • Furthmayr H, Marchesi VT (1976) Subunit structure of human erythrocyte glycophorin A. Biochemistry 15:1137-1144.
    • (1976) Biochemistry , vol.15 , pp. 1137-1144
    • Furthmayr, H.1    Marchesi, V.T.2
  • 26
    • 0242657348 scopus 로고    scopus 로고
    • Membrane protein folding: Beyond the two stage model
    • Engelman DM, et al. (2003) Membrane protein folding: Beyond the two stage model. FEBS Lett 555:122-125.
    • (2003) FEBS Lett , vol.555 , pp. 122-125
    • Engelman, D.M.1
  • 27
    • 46249089993 scopus 로고    scopus 로고
    • Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins
    • Joh NH, et al. (2008) Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins. Nature 453:1266-1270.
    • (2008) Nature , vol.453 , pp. 1266-1270
    • Joh, N.H.1
  • 28
    • 33847242278 scopus 로고    scopus 로고
    • Coarse-grained molecular dynamics simulations of membrane proteins and peptides
    • Bond PJ, Holyoake J, Ivetac A, Khalid S, Sansom MS (2007) Coarse-grained molecular dynamics simulations of membrane proteins and peptides. J Struct Biol 157:593-605.
    • (2007) J Struct Biol , vol.157 , pp. 593-605
    • Bond, P.J.1    Holyoake, J.2    Ivetac, A.3    Khalid, S.4    Sansom, M.S.5
  • 29
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: A measure of transmembrane helix association in a biological membrane
    • Russ WP, Engelman DM (1999) TOXCAT: A measure of transmembrane helix association in a biological membrane. Proc Natl Acad Sci USA 96:863-868.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 30
    • 34447271539 scopus 로고    scopus 로고
    • Changes in apparent free energy of helix-helix dimerization in a biological membrane due to point mutations
    • Duong MT, Jaszewski TM, Fleming KG, MacKenzie KR (2007) Changes in apparent free energy of helix-helix dimerization in a biological membrane due to point mutations. J Mol Biol 371:422-434.
    • (2007) J Mol Biol , vol.371 , pp. 422-434
    • Duong, M.T.1    Jaszewski, T.M.2    Fleming, K.G.3    MacKenzie, K.R.4
  • 31
    • 33751088317 scopus 로고    scopus 로고
    • Sequence dependence of BNIP3 transmembrane domain dimerization implicates side-chain hydrogen bonding and a tandem GxxxG motif in specific helix-helix interactions
    • Sulistijo ES, MacKenzie KR (2006) Sequence dependence of BNIP3 transmembrane domain dimerization implicates side-chain hydrogen bonding and a tandem GxxxG motif in specific helix-helix interactions. J Mol Biol 364:974-990.
    • (2006) J Mol Biol , vol.364 , pp. 974-990
    • Sulistijo, E.S.1    MacKenzie, K.R.2
  • 32
    • 0035969998 scopus 로고    scopus 로고
    • Polar side chains drive the association of model transmembrane peptides
    • Gratkowski H, Lear JD, DeGrado WF (2001) Polar side chains drive the association of model transmembrane peptides. Proc Natl Acad Sci USA 98:880-885.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 880-885
    • Gratkowski, H.1    Lear, J.D.2    DeGrado, W.F.3
  • 33
    • 0033983453 scopus 로고    scopus 로고
    • Asparagine-mediated self-association of a model transmembrane helix
    • Choma C, Gratkowski H, Lear JD, DeGrado WF (2000) Asparagine-mediated self-association of a model transmembrane helix. Nat Struct Biol 7:161-166.
    • (2000) Nat Struct Biol , vol.7 , pp. 161-166
    • Choma, C.1    Gratkowski, H.2    Lear, J.D.3    DeGrado, W.F.4
  • 34
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA
    • Riordan JR, et al. (1989) Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA. Science 245:1066-1073.
    • (1989) Science , vol.245 , pp. 1066-1073
    • Riordan, J.R.1
  • 35
    • 0031926765 scopus 로고    scopus 로고
    • Guidelines for membrane protein engineering derived from de novo designed model peptides
    • Liu LP, Deber CM (1998) Guidelines for membrane protein engineering derived from de novo designed model peptides. Biopolymers 47:41-62.
    • (1998) Biopolymers , vol.47 , pp. 41-62
    • Liu, L.P.1    Deber, C.M.2
  • 36
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (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
  • 38
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • Engelman DM, Steitz TA, Goldman A (1986) Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu Rev Biophys Biophys Chem 15:321-353.
    • (1986) Annu Rev Biophys Biophys Chem , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 39
    • 13444262028 scopus 로고    scopus 로고
    • Recognition of transmembrane helices by the endoplasmic reticulum translocon
    • Hessa T, et al. (2005) Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 433:377-381.
    • (2005) Nature , vol.433 , pp. 377-381
    • Hessa, T.1
  • 40
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White SH, Wimley WC (1999) Membrane protein folding and stability: Physical principles. Annu Rev Biophys Biomol Struct 28:319-365.
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 41
    • 0031595839 scopus 로고    scopus 로고
    • Purification and properties of the F1F0 ATPase of Ilyobacter tartaricus, a sodium ion pump
    • Neumann S, Matthey U, Kaim G, Dimroth P (1998) Purification and properties of the F1F0 ATPase of Ilyobacter tartaricus, a sodium ion pump. J Bacteriol 180:3312-3316.
    • (1998) J Bacteriol , vol.180 , pp. 3312-3316
    • Neumann, S.1    Matthey, U.2    Kaim, G.3    Dimroth, P.4
  • 42
    • 0036606751 scopus 로고    scopus 로고
    • Purification of the Escherichia coli ammonium transporter AmtB reveals a trimeric stoichiometry
    • Blakey D, et al. (2002) Purification of the Escherichia coli ammonium transporter AmtB reveals a trimeric stoichiometry. Biochem J 364:527-535.
    • (2002) Biochem J , vol.364 , pp. 527-535
    • Blakey, D.1
  • 43
    • 0019888608 scopus 로고
    • Purification and reconstitution of functional lactose carrier from Escherichia coli
    • Newman MJ, Foster DL, Wilson TH, Kaback HR (1981) Purification and reconstitution of functional lactose carrier from Escherichia coli. J Biol Chem 256:11804-11808.
    • (1981) J Biol Chem , vol.256 , pp. 11804-11808
    • Newman, M.J.1    Foster, D.L.2    Wilson, T.H.3    Kaback, H.R.4
  • 44
    • 0022548921 scopus 로고
    • Identification of the btuCED polypeptides and evidence for their role in vitamin B12 transport in Escherichia coli
    • de Veaux LC, Clevenson DS, Bradbeer C, Kadner RJ (1986) Identification of the btuCED polypeptides and evidence for their role in vitamin B12 transport in Escherichia coli. J Bacteriol 167:920-927.
    • (1986) J Bacteriol , vol.167 , pp. 920-927
    • de Veaux, L.C.1    Clevenson, D.S.2    Bradbeer, C.3    Kadner, R.J.4
  • 45
    • 0032692857 scopus 로고    scopus 로고
    • High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel
    • Maduke M, Pheasant DJ, Miller C (1999) High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel. J Gen Physiol 114:713-722.
    • (1999) J Gen Physiol , vol.114 , pp. 713-722
    • Maduke, M.1    Pheasant, D.J.2    Miller, C.3
  • 46
    • 0030739227 scopus 로고    scopus 로고
    • Tetrameric stoichiometry of a prokaryotic K+ channel
    • Heginbotham L, Odessey E, Miller C (1997) Tetrameric stoichiometry of a prokaryotic K+ channel. Biochemistry 36:10335-10342.
    • (1997) Biochemistry , vol.36 , pp. 10335-10342
    • Heginbotham, L.1    Odessey, E.2    Miller, C.3
  • 47
    • 0021350781 scopus 로고
    • Phosphorylation-induced mobility shift in phospholamban in sodium dodecyl sulfate-polyacrylamide gels: Evidence for a protein structure consisting of multiple identical phosphorylatable subunits
    • Wegener AD, Jones LR (1984) Phosphorylation-induced mobility shift in phospholamban in sodium dodecyl sulfate-polyacrylamide gels: Evidence for a protein structure consisting of multiple identical phosphorylatable subunits. J Biol Chem 259:1834-1841.
    • (1984) J Biol Chem , vol.259 , pp. 1834-1841
    • Wegener, A.D.1    Jones, L.R.2
  • 48
    • 27244448677 scopus 로고    scopus 로고
    • Expression, purification, and crystallization of the ammonium transporter Amt-1 from Archaeoglobus fulgidus
    • Andrade SL, Dickmanns A, Ficner R, Einsle O (2005) Expression, purification, and crystallization of the ammonium transporter Amt-1 from Archaeoglobus fulgidus. Acta Crystallogr 61:861-863.
    • (2005) Acta Crystallogr , vol.61 , pp. 861-863
    • Andrade, S.L.1    Dickmanns, A.2    Ficner, R.3    Einsle, O.4
  • 49
    • 0034633880 scopus 로고    scopus 로고
    • Secondary structure and oligomerization of the E. coli glycerol facilitator
    • Manley DM, et al. (2000) Secondary structure and oligomerization of the E. coli glycerol facilitator. Biochemistry 39:12303-12311.
    • (2000) Biochemistry , vol.39 , pp. 12303-12311
    • Manley, D.M.1
  • 50
    • 0036280794 scopus 로고    scopus 로고
    • Purification of the small mechanosensitive channel of Escherichia coli (MscS): The subunit structure, conduction, and gating characteristics in liposomes
    • Sukharev S (2002) Purification of the small mechanosensitive channel of Escherichia coli (MscS): The subunit structure, conduction, and gating characteristics in liposomes. Biophys J 83:290-298.
    • (2002) Biophys J , vol.83 , pp. 290-298
    • Sukharev, S.1
  • 51
    • 0036794301 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein
    • Pos KM, Diederichs K (2002) Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein. Acta Crystallogr D Biol Crystallogr 58:1865-1867.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 1865-1867
    • Pos, K.M.1    Diederichs, K.2
  • 52
    • 0035810954 scopus 로고    scopus 로고
    • High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter
    • Auer M, et al. (2001) High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter. Biochemistry 40:6628-6635.
    • (2001) Biochemistry , vol.40 , pp. 6628-6635
    • Auer, M.1
  • 53
    • 0037468462 scopus 로고    scopus 로고
    • Reconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris
    • Karlsson M, et al. (2003) Reconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris. FEBS Lett 537:68-72.
    • (2003) FEBS Lett , vol.537 , pp. 68-72
    • Karlsson, M.1
  • 54
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Wang Y, Zhang Y, Ha Y (2006) Crystal structure of a rhomboid family intramembrane protease. Nature 444:179-180.
    • (2006) Nature , vol.444 , pp. 179-180
    • Wang, Y.1    Zhang, Y.2    Ha, Y.3
  • 55
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang G, Spencer RH, Lee AT, Barclay MT, Rees DC (1998) Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel. Science 282:2220-2226.
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 56
    • 36448978229 scopus 로고    scopus 로고
    • GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function
    • Rosenbaum DM, et al. (2007) GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function. Science 318:1266-1273.
    • (2007) Science , vol.318 , pp. 1266-1273
    • Rosenbaum, D.M.1
  • 57
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang Y, et al. (2002) Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417:515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.