메뉴 건너뛰기




Volumn 94, Issue 2, 2008, Pages 457-468

Two-step folding of recombinant mitochondrial porin in detergent

Author keywords

[No Author keywords available]

Indexed keywords

DETERGENT; DODECYL SULFATE SODIUM; LIPOSOME; MONOSACCHARIDE; PORIN; PROTEINASE; SOLVENT; TRYPTOPHAN; TYROSINE; HIS HIS HIS HIS HIS HIS; HIS-HIS-HIS-HIS-HIS-HIS; HISTIDINE; OLIGOPEPTIDE; PEPTIDE HYDROLASE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 38349016735     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.115196     Document Type: Article
Times cited : (10)

References (71)
  • 1
    • 0028341536 scopus 로고
    • Permeation of hydrophilic solutes through mitochondrial outer membranes: Review on mitochondrial porins
    • Benz, R. 1994. Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins. Biochim. Biophys. Acta. 1197:167-196.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 167-196
    • Benz, R.1
  • 2
    • 0027166197 scopus 로고
    • Structure/function relationships in hexokinase. Site-directed mutational analyses and characterization of overexpressed fragments implicate different functions for the N- and C-terminal halves of the enzyme
    • Arora, K. K., C. R. Filburn, and P. L. Pedersen. 1993. Structure/function relationships in hexokinase. Site-directed mutational analyses and characterization of overexpressed fragments implicate different functions for the N- and C-terminal halves of the enzyme. J. Biol. Chem. 268:18259-18266.
    • (1993) J. Biol. Chem , vol.268 , pp. 18259-18266
    • Arora, K.K.1    Filburn, C.R.2    Pedersen, P.L.3
  • 3
    • 0028034636 scopus 로고
    • In vitro complex formation between the octamer of mitochondrial creatine kinase and porin
    • Brdiczka, D., P. Kaldis, and T. Wallimann. 1994. In vitro complex formation between the octamer of mitochondrial creatine kinase and porin. J. Biol. Chem. 269:27640-27644.
    • (1994) J. Biol. Chem , vol.269 , pp. 27640-27644
    • Brdiczka, D.1    Kaldis, P.2    Wallimann, T.3
  • 4
    • 0029854155 scopus 로고    scopus 로고
    • ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane
    • Rostovtseva, T., and M. Colombini. 1996. ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane. J. Biol. Chem. 271:28006-28008.
    • (1996) J. Biol. Chem , vol.271 , pp. 28006-28008
    • Rostovtseva, T.1    Colombini, M.2
  • 5
    • 0030947935 scopus 로고    scopus 로고
    • VDAC channels mediate and gate the flow of ATP: Implications for the regulation of mitochondrial function
    • Rostovtseva, T., and M. Colombini. 1997. VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function. Biophys. J. 72:1954-1962.
    • (1997) Biophys. J , vol.72 , pp. 1954-1962
    • Rostovtseva, T.1    Colombini, M.2
  • 6
    • 0028158479 scopus 로고
    • NADH regulates the gating of VDAC, the mitochondrial outer membrane channel
    • Zizi, M., M. Forte, E. Blachly-Dyson, and M. Colombini. 1994. NADH regulates the gating of VDAC, the mitochondrial outer membrane channel. J. Biol. Chem. 269:1614-1616.
    • (1994) J. Biol. Chem , vol.269 , pp. 1614-1616
    • Zizi, M.1    Forte, M.2    Blachly-Dyson, E.3    Colombini, M.4
  • 8
    • 33745136102 scopus 로고    scopus 로고
    • The voltage-dependent anion channel (VDAC): Function in intracellular signalling, cell life and cell death
    • Shoshan-Barmatz, V., A. Israelson, D. Brdiczka, and S. S. Sheu. 2006. The voltage-dependent anion channel (VDAC): function in intracellular signalling, cell life and cell death. Curr. Pharm. Des. 12:2249-2270.
    • (2006) Curr. Pharm. Des , vol.12 , pp. 2249-2270
    • Shoshan-Barmatz, V.1    Israelson, A.2    Brdiczka, D.3    Sheu, S.S.4
  • 9
    • 33846207499 scopus 로고    scopus 로고
    • NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL
    • Malia, T. J., and G. Wagner. 2007. NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL. Biochemistry. 46:514-525.
    • (2007) Biochemistry , vol.46 , pp. 514-525
    • Malia, T.J.1    Wagner, G.2
  • 11
    • 0029776714 scopus 로고    scopus 로고
    • Circular dichroism studies of the mitochondrial channel, VDAC, from Neurospora crassa
    • Shao, L., K. W. Kinnally, and C. A. Mannella. 1996. Circular dichroism studies of the mitochondrial channel, VDAC, from Neurospora crassa. Biophys. J. 71:778-786.
    • (1996) Biophys. J , vol.71 , pp. 778-786
    • Shao, L.1    Kinnally, K.W.2    Mannella, C.A.3
  • 12
    • 0030937015 scopus 로고    scopus 로고
    • Study of structure and function of recombinant pea root plastid porin by biophysical methods
    • Popp, B., S. Gebauer, K. Fischer, U. I. Flügge, and R. Benz. 1997. Study of structure and function of recombinant pea root plastid porin by biophysical methods. Biochemistry. 36:2844-2852.
    • (1997) Biochemistry , vol.36 , pp. 2844-2852
    • Popp, B.1    Gebauer, S.2    Fischer, K.3    Flügge, U.I.4    Benz, R.5
  • 13
    • 0032577455 scopus 로고    scopus 로고
    • Bacterial expression and characterization of the mitochondrial outer membrane channel. Effects of N-terminal modi-fications
    • Koppel, D. A., K. W. Kinnally, P. Masters, M. Forte, E. Blachly-Dyson, and C. A. Mannella. 1998. Bacterial expression and characterization of the mitochondrial outer membrane channel. Effects of N-terminal modi-fications. J. Biol. Chem. 273:13794-13800.
    • (1998) J. Biol. Chem , vol.273 , pp. 13794-13800
    • Koppel, D.A.1    Kinnally, K.W.2    Masters, P.3    Forte, M.4    Blachly-Dyson, E.5    Mannella, C.A.6
  • 14
    • 0034468766 scopus 로고    scopus 로고
    • Functional characterization of the conserved "GLK" motif in mitochondrial porin from Neurospora crassa
    • Runke, G., E. Maier, J. D. O'Neil, R. Benz, and D. A. Court. 2000. Functional characterization of the conserved "GLK" motif in mitochondrial porin from Neurospora crassa. J. Bioenerg. Biomembr. 32:563-570.
    • (2000) J. Bioenerg. Biomembr , vol.32 , pp. 563-570
    • Runke, G.1    Maier, E.2    O'Neil, J.D.3    Benz, R.4    Court, D.A.5
  • 15
    • 0024513077 scopus 로고
    • Fusion of the mitochondrial outer membrane: Use in forming large, two-dimensional crystals of the voltage-dependent, anion-selective channel protein
    • Mannella, C. A. 1989. Fusion of the mitochondrial outer membrane: use in forming large, two-dimensional crystals of the voltage-dependent, anion-selective channel protein. Biochim. Biophys. Acta. 981:15-20.
    • (1989) Biochim. Biophys. Acta , vol.981 , pp. 15-20
    • Mannella, C.A.1
  • 16
    • 0025865152 scopus 로고
    • Surface topography and molecular stoichiometry of the mitochondrial channel, VDAC, in crystalline arrays
    • Thomas, L., E. Kocsis, M. Colombini, E. Erbe, B. L. Trus, and A. C. Steven. 1991. Surface topography and molecular stoichiometry of the mitochondrial channel, VDAC, in crystalline arrays. J. Struct. Biol. 106:161-171.
    • (1991) J. Struct. Biol , vol.106 , pp. 161-171
    • Thomas, L.1    Kocsis, E.2    Colombini, M.3    Erbe, E.4    Trus, B.L.5    Steven, A.C.6
  • 17
    • 0027459531 scopus 로고
    • Conformational change in the mitochondrial channel, VDAC, detected by electron cryo-microscopy
    • Guo, X. W., and C. A. Mannella. 1993. Conformational change in the mitochondrial channel, VDAC, detected by electron cryo-microscopy. Biophys. J. 64:545-549.
    • (1993) Biophys. J , vol.64 , pp. 545-549
    • Guo, X.W.1    Mannella, C.A.2
  • 18
    • 0032875663 scopus 로고    scopus 로고
    • Crystallization of the human, mitochondrial voltage-dependent anion-selective channel in the presence of phospholipids
    • Dolder, M., K. Zeth, P. Tittmann, H. Gross, W. Welte, and T. Wallimann. 1999. Crystallization of the human, mitochondrial voltage-dependent anion-selective channel in the presence of phospholipids. J. Struct. Biol. 127:64-71.
    • (1999) J. Struct. Biol , vol.127 , pp. 64-71
    • Dolder, M.1    Zeth, K.2    Tittmann, P.3    Gross, H.4    Welte, W.5    Wallimann, T.6
  • 19
    • 0033932639 scopus 로고    scopus 로고
    • β-Barrel membrane proteins
    • Schulz, G. E. 2000. β-Barrel membrane proteins. Curr. Opin. Struct. Biol. 10:443-447.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 443-447
    • Schulz, G.E.1
  • 20
    • 0036968479 scopus 로고    scopus 로고
    • Origami in the outer membrane: The transmembrane arrangement of mitochondrial porins
    • Bay, D. C., and D. A. Court. 2002. Origami in the outer membrane: the transmembrane arrangement of mitochondrial porins. Biochem. Cell Biol. 80:551-562.
    • (2002) Biochem. Cell Biol , vol.80 , pp. 551-562
    • Bay, D.C.1    Court, D.A.2
  • 21
    • 0018847077 scopus 로고
    • Structure and mode of action of a voltage dependent anion-selective channel (VDAC) located in the outer mitochondrial membrane
    • Colombini, M. 1980. Structure and mode of action of a voltage dependent anion-selective channel (VDAC) located in the outer mitochondrial membrane. Ann. N. Y. Acad. Sci. 341:552-563.
    • (1980) Ann. N. Y. Acad. Sci , vol.341 , pp. 552-563
    • Colombini, M.1
  • 22
    • 0020476642 scopus 로고
    • Identification and characterization of the pore-forming protein in the outer membrane of rat liver mitochondria
    • Roos, N., R. Benz, and D. Brdiczka. 1982. Identification and characterization of the pore-forming protein in the outer membrane of rat liver mitochondria. Biochim. Biophys. Acta. 686:204-214.
    • (1982) Biochim. Biophys. Acta , vol.686 , pp. 204-214
    • Roos, N.1    Benz, R.2    Brdiczka, D.3
  • 23
    • 0020485223 scopus 로고
    • Isolation of mitochondrial porin from Neurospora crassa
    • Freitag, H., G. Genchi, R. Benz, F. Palmieri, and W. Neupert. 1982. Isolation of mitochondrial porin from Neurospora crassa. FEBS Lett. 145:72-76.
    • (1982) FEBS Lett , vol.145 , pp. 72-76
    • Freitag, H.1    Genchi, G.2    Benz, R.3    Palmieri, F.4    Neupert, W.5
  • 27
    • 0025081330 scopus 로고
    • Refolding of an integral membrane protein. OmpA of Escherichia coli
    • Dornmair, K., H. Kiefer, and F. Jahnig. 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
  • 28
    • 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., K. Kameyama, and T. Takagi. 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
  • 29
    • 0035575842 scopus 로고    scopus 로고
    • Escherichia coli OmpA retains a folded structure in the presence of sodium dodecyl sulfate due to a high kinetic barrier to unfolding
    • Ohnishi, S., and K. Kameyama. 2001. Escherichia coli OmpA retains a folded structure in the presence of sodium dodecyl sulfate due to a high kinetic barrier to unfolding. Biochim. Biophys. Acta. 1515:159-166.
    • (2001) Biochim. Biophys. Acta , vol.1515 , pp. 159-166
    • Ohnishi, S.1    Kameyama, K.2
  • 30
    • 0041743087 scopus 로고    scopus 로고
    • Folding of DsbB in mixed micelles: A kinetic analysis of the stability of a bacterial membrane protein
    • Otzen, D. E. 2003. Folding of DsbB in mixed micelles: a kinetic analysis of the stability of a bacterial membrane protein. J. Mol. Biol. 330:641-649.
    • (2003) J. Mol. Biol , vol.330 , pp. 641-649
    • Otzen, D.E.1
  • 31
    • 0033082712 scopus 로고    scopus 로고
    • A method for the purification and refolding of a recombinant form of the nontypeable Haemophilus influenzae P5 outer membrane protein fused to polyhistidine
    • Webb, D. C., and A. W. Cripps. 1999. A method for the purification and refolding of a recombinant form of the nontypeable Haemophilus influenzae P5 outer membrane protein fused to polyhistidine. Protein Expr. Purif. 15:1-7.
    • (1999) Protein Expr. Purif , vol.15 , pp. 1-7
    • Webb, D.C.1    Cripps, A.W.2
  • 32
    • 0031010621 scopus 로고    scopus 로고
    • A method for assessing the stability of a membrane protein
    • Lau, F. W., and J. U. Bowie. 1997. A method for assessing the stability of a membrane protein. Biochemistry. 36:5884-5892.
    • (1997) Biochemistry , vol.36 , pp. 5884-5892
    • Lau, F.W.1    Bowie, J.U.2
  • 33
    • 0029920281 scopus 로고    scopus 로고
    • The role of the N and C termini of recombinant Neurospora mitochondrial porin in channel formation and voltage-dependent gating
    • Popp, B., D. A. Court, R. Benz, W. Neupert, and R. Lill. 1996. The role of the N and C termini of recombinant Neurospora mitochondrial porin in channel formation and voltage-dependent gating. J. Biol. Chem. 271:13593-13599.
    • (1996) J. Biol. Chem , vol.271 , pp. 13593-13599
    • Popp, B.1    Court, D.A.2    Benz, R.3    Neupert, W.4    Lill, R.5
  • 34
    • 0028785347 scopus 로고
    • Kinetics of folding and membrane insertion of a beta-barrel membrane protein
    • Surrey, T., and F. Jahnig. 1995. Kinetics of folding and membrane insertion of a beta-barrel membrane protein. J. Biol. Chem. 270:28199-28203.
    • (1995) J. Biol. Chem , vol.270 , pp. 28199-28203
    • Surrey, T.1    Jahnig, F.2
  • 35
    • 0018956403 scopus 로고
    • Pore size and properties of channels isolated from mitochondria isolated from Neurospora crassa
    • Colombini, M. 1980. Pore size and properties of channels isolated from mitochondria isolated from Neurospora crassa. J. Membr. Biol. 53: 79-84.
    • (1980) J. Membr. Biol , vol.53 , pp. 79-84
    • Colombini, M.1
  • 36
    • 4344691833 scopus 로고    scopus 로고
    • Highly efficient gene replacements in Neurospora strains deficient for nonhomologous end-joining
    • Ninomiya, Y., K. Suzuki, C. Ishii, and H. Inoue. 2004. Highly efficient gene replacements in Neurospora strains deficient for nonhomologous end-joining. Proc. Natl. Acad. Sci. USA. 101:12248-12253.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12248-12253
    • Ninomiya, Y.1    Suzuki, K.2    Ishii, C.3    Inoue, H.4
  • 37
    • 0028047616 scopus 로고
    • Inactivation of the Neurospora crassa gene encoding the mitochondrial protein import receptor MOM19 by the technique of "sheltered RIP
    • Harkness, T. A., R. L. Metzenberg, H. Schneider, R. Lill, W. Neupert, and F. E. Nargang. 1994. Inactivation of the Neurospora crassa gene encoding the mitochondrial protein import receptor MOM19 by the technique of "sheltered RIP". Genetics. 136:107-118.
    • (1994) Genetics , vol.136 , pp. 107-118
    • Harkness, T.A.1    Metzenberg, R.L.2    Schneider, H.3    Lill, R.4    Neupert, W.5    Nargang, F.E.6
  • 38
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 39
    • 0021759419 scopus 로고
    • Determination of tyrosine exposure in proteins by second-derivative spectroscopy
    • Ragone, R., G. Colonna, C. Balestrieri, L. Servillo, and G. Irace. 1984. Determination of tyrosine exposure in proteins by second-derivative spectroscopy. Biochemistry. 23:1871-1875.
    • (1984) Biochemistry , vol.23 , pp. 1871-1875
    • Ragone, R.1    Colonna, G.2    Balestrieri, C.3    Servillo, L.4    Irace, G.5
  • 40
    • 1542674158 scopus 로고    scopus 로고
    • Preparation of glycerol facilitator for protein structure and folding studies in solution
    • Manley, D., and J. D. O'Neil. 2003. Preparation of glycerol facilitator for protein structure and folding studies in solution. Methods Mol. Biol. 228:89-101.
    • (2003) Methods Mol. Biol , vol.228 , pp. 89-101
    • Manley, D.1    O'Neil, J.D.2
  • 41
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton, L. A., and W. C. Johnson, Jr. 1986. Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 155:155-167.
    • (1986) Anal. Biochem , vol.155 , pp. 155-167
    • Compton, L.A.1    Johnson Jr., W.C.2
  • 42
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra
    • Manavalan, P., and W. C. Johnson, Jr. 1987. Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167:76-85.
    • (1987) Anal. Biochem , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson Jr., W.C.2
  • 43
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis
    • Sreerama, N., S. Y. Venyaminov, and R. W. Woody. 2000. Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal. Biochem. 287:243-251.
    • (2000) Anal. Biochem , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 44
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L., and B. A. Wallace. 2004. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32:W668-W673.
    • (2004) Nucleic Acids Res , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 45
    • 33947324465 scopus 로고    scopus 로고
    • Correct folding of the beta-barrel of the human membrane protein VDAC requires a lipid bilayer
    • Shanmugavadivu, B., H. J. Apell, T. Meins, K. Zeth, and J. H. Kleinschmidt. 2007. Correct folding of the beta-barrel of the human membrane protein VDAC requires a lipid bilayer. J. Mol. Biol. 368:66-78.
    • (2007) J. Mol. Biol , vol.368 , pp. 66-78
    • Shanmugavadivu, B.1    Apell, H.J.2    Meins, T.3    Zeth, K.4    Kleinschmidt, J.H.5
  • 46
    • 0029822373 scopus 로고    scopus 로고
    • Folding intermediates of a beta-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism
    • Kleinschmidt, J. H., and L. K. Tamm. 1996. Folding intermediates of a beta-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism. Biochemistry. 35:12993-13000.
    • (1996) Biochemistry , vol.35 , pp. 12993-13000
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 47
    • 0020170385 scopus 로고
    • Biosynthesis of mitochondrial porin and insertion into the outer mitochondrial membrane of Neurospora crassa
    • Freitag, H., M. Janes, and W. Neupert. 1982. Biosynthesis of mitochondrial porin and insertion into the outer mitochondrial membrane of Neurospora crassa. Eur. J. Biochem. 126:197-202.
    • (1982) Eur. J. Biochem , vol.126 , pp. 197-202
    • Freitag, H.1    Janes, M.2    Neupert, W.3
  • 48
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein, E. A., N. S. Vedenkina, and M. N. Ivkova. 1973. Fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol. 18:263-279.
    • (1973) Photochem. Photobiol , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 49
    • 0034877118 scopus 로고    scopus 로고
    • Decomposition of protein tryptophan fluorescence spectra into log-normal components. III. Correlation between fluorescence and microenvironment parameters of individual tryptophan residues
    • Reshetnyak, Y. K., Y. Koshevnik, and E. A. Burstein. 2001. Decomposition of protein tryptophan fluorescence spectra into log-normal components. III. Correlation between fluorescence and microenvironment parameters of individual tryptophan residues. Biophys. J. 81:1735-1758.
    • (2001) Biophys. J , vol.81 , pp. 1735-1758
    • Reshetnyak, Y.K.1    Koshevnik, Y.2    Burstein, E.A.3
  • 50
    • 0034641678 scopus 로고    scopus 로고
    • In vitro reconstitution and biophysical characterization of OEP16, an outer envelope pore protein of pea chloroplasts
    • Linke, D., J. Frank, J. F. Holzwarth, J. Soll, C. Boettcher, and P. Fromme. 2000. In vitro reconstitution and biophysical characterization of OEP16, an outer envelope pore protein of pea chloroplasts. Biochemistry. 39:11050-11056.
    • (2000) Biochemistry , vol.39 , pp. 11050-11056
    • Linke, D.1    Frank, J.2    Holzwarth, J.F.3    Soll, J.4    Boettcher, C.5    Fromme, P.6
  • 51
    • 0036441481 scopus 로고    scopus 로고
    • Secondary and tertiary structure formation of the beta-barrel membrane protein OmpA is synchronized and depends on membrane thickness
    • Kleinschmidt, J. H., and L. K. Tamm. 2002. Secondary and tertiary structure formation of the beta-barrel membrane protein OmpA is synchronized and depends on membrane thickness. J. Mol. Biol. 324:319-330.
    • (2002) J. Mol. Biol , vol.324 , pp. 319-330
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 52
    • 28944441575 scopus 로고    scopus 로고
    • The major outer membrane protein of Fusobacterium nucleatum (FomA) folds and inserts into lipid bilayers via parallel folding pathways
    • Pocanschi, C. L., H. J. Apell, P. Puntervoll, B. Hogh, H. B. Jensen, W. Welte, and J. H. Kleinschmidt. 2006. The major outer membrane protein of Fusobacterium nucleatum (FomA) folds and inserts into lipid bilayers via parallel folding pathways. J. Mol. Biol. 355:548-561.
    • (2006) J. Mol. Biol , vol.355 , pp. 548-561
    • Pocanschi, C.L.1    Apell, H.J.2    Puntervoll, P.3    Hogh, B.4    Jensen, H.B.5    Welte, W.6    Kleinschmidt, J.H.7
  • 53
    • 0030888166 scopus 로고    scopus 로고
    • Structural and functional characterization of a recombinant PorB class 2 protein from Neisseria meningitidis. Conformational stability and porin activity
    • Minetti, C. A., J. Y. Tai, M. S. Blake, J. K. Pullen, S. M. Liang, and D. P. Remeta. 1997. Structural and functional characterization of a recombinant PorB class 2 protein from Neisseria meningitidis. Conformational stability and porin activity. J. Biol. Chem. 272:10710-10720.
    • (1997) J. Biol. Chem , vol.272 , pp. 10710-10720
    • Minetti, C.A.1    Tai, J.Y.2    Blake, M.S.3    Pullen, J.K.4    Liang, S.M.5    Remeta, D.P.6
  • 54
    • 0032566609 scopus 로고    scopus 로고
    • Characterization of the structure, function, and conformational stability of PorB class 3 protein from Neisseria meningitidis. A porin with unusual physicochemical properties
    • Minetti, C. A., M. S. Blake, and D. P. Remeta. 1998. Characterization of the structure, function, and conformational stability of PorB class 3 protein from Neisseria meningitidis. A porin with unusual physicochemical properties. J. Biol. Chem. 273:25329-25338.
    • (1998) J. Biol. Chem , vol.273 , pp. 25329-25338
    • Minetti, C.A.1    Blake, M.S.2    Remeta, D.P.3
  • 56
    • 0034468766 scopus 로고    scopus 로고
    • Functional characterization of the conserved "GLK" motif in mitochondrial porin from Neurospora crassa
    • Runke, G., E. Maier, J. D. O'Neil, R. Benz, and D. A. Court. 2000. Functional characterization of the conserved "GLK" motif in mitochondrial porin from Neurospora crassa. J. Bioenerg. Biomembr. 32:563-570.
    • (2000) J. Bioenerg. Biomembr , vol.32 , pp. 563-570
    • Runke, G.1    Maier, E.2    O'Neil, J.D.3    Benz, R.4    Court, D.A.5
  • 57
    • 0037024368 scopus 로고    scopus 로고
    • A 3D model of the voltage-dependent anion channel (VDAC)
    • Casadio, R., I. Jacoboni, A. Messina, and V. De Pinto. 2002. A 3D model of the voltage-dependent anion channel (VDAC). FEBS Lett. 520:1-7.
    • (2002) FEBS Lett , vol.520 , pp. 1-7
    • Casadio, R.1    Jacoboni, I.2    Messina, A.3    De Pinto, V.4
  • 58
    • 33646155114 scopus 로고    scopus 로고
    • Deletion variants of Neurospora mitochondrial porin: Electrophysiological and spectroscopic analysis
    • Runke, G., E. Maier, W. A. Summers, D. C. Bay, R. Benz, and D. A. Court. 2006. Deletion variants of Neurospora mitochondrial porin: electrophysiological and spectroscopic analysis. Biophys. J. 90:3155-3164.
    • (2006) Biophys. J , vol.90 , pp. 3155-3164
    • Runke, G.1    Maier, E.2    Summers, W.A.3    Bay, D.C.4    Benz, R.5    Court, D.A.6
  • 60
    • 0034604260 scopus 로고    scopus 로고
    • Circular dichroic investigation of the native and non-native conformational states of the growth factor receptor-binding protein 2 N-terminal src homology domain 3: Effect of binding to a proline-rich peptide from guanine nucleotide exchange factor
    • Bousquet, J. A., C. Garbay, B. P. Roques, and Y. Mely. 2000. Circular dichroic investigation of the native and non-native conformational states of the growth factor receptor-binding protein 2 N-terminal src homology domain 3: effect of binding to a proline-rich peptide from guanine nucleotide exchange factor. Biochemistry. 39:7722-7735.
    • (2000) Biochemistry , vol.39 , pp. 7722-7735
    • Bousquet, J.A.1    Garbay, C.2    Roques, B.P.3    Mely, Y.4
  • 62
    • 0031026889 scopus 로고    scopus 로고
    • Characterization of a partially structured state in an all-beta-sheet protein
    • Sivaraman, T., T. K. Kumar, G. Jayaraman, C. C. Han, and C. Yu. 1997. Characterization of a partially structured state in an all-beta-sheet protein. Biochem. J. 321:457-464.
    • (1997) Biochem. J , vol.321 , pp. 457-464
    • Sivaraman, T.1    Kumar, T.K.2    Jayaraman, G.3    Han, C.C.4    Yu, C.5
  • 63
    • 0035881236 scopus 로고    scopus 로고
    • Biophysical characterization of a soluble CD40 ligand (CD154) coiled-coil trimer: Evidence of a reversible acid-denatured molten globule
    • Matsuura, J. E., A. E. Morris, R. R. Ketchem, E. H. Braswell, R. Klinke, W. R. Gombotz, and R. L. Remmele, Jr. 2001. Biophysical characterization of a soluble CD40 ligand (CD154) coiled-coil trimer: evidence of a reversible acid-denatured molten globule. Arch. Biochem. Biophys. 392:208-218.
    • (2001) Arch. Biochem. Biophys , vol.392 , pp. 208-218
    • Matsuura, J.E.1    Morris, A.E.2    Ketchem, R.R.3    Braswell, E.H.4    Klinke, R.5    Gombotz, W.R.6    Remmele Jr., R.L.7
  • 64
    • 0029781028 scopus 로고    scopus 로고
    • Induction of alpha-helix in the beta-sheet protein tumor necrosis factor-alpha: Thermal- and trifluoroethanol-induced denaturation at neutral pH
    • Narhi, L. O., J. S. Philo, T. Li, M. Zhang, B. Samal, and T. Arakawa. 1996. Induction of alpha-helix in the beta-sheet protein tumor necrosis factor-alpha: thermal- and trifluoroethanol-induced denaturation at neutral pH. Biochemistry. 35:11447-11453.
    • (1996) Biochemistry , vol.35 , pp. 11447-11453
    • Narhi, L.O.1    Philo, J.S.2    Li, T.3    Zhang, M.4    Samal, B.5    Arakawa, T.6
  • 65
    • 14244269224 scopus 로고    scopus 로고
    • Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria
    • Zalk, R., A. Israelson, E. S. Garty, H. Azoulay-Zohar, and V. Shoshan-Barmatz. 2005. Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria. Biochem. J. 386:73-83.
    • (2005) Biochem. J , vol.386 , pp. 73-83
    • Zalk, R.1    Israelson, A.2    Garty, E.S.3    Azoulay-Zohar, H.4    Shoshan-Barmatz, V.5
  • 66
    • 33749238923 scopus 로고    scopus 로고
    • Hunting interactomes of a membrane protein: Obtaining the largest set of VDAC-interacting protein epitopes
    • Roman, I., J. Figys, G. Steurs, and M. Zizi. 2006. Hunting interactomes of a membrane protein: obtaining the largest set of VDAC-interacting protein epitopes. Mol. Cell. Proteomics. 9:1667-1680.
    • (2006) Mol. Cell. Proteomics , vol.9 , pp. 1667-1680
    • Roman, I.1    Figys, J.2    Steurs, G.3    Zizi, M.4
  • 67
    • 0024347661 scopus 로고
    • Interaction of non-classical detergents with the mitochondrial porin. A new purification procedure and characterization of the pore-forming unit
    • De Pinto, V., R. Benz, and F. Palmieri. 1989. Interaction of non-classical detergents with the mitochondrial porin. A new purification procedure and characterization of the pore-forming unit. Eur. J. Biochem. 183:179-187.
    • (1989) Eur. J. Biochem , vol.183 , pp. 179-187
    • De Pinto, V.1    Benz, R.2    Palmieri, F.3
  • 68
    • 0035066331 scopus 로고    scopus 로고
    • Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
    • Arora, A., F. Abildgaard, J. H. Bushweller, and L. K. Tamm. 2001. Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nat. Struct. Biol. 8:334-338.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 334-338
    • Arora, A.1    Abildgaard, F.2    Bushweller, J.H.3    Tamm, L.K.4
  • 69
    • 0035979788 scopus 로고    scopus 로고
    • Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli
    • Fernández, C., C. Hilty, S. Bonjour, K. Adeishvili, K. Pervushin, and K. Wüthrich. 2001. Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli. FEBS Lett. 504:173-178.
    • (2001) FEBS Lett , vol.504 , pp. 173-178
    • Fernández, C.1    Hilty, C.2    Bonjour, S.3    Adeishvili, K.4    Pervushin, K.5    Wüthrich, K.6
  • 70
    • 0035956956 scopus 로고    scopus 로고
    • Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles
    • Fernández, C., K. Adeishvili, and K. Wüthrich. 2001. Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles. Proc. Natl. Acad. Sci. USA. 98:2358-2363.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2358-2363
    • Fernández, C.1    Adeishvili, K.2    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.