메뉴 건너뛰기




Volumn 293, Issue 2, 1999, Pages 367-379

A day in the life of Dr K. or how I learned to stop worrying and love lysozyme: A tragedy in six acts

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 0032744963     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2998     Document Type: Article
Times cited : (26)

References (79)
  • 1
    • 0029557910 scopus 로고
    • Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban
    • Adams P. D., Arkin I. T., Engelman D. M., Brünger A. T. Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban. Nature Struct. Biol. 2:1995;154-162.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 154-162
    • Adams, P.D.1    Arkin, I.T.2    Engelman, D.M.3    Brünger, A.T.4
  • 2
    • 0029847652 scopus 로고    scopus 로고
    • Improved prediction for the structure of a dimeric transmembrane domain of glycophorin A obtained through global searching
    • Adams P., Engelman D., Brünger A. Improved prediction for the structure of a dimeric transmembrane domain of glycophorin A obtained through global searching. Proteins: Struct. Funct. Genet. 26:1996;257-261.
    • (1996) Proteins: Struct. Funct. Genet. , vol.26 , pp. 257-261
    • Adams, P.1    Engelman, D.2    Brünger, A.3
  • 3
    • 0023395661 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The protein subunits
    • Allen J., Feher G., Yeates T., Komiya H., Rees D. Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits. Proc. Natl Acad. Sci. USA. 84:1987;6162-6166.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 6162-6166
    • Allen, J.1    Feher, G.2    Yeates, T.3    Komiya, H.4    Rees, D.5
  • 5
    • 0032006712 scopus 로고    scopus 로고
    • The role of the ribosome-translocon complex in translation and assembly of polytopic membrane proteins
    • Bibi E. The role of the ribosome-translocon complex in translation and assembly of polytopic membrane proteins. Trends Biochem. Sci. 23:1998;51-55.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 51-55
    • Bibi, E.1
  • 6
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang G., Spencer R., Lee A., Barclay M., Rees D. Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science. 282:1998;2220-2226.
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.2    Lee, A.3    Barclay, M.4    Rees, D.5
  • 7
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure prediction
    • Claros M. G., von Heijne G. TopPred II: an improved software for membrane protein structure prediction. CABIOS. 10:1994;685-686.
    • (1994) CABIOS , vol.10 , pp. 685-686
    • Claros, M.G.1    Von Heijne, G.2
  • 9
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • Crowley K. S., Liao S. R., Worrell V. E., Reinhart G. D., Johnson A. E. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell. 78:1994;461-471.
    • (1994) Cell , vol.78 , pp. 461-471
    • Crowley, K.S.1    Liao, S.R.2    Worrell, V.E.3    Reinhart, G.D.4    Johnson, A.E.5
  • 10
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane α-helices in prokaryotic membrane proteins: The dense alignment surface method
    • Cserzö M., Wallin E., Simon I., von Heijne G., Elofsson A. Prediction of transmembrane α-helices in prokaryotic membrane proteins: the dense alignment surface method. Protein Eng. 10:1997;673-676.
    • (1997) Protein Eng. , vol.10 , pp. 673-676
    • Cserzö, M.1    Wallin, E.2    Simon, I.3    Von Heijne, G.4    Elofsson, A.5
  • 12
    • 0032430831 scopus 로고    scopus 로고
    • Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli
    • de Gier J.-W. L., Scotti P. A., Sääf A., Valent Q. A., Kuhn A., Luirink J., von Heijne G. Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli. Proc. Natl Acad. Sci. USA. 95:1998;14646-14651.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14646-14651
    • De Gier, J.-W.L.1    Scotti, P.A.2    Sääf, A.3    Valent, Q.A.4    Kuhn, A.5    Luirink, J.6    Von Heijne, G.7
  • 13
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution
    • Deisenhofer J., Epp O., Miki K., Huber R., Michel H. Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution. Nature. 318:1985;618-624.
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 14
    • 0342995731 scopus 로고    scopus 로고
    • The cotransational integration of membrane proteins into the phospholipid bilayer is a multistep process
    • Do H., Falcone D., Lin J., Andrews D. W., Johnson A. E. The cotransational integration of membrane proteins into the phospholipid bilayer is a multistep process. Cell. 85:1996;369-378.
    • (1996) Cell , vol.85 , pp. 369-378
    • Do, H.1    Falcone, D.2    Lin, J.3    Andrews, D.W.4    Johnson, A.E.5
  • 16
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • Essen L. O., Siegert R., Lehmannn W. D., Oesterhelt D. Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex. Proc. Natl Acad. Sci. USA. 95:1998;11673-11678.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 11673-11678
    • Essen, L.O.1    Siegert, R.2    Lehmannn, W.D.3    Oesterhelt, D.4
  • 17
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport; Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson A., Hofmann E., Coulton J., Diedrichs K., Welte W. Siderophore-mediated iron transport; crystal structure of FhuA with bound lipopolysaccharide. Science. 282:1998;2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.1    Hofmann, E.2    Coulton, J.3    Diedrichs, K.4    Welte, W.5
  • 18
    • 0030460146 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae mitochondria lack a bacterial-type Sec machinery
    • Glick B. S., von Heijne G. Saccharomyces cerevisiae mitochondria lack a bacterial-type Sec machinery. Protein Sci. 5:1996;2651-2652.
    • (1996) Protein Sci. , vol.5 , pp. 2651-2652
    • Glick, B.S.1    Von Heijne, G.2
  • 20
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • Grisshammer R., Tate C. G. Overexpression of integral membrane proteins for structural studies. Quart. Rev. Biophys. 28:1995;315-422.
    • (1995) Quart. Rev. Biophys. , vol.28 , pp. 315-422
    • Grisshammer, R.1    Tate, C.G.2
  • 21
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman B. D., Hendershot L. M., Johnson A. E. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell. 92:1998;747-758.
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 23
    • 0029082813 scopus 로고
    • The projection structure of microsomal glutathione transferase
    • Hebert H., Schmidtkrey I., Morgenstern R. The projection structure of microsomal glutathione transferase. EMBO J. 14:1995;3864-3869.
    • (1995) EMBO J. , vol.14 , pp. 3864-3869
    • Hebert, H.1    Schmidtkrey, I.2    Morgenstern, R.3
  • 24
    • 0032478139 scopus 로고    scopus 로고
    • Oxa1p, an essential component of the N-tail protein export machinery in mitochondria
    • Hell K., Herrmann J. M., Pratje E., Neupert W., Stuart R. A. Oxa1p, an essential component of the N-tail protein export machinery in mitochondria. Proc. Natl Acad. Sci. USA. 95:1998;2250-2255.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 2250-2255
    • Hell, K.1    Herrmann, J.M.2    Pratje, E.3    Neupert, W.4    Stuart, R.A.5
  • 25
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R., Unwin P. N. T. Three-dimensional model of purple membrane obtained by electron microscopy. Nature. 257:1975;28-32.
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 26
    • 0025292355 scopus 로고
    • A model for the structure of bacteriorhodopsin based on high resolution electron cryo-microscopy
    • Henderson R., Baldwin J. M., Ceska T. A., Zemlin F., Beckmann E., Downing K. H. A model for the structure of bacteriorhodopsin based on high resolution electron cryo-microscopy. J. Mol. Biol. 213:1990;899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 27
    • 0028890031 scopus 로고
    • Structure at 2. 8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2. 8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:1995;660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 29
    • 77956817521 scopus 로고    scopus 로고
    • The lactose permease of Escherichia coli: Past, present, and future
    • W. N. Konings, H. R. Kaback, & J. S. Lolkema. Amsterdam: Elsevier
    • Kaback H. R. The lactose permease of Escherichia coli: past, present, and future. Konings W. N., Kaback H. R., Lolkema J. S. Handbook of Biophysics: Transport Processes in Eukaryotic and Prokaryotic Organisms. 1996;203-227 Elsevier, Amsterdam.
    • (1996) Handbook of Biophysics: Transport Processes in Eukaryotic and Prokaryotic Organisms , pp. 203-227
    • Kaback, H.R.1
  • 31
    • 0021847027 scopus 로고
    • The detection and classification of membrane-spanning proteins
    • Klein P., Kanehisa M., DeLisi C. The detection and classification of membrane-spanning proteins. Biochim. Biophys. Acta. 815:1985;468-476.
    • (1985) Biochim. Biophys. Acta , vol.815 , pp. 468-476
    • Klein, P.1    Kanehisa, M.2    Delisi, C.3
  • 33
    • 0032536045 scopus 로고    scopus 로고
    • Import of mitochondrial carriers mediated by essential proteins of the intermembrane space
    • Koehler C. M., Jarosch E., Tokatlidis K., Schmid K., Schweyen R. J., Schatz G. Import of mitochondrial carriers mediated by essential proteins of the intermembrane space. Science. 279:1998b;369-373.
    • (1998) Science , vol.279 , pp. 369-373
    • Koehler, C.M.1    Jarosch, E.2    Tokatlidis, K.3    Schmid, K.4    Schweyen, R.J.5    Schatz, G.6
  • 34
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 35
    • 0028140564 scopus 로고
    • Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution
    • Kreusch A., Neubuser A., Schiltz E., Weckesser J., Schulz G. E. Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution. Protein Sci. 3:1994;58-63.
    • (1994) Protein Sci. , vol.3 , pp. 58-63
    • Kreusch, A.1    Neubuser, A.2    Schiltz, E.3    Weckesser, J.4    Schulz, G.E.5
  • 36
    • 0025898707 scopus 로고
    • Three-dimensional structure of plant light-harvesting complex determined by electron crystallography
    • Kühlbrandt W., Wang D. N. Three-dimensional structure of plant light-harvesting complex determined by electron crystallography. Nature. 350:1991;130-134.
    • (1991) Nature , vol.350 , pp. 130-134
    • Kühlbrandt, W.1    Wang, D.N.2
  • 37
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt W., Wang D. N., Fujiyoshi Y. Atomic model of plant light-harvesting complex by electron crystallography. Nature. 367:1994;614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 39
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao S., Lin J., Do H., Johnson A. Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell. 90:1997;31-41.
    • (1997) Cell , vol.90 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.4
  • 40
    • 0032481104 scopus 로고    scopus 로고
    • The univector plasmid-fusion system, a method for rapid construction of recombinant DNA without restriction enzymes
    • Liu Q., Li M. Z., Leibham D., Cortez D., Elledge S. J. The univector plasmid-fusion system, a method for rapid construction of recombinant DNA without restriction enzymes. Curr. Biol. 8:1998;1300-1309.
    • (1998) Curr. Biol. , vol.8 , pp. 1300-1309
    • Liu, Q.1    Li, M.Z.2    Leibham, D.3    Cortez, D.4    Elledge, S.J.5
  • 41
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal aloosteric changes
    • Locher K., Rees B., Koebnik R., Mitschler A., Moulinier L., Rosenbusch J., Moras D. Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal aloosteric changes. Cell. 95:1998;771-778.
    • (1998) Cell , vol.95 , pp. 771-778
    • Locher, K.1    Rees, B.2    Koebnik, R.3    Mitschler, A.4    Moulinier, L.5    Rosenbusch, J.6    Moras, D.7
  • 42
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
    • Luecke H., Richter H., Lanyi J. Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution. Science. 280:1998;1934-1937.
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.2    Lanyi, J.3
  • 43
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie K. R., Prestegard J. H., Engelman D. M. A transmembrane helix dimer: structure and implications. Science. 276:1997;131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 44
    • 0025095225 scopus 로고
    • Alkaline phosphatase fusions - sensors of subcellular location
    • Manoil C., Mekalanos J. J., Beckwith J. Alkaline phosphatase fusions - sensors of subcellular location. J. Bacteriol. 172:1990;515-518.
    • (1990) J. Bacteriol. , vol.172 , pp. 515-518
    • Manoil, C.1    Mekalanos, J.J.2    Beckwith, J.3
  • 46
    • 0031557404 scopus 로고    scopus 로고
    • Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside
    • Meyer J., Hofnung M., Schulz G. Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J. Mol. Biol. 266:1997;761-775.
    • (1997) J. Mol. Biol. , vol.266 , pp. 761-775
    • Meyer, J.1    Hofnung, M.2    Schulz, G.3
  • 47
    • 0345196631 scopus 로고    scopus 로고
    • The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex
    • Meyer T. H., Menetret J. F., Breitling R., Miller K. R., Akey C. W., Rapoport T. A. The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex. J. Mol. Biol. 285:1999;1789-1800.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1789-1800
    • Meyer, T.H.1    Menetret, J.F.2    Breitling, R.3    Miller, K.R.4    Akey, C.W.5    Rapoport, T.A.6
  • 48
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., Walker J. E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260:1996;289-298.
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 49
    • 0032509124 scopus 로고    scopus 로고
    • Positively and negatively charged residues have different effects on the position in the membrane of a model transmembrane helix
    • Monné M., Nilsson I., Johansson M., Elmhed N., von Heijne G. Positively and negatively charged residues have different effects on the position in the membrane of a model transmembrane helix. J. Mol. Biol. 284:1998;1177-1183.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1177-1183
    • Monné, M.1    Nilsson, I.2    Johansson, M.3    Elmhed, N.4    Von Heijne, G.5
  • 50
    • 0033597281 scopus 로고    scopus 로고
    • A turn propensity scale for transmembrane helices
    • Monné M., Hermansson M., von Heijne G. A turn propensity scale for transmembrane helices. J. Mol. Biol. 288:1999;141-145.
    • (1999) J. Mol. Biol. , vol.288 , pp. 141-145
    • Monné, M.1    Hermansson, M.2    Von Heijne, G.3
  • 52
    • 0032509153 scopus 로고    scopus 로고
    • Breaking the camel's back: Proline-induced turns in a model transmembrane helix
    • Nilsson I., von Heijne G. Breaking the camel's back: proline-induced turns in a model transmembrane helix. J. Mol. Biol. 284:1998;1185-1189.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1185-1189
    • Nilsson, I.1    Von Heijne, G.2
  • 53
  • 54
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • Pautsch A., Schulz G. E. Structure of the outer membrane protein A transmembrane domain. Nature Struct. Biol. 5:1998;1013-1017.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 55
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 Å from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula E., Rummel G., Rosenbusch J., Landau E. X-ray structure of bacteriorhodopsin at 2.5 Å from microcrystals grown in lipidic cubic phases. Science. 277:1997;1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.3    Landau, E.4
  • 56
    • 0030020734 scopus 로고    scopus 로고
    • Topology prediction of membrane proteins
    • Persson B., Argos P. Topology prediction of membrane proteins. Protein Sci. 5:1996;363-371.
    • (1996) Protein Sci. , vol.5 , pp. 363-371
    • Persson, B.1    Argos, P.2
  • 58
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport T. A., Jungnickel B., Kutay U. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65:1996;271-303.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 59
    • 0030038634 scopus 로고    scopus 로고
    • Topology prediction for helical transmembrane proteins at 86 % accuracy
    • Rost B., Fariselli P., Casadio R. Topology prediction for helical transmembrane proteins at 86 % accuracy. Protein Sci. 5:1996;1704-1718.
    • (1996) Protein Sci. , vol.5 , pp. 1704-1718
    • Rost, B.1    Fariselli, P.2    Casadio, R.3
  • 60
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: A measure of transmembrane helix association in a biological membrane
    • Russ W. P., Engelman D. M. TOXCAT: a measure of transmembrane helix association in a biological membrane. Proc. Natl Acad. Sci. USA. 96:1999;863-868.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 61
    • 0032515148 scopus 로고    scopus 로고
    • Membrane topology of the 60-kDa Oxalp homologue from Escherichia coli
    • Sääf A., Monné M., de Gier J. W., von Heijne G. Membrane topology of the 60-kDa Oxalp homologue from Escherichia coli. J. Biol. Chem. 273:1998;30415-30418.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30415-30418
    • Sääf, A.1    Monné, M.2    De Gier, J.W.3    Von Heijne, G.4
  • 62
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 angstrom resolution
    • Schirmer T., Keller T. A., Wang Y. F., Rosenbusch J. P. Structural basis for sugar translocation through maltoporin channels at 3.1 angstrom resolution. Science. 267:1995;512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbusch, J.P.4
  • 63
    • 0032568029 scopus 로고    scopus 로고
    • Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5
    • Sirrenberg C., Endres M., Folsch H., Stuart R. A., Neupert W., Brunner M. Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5. Nature. 391:1998;912-915.
    • (1998) Nature , vol.391 , pp. 912-915
    • Sirrenberg, C.1    Endres, M.2    Folsch, H.3    Stuart, R.A.4    Neupert, W.5    Brunner, M.6
  • 64
    • 0031614678 scopus 로고    scopus 로고
    • A hidden Markov model for predicting transmembrane helices in protein sequences
    • Sonnhammer E., von Heijne G., Krogh A. A hidden Markov model for predicting transmembrane helices in protein sequences. Intell. Syst. Mol. Biol. 6:1998;175-182.
    • (1998) Intell. Syst. Mol. Biol. , vol.6 , pp. 175-182
    • Sonnhammer, E.1    Von Heijne, G.2    Krogh, A.3
  • 65
    • 0032509302 scopus 로고    scopus 로고
    • Science. 282:1998;2012-2018.
    • (1998) Science , vol.282 , pp. 2012-2018
  • 67
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: Application to topology prediction
    • Tusnady G. E., Simon I. Principles governing amino acid composition of integral membrane proteins: application to topology prediction. J. Mol. Biol. 283:1998;489-506.
    • (1998) J. Mol. Biol. , vol.283 , pp. 489-506
    • Tusnady, G.E.1    Simon, I.2
  • 68
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 Å resolution
    • Unwin N. Nicotinic acetylcholine receptor at 9 Å resolution. J. Mol. Biol. 229:1993;1101-1124.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 69
    • 0033613965 scopus 로고    scopus 로고
    • Insertion of a bacterial secondary transport protein in the endoplasmic reticulum membrane
    • van Geest M., Nilsson I., von Heijne G., Lolkema J. S. Insertion of a bacterial secondary transport protein in the endoplasmic reticulum membrane. J. Biol. Chem. 274:1999;2816-2823.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2816-2823
    • Van Geest, M.1    Nilsson, I.2    Von Heijne, G.3    Lolkema, J.S.4
  • 70
    • 0030431744 scopus 로고    scopus 로고
    • Principles of membrane protein assembly and structure
    • von Heijne G. Principles of membrane protein assembly and structure. Prog. Biophys. Mol. Biol. 66:1996;113-139.
    • (1996) Prog. Biophys. Mol. Biol. , vol.66 , pp. 113-139
    • Von Heijne, G.1
  • 71
    • 0030681217 scopus 로고    scopus 로고
    • Site-directed spin-labeling of transmembrane domain VII and the 4B1 antibody epitope in the lactose permease of Escherichia coli
    • Voss J., Hubbell W. L., HernandezBorrell J., Kaback H. R. Site-directed spin-labeling of transmembrane domain VII and the 4B1 antibody epitope in the lactose permease of Escherichia coli. Biochemistry. 36:1997;15055-15061.
    • (1997) Biochemistry , vol.36 , pp. 15055-15061
    • Voss, J.1    Hubbell, W.L.2    Hernandezborrell, J.3    Kaback, H.R.4
  • 72
    • 0033537639 scopus 로고    scopus 로고
    • Helix packing in the lactose permease of Escherichia coli determined by site-directed thiol cross-linking: Helix I is close to helices V and XI
    • Wang Q. D., Kaback H. R. Helix packing in the lactose permease of Escherichia coli determined by site-directed thiol cross-linking: helix I is close to helices V and XI. Biochem. USA. 38:1999;3120-3126.
    • (1999) Biochem. USA , vol.38 , pp. 3120-3126
    • Wang, Q.D.1    Kaback, H.R.2
  • 73
    • 0031565721 scopus 로고    scopus 로고
    • Channel specificity: Structural basis for sugar discrimination and differential flux rates in maltoporin
    • Wang Y.-F., Dutzler R., Rizkallah P., Rosenbusch J., Schirmer T. Channel specificity: structural basis for sugar discrimination and differential flux rates in maltoporin. J. Mol. Biol. 272:1997;56-63.
    • (1997) J. Mol. Biol. , vol.272 , pp. 56-63
    • Wang, Y.-F.1    Dutzler, R.2    Rizkallah, P.3    Rosenbusch, J.4    Schirmer, T.5
  • 74
    • 0026331041 scopus 로고
    • Molecular architecture and electrostatic properties of a bacterial porin
    • Weiss M. S., Abele U., Weckesser J., Welte W., Schiltz E., Schulz G. E. Molecular architecture and electrostatic properties of a bacterial porin. Science. 254:1991a;1627-1630.
    • (1991) Science , vol.254 , pp. 1627-1630
    • Weiss, M.S.1    Abele, U.2    Weckesser, J.3    Welte, W.4    Schiltz, E.5    Schulz, G.E.6
  • 76
    • 0030025319 scopus 로고    scopus 로고
    • Exploring the allowed sequence space of a membrane protein
    • Wen J. A., Chen X., Bowie J. U. Exploring the allowed sequence space of a membrane protein. Nature Struct. Biol. 3:1996;141-148.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 141-148
    • Wen, J.A.1    Chen, X.2    Bowie, J.U.3
  • 77
    • 0033010801 scopus 로고    scopus 로고
    • Site-directed chemical cross-linking demonstrates that helix IV is close to helices VII and XI in the lactose permease
    • Wu J. H., Hardy D., Kaback H. R. Site-directed chemical cross-linking demonstrates that helix IV is close to helices VII and XI in the lactose permease. Biochem. USA. 38:1999;1715-1720.
    • (1999) Biochem. USA , vol.38 , pp. 1715-1720
    • Wu, J.H.1    Hardy, D.2    Kaback, H.R.3
  • 78
    • 0023410587 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides: Membrane-protein interactions
    • Yeates T. O., Komiya H., Rees D. C., Allen J. P., Feher G. Structure of the reaction center from Rhodobacter sphaeroides: membrane-protein interactions. Proc. Natl Acad. Sci. USA. 84:1987;6438-6442.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 6438-6442
    • Yeates, T.O.1    Komiya, H.2    Rees, D.C.3    Allen, J.P.4    Feher, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.