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1
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0029647451
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2O channel, AQP-CHIP, in projection at 3.5 Å resolution
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2O channel, AQP-CHIP, in projection at 3.5 Å resolution. J Mol Biol. 251:1995;413-420.
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J Mol Biol
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Jap, B.K.1
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2
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0029645574
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The structure of OmpF porin in a tetragonal crystal form
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of special interest. The structure of the first crystal form of an integral membrane protein that permitted an X-ray structure analysis.
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of special interest Cowan SW, Garavito RM, Jansonius JN, Jenkins JA, Karlsson R, König N, Pai EF, Pauptit RA, Rizkallah PJ, Rosenbusch JP, et al. The structure of OmpF porin in a tetragonal crystal form. Structure. 3:1995;1041-1050 The structure of the first crystal form of an integral membrane protein that permitted an X-ray structure analysis.
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Cowan, S.W.1
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Rizkallah, P.J.9
Rosenbusch, J.P.10
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3
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0025345316
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The three-dimensional structure of porin from Rhodobacter capsulatus at 3 Å resolution
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Weiss MS, Wacker T, Weckesser J, Welte W, Schulz GE. The three-dimensional structure of porin from Rhodobacter capsulatus at 3 Å resolution. FEBS Lett. 267:1990;268-272.
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Weiss, M.S.1
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Schulz, G.E.5
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4
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0026779245
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Crystal structures explain functional properties of two E. coli porins
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Cowan SW, Schirmer T, Rummel G, Steiert M, Ghosh R, Pauptit RA, Jansonius JN, Rosenbusch JP. Crystal structures explain functional properties of two E. coli porins. Nature. 358:1992;727-733.
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Cowan, S.W.1
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Jansonius, J.N.7
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5
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0028140564
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The structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution
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Kreusch A, Neubüser A, Schiltz E, Weckesser J, Schulz GE. The structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution. Protein Sci. 3:1994;58-63.
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Protein Sci
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Kreusch, A.1
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Schulz, G.E.5
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6
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0028153088
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Refined structure of the porin from Rhodopseudomonas blastica and comparison with the porin from Rhodobacter capsulatus
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Kreusch A, Schulz GE. Refined structure of the porin from Rhodopseudomonas blastica and comparison with the porin from Rhodobacter capsulatus. J Mol Biol. 243:1994;891-905.
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Kreusch, A.1
Schulz, G.E.2
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7
-
-
0028946962
-
Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
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of outstanding interest. The first structure elucidation of a `specific' porin showed a very narrow channel, just wide a enough for a malto-oligosaccharide.
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of outstanding interest Schirmer T, Keller TA, Wang YF, Rosenbusch JP. Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science. 267:1995;512-514 The first structure elucidation of a `specific' porin showed a very narrow channel, just wide a enough for a malto-oligosaccharide.
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Science
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Schirmer, T.1
Keller, T.A.2
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Rosenbusch, J.P.4
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8
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-
0029644059
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Crystal structures of various maltooligosacharides bound to maltoporin reveal a specific sugar translocation pathway
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of special interest. The binding mode of malto-oligosaccharides stuck in the channel eyelet is shown in detail.
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of special interest Dutzler R, Wang YF, Rizkallah PJ, Rosenbusch JP, Schirmer T. Crystal structures of various maltooligosacharides bound to maltoporin reveal a specific sugar translocation pathway. Structure. 4:1996;127-134 The binding mode of malto-oligosaccharides stuck in the channel eyelet is shown in detail.
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Dutzler, R.1
Wang, Y.F.2
Rizkallah, P.J.3
Rosenbusch, J.P.4
Schirmer, T.5
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10
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56349117812
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The porin superfamily: Diversity and common features
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J.M. Ghuysen, Hakenbeck R. Amsterdam: Elsevier
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Jeanteur D, Lakey JH, Pattus F. The porin superfamily: diversity and common features. Ghuysen JM, Hakenbeck R. Bacterial Cell Wall. 1994;363-380 Elsevier, Amsterdam.
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Bacterial Cell Wall
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Jeanteur, D.1
Lakey, J.H.2
Pattus, F.3
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0028351141
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On the structure of mitochondrial porins and its homologies with bacterial porins
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Rauch G, Moran O. On the structure of mitochondrial porins and its homologies with bacterial porins. Biochem Biophys Res Commun. 200:1994;908-915.
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Biochem Biophys Res Commun
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Rauch, G.1
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12
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0027392414
-
Purification and characterization of protein H, the major porin of Pasteurella multocida
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Chevalier G, Duchlohier H, Thomas D, Schechter E, Wroblewski H. Purification and characterization of protein H, the major porin of Pasteurella multocida. J Bacteriol. 175:1993;266-276.
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Chevalier, G.1
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Thomas, D.3
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Wroblewski, H.5
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13
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0029069967
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Porin activity and sequence analysis of a 31-kilodalton Treponema pallidum subsp. pallidum rare outer membrane protein (Tromp1)
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Blanco DR, Champion CI, Exner MM, Erdjument-Bromage H, Hancock REW, Tempst P, Miller JN, Lovett MA. Porin activity and sequence analysis of a 31-kilodalton Treponema pallidum subsp. pallidum rare outer membrane protein (Tromp1). J Bacteriol. 177:1995;3556-3562.
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Blanco, D.R.1
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Miller, J.N.7
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14
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0028822012
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The Fusobacterium nucleatum major outer-membrane protein (FomA) forms trimeric, water-filled channels in lipid bilayer membranes
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Kleivdal H, Benz R, Jensen HB. The Fusobacterium nucleatum major outer-membrane protein (FomA) forms trimeric, water-filled channels in lipid bilayer membranes. Eur J Biochem. 233:1995;310-316.
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Kleivdal, H.1
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15
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0029101289
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Membrane topology and site-specific mutangenesis of Pseudomonas aeruginosa porin OprD
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Huang H, Jeanteur D, Pattus F, Hancock REW. Membrane topology and site-specific mutangenesis of Pseudomonas aeruginosa porin OprD. Mol Microbiol. 16:1995;931-941.
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Huang, H.1
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Hancock, R.E.W.4
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16
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0028345036
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Cloning and nucleotide sequence of the Pseudomonas aeruginosa glucose-selective OprB porin gene and distribution of OprB within the family of Pseudomonadaceae
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Wylie JL, Worobec EA. Cloning and nucleotide sequence of the Pseudomonas aeruginosa glucose-selective OprB porin gene and distribution of OprB within the family of Pseudomonadaceae. Eur J Biochem. 220:1994;505-512.
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Wylie, J.L.1
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17
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0027471832
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Crystallization and preliminary X-ray diffraction analysis of SrcY, a specific bacterial outer membrane porin
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Forst D, Schülen K, Wacker T, Diederichs K, Kreutz W, Benz R, Welte W. Crystallization and preliminary X-ray diffraction analysis of SrcY, a specific bacterial outer membrane porin. J Mol Biol. 229:1993;258-262.
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Forst, D.1
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Diederichs, K.4
Kreutz, W.5
Benz, R.6
Welte, W.7
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18
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0027959128
-
A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis
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Klebba PE, Hofnung M, Charbit A. A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis. EMBO J. 13:1994;4670-4675.
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Klebba, P.E.1
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19
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0028815284
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Forces and factors that contribute to the structural stability of membrane proteins
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Haltia T, Freire E. Forces and factors that contribute to the structural stability of membrane proteins. Biochim Biophys Acta. 1228:1995;1-27.
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Biochim Biophys Acta
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Haltia, T.1
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20
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0029124070
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Transbilayer pores formed by β-barrels, molecular modeling of pore structures and properties
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Sansom MSP, Kerr ID. Transbilayer pores formed by β-barrels, molecular modeling of pore structures and properties. Biophys J. 69:1995;1334-1343.
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Sansom, M.S.P.1
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21
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0026737314
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Structure of porin refined at 1.8 Å resolution
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Weiss MS, Schulz GE. Structure of porin refined at 1.8 Å resolution. J Mol Biol. 227:1992;493-509.
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Weiss, M.S.1
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0000589242
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Structure - Function relationships in the membrane channel porin
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of special interest. Dalbey R.E. JAI Press Greenwich, Connecticut. Several hypotheses on porin function, electrostatic properties, stability and folding are presented, all of them based on the known structures.
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of special interest Schulz GE. Structure - function relationships in the membrane channel porin. Dalbey RE. Advances in Cell and Molecular Biology of Membranes and Organelles. 4:1995;175-187 JAI Press, Greenwich, Connecticut, Several hypotheses on porin function, electrostatic properties, stability and folding are presented, all of them based on the known structures.
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Advances in Cell and Molecular Biology of Membranes and Organelles
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Schulz, G.E.1
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23
-
-
0029645582
-
Detergent structure in tetragonal crystals of OmpF porin
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of special interest. Structures or distributions of detergents in crystals can be determined by deuteration and neutron diffraction if the X-ray structure of the protein is known ([2] in this case). Such analyses are very rare.
-
of special interest Pebaypeyroula E, Garavito RM, Rosenbusch JP, Zulauf M, Timmins PA. Detergent structure in tetragonal crystals of OmpF porin. Structure. 3:1995;1051-1059 Structures or distributions of detergents in crystals can be determined by deuteration and neutron diffraction if the X-ray structure of the protein is known ([2] in this case). Such analyses are very rare.
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(1995)
Structure
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, pp. 1051-1059
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Pebaypeyroula, E.1
Garavito, R.M.2
Rosenbusch, J.P.3
Zulauf, M.4
Timmins, P.A.5
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24
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0029081798
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Structurally identical porin in lithoauto- and organoheterotrophically grown Rhodobacter capsulatus cells
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Waldmann U, Robledano M, Weckesser J, Schulz GE. Structurally identical porin in lithoauto- and organoheterotrophically grown Rhodobacter capsulatus cells. FEMS Microbiol Lett. 131:1995;343-346.
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FEMS Microbiol Lett
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Waldmann, U.1
Robledano, M.2
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Schulz, G.E.4
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25
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0028025336
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Porins and specific diffusion channels in bacterial outer membranes
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Nikaido H. Porins and specific diffusion channels in bacterial outer membranes. J Biol Chem. 269:1994;3905-3908.
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Nikaido, H.1
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0027220893
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Porin conformation in the absence of calcium; Refined structure at 2.5 Å resolution
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Weiss MS, Schulz GE. Porin conformation in the absence of calcium; refined structure at 2.5 Å resolution. J Mol Biol. 231:1993;817-824.
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Weiss, M.S.1
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27
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0029087726
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The deletion of 70 amino acids near the N-terminal end of the sucrose-specific porin SrcY causes its functional similarity to LamB in vivo and in vitro
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Schülein K, Andersen C, Benz R. The deletion of 70 amino acids near the N-terminal end of the sucrose-specific porin SrcY causes its functional similarity to LamB in vivo and in vitro. Mol Microbiol. 17:1995;757-767.
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Schülein, K.1
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The OprB porin plays a central role in carbohydrate uptake in Pseudomonas aeruginosa
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Wylie JL, Worobec EA. The OprB porin plays a central role in carbohydrate uptake in Pseudomonas aeruginosa. J Bacteriol. 177:1995;3021-3026.
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Wylie, J.L.1
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29
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0028926959
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Evaluation of the rate constants of sugar transport through maltoporin (LamB) of Escherichia coli from the sugar-induced current noise
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of outstanding interest. Shows a most interesting way of monitoring the binding of noncharged molecules in a channel by measuring their influence on the current carried by ions through this channel.
-
of outstanding interest Andersen C, Jordy M, Benz R. Evaluation of the rate constants of sugar transport through maltoporin (LamB) of Escherichia coli from the sugar-induced current noise. J Gen Physiol. 105:1995;385-401 Shows a most interesting way of monitoring the binding of noncharged molecules in a channel by measuring their influence on the current carried by ions through this channel.
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J Gen Physiol
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, pp. 385-401
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Andersen, C.1
Jordy, M.2
Benz, R.3
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30
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0028206457
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Characterization of the porin of Rhodobacter capsulatus 37b4 in planar lipid bilayers
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Bishop ND, Lea EJ. Characterization of the porin of Rhodobacter capsulatus 37b4 in planar lipid bilayers. FEBS Lett. 349:1994;69-74.
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Bishop, N.D.1
Lea, E.J.2
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0027476160
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Asymmetry of orientation and voltage gating of the Acidovorax delafieldii porin Omp34 in lipid bilayers
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Brunen M, Engelhardt H. Asymmetry of orientation and voltage gating of the Acidovorax delafieldii porin Omp34 in lipid bilayers. Eur J Biochem. 212:1993;129-135.
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Eur J Biochem
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Brunen, M.1
Engelhardt, H.2
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32
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0030025654
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Altered voltage sensitivity of mutant OmpC porin channels
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of special interest. This work provides a clear hint on the presence of multiple substates of the pore eyelet which account for its voltage dependence.
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of special interest Bishop ND, Lea EJA, Mobasheri H, Spiro S. Altered voltage sensitivity of mutant OmpC porin channels. FEBS Lett. 379:1996;295-298 This work provides a clear hint on the presence of multiple substates of the pore eyelet which account for its voltage dependence.
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FEBS Lett
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Bishop, N.D.1
Lea, E.J.A.2
Mobasheri, H.3
Spiro, S.4
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Biochemical, molecular and functional characterization of porin isoforms from potato mitochondria
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Heins L, Mentzel H, Schmid A, Benz R, Schmitz UK. Biochemical, molecular and functional characterization of porin isoforms from potato mitochondria. J Biol Chem. 269:1994;26402-26410.
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Heins, L.1
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Schmid, A.3
Benz, R.4
Schmitz, U.K.5
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34
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0028828533
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Cadaverine induces closing of E. coli porins
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of special interest. This is the first indication that a bacterial porin may be regulated by a periplasmic molecule functioning as a stopper.
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of special interest Dela Vega AL, Delcour AH. Cadaverine induces closing of E. coli porins. EMBO J. 14:1995;6058-6065 This is the first indication that a bacterial porin may be regulated by a periplasmic molecule functioning as a stopper.
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Dela Vega, A.L.1
Delcour, A.H.2
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35
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0029016857
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Molecular design of the voltage-dependent, anion-selective channel in the mitochondrial outer membrane
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of outstanding interest. A very comprehensive study on mitochondrial porins, which indicates strongly that they are structurally similar to their bacterial counterparts.
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of outstanding interest Guo XW, Smith PR, Cognon B, d'Arcangelis D, Dolginova E, Mannella CA. Molecular design of the voltage-dependent, anion-selective channel in the mitochondrial outer membrane. J Struct Biol. 114:1995;41-59 A very comprehensive study on mitochondrial porins, which indicates strongly that they are structurally similar to their bacterial counterparts.
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J Struct Biol
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Guo, X.W.1
Smith, P.R.2
Cognon, B.3
D'Arcangelis, D.4
Dolginova, E.5
Mannella, C.A.6
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36
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0028986125
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Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy
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Schabert FA, Henn C, Engel A. Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy. Science. 268:1995;92-94.
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Science
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Schabert, F.A.1
Henn, C.2
Engel, A.3
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0028939947
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L3 loop-mediated mechanisms of pore closing in porin: A molecular dynamics perturbation approach
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Soares CM, Björksten J, Tapia O. L3 loop-mediated mechanisms of pore closing in porin: a molecular dynamics perturbation approach. Protein Eng. 8:1995;5-12.
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Protein Eng
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Soares, C.M.1
Björksten, J.2
Tapia, O.3
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38
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0028818855
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Lysine residues at positions 234 and 236 in yeast porin are involved in its assembly into the mitochondrial outer membrane
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Smith MD, Petrak M, Boucher PD, Barton KN, Carter L, Reddy G, Blachly-Dyson E, Forte M, Price J, Verner K, McCauley RB. Lysine residues at positions 234 and 236 in yeast porin are involved in its assembly into the mitochondrial outer membrane. J Biol Chem. 270:1995;28331-28336.
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J Biol Chem
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Smith, M.D.1
Petrak, M.2
Boucher, P.D.3
Barton, K.N.4
Carter, L.5
Reddy, G.6
Blachly-Dyson, E.7
Forte, M.8
Price, J.9
Verner, K.10
McCauley, R.B.11
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39
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0029041382
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Studies on human porin: XIII, the type-1 VDAC `porin 31HL' biotinylated at the plasmalemma of trypan blue excluding human B lymphocytes
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of special interest. It is shown that the eukaryotic cell surface porin must be tightly closed for cell survival.
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of special interest Jakob C, Götz H, Hellmann T, Hellmann KP, Reymann S, Florke H, Thinnes FP, Hilschmann N. Studies on human porin: XIII, the type-1 VDAC `porin 31HL' biotinylated at the plasmalemma of trypan blue excluding human B lymphocytes. FEBS Lett. 368:1995;5-9 It is shown that the eukaryotic cell surface porin must be tightly closed for cell survival.
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FEBS Lett
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Jakob, C.1
Götz, H.2
Hellmann, T.3
Hellmann, K.P.4
Reymann, S.5
Florke, H.6
Thinnes, F.P.7
Hilschmann, N.8
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Eisele JL, Rosenbusch JP. In vitro folding and oligomerization of a membrane protein. J Biol Chem. 265:1990;10217-10220.
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Surrey T, Schmid A, Jähnig F. Folding and membrane insertion of the trimeric β-barrel protein OmpF. Biochemistry. 35:1996;2283-2288.
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Detergent-induced folding of the outer-membrane protein PhoE, a pore protein induced by phosphate limitation
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Van Gelder P, DeCock H, Tommassen J. Detergent-induced folding of the outer-membrane protein PhoE, a pore protein induced by phosphate limitation. Eur J Biochem. 226:1994;783-787.
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Kinetics of folding and membrane insertion of a β-barrel membrane protein
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Surrey T, Jähnig F. Kinetics of folding and membrane insertion of a β-barrel membrane protein. J Biol Chem. 270:1995;28199-28203.
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Surrey, T.1
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Evidence for a loop-like insertion mechanism of pro-OmpA into the inner membrane of Escherichia coli
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Kuhn A, Kiefer D, Kohne C, Zhu HY, Tschantz WR, Dalbey RE. Evidence for a loop-like insertion mechanism of pro-OmpA into the inner membrane of Escherichia coli. Eur J Biochem. 226:1994;891-897.
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Kuhn, A.1
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Dalbey, R.E.6
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46
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0027178559
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Immunological properties of recombinant porin of Haemophilus influenzae type b expressed in Bacillus subtilis
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Srikumar R, Dahan D, Gras MF, Saarinen L, Käyhty H, Sarvas M, Vogel L, Coulton JW. Immunological properties of recombinant porin of Haemophilus influenzae type b expressed in Bacillus subtilis. Infect Immun. 61:1993;3334-3341.
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(1993)
Infect Immun
, vol.61
, pp. 3334-3341
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Srikumar, R.1
Dahan, D.2
Gras, M.F.3
Saarinen, L.4
Käyhty, H.5
Sarvas, M.6
Vogel, L.7
Coulton, J.W.8
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47
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0028306035
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Expression of large amounts of Neisserial porin proteins in Escherichia coli and refolding of the proteins into native trimers
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Qi HL, Tai JY, Blake MS. Expression of large amounts of Neisserial porin proteins in Escherichia coli and refolding of the proteins into native trimers. Infect Immun. 62:1994;2432-2439.
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(1994)
Infect Immun
, vol.62
, pp. 2432-2439
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Qi, H.L.1
Tai, J.Y.2
Blake, M.S.3
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48
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0028837021
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Production of Haemophilus influenzae type-b porin in Escherichia coli and its folding into the trimeric form
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Pullen JK, Liang SM, Blake MS, Mates S, Tai JY. Production of Haemophilus influenzae type-b porin in Escherichia coli and its folding into the trimeric form. Gene. 152:1995;85-88.
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(1995)
Gene
, vol.152
, pp. 85-88
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Pullen, J.K.1
Liang, S.M.2
Blake, M.S.3
Mates, S.4
Tai, J.Y.5
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49
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18744422713
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Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure
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of special interest. Using detergents, a recombinant oligomeric integral membrane protein that contains only β-sheet structure is recovered in large amounts from inclusion bodies. It is shown by crystal structure analysis to assume its truly authentic conformation. This opens a new pathway for channel engineering.
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of special interest Schmid B, Krömer M, Schulz GE. Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure. FEBS Lett. 381:1996;111-114 Using detergents, a recombinant oligomeric integral membrane protein that contains only β-sheet structure is recovered in large amounts from inclusion bodies. It is shown by crystal structure analysis to assume its truly authentic conformation. This opens a new pathway for channel engineering.
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(1996)
FEBS Lett
, vol.381
, pp. 111-114
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Schmid, B.1
Krömer, M.2
Schulz, G.E.3
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50
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0028321391
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OmpA protein of Escherichia coli outer membranes occurs in open and closed channel forms
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Sugawara E, Nikaido H. OmpA protein of Escherichia coli outer membranes occurs in open and closed channel forms. J Biol Chem. 269:1994;17981-17987.
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(1994)
J Biol Chem
, vol.269
, pp. 17981-17987
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Sugawara, E.1
Nikaido, H.2
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51
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0028986697
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Characterization of two membrane-bound forms of OmpA
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Rodionova NA, Tatulian SA, Surrey T, Jähnig F, Tamm LK. Characterization of two membrane-bound forms of OmpA. Biochemistry. 34:1995;1921-1929.
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(1995)
Biochemistry
, vol.34
, pp. 1921-1929
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Rodionova, N.A.1
Tatulian, S.A.2
Surrey, T.3
Jähnig, F.4
Tamm, L.K.5
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52
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0029128758
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Membrane assembly of circularly permuted variants of the E. coli outer membrane protein OmpA
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of outstanding interest. Circular permutations demonstrate that the putative eight-stranded β barrel consists of all-next-neighbor strands. This is an elegant chemical means of supporting a suggested topology.
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of outstanding interest Koebnik R, Kramer L. Membrane assembly of circularly permuted variants of the E. coli outer membrane protein OmpA. J Mol Biol. 250:1995;617-626 Circular permutations demonstrate that the putative eight-stranded β barrel consists of all-next-neighbor strands. This is an elegant chemical means of supporting a suggested topology.
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(1995)
J Mol Biol
, vol.250
, pp. 617-626
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Koebnik, R.1
Kramer, L.2
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53
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0029118738
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Actinobacillus actinomycetemcomitans leukotoxin forms large conductance voltage-gated ion channels when incorporated into planar lipid bilayers
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Lear JD, Furblur UG, Lally ET, Tanaka JC. Actinobacillus actinomycetemcomitans leukotoxin forms large conductance voltage-gated ion channels when incorporated into planar lipid bilayers. Biochim Biophys Acta. 1238:1995;34-41.
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(1995)
Biochim Biophys Acta
, vol.1238
, pp. 34-41
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Lear, J.D.1
Furblur, U.G.2
Lally, E.T.3
Tanaka, J.C.4
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54
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0028790410
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Antimicrobial peptide pores in membranes detected by neutron in-plane scattering
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He K, Ludtke SJ, Huang HW, Worcester DL. Antimicrobial peptide pores in membranes detected by neutron in-plane scattering. Biochemistry. 34:1995;15614-15618.
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(1995)
Biochemistry
, vol.34
, pp. 15614-15618
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He, K.1
Ludtke, S.J.2
Huang, H.W.3
Worcester, D.L.4
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55
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0028931417
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Voltage-dependent gating of an asymmetric gramicidin channel
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Oiki S, Koeppe RE, Anderson OS. Voltage-dependent gating of an asymmetric gramicidin channel. Proc Natl Acad Sci USA. 92:1995;2121-2125.
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(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 2121-2125
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Oiki, S.1
Koeppe, R.E.2
Anderson, O.S.3
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56
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0028904603
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The properties of ion channels formed by the coumarin antibiotic novobiocin in lipid bilayers
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Feigin AM, Aronov EV, Teeter JH, Brand JG. The properties of ion channels formed by the coumarin antibiotic novobiocin in lipid bilayers. Biochim Biophys Acta. 1234:1995;43-51.
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(1995)
Biochim Biophys Acta
, vol.1234
, pp. 43-51
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Feigin, A.M.1
Aronov, E.V.2
Teeter, J.H.3
Brand, J.G.4
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57
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0029150299
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Design of molecular function; Channels of communication
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Montal M. Design of molecular function; channels of communication. Annu Rev Biophys Biomol Struct. 24:1995;31-57.
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(1995)
Annu Rev Biophys Biomol Struct
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, pp. 31-57
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Montal, M.1
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58
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0029153215
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Peptides in membranes: Helicity and hydrophobicity
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Deber CM, Li SC. Peptides in membranes: helicity and hydrophobicity. Biopolymers. 37:1995;295-318.
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(1995)
Biopolymers
, vol.37
, pp. 295-318
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Deber, C.M.1
Li, S.C.2
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59
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0029017836
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Conformation, pore-forming activity, and antigenicity of synthetic peptide analogues of a spiralin putative amphipathic α-helix
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of special interest. This channel design follows a natural example. It can be further developed to yield increased selectivity.
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of special interest Brenner C, Duclohier H, Krchnak V, Wroblewski H. Conformation, pore-forming activity, and antigenicity of synthetic peptide analogues of a spiralin putative amphipathic α-helix. Biochim Biophys Acta. 1235:1995;161-168 This channel design follows a natural example. It can be further developed to yield increased selectivity.
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(1995)
Biochim Biophys Acta
, vol.1235
, pp. 161-168
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Brenner, C.1
Duclohier, H.2
Krchnak, V.3
Wroblewski, H.4
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60
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0028956341
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2
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of special interest. A very simple de novo design approach yields channels that are well characterized. It should be possible to introduce specificities. This paper is of great interest, although it is not the first study on such oligopeptide channels.
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2. Biophys J. 68:1995;1347-1358 A very simple de novo design approach yields channels that are well characterized. It should be possible to introduce specificities. This paper is of great interest, although it is not the first study on such oligopeptide channels.
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(1995)
Biophys J
, vol.68
, pp. 1347-1358
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Kienker, P.K.1
Lear, J.D.2
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61
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0028174318
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Artificial transmembrane ion channels from self-assembling peptide nanotubes
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Ghadiri MR, Granja JR, Buehler LK. Artificial transmembrane ion channels from self-assembling peptide nanotubes. Nature. 369:1994;301-304.
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(1994)
Nature
, vol.369
, pp. 301-304
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Ghadiri, M.R.1
Granja, J.R.2
Buehler, L.K.3
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