-
2
-
-
0032479329
-
Crystal structure of lambda-Cro bound to a consensus operator at 3.0 Å resolution
-
Albright R.A., Matthews B.W. Crystal structure of lambda-Cro bound to a consensus operator at 3.0 Å resolution. J. Mol. Biol. 280:1998;137-151.
-
(1998)
J. Mol. Biol.
, vol.280
, pp. 137-151
-
-
Albright, R.A.1
Matthews, B.W.2
-
3
-
-
0030801002
-
Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
-
Altschul S.F., Madden T.L., Schaffer A.A., Zhang J., Zhang Z., Miller W., Lipman D.J. Gapped BLAST and PSI-BLAST. a new generation of protein database search programs Nucleic Acids Res. 25:1997;3389-3402.
-
(1997)
Nucleic Acids Res.
, vol.25
, pp. 3389-3402
-
-
Altschul, S.F.1
Madden, T.L.2
Schaffer, A.A.3
Zhang, J.4
Zhang, Z.5
Miller, W.6
Lipman, D.J.7
-
4
-
-
0023937834
-
Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance
-
Arseniev A., Schultze P., Worgotter E., Braun W., Wagner G., Vasak M., Kagi J.H., Wuthrich K. Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance. J. Mol. Biol. 201:1988;637-657.
-
(1988)
J. Mol. Biol.
, vol.201
, pp. 637-657
-
-
Arseniev, A.1
Schultze, P.2
Worgotter, E.3
Braun, W.4
Wagner, G.5
Vasak, M.6
Kagi, J.H.7
Wuthrich, K.8
-
6
-
-
0028673482
-
Measurement of homo- and heteronuclear J couplings from quantitative J correlation
-
Bax A., Vuister G.W., Grzesiek S., Delaglio F., Wang A.C., Tschudin R., Zhu G. Measurement of homo- and heteronuclear J couplings from quantitative J correlation. Methods Enzymol. 239:1994;79-105.
-
(1994)
Methods Enzymol.
, vol.239
, pp. 79-105
-
-
Bax, A.1
Vuister, G.W.2
Grzesiek, S.3
Delaglio, F.4
Wang, A.C.5
Tschudin, R.6
Zhu, G.7
-
7
-
-
0034777598
-
Clustering protein sequences - Structure prediction by transitive homology
-
Bolten E., Schliep A., Schneckener S., Schomburg D., Schrader R. Clustering protein sequences - structure prediction by transitive homology. Bioinformatics. 17:2001;935-941.
-
(2001)
Bioinformatics
, vol.17
, pp. 935-941
-
-
Bolten, E.1
Schliep, A.2
Schneckener, S.3
Schomburg, D.4
Schrader, R.5
-
9
-
-
3543012707
-
Crystallography & NMR system: A new software suite for macromolecular structure determination
-
Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S.et al. Crystallography & NMR system. a new software suite for macromolecular structure determination Acta Crystallogr. D Biol. Crystallogr. 54:1998;905-921.
-
(1998)
Acta Crystallogr. D Biol. Crystallogr.
, vol.54
, pp. 905-921
-
-
Brunger, A.T.1
Adams, P.D.2
Clore, G.M.3
Delano, W.L.4
Gros, P.5
Grosse-Kunstleve, R.W.6
Jiang, J.S.7
Kuszewski, J.8
Nilges, M.9
Pannu, N.S.10
-
10
-
-
0032555696
-
Prediction of local structure in proteins using a library of sequence-structure motifs
-
Bystroff C., Baker D. Prediction of local structure in proteins using a library of sequence-structure motifs. J. Mol. Biol. 281:1998;565-577.
-
(1998)
J. Mol. Biol.
, vol.281
, pp. 565-577
-
-
Bystroff, C.1
Baker, D.2
-
11
-
-
0037825641
-
Prophages and bacterial genomics: What have we learned so far?
-
Casjens S. Prophages and bacterial genomics. what have we learned so far? Mol. Microbiol. 49:2003;277-300.
-
(2003)
Mol. Microbiol.
, vol.49
, pp. 277-300
-
-
Casjens, S.1
-
13
-
-
0033668488
-
An evolutionary bridge to a new protein fold
-
Cordes M.H., Burton R.E., Walsh N.P., McKnight C.J., Sauer R.T. An evolutionary bridge to a new protein fold. Nat. Struct. Biol. 7:2000;1129-1132.
-
(2000)
Nat. Struct. Biol.
, vol.7
, pp. 1129-1132
-
-
Cordes, M.H.1
Burton, R.E.2
Walsh, N.P.3
McKnight, C.J.4
Sauer, R.T.5
-
14
-
-
0034687127
-
Coupled energetics of lambda cro repressor self-assembly and site- specific DNA operator binding I: Analysis of cro dimerization from nanomolar to micromolar concentrations
-
Darling P.J., Holt J.M., Ackers G.K. Coupled energetics of lambda cro repressor self-assembly and site- specific DNA operator binding I. analysis of cro dimerization from nanomolar to micromolar concentrations Biochemistry. 39:2000;11500-11507.
-
(2000)
Biochemistry
, vol.39
, pp. 11500-11507
-
-
Darling, P.J.1
Holt, J.M.2
Ackers, G.K.3
-
15
-
-
0029400480
-
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
-
Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., Bax A. NMRPipe. a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR. 6:1995;277-293.
-
(1995)
J. Biomol. NMR
, vol.6
, pp. 277-293
-
-
Delaglio, F.1
Grzesiek, S.2
Vuister, G.W.3
Zhu, G.4
Pfeifer, J.5
Bax, A.6
-
16
-
-
0019858614
-
Similar amino acid sequences: Chance or common ancestry?
-
Doolittle R.F. Similar amino acid sequences. chance or common ancestry? Science. 214:1981;149-159.
-
(1981)
Science
, vol.214
, pp. 149-159
-
-
Doolittle, R.F.1
-
17
-
-
0034274870
-
An open graph visualization system and its applications to software engineering
-
Gansner E.R., North S.C. An open graph visualization system and its applications to software engineering. Software Pract. Exp. 30:2000;1203-1233.
-
(2000)
Software Pract. Exp.
, vol.30
, pp. 1203-1233
-
-
Gansner, E.R.1
North, S.C.2
-
18
-
-
0035783063
-
Fold change in evolution of protein structures
-
Grishin N.V. Fold change in evolution of protein structures. J. Struct. Biol. 134:2001;167-185.
-
(2001)
J. Struct. Biol.
, vol.134
, pp. 167-185
-
-
Grishin, N.V.1
-
19
-
-
0028935887
-
Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding
-
Huang G.S., Oas T.G. Structure and stability of monomeric lambda repressor. NMR evidence for two-state folding Biochemistry. 34:1995;3884-3892.
-
(1995)
Biochemistry
, vol.34
, pp. 3884-3892
-
-
Huang, G.S.1
Oas, T.G.2
-
20
-
-
44949272730
-
A time-efficient, linear-space local similarity algorithm
-
Huang X., Miller W. A time-efficient, linear-space local similarity algorithm. Adv. Appl. Math. 12:1991;337-357.
-
(1991)
Adv. Appl. Math.
, vol.12
, pp. 337-357
-
-
Huang, X.1
Miller, W.2
-
21
-
-
0030828503
-
A folded monomeric intermediate in the formation of lambda Cro dimer- DNA complexes
-
Jana R., Hazbun T.R., Mollah A.K., Mossing M.C. A folded monomeric intermediate in the formation of lambda Cro dimer- DNA complexes. J. Mol. Biol. 273:1997;402-416.
-
(1997)
J. Mol. Biol.
, vol.273
, pp. 402-416
-
-
Jana, R.1
Hazbun, T.R.2
Mollah, A.K.3
Mossing, M.C.4
-
22
-
-
34249765651
-
NMRView. A computer program for the visualization and analysis of NMR data
-
Johnson B.A., Blevins R. NMRView. A computer program for the visualization and analysis of NMR data. J. Biomol. NMR. 4:1994;603-614.
-
(1994)
J. Biomol. NMR
, vol.4
, pp. 603-614
-
-
Johnson, B.A.1
Blevins, R.2
-
23
-
-
0007208716
-
Interactions between DNA-bound repressors govern regulation by the lambda phage repressor
-
Johnson A.D., Meyer B.J., Ptashne M. Interactions between DNA-bound repressors govern regulation by the lambda phage repressor. Proc. Natl. Acad. Sci. USA. 76:1979;5061-5065.
-
(1979)
Proc. Natl. Acad. Sci. USA
, vol.76
, pp. 5061-5065
-
-
Johnson, A.D.1
Meyer, B.J.2
Ptashne, M.3
-
24
-
-
0036600834
-
Evolution of protein structures and functions
-
Kinch L.N., Grishin N.V. Evolution of protein structures and functions. Curr. Opin. Struct. Biol. 12:2002;400-408.
-
(2002)
Curr. Opin. Struct. Biol.
, vol.12
, pp. 400-408
-
-
Kinch, L.N.1
Grishin, N.V.2
-
25
-
-
0029881007
-
Molmol: A program for display and analysis of macromolecular structures
-
29-32
-
Koradi R., Billeter M., Wuthrich K. Molmol. a program for display and analysis of macromolecular structures J. Mol. Graph. 14:1996;51-55. 29-32.
-
(1996)
J. Mol. Graph.
, vol.14
, pp. 51-55
-
-
Koradi, R.1
Billeter, M.2
Wuthrich, K.3
-
26
-
-
0026244229
-
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. Crystallogr. 24:1991;946-950.
-
(1991)
J. Appl. Crystallogr.
, vol.24
, pp. 946-950
-
-
Kraulis, P.J.1
-
27
-
-
0030339738
-
Aqua and procheck-nmr: Programs for checking the quality of protein structures solved by nmr
-
Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., Thornton J.M. Aqua and procheck-nmr. programs for checking the quality of protein structures solved by nmr J. Biomol. NMR. 8:1996;477-486.
-
(1996)
J. Biomol. NMR
, vol.8
, pp. 477-486
-
-
Laskowski, R.A.1
Rullmannn, J.A.2
MacArthur, M.W.3
Kaptein, R.4
Thornton, J.M.5
-
28
-
-
0344642994
-
Homologous proteins with different folds: The three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI
-
Lauber T., Schulz A., Schweimer K., Adermann K., Marx U.C. Homologous proteins with different folds. the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI J. Mol. Biol. 328:2003;205-219.
-
(2003)
J. Mol. Biol.
, vol.328
, pp. 205-219
-
-
Lauber, T.1
Schulz, A.2
Schweimer, K.3
Adermann, K.4
Marx, U.C.5
-
29
-
-
0037418253
-
Retroevolution of lambda Cro toward a stable monomer
-
LeFevre K.R., Cordes M.H. Retroevolution of lambda Cro toward a stable monomer. Proc. Natl. Acad. Sci. USA. 100:2003;2345-2350.
-
(2003)
Proc. Natl. Acad. Sci. USA
, vol.100
, pp. 2345-2350
-
-
Lefevre, K.R.1
Cordes, M.H.2
-
30
-
-
0029610385
-
Three-dimensional dimer structure of the lambda-Cro repressor in solution as determined by heteronuclear multidimensional NMR
-
Matsuo H., Shirakawa M., Kyogoku Y. Three-dimensional dimer structure of the lambda-Cro repressor in solution as determined by heteronuclear multidimensional NMR. J. Mol. Biol. 254:1995;668-680.
-
(1995)
J. Mol. Biol.
, vol.254
, pp. 668-680
-
-
Matsuo, H.1
Shirakawa, M.2
Kyogoku, Y.3
-
31
-
-
0030815133
-
Raster3D: Photorealistic molecular graphics
-
Merritt E.A., Bacon D.J. Raster3D. photorealistic molecular graphics Methods Enzymol. 277:1997;505-524.
-
(1997)
Methods Enzymol.
, vol.277
, pp. 505-524
-
-
Merritt, E.A.1
Bacon, D.J.2
-
32
-
-
0024961628
-
Structure of the amino-terminal domain of phage 434 repressor at 2.0 Å resolution
-
a
-
Mondragon A., Subbiah S., Almo S.C., Drottar M., Harrison S.C. Structure of the amino-terminal domain of phage 434 repressor at 2.0 Å resolution. J. Mol. Biol. 205:1989;189-200. a.
-
(1989)
J. Mol. Biol.
, vol.205
, pp. 189-200
-
-
Mondragon, A.1
Subbiah, S.2
Almo, S.C.3
Drottar, M.4
Harrison, S.C.5
-
33
-
-
0024961623
-
Structure of phage 434 Cro protein at 2.35 a resolution
-
b
-
Mondragon A., Wolberger C., Harrison S.C. Structure of phage 434 Cro protein at 2.35 A resolution. J. Mol. Biol. 205:1989;179-188. b.
-
(1989)
J. Mol. Biol.
, vol.205
, pp. 179-188
-
-
Mondragon, A.1
Wolberger, C.2
Harrison, S.C.3
-
34
-
-
0025712476
-
Stable, monomeric variants of lambda Cro obtained by insertion of a designed beta-hairpin sequence
-
Mossing M.C., Sauer R.T. Stable, monomeric variants of lambda Cro obtained by insertion of a designed beta-hairpin sequence. Science. 250:1990;1712-1715.
-
(1990)
Science
, vol.250
, pp. 1712-1715
-
-
Mossing, M.C.1
Sauer, R.T.2
-
35
-
-
0004155865
-
-
Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press
-
Mount D.W. Bioinformatics. 2001;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
-
(2001)
Bioinformatics
-
-
Mount, D.W.1
-
36
-
-
0032104477
-
How far divergent evolution goes in proteins
-
Murzin A.G. How far divergent evolution goes in proteins. Curr. Opin. Struct. Biol. 8:1998;380-387.
-
(1998)
Curr. Opin. Struct. Biol.
, vol.8
, pp. 380-387
-
-
Murzin, A.G.1
-
37
-
-
0028961335
-
Scop: A structural classification of proteins database for the investigation of sequences and structures
-
Murzin A.G., Brenner S.E., Hubbard T., Chothia C. Scop. a structural classification of proteins database for the investigation of sequences and structures J. Mol. Biol. 247:1995;536-540.
-
(1995)
J. Mol. Biol.
, vol.247
, pp. 536-540
-
-
Murzin, A.G.1
Brenner, S.E.2
Hubbard, T.3
Chothia, C.4
-
38
-
-
0026547676
-
Determination of the nuclear magnetic resonance solution structure of the DNA-binding domain (residues 1 to 69) of the 434 repressor and comparison with the X-ray crystal structure
-
Neri D., Billeter M., Wuthrich K. Determination of the nuclear magnetic resonance solution structure of the DNA-binding domain (residues 1 to 69) of the 434 repressor and comparison with the X-ray crystal structure. J. Mol. Biol. 223:1992;743-767.
-
(1992)
J. Mol. Biol.
, vol.223
, pp. 743-767
-
-
Neri, D.1
Billeter, M.2
Wuthrich, K.3
-
39
-
-
0024435833
-
Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling
-
Neri D., Szyperski T., Otting G., Senn H., Wuthrich K. Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling. Biochemistry. 28:1989;7510-7516.
-
(1989)
Biochemistry
, vol.28
, pp. 7510-7516
-
-
Neri, D.1
Szyperski, T.2
Otting, G.3
Senn, H.4
Wuthrich, K.5
-
40
-
-
0032479285
-
Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity
-
Ohlendorf D.H., Tronrud D.E., Matthews B.W. Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity. J. Mol. Biol. 280:1998;129-136.
-
(1998)
J. Mol. Biol.
, vol.280
, pp. 129-136
-
-
Ohlendorf, D.H.1
Tronrud, D.E.2
Matthews, B.W.3
-
41
-
-
0030777303
-
Cath: A hierarchic classification of protein domain structures
-
Orengo C.A., Michie A.D., Jones S., Jones D.T., Swindells M.B., Thornton J.M. Cath. a hierarchic classification of protein domain structures Structure. 5:1997;1093-1108.
-
(1997)
Structure
, vol.5
, pp. 1093-1108
-
-
Orengo, C.A.1
Michie, A.D.2
Jones, S.3
Jones, D.T.4
Swindells, M.B.5
Thornton, J.M.6
-
42
-
-
0019977222
-
The operator-binding domain of lambda repressor: Structure and DNA recognition
-
Pabo C.O., Lewis M. The operator-binding domain of lambda repressor. structure and DNA recognition Nature. 298:1982;443-447.
-
(1982)
Nature
, vol.298
, pp. 443-447
-
-
Pabo, C.O.1
Lewis, M.2
-
43
-
-
0343051851
-
Three-dimensional solution structure and stability of phage 434 Cro protein
-
Padmanabhan S., Jimenez M.A., Gonzalez C., Sanz J.M., Gimenez-Gallego G., Rico M. Three-dimensional solution structure and stability of phage 434 Cro protein. Biochemistry. 36:1997;6424-6436.
-
(1997)
Biochemistry
, vol.36
, pp. 6424-6436
-
-
Padmanabhan, S.1
Jimenez, M.A.2
Gonzalez, C.3
Sanz, J.M.4
Gimenez-Gallego, G.5
Rico, M.6
-
44
-
-
0027332116
-
Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
-
Pan K.M., Baldwin M., Nguyen J., Gasset M., Serban A., Groth D., Mehlhorn I., Huang Z., Fletterick R.J., Cohen F.E.et al. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA. 90:1993;10962-10966.
-
(1993)
Proc. Natl. Acad. Sci. USA
, vol.90
, pp. 10962-10966
-
-
Pan, K.M.1
Baldwin, M.2
Nguyen, J.3
Gasset, M.4
Serban, A.5
Groth, D.6
Mehlhorn, I.7
Huang, Z.8
Fletterick, R.J.9
Cohen, F.E.10
-
45
-
-
0029933671
-
Effective protein sequence comparison
-
Pearson W.R. Effective protein sequence comparison. Methods Enzymol. 266:1996;227-258.
-
(1996)
Methods Enzymol.
, vol.266
, pp. 227-258
-
-
Pearson, W.R.1
-
46
-
-
0023048289
-
Bacteriophage P22 Cro protein: Sequence, purification, and properties
-
Poteete A.R., Hehir K., Sauer R.T. Bacteriophage P22 Cro protein. sequence, purification, and properties Biochemistry. 25:1986;251-256.
-
(1986)
Biochemistry
, vol.25
, pp. 251-256
-
-
Poteete, A.R.1
Hehir, K.2
Sauer, R.T.3
-
48
-
-
0034201441
-
Emboss: The european molecular biology open software suite
-
Rice P., Longden I., Bleasby A. Emboss. the european molecular biology open software suite Trends Genet. 16:2000;276-277.
-
(2000)
Trends Genet.
, vol.16
, pp. 276-277
-
-
Rice, P.1
Longden, I.2
Bleasby, A.3
-
49
-
-
0019974092
-
Homology among DNA-binding proteins suggests use of a conserved super-secondary structure
-
Sauer R.T., Yocum R.R., Doolittle R.F., Lewis M., Pabo C.O. Homology among DNA-binding proteins suggests use of a conserved super-secondary structure. Nature. 298:1982;447-451.
-
(1982)
Nature
, vol.298
, pp. 447-451
-
-
Sauer, R.T.1
Yocum, R.R.2
Doolittle, R.F.3
Lewis, M.4
Pabo, C.O.5
-
50
-
-
0032514655
-
Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: An alpha-helical to beta-sheet transition identified by fluorescence spectroscopy
-
Shepard L.A., Heuck A.P., Hamman B.D., Rossjohn J., Parker M.W., Ryan K.R., Johnson A.E., Tweten R.K. Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O. an alpha-helical to beta-sheet transition identified by fluorescence spectroscopy Biochemistry. 37:1998;14563-14574.
-
(1998)
Biochemistry
, vol.37
, pp. 14563-14574
-
-
Shepard, L.A.1
Heuck, A.P.2
Hamman, B.D.3
Rossjohn, J.4
Parker, M.W.5
Ryan, K.R.6
Johnson, A.E.7
Tweten, R.K.8
-
51
-
-
0029645579
-
The solution structure of the Mu Ner protein reveals a helix-turn-helix DNA recognition motif
-
Strzelecka T.E., Clore G.M., Gronenborn A.M. The solution structure of the Mu Ner protein reveals a helix-turn-helix DNA recognition motif. Structure. 3:1995;1087-1095.
-
(1995)
Structure
, vol.3
, pp. 1087-1095
-
-
Strzelecka, T.E.1
Clore, G.M.2
Gronenborn, A.M.3
-
52
-
-
0031574072
-
The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
-
Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL_X windows interface. flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res. 25:1997;4876-4882.
-
(1997)
Nucleic Acids Res.
, vol.25
, pp. 4876-4882
-
-
Thompson, J.D.1
Gibson, T.J.2
Plewniak, F.3
Jeanmougin, F.4
Higgins, D.G.5
-
55
-
-
0026597879
-
The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
-
Wishart D.S., Sykes B.D., Richards F.M. The chemical shift index. a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy Biochemistry. 31:1992;1647-1651.
-
(1992)
Biochemistry
, vol.31
, pp. 1647-1651
-
-
Wishart, D.S.1
Sykes, B.D.2
Richards, F.M.3
-
56
-
-
0017822448
-
Aromatic side-chain contributions to the far ultraviolet circular dichroism of peptides and proteins
-
Woody R.W. Aromatic side-chain contributions to the far ultraviolet circular dichroism of peptides and proteins. Biopolymers. 17:1978;1451-1467.
-
(1978)
Biopolymers
, vol.17
, pp. 1451-1467
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-
Woody, R.W.1
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