-
1
-
-
0032479329
-
Crystal structure of λ-Cro bound to a consensus operator at 3.0 Å resolution
-
Albright R.A., Matthews B.W. Crystal structure of λ-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
-
2
-
-
0030067028
-
High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer
-
Albright R.A., Mossing M.C., Matthews B.W. High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer. Biochemistry. 35:1996;735-742
-
(1996)
Biochemistry
, vol.35
, pp. 735-742
-
-
Albright, R.A.1
Mossing, M.C.2
Matthews, B.W.3
-
3
-
-
0018782255
-
The structure of a repressor: Crystallographic data for the cro regulatory protein of bacteriophage λ
-
Anderson W.F., Takeda Y., Echols H., Matthews B.W. The structure of a repressor Crystallographic data for the cro regulatory protein of bacteriophage λ J. Mol. Biol. 130:1979;507-510
-
(1979)
J. Mol. Biol.
, vol.130
, pp. 507-510
-
-
Anderson, W.F.1
Takeda, Y.2
Echols, H.3
Matthews, B.W.4
-
4
-
-
0019456340
-
Structure of the cro repressor from bacteriophage λ and its interaction with DNA
-
Anderson W.F., Ohlendorf D.H., Takeda Y., Matthews B.W. Structure of the cro repressor from bacteriophage λ and its interaction with DNA. Nature. 290:1981;754-758
-
(1981)
Nature
, vol.290
, pp. 754-758
-
-
Anderson, W.F.1
Ohlendorf, D.H.2
Takeda, Y.3
Matthews, B.W.4
-
5
-
-
0020491009
-
Proposed α-helical super-secondary structure associated with protein-DNA recognition
-
Anderson W.F., Takeda Y., Ohlendorf D.H., Matthews B.W. Proposed α-helical super-secondary structure associated with protein-DNA recognition. J. Mol. Biol. 159:1982;745-751
-
(1982)
J. Mol. Biol.
, vol.159
, pp. 745-751
-
-
Anderson, W.F.1
Takeda, Y.2
Ohlendorf, D.H.3
Matthews, B.W.4
-
6
-
-
0024571640
-
The helix-turn-helix DNA-binding motif
-
Brennan R.G., Matthews B.W. The helix-turn-helix DNA-binding motif. J. Biol. Chem. 264:1989;1903-1906
-
(1989)
J. Biol. Chem.
, vol.264
, pp. 1903-1906
-
-
Brennan, R.G.1
Matthews, B.W.2
-
7
-
-
0025009802
-
Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex
-
Brennan R.G., Roderick S.L., Takeda Y., Matthews B.W. Protein-DNA conformational changes in the crystal structure of a lambda Cro-operator complex. Proc. Natl Acad. Sci. USA. 87:1990;8165-8169
-
(1990)
Proc. Natl Acad. Sci. USA
, vol.87
, pp. 8165-8169
-
-
Brennan, R.G.1
Roderick, S.L.2
Takeda, Y.3
Matthews, B.W.4
-
8
-
-
0022706389
-
The relation between the divergence of sequence and structure in proteins
-
Chothia C., Lesk A.M. The relation between the divergence of sequence and structure in proteins. EMBO J. 5:1986;823-826
-
(1986)
EMBO J.
, vol.5
, pp. 823-826
-
-
Chothia, C.1
Lesk, A.M.2
-
9
-
-
84918314491
-
Refinement of large structures by simultaneous minimization of energy and R factor
-
Jack A., Levitt M. Refinement of large structures by simultaneous minimization of energy and R factor. Acta Crystallog. sect. A. 34:1978;931-935
-
(1978)
Acta Crystallog. Sect. a
, vol.34
, pp. 931-935
-
-
Jack, A.1
Levitt, M.2
-
11
-
-
0015222647
-
The interpretation of protein structures: Estimation of static accessibility
-
Lee B., Richards F.M. The interpretation of protein structures estimation of static accessibility. J. Mol. Biol. 55:1971;379-400
-
(1971)
J. Mol. Biol.
, vol.55
, pp. 379-400
-
-
Lee, B.1
Richards, F.M.2
-
12
-
-
0029610385
-
Three-dimensional dimer structure of the λ-Cro repressor in solution as determined by heteronuclear multidimensional NMR
-
Matsuo H., Shirakawa M., Kyogoku Y. Three-dimensional dimer structure of the λ-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
-
13
-
-
0024273441
-
Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles
-
Nicholson H., Becktel W.J., Matthews B.W. Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles. Nature. 336:1988;651-656
-
(1988)
Nature
, vol.336
, pp. 651-656
-
-
Nicholson, H.1
Becktel, W.J.2
Matthews, B.W.3
-
14
-
-
0026010011
-
Analysis of the interaction between charged side-chains and the α-helix dipole using designed thermostable mutants of phage T4 lysozyme
-
Nicholson H., Anderson D.E., Dao-pin S., Matthews B.W. Analysis of the interaction between charged side-chains and the α-helix dipole using designed thermostable mutants of phage T4 lysozyme. Biochemistry. 30:1991;9816-9828
-
(1991)
Biochemistry
, vol.30
, pp. 9816-9828
-
-
Nicholson, H.1
Anderson, D.E.2
Dao-Pin, S.3
Matthews, B.W.4
-
15
-
-
0019956313
-
The molecular basis of DNA-protein recognition inferred from the structure of cro repressor
-
Ohlendorf D.H., Anderson W.F., Fisher R.G., Takeda Y., Matthews B.W. The molecular basis of DNA-protein recognition inferred from the structure of cro repressor. Nature. 298:1982;718-723
-
(1982)
Nature
, vol.298
, pp. 718-723
-
-
Ohlendorf, D.H.1
Anderson, W.F.2
Fisher, R.G.3
Takeda, Y.4
Matthews, B.W.5
-
16
-
-
0020616785
-
Many gene-regulatory proteins appear to have a similar α-helical fold that binds DNA and evolved from a common precursor
-
Ohlendorf D.H., Anderson W.F., Matthews B.W. Many gene-regulatory proteins appear to have a similar α-helical fold that binds DNA and evolved from a common precursor. J. Mol. Evol. 19:1983;109-114
-
(1983)
J. Mol. Evol.
, vol.19
, pp. 109-114
-
-
Ohlendorf, D.H.1
Anderson, W.F.2
Matthews, B.W.3
-
18
-
-
0024363466
-
Amino acid substitutions that increase the thermal stability of the λ Cro protein
-
Pakula A.A., Sauer R.T. Amino acid substitutions that increase the thermal stability of the λ Cro protein. Proteins: Struct. Funct. Genet. 5:1989;202-210
-
(1989)
Proteins: Struct. Funct. Genet.
, vol.5
, pp. 202-210
-
-
Pakula, A.A.1
Sauer, R.T.2
-
19
-
-
0025317840
-
Reverse hydrophobic effects relieved by amino-acid substitutions at a protein surface
-
Pakula A.A., Sauer R.T. Reverse hydrophobic effects relieved by amino-acid substitutions at a protein surface. Nature. 344:1990;363-364
-
(1990)
Nature
, vol.344
, pp. 363-364
-
-
Pakula, A.A.1
Sauer, R.T.2
-
21
-
-
0019443447
-
The anatomy and taxonomy of protein structure
-
Richardson J.S. The anatomy and taxonomy of protein structure. Advan. Protein Chem. 34:1981;167-339
-
(1981)
Advan. Protein Chem.
, vol.34
, pp. 167-339
-
-
Richardson, J.S.1
-
22
-
-
0000731339
-
Processing oscillation diffraction data for very large unit cells with an automatic convolution technique and profile fitting
-
Rossmann M.G. Processing oscillation diffraction data for very large unit cells with an automatic convolution technique and profile fitting. J. Appl. Crystallog. 12:1979;225-239
-
(1979)
J. Appl. Crystallog.
, vol.12
, pp. 225-239
-
-
Rossmann, M.G.1
-
23
-
-
0001428018
-
l conformation at the ends of helices
-
R. Jaenicke. New York: Elsevier/North-Holland Biomedical Press
-
L conformation at the ends of helices. Jaenicke R. Protein Folding. 1980;53-61 Elsevier/North-Holland Biomedical Press, New York
-
(1980)
Protein Folding
, pp. 53-61
-
-
Schellman, C.1
-
24
-
-
0000413367
-
An oscillation data collection system for high-resolution protein crystallography
-
Schmid M.F., Weaver L.H., Holmes M.A., Grutter M.G., Ohlendorf D.H., Reynolds R.A., Remington S.J., Matthews B.W. An oscillation data collection system for high-resolution protein crystallography. Acta Crystallog. sect. A. 37:1981;701-710
-
(1981)
Acta Crystallog. Sect. a
, vol.37
, pp. 701-710
-
-
Schmid, M.F.1
Weaver, L.H.2
Holmes, M.A.3
Grutter, M.G.4
Ohlendorf, D.H.5
Reynolds, R.A.6
Remington, S.J.7
Matthews, B.W.8
-
25
-
-
0017759227
-
Cro regulatory protein specified by bacteriophage lambda. Structure, DNA-binding and repression of RNA synthesis
-
Takeda Y., Folkmanis A., Echols H. Cro regulatory protein specified by bacteriophage lambda. Structure, DNA-binding and repression of RNA synthesis. J. Biol. Chem. 252:1977;6177-6183
-
(1977)
J. Biol. Chem.
, vol.252
, pp. 6177-6183
-
-
Takeda, Y.1
Folkmanis, A.2
Echols, H.3
-
26
-
-
0022971596
-
Different interactions used by Cro repressor in specific and nonspecific DNA binding
-
Takeda Y., Kim J., Caday C.G., Steers E. Jr, Ohlendorf D.H., Anderson W.F., Matthews B.W. Different interactions used by Cro repressor in specific and nonspecific DNA binding. J. Biol. Chem. 261:1986;8608-8616
-
(1986)
J. Biol. Chem.
, vol.261
, pp. 8608-8616
-
-
Takeda, Y.1
Kim, J.2
Caday, C.G.3
Steers Jr., E.4
Ohlendorf, D.H.5
Anderson, W.F.6
Matthews, B.W.7
-
27
-
-
0028027354
-
Helix-capping interaction in (Cro protein: A free energy simulation analysis
-
Tidor B. Helix-capping interaction in (Cro protein a free energy simulation analysis. Proteins: Struct. Funct. Genet. 19:1994;310-323
-
(1994)
Proteins: Struct. Funct. Genet.
, vol.19
, pp. 310-323
-
-
Tidor, B.1
-
28
-
-
84945074880
-
Conjugate-direction minimization: An improved method for the refinement of macromolecules
-
Tronrud D.E. Conjugate-direction minimization an improved method for the refinement of macromolecules. Acta Crystallog. sect. A. 48:1992;912-916
-
(1992)
Acta Crystallog. Sect. a
, vol.48
, pp. 912-916
-
-
Tronrud, D.E.1
-
29
-
-
0002518563
-
Knowledge-based B-factor restraints for the refinement of proteins
-
Tronrud D.E. Knowledge-based B-factor restraints for the refinement of proteins. J. Appl. Crystallog. 29:1996;100-104
-
(1996)
J. Appl. Crystallog.
, vol.29
, pp. 100-104
-
-
Tronrud, D.E.1
-
30
-
-
84913050729
-
An efficient general-purpose least-squares refinement program for macromolecular structures
-
Tronrud D.E., Ten EyckL.F., Matthews B.W. An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallog. sect. A. 43:1987;489-503
-
(1987)
Acta Crystallog. Sect. a
, vol.43
, pp. 489-503
-
-
Tronrud, D.E.1
Ten, EyckL.F.2
Matthews, B.W.3
-
31
-
-
0014347799
-
Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units
-
Venkatachalam C.M. Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units. Biopolymers. 6:1968;1425-1436
-
(1968)
Biopolymers
, vol.6
, pp. 1425-1436
-
-
Venkatachalam, C.M.1
-
32
-
-
0026651557
-
NMR structure determination in solution: A critique and comparison with X-ray crystallography
-
Wagner G., Hyberts S.G., Havel T.F. NMR structure determination in solution a critique and comparison with X-ray crystallography. Annu. Rev. Biophys. Biomol. Struct. 21:1992;167-198
-
(1992)
Annu. Rev. Biophys. Biomol. Struct.
, vol.21
, pp. 167-198
-
-
Wagner, G.1
Hyberts, S.G.2
Havel, T.F.3
-
33
-
-
0028878767
-
EDPDB: A multi-functional tool for protein structure analysis
-
Zhang X.-J., Matthews B.W. EDPDB a multi-functional tool for protein structure analysis. J. Appl. Crystallog. 28:1995;624-630
-
(1995)
J. Appl. Crystallog.
, vol.28
, pp. 624-630
-
-
Zhang, X.-J.1
Matthews, B.W.2
-
34
-
-
0029150760
-
Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme
-
Zhang X.-J., Wozniak J.A., Matthews B.W. Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme. J. Mol. Biol. 250:1995;527-552
-
(1995)
J. Mol. Biol.
, vol.250
, pp. 527-552
-
-
Zhang, X.-J.1
Wozniak, J.A.2
Matthews, B.W.3
|