-
1
-
-
0027261284
-
Structure, function and application of the coiled-coil protein folding motif
-
Adamson J.G., Zhou N.E., Hodges R.S. Structure, function and application of the coiled-coil protein folding motif. Curr. Opin. Biotechnol. 4:1993;428-437
-
(1993)
Curr. Opin. Biotechnol.
, vol.4
, pp. 428-437
-
-
Adamson, J.G.1
Zhou, N.E.2
Hodges, R.S.3
-
2
-
-
0026058176
-
Dimer-to tetramer assembly of lac repressor involves a leucine heptad repeat
-
Alberti S., Oehler S., Wilcken-Bergmann B.V., Kramer H., Muller-Hill B. Dimer-to tetramer assembly of lac repressor involves a leucine heptad repeat. New Biol. 3:1991;57-62
-
(1991)
New Biol.
, vol.3
, pp. 57-62
-
-
Alberti, S.1
Oehler, S.2
Wilcken-Bergmann, B.V.3
Kramer, H.4
Muller-Hill, B.5
-
3
-
-
0027297241
-
Genetic analysis of the leucine heptad repeats of Lac repressor: Evidence for a 4-helical bundle
-
Alberti S., Oehler S., von Wilcken-Bergmann B., Muller-Hill B. Genetic analysis of the leucine heptad repeats of Lac repressor evidence for a 4-helical bundle. EMBO J. 12:1993;3227-3236
-
(1993)
EMBO J.
, vol.12
, pp. 3227-3236
-
-
Alberti, S.1
Oehler, S.2
Von Wilcken-Bergmann, B.3
Muller-Hill, B.4
-
4
-
-
0025234587
-
PH-Induced denaturation of proteins: A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme
-
Anderson D.E., Becktel W.J., Dahlquist F.W. pH-Induced denaturation of proteins A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry. 29:1990;2403-2408
-
(1990)
Biochemistry
, vol.29
, pp. 2403-2408
-
-
Anderson, D.E.1
Becktel, W.J.2
Dahlquist, F.W.3
-
5
-
-
0030200215
-
Acetylcholinesterase: Role of the enzyme's charge distribution in steering charged ligands toward the active site
-
Antosiewicz J., Wlodek S.T., McCammon J.A. Acetylcholinesterase role of the enzyme's charge distribution in steering charged ligands toward the active site. Biopolymers. 39:1996;85-94
-
(1996)
Biopolymers
, vol.39
, pp. 85-94
-
-
Antosiewicz, J.1
Wlodek, S.T.2
McCammon, J.A.3
-
6
-
-
0027537576
-
Interaction of coiled-coils in transcription factors: Where is the specificity?
-
Baxevanis A.D., Vinson C.R. Interaction of coiled-coils in transcription factors where is the specificity? Curr. Opin. Genet. Dev. 3:1993;278-285
-
(1993)
Curr. Opin. Genet. Dev.
, vol.3
, pp. 278-285
-
-
Baxevanis, A.D.1
Vinson, C.R.2
-
7
-
-
0030983330
-
A single amino acid can switch the oligomerization state of the α-helical coiled-coil domain of cartilage matrix protein
-
Beck K., Gambee J.E., Kamawal A., Bächinger H.P. A single amino acid can switch the oligomerization state of the α-helical coiled-coil domain of cartilage matrix protein. EMBO J. 16:1997;3767-3777
-
(1997)
EMBO J.
, vol.16
, pp. 3767-3777
-
-
Beck, K.1
Gambee, J.E.2
Kamawal, A.3
Bächinger, H.P.4
-
8
-
-
0029154811
-
Native-like and structurally characterized designed α-helical bundles
-
Betz S.F., Bryson J.W., DeGrado W.F. Native-like and structurally characterized designed α-helical bundles. Curr. Opin. Struct. Biol. 5:1995;457-463
-
(1995)
Curr. Opin. Struct. Biol.
, vol.5
, pp. 457-463
-
-
Betz, S.F.1
Bryson, J.W.2
Degrado, W.F.3
-
9
-
-
0027236794
-
Structural basis of amino acid α-helix propensity
-
Blaber M., Zhang X.-J., Matthews B.W. Structural basis of amino acid α-helix propensity. Science. 260:1993;1637-1640
-
(1993)
Science
, vol.260
, pp. 1637-1640
-
-
Blaber, M.1
Zhang, X.-J.2
Matthews, B.W.3
-
10
-
-
0030445131
-
Thermodynamic analysis of a designed three-stranded coiled coil
-
Boice J.A., Dieckmann G.R., DeGrado W.F., Fairman R. Thermodynamic analysis of a designed three-stranded coiled coil. Biochemistry. 35:1996;14480-14485
-
(1996)
Biochemistry
, vol.35
, pp. 14480-14485
-
-
Boice, J.A.1
Dieckmann, G.R.2
Degrado, W.F.3
Fairman, R.4
-
11
-
-
0028824042
-
Protein design: A hierarchic approach
-
Bryson J.W., Betz S.F., Lu H.S., Suich D.J., Zhou H.X., O'Neil K.T., DeGrado W.F. Protein design a hierarchic approach. Science. 270:1995;935-941
-
(1995)
Science
, vol.270
, pp. 935-941
-
-
Bryson, J.W.1
Betz, S.F.2
Lu, H.S.3
Suich, D.J.4
Zhou, H.X.5
O'Neil, K.T.6
Degrado, W.F.7
-
12
-
-
0028222235
-
Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions
-
Chakrabartty A., Kortemme T., Baldwin R.L. Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Protein Sci. 3:1994;843-852
-
(1994)
Protein Sci.
, vol.3
, pp. 843-852
-
-
Chakrabartty, A.1
Kortemme, T.2
Baldwin, R.L.3
-
13
-
-
0031891022
-
Computation of electrostatic complements to proteins: A case of charge stabilized binding
-
Chong L.T., Dempster S.E., Hendsch Z.S., Lee L.P., Tidor B. Computation of electrostatic complements to proteins a case of charge stabilized binding. Protein Sci. 7:1998;206-210
-
(1998)
Protein Sci.
, vol.7
, pp. 206-210
-
-
Chong, L.T.1
Dempster, S.E.2
Hendsch, Z.S.3
Lee, L.P.4
Tidor, B.5
-
14
-
-
0025272940
-
α-Helical coiled coils and bundles: How to design an α-helical protein
-
Cohen C., Parry D.A.D. α-Helical coiled coils and bundles how to design an α-helical protein. Proteins: Struct. Funct. Genet. 7:1990;1-15
-
(1990)
Proteins: Struct. Funct. Genet.
, vol.7
, pp. 1-15
-
-
Cohen, C.1
Parry, D.A.D.2
-
15
-
-
0028293441
-
α-helical coiled-coils: More facts and better predictions
-
Cohen C., Parry D.A.D. α-helical coiled-coils more facts and better predictions. Science. 263:1994;488-489
-
(1994)
Science
, vol.263
, pp. 488-489
-
-
Cohen, C.1
Parry, D.A.D.2
-
16
-
-
0027513776
-
Molecular modeling of coiled-coil α-tropomyosin: Analysis of staggered and in register helix-helix interactions
-
Cregut D., Liautard J.P., Heitz F., Chiche L. Molecular modeling of coiled-coil α-tropomyosin analysis of staggered and in register helix-helix interactions. Protein Eng. 6:1993;51-58
-
(1993)
Protein Eng.
, vol.6
, pp. 51-58
-
-
Cregut, D.1
Liautard, J.P.2
Heitz, F.3
Chiche, L.4
-
17
-
-
0025718955
-
Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by direct mutagenesis
-
Dao-pin S., Sauer U., Nicholson H., Matthews B.M. Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by direct mutagenesis. Biochemistry. 30:1991;7142-7153
-
(1991)
Biochemistry
, vol.30
, pp. 7142-7153
-
-
Dao-Pin, S.1
Sauer, U.2
Nicholson, H.3
Matthews, B.M.4
-
18
-
-
0031022887
-
Additivity principles in biochemistry
-
Dill K.A. Additivity principles in biochemistry. J. Biol. Chem. 272:1997;701-704
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 701-704
-
-
Dill, K.A.1
-
19
-
-
0028871798
-
Side-chain conformational entropy in protein folding
-
Doig A.J., Sternberg M.J.E. Side-chain conformational entropy in protein folding. Protein Sci. 4:1995;2247-2251
-
(1995)
Protein Sci.
, vol.4
, pp. 2247-2251
-
-
Doig, A.J.1
Sternberg, M.J.E.2
-
20
-
-
0027049805
-
The GCN4 basic region leucine zipper binds DNA as a dimer of uniterrupted α-helices: Crystal structure of the protein-DNA complex
-
Ellenberger T.E., Brandl C.J., Struhl K., Harrison S.C. The GCN4 basic region leucine zipper binds DNA as a dimer of uniterrupted α-helices crystal structure of the protein-DNA complex. Cell. 71:1992;1223-1237
-
(1992)
Cell
, vol.71
, pp. 1223-1237
-
-
Ellenberger, T.E.1
Brandl, C.J.2
Struhl, K.3
Harrison, S.C.4
-
21
-
-
0029997591
-
On the choice of reference mutant states in the application of the double-mutant cycle method
-
Faiman G.A., Horovitz A. On the choice of reference mutant states in the application of the double-mutant cycle method. Protein Eng. 9:1996;315-316
-
(1996)
Protein Eng.
, vol.9
, pp. 315-316
-
-
Faiman, G.A.1
Horovitz, A.2
-
22
-
-
0029144593
-
Characterization of a new four-chain coiled-coil: Influence of chain length on stability
-
Fairman R., Chao H.-G., Mueller L., Lavoie T.B., Shen L., Novotny J., Matsueda G.R. Characterization of a new four-chain coiled-coil influence of chain length on stability. Protein Sci. 4:1995;1457-1469
-
(1995)
Protein Sci.
, vol.4
, pp. 1457-1469
-
-
Fairman, R.1
Chao, H.-G.2
Mueller, L.3
Lavoie, T.B.4
Shen, L.5
Novotny, J.6
Matsueda, G.R.7
-
23
-
-
0015505502
-
Conformational equilibria in α- And δ-chymotrypsin. the energetics and importance of the salt bridge
-
Fersht A.R. Conformational equilibria in α- and δ-chymotrypsin. The energetics and importance of the salt bridge. J. Mol. Biol. 64:1972;497-509
-
(1972)
J. Mol. Biol.
, vol.64
, pp. 497-509
-
-
Fersht, A.R.1
-
24
-
-
0031008575
-
On the calculation of binding free energies using continuum methods: Application to MHC class I protein-peptide interactions
-
Froloff N., Windemuth A., Honig B. On the calculation of binding free energies using continuum methods application to MHC class I protein-peptide interactions. Protein Sci. 6:1997;1293-1301
-
(1997)
Protein Sci.
, vol.6
, pp. 1293-1301
-
-
Froloff, N.1
Windemuth, A.2
Honig, B.3
-
25
-
-
0028894384
-
Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA
-
Glover J.N.M., Harrison S.C. Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature. 373:1995;257-261
-
(1995)
Nature
, vol.373
, pp. 257-261
-
-
Glover, J.N.M.1
Harrison, S.C.2
-
26
-
-
16944366990
-
Buried polar residues and structural specificity in the GCN4 leucine zipper
-
Gonzalez L. Jr, Woolfson D.N., Alber T. Buried polar residues and structural specificity in the GCN4 leucine zipper. Nature Struct. Biol. 3:1996;1011-1018
-
(1996)
Nature Struct. Biol.
, vol.3
, pp. 1011-1018
-
-
Gonzalez Jr., L.1
Woolfson, D.N.2
Alber, T.3
-
27
-
-
0027146666
-
Controlled formation of model homo- and heterodimer coiled-coil polypeptides
-
Graddis T.J., Myszka D.G., Chaiken I.M. Controlled formation of model homo- and heterodimer coiled-coil polypeptides. Biochemistry. 32:1993;12664-12671
-
(1993)
Biochemistry
, vol.32
, pp. 12664-12671
-
-
Graddis, T.J.1
Myszka, D.G.2
Chaiken, I.M.3
-
28
-
-
0026755510
-
Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease: Evidence for mutational effects on the free energy of the denatured state
-
Green S.M., Meeker A.K., Shortle D. Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease evidence for mutational effects on the free energy of the denatured state. Biochemistry. 31:1992;5717-5728
-
(1992)
Biochemistry
, vol.31
, pp. 5717-5728
-
-
Green, S.M.1
Meeker, A.K.2
Shortle, D.3
-
29
-
-
0027177971
-
Metal ion-dependent modulation of the dynamics of a designed protein
-
Handel T.M., Williams S.A., DeGrado W.F. Metal ion-dependent modulation of the dynamics of a designed protein. Science. 261:1993;879-885
-
(1993)
Science
, vol.261
, pp. 879-885
-
-
Handel, T.M.1
Williams, S.A.2
Degrado, W.F.3
-
30
-
-
0027756896
-
A switch between two-, three-, and four-stranded coiled-coils in GCN4 leucine zipper mutants
-
Harbury P.B., Zhang T., Kim P.S., Alber T. A switch between two-, three-, and four-stranded coiled-coils in GCN4 leucine zipper mutants. Science. 262:1993;1401-1407
-
(1993)
Science
, vol.262
, pp. 1401-1407
-
-
Harbury, P.B.1
Zhang, T.2
Kim, P.S.3
Alber, T.4
-
31
-
-
0027934571
-
Crystal structure of an isoleucine-zipper trimer
-
Harbury P.B., Kim P.S., Alber T. Crystal structure of an isoleucine-zipper trimer. Nature. 371:1994;80-83
-
(1994)
Nature
, vol.371
, pp. 80-83
-
-
Harbury, P.B.1
Kim, P.S.2
Alber, T.3
-
32
-
-
0028204490
-
Do salt bridges stabilize proteins? a continuum electrostatic analysis
-
Hendsch Z.S., Tidor B. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci. 3:1994;211-226
-
(1994)
Protein Sci.
, vol.3
, pp. 211-226
-
-
Hendsch, Z.S.1
Tidor, B.2
-
33
-
-
0030345054
-
De novo design of α-helical proteins: Basic research to medical applications
-
Hodges R.S. De novo design of α-helical proteins basic research to medical applications. Biochem. Cell Biol. 74:1996;133-154
-
(1996)
Biochem. Cell Biol.
, vol.74
, pp. 133-154
-
-
Hodges, R.S.1
-
34
-
-
0028929583
-
Free energy balance in protein folding
-
Honig B., Yang A.-S. Free energy balance in protein folding. Adv. Protein Chem. 46:1995;27-58
-
(1995)
Adv. Protein Chem.
, vol.46
, pp. 27-58
-
-
Honig, B.1
Yang, A.-S.2
-
35
-
-
0025663105
-
Strength and cooperativity of contributions of surface salt bridges to protein stability
-
Horovitz A., Serrano L., Avron B., Bycroft M., Fersht A.R. Strength and cooperativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 216:1990;1031-1044
-
(1990)
J. Mol. Biol.
, vol.216
, pp. 1031-1044
-
-
Horovitz, A.1
Serrano, L.2
Avron, B.3
Bycroft, M.4
Fersht, A.R.5
-
36
-
-
0026674251
-
α-Helix stability in proteins. II. Factors that influence stability at an internal position
-
Horovitz A., Matthews J.M., Fersht A.R. α-Helix stability in proteins. II. Factors that influence stability at an internal position. J. Mol. Biol. 227:1992;560-658
-
(1992)
J. Mol. Biol.
, vol.227
, pp. 560-658
-
-
Horovitz, A.1
Matthews, J.M.2
Fersht, A.R.3
-
37
-
-
0003151250
-
The basic-region leucine-zipper family of DNA binding proteins
-
Hu J.C., Sauer R.T. The basic-region leucine-zipper family of DNA binding proteins. Nucl. Acids Mol. Biol. 6:1992;82-101
-
(1992)
Nucl. Acids Mol. Biol.
, vol.6
, pp. 82-101
-
-
Hu, J.C.1
Sauer, R.T.2
-
38
-
-
0025598302
-
Sequence requirements for coiled-coils: Analysis with λ-repressor-GCN4 leucine zipper fusions
-
Hu J.C., O'Shea E.K., Kim P.S., Sauer R.T. Sequence requirements for coiled-coils Analysis with λ-repressor-GCN4 leucine zipper fusions. Science. 250:1990;1400-1403
-
(1990)
Science
, vol.250
, pp. 1400-1403
-
-
Hu, J.C.1
O'Shea, E.K.2
Kim, P.S.3
Sauer, R.T.4
-
39
-
-
0027180729
-
Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenensis
-
Hu J.C., Newell N.E., Tidor B., Sauer R.T. Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenensis. Protein Sci. 2:1993;1072-1084
-
(1993)
Protein Sci.
, vol.2
, pp. 1072-1084
-
-
Hu, J.C.1
Newell, N.E.2
Tidor, B.3
Sauer, R.T.4
-
40
-
-
0028882032
-
Measuring the strength of side-chain hydrogen bonds in peptide helices: The Gln·Asp (i,i+4) interaction
-
Huyghues-Despointes B.M.P., Klingler T.M., Baldwin R.L. Measuring the strength of side-chain hydrogen bonds in peptide helices the Gln·Asp (i,i+4) interaction. Biochemistry. 34:1995;13267-13271
-
(1995)
Biochemistry
, vol.34
, pp. 13267-13271
-
-
Huyghues-Despointes, B.M.P.1
Klingler, T.M.2
Baldwin, R.L.3
-
41
-
-
0032562663
-
Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil α-helices
-
Kammerer R.A., Schulthess T., Landwehr R., Lustig A., Fischer D., Engl J. Tenascin-C hexabrachion assembly is a sequential two-step process initiated by coiled-coil α-helices. J. Biol. Chem. 273:1998;10602-10608
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 10602-10608
-
-
Kammerer, R.A.1
Schulthess, T.2
Landwehr, R.3
Lustig, A.4
Fischer, D.5
Engl, J.6
-
42
-
-
0031008576
-
Hydrophobicity regained
-
Karplus P.A. Hydrophobicity regained. Protein Sci. 6:1997;1302-1307
-
(1997)
Protein Sci.
, vol.6
, pp. 1302-1307
-
-
Karplus, P.A.1
-
43
-
-
0032167466
-
De novo design of α-helical coiled-coils and bundles: Models for development of protein design principles
-
Kohn W.D., Hodges R.S. De novo design of α-helical coiled-coils and bundles models for development of protein design principles. Trends Biotech. 16:1998;379-389
-
(1998)
Trends Biotech.
, vol.16
, pp. 379-389
-
-
Kohn, W.D.1
Hodges, R.S.2
-
44
-
-
0028959280
-
Protein destabilization by electrostatic repulsions in the two-stranded α-helical coiled-coil
-
Kohn W.D., Kay C.M., Hodges R.S. Protein destabilization by electrostatic repulsions in the two-stranded α-helical coiled-coil. Protein Sci. 4:1995;237-250
-
(1995)
Protein Sci.
, vol.4
, pp. 237-250
-
-
Kohn, W.D.1
Kay, C.M.2
Hodges, R.S.3
-
45
-
-
0028805884
-
The effects of interhelical repulsions between glutamic acid residues in controlling the dimerization and stability of two-stranded α-helical coiled-coils
-
Kohn W.D., Monera O.D., Kay C.M., Hodges R.S. The effects of interhelical repulsions between glutamic acid residues in controlling the dimerization and stability of two-stranded α-helical coiled-coils. J. Biol. Chem. 270:1995;25495-25506
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 25495-25506
-
-
Kohn, W.D.1
Monera, O.D.2
Kay, C.M.3
Hodges, R.S.4
-
46
-
-
0031564608
-
Salt effects on protein stability: Two-stranded α-helical coiled-coils containing inter- or intrahelical ion-pairs
-
Kohn W.D., Kay C.M., Hodges R.S. Salt effects on protein stability two-stranded α-helical coiled-coils containing inter- or intrahelical ion-pairs. J. Mol. Biol. 267:1997;1039-1052
-
(1997)
J. Mol. Biol.
, vol.267
, pp. 1039-1052
-
-
Kohn, W.D.1
Kay, C.M.2
Hodges, R.S.3
-
48
-
-
0031133303
-
Positional dependence of the effects of negatively charged Glu side-chains on the stability of two-stranded α-helical coiled-coils
-
Kohn W.K., Kay C.M., Hodges R.S. Positional dependence of the effects of negatively charged Glu side-chains on the stability of two-stranded α-helical coiled-coils. J. Pept. Sci. 3:1997;209-223
-
(1997)
J. Pept. Sci.
, vol.3
, pp. 209-223
-
-
Kohn, W.K.1
Kay, C.M.2
Hodges, R.S.3
-
49
-
-
0031885037
-
Effects of lanthanide binding on the stability of de novo designed α-helical coiled-coils
-
Kohn W.D., Kay C.M., Hodges R.S. Effects of lanthanide binding on the stability of de novo designed α-helical coiled-coils. J. Pept. Res. 51:1998;9-18
-
(1998)
J. Pept. Res.
, vol.51
, pp. 9-18
-
-
Kohn, W.D.1
Kay, C.M.2
Hodges, R.S.3
-
50
-
-
0032542575
-
Metal ion-induced folding of a de novo designed coiled-coil peptide
-
Kohn W.D., Kay C.M., Sykes B.D., Hodges R.S. Metal ion-induced folding of a de novo designed coiled-coil peptide. J. Am. Chem. Soc. 120:1998;1124-1132
-
(1998)
J. Am. Chem. Soc.
, vol.120
, pp. 1124-1132
-
-
Kohn, W.D.1
Kay, C.M.2
Sykes, B.D.3
Hodges, R.S.4
-
51
-
-
0027377202
-
The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility
-
König P., Richmond T.J. The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility. J. Mol. Biol. 233:1993;139-154
-
(1993)
J. Mol. Biol.
, vol.233
, pp. 139-154
-
-
König, P.1
Richmond, T.J.2
-
52
-
-
0028303384
-
A thermodynamic scale for leucine zipper stability and dimerization specificity: E and g interhelical interactions
-
Krylov D., Mikhailenko I., Vinson C. A thermodynamic scale for leucine zipper stability and dimerization specificity e and g interhelical interactions. EMBO J. 13:1994;2849-2861
-
(1994)
EMBO J.
, vol.13
, pp. 2849-2861
-
-
Krylov, D.1
Mikhailenko, I.2
Vinson, C.3
-
53
-
-
0029926150
-
Interhelical salt bridges, coiled-coil stability, and specificity of dimerization
-
Lavigne P., Sonnichsen F.D., Kay C.M., Hodges R.S. Interhelical salt bridges, coiled-coil stability, and specificity of dimerization. Science. 271:1996;1136-1137
-
(1996)
Science
, vol.271
, pp. 1136-1137
-
-
Lavigne, P.1
Sonnichsen, F.D.2
Kay, C.M.3
Hodges, R.S.4
-
54
-
-
0030917740
-
Exceptionally stable salt bridges in cytochrome P450cam have functional roles
-
Lounnas V., Wade R.C. Exceptionally stable salt bridges in cytochrome P450cam have functional roles. Biochemistry. 36:1997;5402-5417
-
(1997)
Biochemistry
, vol.36
, pp. 5402-5417
-
-
Lounnas, V.1
Wade, R.C.2
-
55
-
-
0000820879
-
Comparative study of the α-helical muscle proteins. Tyrosyl titration and effect of pH on conformation
-
Lowey S. Comparative study of the α-helical muscle proteins. Tyrosyl titration and effect of pH on conformation. J. Biol. Chem. 240:1965;2421-2427
-
(1965)
J. Biol. Chem.
, vol.240
, pp. 2421-2427
-
-
Lowey, S.1
-
56
-
-
0029008590
-
A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil
-
Lumb K.J., Kim P.S. A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil. Biochemistry. 34:1995;8642-8648
-
(1995)
Biochemistry
, vol.34
, pp. 8642-8648
-
-
Lumb, K.J.1
Kim, P.S.2
-
57
-
-
0029030233
-
Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper
-
Lumb K.J., Kim P.S. Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper. Science. 268:1995;436-439
-
(1995)
Science
, vol.268
, pp. 436-439
-
-
Lumb, K.J.1
Kim, P.S.2
-
58
-
-
0029926150
-
Interhelical salt bridges, coiled-coil stability, and specificity of dimerization
-
Lumb K.J., Kim P.S. Interhelical salt bridges, coiled-coil stability, and specificity of dimerization. Science. 271:1996;1137-1138
-
(1996)
Science
, vol.271
, pp. 1137-1138
-
-
Lumb, K.J.1
Kim, P.S.2
-
59
-
-
0030271515
-
Coiled coils: New structures and new functions
-
Lupas A. Coiled coils new structures and new functions. Trends Biochem. Sci. 21:1996;375-382
-
(1996)
Trends Biochem. Sci.
, vol.21
, pp. 375-382
-
-
Lupas, A.1
-
60
-
-
0026565486
-
Energetic contribution of solvent-exposed ion pairs to alpha-helix structure
-
Lyu P.C., Gans P.J., Kallenbach N.R. Energetic contribution of solvent-exposed ion pairs to alpha-helix structure. J. Mol. Biol. 223:1992;343-350
-
(1992)
J. Mol. Biol.
, vol.223
, pp. 343-350
-
-
Lyu, P.C.1
Gans, P.J.2
Kallenbach, N.R.3
-
61
-
-
0016774265
-
Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
-
McLachlan A.D., Stewart M. Tropomyosin coiled-coil interactions evidence for an unstaggered structure. J. Mol. Biol. 98:1975;293-304
-
(1975)
J. Mol. Biol.
, vol.98
, pp. 293-304
-
-
McLachlan, A.D.1
Stewart, M.2
-
62
-
-
0025666831
-
The thermal denaturation of nonpolymerizable αα-tropomyosin and its segments as a function of ionic strength
-
Mo J., Holtzer M.E., Holtzer A. The thermal denaturation of nonpolymerizable αα-tropomyosin and its segments as a function of ionic strength. Biopolymers. 30:1990;921-927
-
(1990)
Biopolymers
, vol.30
, pp. 921-927
-
-
Mo, J.1
Holtzer, M.E.2
Holtzer, A.3
-
63
-
-
0030804094
-
Leucine is the most stabilizing aliphatic amino acid in the d position of a dimeric leucine zipper coiled coil
-
Moitra J., Szilak L., Krylov D., Vinson C. Leucine is the most stabilizing aliphatic amino acid in the d position of a dimeric leucine zipper coiled coil. Biochemistry. 36:1997;12567-12573
-
(1997)
Biochemistry
, vol.36
, pp. 12567-12573
-
-
Moitra, J.1
Szilak, L.2
Krylov, D.3
Vinson, C.4
-
64
-
-
0028330850
-
Electrostatic interactions control the parallel and antiparallel orientation of α-helical chains in two-stranded α-helical coiled-coils
-
Monera O.D., Kay C.M., Hodges R.S. Electrostatic interactions control the parallel and antiparallel orientation of α-helical chains in two-stranded α-helical coiled-coils. Biochemistry. 33:1994;3862-3871
-
(1994)
Biochemistry
, vol.33
, pp. 3862-3871
-
-
Monera, O.D.1
Kay, C.M.2
Hodges, R.S.3
-
65
-
-
0028569153
-
Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
-
Monera O.D., Kay C.M., Hodges R.S. Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3:1994;1984-1991
-
(1994)
Protein Sci.
, vol.3
, pp. 1984-1991
-
-
Monera, O.D.1
Kay, C.M.2
Hodges, R.S.3
-
66
-
-
0032031405
-
Electrostatic contributions to protein-protein binding affinities: Application to Rap/Raf interaction
-
Muegge I., Schweins T., Warshel A. Electrostatic contributions to protein-protein binding affinities application to Rap/Raf interaction. Proteins: Struct. Funct. Genet. 30:1998;407-423
-
(1998)
Proteins: Struct. Funct. Genet.
, vol.30
, pp. 407-423
-
-
Muegge, I.1
Schweins, T.2
Warshel, A.3
-
67
-
-
0029843132
-
Hydrogen bonding stabilizes globular proteins
-
Myers J.K., Pace C.N. Hydrogen bonding stabilizes globular proteins. Biophys. J. 71:1996;2033-2039
-
(1996)
Biophys. J.
, vol.71
, pp. 2033-2039
-
-
Myers, J.K.1
Pace, C.N.2
-
68
-
-
0030858237
-
Helix propensities are identical in proteins and peptides
-
Myers J.K., Pace C.N., Scholtz J.M. Helix propensities are identical in proteins and peptides. Biochemistry. 36:1997;10923-10929
-
(1997)
Biochemistry
, vol.36
, pp. 10923-10929
-
-
Myers, J.K.1
Pace, C.N.2
Scholtz, J.M.3
-
70
-
-
0027502369
-
Successful prediction of the coiled-coil geometry of the GCN4 leucine zipper domain by simulated annealing: Comparison to the X-ray structure
-
Nilges M., Brunger A.T. Successful prediction of the coiled-coil geometry of the GCN4 leucine zipper domain by simulated annealing comparison to the X-ray structure. Proteins: Struct. Funct. Genet. 15:1993;133-146
-
(1993)
Proteins: Struct. Funct. Genet.
, vol.15
, pp. 133-146
-
-
Nilges, M.1
Brunger, A.T.2
-
72
-
-
0025222978
-
A thermodynamic scale for the helix-forming tendencies of the commonly occuring amino acids
-
O'Neil K.T., DeGrado W.F. A thermodynamic scale for the helix-forming tendencies of the commonly occuring amino acids. Science. 250:1990;646-651
-
(1990)
Science
, vol.250
, pp. 646-651
-
-
O'Neil, K.T.1
Degrado, W.F.2
-
73
-
-
0026331267
-
X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled-coil
-
O'Shea E.K., Klemm J.D., Kim P.S., Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled-coil. Science. 254:1991;539-544
-
(1991)
Science
, vol.254
, pp. 539-544
-
-
O'Shea, E.K.1
Klemm, J.D.2
Kim, P.S.3
Alber, T.4
-
74
-
-
0026571898
-
Mechanism of specificity in the Fos-Jun oncoprotein heterodimer
-
O'Shea E.K., Rutkowski R., Kim P.S. Mechanism of specificity in the Fos-Jun oncoprotein heterodimer. Cell. 68:1992;699-708
-
(1992)
Cell
, vol.68
, pp. 699-708
-
-
O'Shea, E.K.1
Rutkowski, R.2
Kim, P.S.3
-
75
-
-
0000236570
-
Peptide "velcro": Design of a heterodimeric coiled-coil
-
O'Shea E.K., Lumb K.J., Kim P.S. Peptide "Velcro" design of a heterodimeric coiled-coil. Curr. Biol. 3:1993;658-667
-
(1993)
Curr. Biol.
, vol.3
, pp. 658-667
-
-
O'Shea, E.K.1
Lumb, K.J.2
Kim, P.S.3
-
76
-
-
0022555885
-
Determination and analysis of urea and guanidine hydrochloride denaturation curves
-
Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;266-280
-
(1986)
Methods Enzymol.
, vol.131
, pp. 266-280
-
-
Pace, C.N.1
-
77
-
-
0026777217
-
Contribution of the hydrophobic effect to globular protein stability
-
Pace C.N. Contribution of the hydrophobic effect to globular protein stability. J. Mol. Biol. 226:1992;29-35
-
(1992)
J. Mol. Biol.
, vol.226
, pp. 29-35
-
-
Pace, C.N.1
-
78
-
-
0030059689
-
Forces contributing to the conformational stability of proteins
-
Pace C.N., Shirley B.A., McNutt M., Gajiwala K. Forces contributing to the conformational stability of proteins. FASEB J. 10:1996;75-83
-
(1996)
FASEB J.
, vol.10
, pp. 75-83
-
-
Pace, C.N.1
Shirley, B.A.2
McNutt, M.3
Gajiwala, K.4
-
79
-
-
0029124248
-
Molten globule and protein folding
-
Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 47:1995;83-229
-
(1995)
Adv. Protein Chem.
, vol.47
, pp. 83-229
-
-
Ptitsyn, O.B.1
-
80
-
-
0027321875
-
Dimerization of leucine zippers analyzed by random selection
-
Pu W.T., Struhl K. Dimerization of leucine zippers analyzed by random selection. Nucl. Acids Res. 21:1993;4348-4355
-
(1993)
Nucl. Acids Res.
, vol.21
, pp. 4348-4355
-
-
Pu, W.T.1
Struhl, K.2
-
81
-
-
0030447864
-
Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol
-
Rohl C.A., Chakrabartty A., Baldwin R.L. Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol. Protein Sci. 5:1996;2623-2637
-
(1996)
Protein Sci.
, vol.5
, pp. 2623-2637
-
-
Rohl, C.A.1
Chakrabartty, A.2
Baldwin, R.L.3
-
82
-
-
0025911856
-
Surface electrostatic interactions contribute little to stability of barnase
-
Sali D., Baycroft M., Fersht A.R. Surface electrostatic interactions contribute little to stability of barnase. J. Mol. Biol. 220:1991;779-788
-
(1991)
J. Mol. Biol.
, vol.220
, pp. 779-788
-
-
Sali, D.1
Baycroft, M.2
Fersht, A.R.3
-
83
-
-
0025816574
-
The solution structure of a leucine-zipper motif peptide
-
Saudek V., Pastore A., Castiglione MorelliM.A., Frank R., Gausepohl H., Gibson T. The solution structure of a leucine-zipper motif peptide. Protein Eng. 4,:1991;519-529
-
(1991)
Protein Eng.
, vol.4
, pp. 519-529
-
-
Saudek, V.1
Pastore, A.2
Castiglione, MorelliM.A.3
Frank, R.4
Gausepohl, H.5
Gibson, T.6
-
84
-
-
0025938866
-
Construction, purification, and characterization of a hybrid protein comprising the DNA binding domain of the LexA repressor and the Jun leucine zipper: A circular dichroism and mutagenesis study
-
Schmidt-Dörr T., Oertel-Buchheit P., Pernelle C., Bracco L., Schnarr M., Granger-Schnarr M. Construction, purification, and characterization of a hybrid protein comprising the DNA binding domain of the LexA repressor and the Jun leucine zipper a circular dichroism and mutagenesis study. Biochemistry. 30:1991;9657-9664
-
(1991)
Biochemistry
, vol.30
, pp. 9657-9664
-
-
Schmidt-Dörr, T.1
Oertel-Buchheit, P.2
Pernelle, C.3
Bracco, L.4
Schnarr, M.5
Granger-Schnarr, M.6
-
85
-
-
0027497118
-
The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide
-
Scholtz J.M., Qian H., Robbins V.H., Baldwin R.L. The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide. Biochemistry. 32:1993;9668-9676
-
(1993)
Biochemistry
, vol.32
, pp. 9668-9676
-
-
Scholtz, J.M.1
Qian, H.2
Robbins, V.H.3
Baldwin, R.L.4
-
86
-
-
0026073643
-
Non-leucine residues in the leucine repeats of Fos and Jun contribute to the stability and determine the specificity of dimerization
-
Schuermann M., Hunter J.B., Hennig G., Muller R. Non-leucine residues in the leucine repeats of Fos and Jun contribute to the stability and determine the specificity of dimerization. Nucl. Acids Res. 19:1991;739-746
-
(1991)
Nucl. Acids Res.
, vol.19
, pp. 739-746
-
-
Schuermann, M.1
Hunter, J.B.2
Hennig, G.3
Muller, R.4
-
87
-
-
0028113997
-
Reversed-phase chromatography of synthetic amphipathic α-helical peptides as a model for ligand/receptor interactions: Effect of changing hydrophobic environment on the relative hydrophilicity/hydrophobicity of amino acid side-chains
-
Sereda T.J., Mant C.T., Sonnichsen F.D., Hodges R.S. Reversed-phase chromatography of synthetic amphipathic α-helical peptides as a model for ligand/receptor interactions effect of changing hydrophobic environment on the relative hydrophilicity/hydrophobicity of amino acid side-chains. J. Chromatog. 676:1994;139-153
-
(1994)
J. Chromatog.
, vol.676
, pp. 139-153
-
-
Sereda, T.J.1
Mant, C.T.2
Sonnichsen, F.D.3
Hodges, R.S.4
-
88
-
-
0025093185
-
Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles
-
Serrano L., Horovitz A., Avron B., Bycroft M., Fersht A.R. Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles. Biochemistry. 29:1990;9343-9352
-
(1990)
Biochemistry
, vol.29
, pp. 9343-9352
-
-
Serrano, L.1
Horovitz, A.2
Avron, B.3
Bycroft, M.4
Fersht, A.R.5
-
89
-
-
0026926768
-
The contribution of residue ion pairs to the helical stability of a model peptide
-
Stellwagen E., Park S.H., Shalongo W., Jain A. The contribution of residue ion pairs to the helical stability of a model peptide. Biopolymers. 32:1992;1193-1200
-
(1992)
Biopolymers
, vol.32
, pp. 1193-1200
-
-
Stellwagen, E.1
Park, S.H.2
Shalongo, W.3
Jain, A.4
-
90
-
-
0001647480
-
Tropomyosin: A model protein for studying coiled-coil and α-helix stabilization
-
Talbot J.A., Hodges R.S. Tropomyosin a model protein for studying coiled-coil and α-helix stabilization. Acc. Chem. Res. 15:1982;224-230
-
(1982)
Acc. Chem. Res.
, vol.15
, pp. 224-230
-
-
Talbot, J.A.1
Hodges, R.S.2
-
91
-
-
0029146297
-
A calorimetric characterization of the salt dependence of the stability of the GCN4 leucine zipper
-
Thompson-Kenar K., Garcia-Moreno B., Freire E. A calorimetric characterization of the salt dependence of the stability of the GCN4 leucine zipper. Protein Sci. 4:1995;1934-1938
-
(1995)
Protein Sci.
, vol.4
, pp. 1934-1938
-
-
Thompson-Kenar, K.1
Garcia-Moreno, B.2
Freire, E.3
-
92
-
-
0027176792
-
Dimerization specificity of the leucine zipper-containing bZIP motif on DNA binding: Prediction and rational design
-
Vinson C.R., Hai T., Boyd S.M. Dimerization specificity of the leucine zipper-containing bZIP motif on DNA binding prediction and rational design. Genes Dev. 7:1993;1047-1058
-
(1993)
Genes Dev.
, vol.7
, pp. 1047-1058
-
-
Vinson, C.R.1
Hai, T.2
Boyd, S.M.3
-
93
-
-
0021476470
-
Calculations of electrostatic interactions in biological systems and in solutions
-
Warshel A., Russell S.T. Calculations of electrostatic interactions in biological systems and in solutions. Quart. Rev. Biophys. 17:1984;283-422
-
(1984)
Quart. Rev. Biophys.
, vol.17
, pp. 283-422
-
-
Warshel, A.1
Russell, S.T.2
-
94
-
-
0031561809
-
Protein binding versus-protein folding: The role of hydrophilic bridges in protein associations
-
Xu D., Lin S.L., Nussinov R. Protein binding versus-protein folding the role of hydrophilic bridges in protein associations. J. Mol. Biol. 265:1997;68-84
-
(1997)
J. Mol. Biol.
, vol.265
, pp. 68-84
-
-
Xu, D.1
Lin, S.L.2
Nussinov, R.3
-
95
-
-
0027231258
-
On the pH dependence of protein stability
-
Yang A.-S., Honig B. On the pH dependence of protein stability. J. Mol. Biol. 231:1993;459-474
-
(1993)
J. Mol. Biol.
, vol.231
, pp. 459-474
-
-
Yang, A.-S.1
Honig, B.2
-
96
-
-
0030925636
-
The role of context on α-helix stabilization: Host-guest analysis in a mixed background peptide model
-
Yang J., Spek E.J., Gong Y., Zhou H., Kallenbach N.R. The role of context on α-helix stabilization Host-guest analysis in a mixed background peptide model. Protein Sci. 6:1997;1264-1272
-
(1997)
Protein Sci.
, vol.6
, pp. 1264-1272
-
-
Yang, J.1
Spek, E.J.2
Gong, Y.3
Zhou, H.4
Kallenbach, N.R.5
-
97
-
-
13244249836
-
The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures
-
Yip K.S.P., Stillman T.J., Britton K.L., Artymiuk P.J., Baker P.J., Sedelnikova S.E., Engel P.C., Pasquo A., Chiaraluce R., Consalvi V., Scandurra R., Rice D.W. The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure. 3:1995;1147-1158
-
(1995)
Structure
, vol.3
, pp. 1147-1158
-
-
Yip, K.S.P.1
Stillman, T.J.2
Britton, K.L.3
Artymiuk, P.J.4
Baker, P.J.5
Sedelnikova, S.E.6
Engel, P.C.7
Pasquo, A.8
Chiaraluce, R.9
Consalvi, V.10
Scandurra, R.11
Rice, D.W.12
-
99
-
-
0029919676
-
Ion pairs significantly stabilize coiled-coils in the absence of electrolyte
-
Yu Y., Monera O.D., Hodges R.S., Privalov P.L. Ion pairs significantly stabilize coiled-coils in the absence of electrolyte. J. Mol. Biol. 255:1996;367-372
-
(1996)
J. Mol. Biol.
, vol.255
, pp. 367-372
-
-
Yu, Y.1
Monera, O.D.2
Hodges, R.S.3
Privalov, P.L.4
-
100
-
-
0030769231
-
Oligomerization properties of GCN4 leucine zipper e and g position mutants
-
Zeng X., Zhu H., Lashuel H.A., Hu J.C. Oligomerization properties of GCN4 leucine zipper e and g position mutants. Protein Sci. 6:1997;2218-2226
-
(1997)
Protein Sci.
, vol.6
, pp. 2218-2226
-
-
Zeng, X.1
Zhu, H.2
Lashuel, H.A.3
Hu, J.C.4
-
101
-
-
0026795513
-
Synthetic model proteins: Positional effects of interchain hydrophobic interactions on stability of two-stranded α-helical coiled-coils
-
Zhou N.E., Kay C.M., Hodges R.S. Synthetic model proteins positional effects of interchain hydrophobic interactions on stability of two-stranded α-helical coiled-coils. J. Biol. Chem. 267:1992;2664-2670
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 2664-2670
-
-
Zhou, N.E.1
Kay, C.M.2
Hodges, R.S.3
-
102
-
-
0026650710
-
Synthetic model proteins: The relative contribution of leucine residues at the non-equivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded α-helical coiled-coil
-
Zhou N.E., Kay C.M., Hodges R.S. Synthetic model proteins the relative contribution of leucine residues at the non-equivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded α-helical coiled-coil. Biochemistry. 31:1992;5739-5746
-
(1992)
Biochemistry
, vol.31
, pp. 5739-5746
-
-
Zhou, N.E.1
Kay, C.M.2
Hodges, R.S.3
-
103
-
-
0026609553
-
The two-stranded α-helical coiled-coil is an ideal model for studying protein stability and subunit interactions
-
Zhou N.E., Zhu B.-Y., Kay C.M., Hodges R.S. The two-stranded α-helical coiled-coil is an ideal model for studying protein stability and subunit interactions. Biopolymers. 32:1992;419-426
-
(1992)
Biopolymers
, vol.32
, pp. 419-426
-
-
Zhou, N.E.1
Zhu, B.-Y.2
Kay, C.M.3
Hodges, R.S.4
-
104
-
-
0027480940
-
Disulfide bond contribution to protein stability: Positional effects of substitution in the hydrophobic core of the two-stranded α-helical coiled-coil
-
Zhou N.E., Kay C.M., Hodges R.S. Disulfide bond contribution to protein stability positional effects of substitution in the hydrophobic core of the two-stranded α-helical coiled-coil. Biochemistry. 32:1993;3178-3187
-
(1993)
Biochemistry
, vol.32
, pp. 3178-3187
-
-
Zhou, N.E.1
Kay, C.M.2
Hodges, R.S.3
-
105
-
-
0027949381
-
The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability
-
Zhou N.E., Kay C.M., Hodges R.S. The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability. Protein Eng. 7:1994;1365-1372
-
(1994)
Protein Eng.
, vol.7
, pp. 1365-1372
-
-
Zhou, N.E.1
Kay, C.M.2
Hodges, R.S.3
-
106
-
-
0028364239
-
The role of interhelical ionic interactions in controlling protein folding and stability: De novo designed synthetic two-stranded α-helical coiled-coils
-
Zhou N.E., Kay C.M., Hodges R.S. The role of interhelical ionic interactions in controlling protein folding and stability de novo designed synthetic two-stranded α-helical coiled-coils. J. Mol. Biol. 237:1994;500-512
-
(1994)
J. Mol. Biol.
, vol.237
, pp. 500-512
-
-
Zhou, N.E.1
Kay, C.M.2
Hodges, R.S.3
-
107
-
-
0027995873
-
α-Helical propensities of amino acids in the hydrophobic face of an amphipathic α-helix
-
Zhou N.E., Monera O.D., Kay C.M., Hodges R.S. α-Helical propensities of amino acids in the hydrophobic face of an amphipathic α-helix. Protein Pept. Letters. 1:1994;114-119
-
(1994)
Protein Pept. Letters
, vol.1
, pp. 114-119
-
-
Zhou, N.E.1
Monera, O.D.2
Kay, C.M.3
Hodges, R.S.4
-
108
-
-
0027475082
-
Packing and hydrophobicity effects on protein folding and stability: Effects of β-branched amino acids, valine and isoleucine, on the formation and stability of two-stranded α-helical coiled-coils/leucine zippers
-
Zhu B.Y., Zhou N.E., Kay C.M., Hodges R.S. Packing and hydrophobicity effects on protein folding and stability effects of β-branched amino acids, valine and isoleucine, on the formation and stability of two-stranded α-helical coiled-coils/leucine zippers. Protein Sci. 2:1993;383-394
-
(1993)
Protein Sci.
, vol.2
, pp. 383-394
-
-
Zhu, B.Y.1
Zhou, N.E.2
Kay, C.M.3
Hodges, R.S.4
|