The Citing articles tool gives a list of articles citing the current article. The citing articles come from EDP Sciences database, as well as other publishers participating in CrossRef Cited-by Linking Program . You can set up your personal account to receive an email alert each time this article is cited by a new article (see the menu on the right-hand side of the abstract page).
Cited article:
Cyrus Levinthal
J. Chim. Phys., 65 (1968) 44-45
Published online: 2017-05-28
This article has been cited by the following article(s):
1063 articles | Pages:
Photophysical and Photochemical Tools in Polymer Science
Elisha Haas Photophysical and Photochemical Tools in Polymer Science 325 (1986) https://doi.org/10.1007/978-94-009-4726-9_14
Native or nativelike species are transient intermediates in folding of alkaline iso-2 cytochrome c
Barry T. Nall Biochemistry 25 (10) 2974 (1986) https://doi.org/10.1021/bi00358a036
Enzyme Structure Part K
Mollie Pflumm, Jeremy Luchins and Sherman Beychok Methods in Enzymology, Enzyme Structure Part K 130 519 (1986) https://doi.org/10.1016/0076-6879(86)30024-7
Theory for the folding and stability of globular proteins
Ken A. Dill Biochemistry 24 (6) 1501 (1985) https://doi.org/10.1021/bi00327a032
Energetics of protein structure and folding
David P. Goldenberg and Thomas E. Creighton Biopolymers 24 (1) 167 (1985) https://doi.org/10.1002/bip.360240114
Folding of thermolysin fragments
Daniele Dalzoppo, Claudio Vita and Angelo Fontana Journal of Molecular Biology 182 (2) 331 (1985) https://doi.org/10.1016/0022-2836(85)90349-3
The Impact of Protein Chemistry on the Biomedical Sciences
HIROSHI TANIUCHI The Impact of Protein Chemistry on the Biomedical Sciences 67 (1984) https://doi.org/10.1016/B978-0-12-622780-2.50013-4
Biopolymers
D A D Parry and E N Baker Reports on Progress in Physics 47 (9) 1133 (1984) https://doi.org/10.1088/0034-4885/47/9/002
Protein Folding and Protein Association
Rainer Jaenicke Angewandte Chemie International Edition in English 23 (6) 395 (1984) https://doi.org/10.1002/anie.198403953
The Formation of Three‐Dimensional Biological Structures
CYRUS LEVINTHAL Annals of the New York Academy of Sciences 426 (1) 171 (1984) https://doi.org/10.1111/j.1749-6632.1984.tb16519.x
Proteinfaltung und Proteinassoziation
Rainer Jaenicke Angewandte Chemie 96 (6) 385 (1984) https://doi.org/10.1002/ange.19840960604
Evolutionary conservation and variation of protein folding pathways
Michelle Hollecker and Thomas E. Creighton Journal of Molecular Biology 168 (2) 409 (1983) https://doi.org/10.1016/S0022-2836(83)80026-6
Protein folding by restrained energy minimization and molecular dynamics
Michael Levitt Journal of Molecular Biology 170 (3) 723 (1983) https://doi.org/10.1016/S0022-2836(83)80129-6
Biological Oxidations
R. Jaenicke and R. Rudolph Biological Oxidations 62 (1983) https://doi.org/10.1007/978-3-642-69467-7_4
Protein Folding
Protein Folding 522 (1982) https://doi.org/10.1016/B978-0-12-281520-1.50022-6
Assembly of adenovirus major capsid protein is mediated by a nonvirion protein
Constance L. Cepko and Phillip A. Sharp Cell 31 (2) 407 (1982) https://doi.org/10.1016/0092-8674(82)90134-9
Equilibrium folding and unfolding pathways for a model protein
S. Miyazawa and R. L. Jernigan Biopolymers 21 (7) 1333 (1982) https://doi.org/10.1002/bip.360210706
Folding and association of proteins
R. Jaenicke Biophysics of Structure and Mechanism 8 (4) 231 (1982) https://doi.org/10.1007/BF00537204
Folding domains as functional tools in allosteric systems: a heme-dependent domain in hemoglobin .beta. subunits
Dionigio Franchi, Clara Fronticelli and Enrico Bucci Biochemistry 21 (24) 6181 (1982) https://doi.org/10.1021/bi00267a024
Biomolecular Structure, Conformation, Function, and Evolution
A.A. RASHIN Biomolecular Structure, Conformation, Function, and Evolution 133 (1981) https://doi.org/10.1016/B978-1-4832-8364-7.50070-2
Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein
David P. Goldenberg and Jonathan King Journal of Molecular Biology 145 (4) 633 (1981) https://doi.org/10.1016/0022-2836(81)90307-7
Advances in Protein Chemistry Volume 34
Jane S. Richardson Advances in Protein Chemistry, Advances in Protein Chemistry Volume 34 34 167 (1981) https://doi.org/10.1016/S0065-3233(08)60520-3
Biomolecular Structure, Conformation, Function, and Evolution
O.B. PTITSYN and A.V. FINKELSTEIN Biomolecular Structure, Conformation, Function, and Evolution 119 (1981) https://doi.org/10.1016/B978-1-4832-8364-7.50015-5
Biological Regulation and Development
Kenneth A. Thomas and Alan N. Schechter Biological Regulation and Development 43 (1980) https://doi.org/10.1007/978-1-4684-9933-9_2
Kinetic study of protein unfolding and refolding using urea gradient electrophoresis
Thomas E. Creighton Journal of Molecular Biology 137 (1) 61 (1980) https://doi.org/10.1016/0022-2836(80)90157-6
Logical analysis of the mechanism of protein folding
Kozo Nagano Journal of Molecular Biology 138 (4) 797 (1980) https://doi.org/10.1016/0022-2836(80)90066-2
Ultraviolet difference spectroscopy of intermediates trapped in unfolding and refolding of bovine pancreatic trypsin inhibitor
Phyllis Anne Kosen, Thomas E. Creighton and Elkan R. Blout Biochemistry 19 (21) 4936 (1980) https://doi.org/10.1021/bi00562a037
Optically detected magnetic resonance of tryptophan triplet states in native and urea-denatured proteins and polypeptides
J. B. Alexander Ross, K. W. Rousslang and A. L. Kwiram Biochemistry 19 (5) 876 (1980) https://doi.org/10.1021/bi00546a008
On the prediction of protein structure: The significance of the root-mean-square deviation
Fred E. Cohen and Michael J.E. Sternberg Journal of Molecular Biology 138 (2) 321 (1980) https://doi.org/10.1016/0022-2836(80)90289-2
Experimental studies of protein folding and unfolding
Thomas E. Creighton Progress in Biophysics and Molecular Biology 33 231 (1979) https://doi.org/10.1016/0079-6107(79)90030-0
Mechanism of protein folding
O. B. Ptitsyn and A. V. Finkelstein International Journal of Quantum Chemistry 16 (3) 407 (1979) https://doi.org/10.1002/qua.560160302
Hierarchic organization of domains in globular proteins
George D. Rose Journal of Molecular Biology 134 (3) 447 (1979) https://doi.org/10.1016/0022-2836(79)90363-2
Refolding of bovine trypsinogen with one and two disulfide bonds reduced and carboxymethylated.
A. Light and T.W. Odorzynski Journal of Biological Chemistry 254 (18) 9162 (1979) https://doi.org/10.1016/S0021-9258(19)86825-4
Advances in Protein Chemistry Volume 33
P.L. Privalov Advances in Protein Chemistry, Advances in Protein Chemistry Volume 33 33 167 (1979) https://doi.org/10.1016/S0065-3233(08)60460-X
Early steps in the refolding reaction of reduced ribonuclease A
Jean-Renaud Garel Journal of Molecular Biology 118 (3) 331 (1978) https://doi.org/10.1016/0022-2836(78)90232-2
Some aspects of protein folding
Jeannine M. Yon Biochimie 60 (6-7) 581 (1978) https://doi.org/10.1016/S0300-9084(78)80776-7
Prediction of protein structure from amino acid sequence
Michael J. E. Sternberg and Janet M. Thornton Nature 271 (5640) 15 (1978) https://doi.org/10.1038/271015a0
Statistical Mechanical Theory of the Protein Conformation. II. Folding Pathway for Protein
Hiroshi Wako and Nobuhiko Saitô Journal of the Physical Society of Japan 44 (6) 1939 (1978) https://doi.org/10.1143/JPSJ.44.1939
Conformation of amino acid side-chains in proteins
Joël Janin, Shoshanna Wodak, Michael Levitt and Bernard Maigret Journal of Molecular Biology 125 (3) 357 (1978) https://doi.org/10.1016/0022-2836(78)90408-4
Folding and association of oligomeric enzymes
Rainer Jaenicke Naturwissenschaften 65 (11) 569 (1978) https://doi.org/10.1007/BF00364906
Mechanisms of the multiphasic kinetics in the folding and unfolding of globular proteins
Minoru I. Kanehisa and Tian Yow Tsong Journal of Molecular Biology 124 (1) 177 (1978) https://doi.org/10.1016/0022-2836(78)90155-9
Protein folding
George Némethy and Harold A. Scheraga Quarterly Reviews of Biophysics 10 (3) 239 (1977) https://doi.org/10.1017/S0033583500002936
Conformational restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitor
Thomas E. Creighton Journal of Molecular Biology 113 (2) 275 (1977) https://doi.org/10.1016/0022-2836(77)90142-5
Theory of protein molecule self‐organization. I. Thermodynamic parameters of local secondary structures in the unfolded protein chain
A. V. Finkelstein and O. B. Ptitsyn Biopolymers 16 (3) 469 (1977) https://doi.org/10.1002/bip.1977.360160302
Immunochemistry of Proteins
A. F. S. A. Habeeb Immunochemistry of Proteins 163 (1977) https://doi.org/10.1007/978-1-4613-4190-1_2
Energetics of folding and unfolding of pancreatic trypsin inhibitor
Thomas E. Creighton Journal of Molecular Biology 113 (2) 295 (1977) https://doi.org/10.1016/0022-2836(77)90143-7
Study of RNase A mechanism and folding by means of synthetic 63-residue analogs.
B Gutte Journal of Biological Chemistry 252 (2) 663 (1977) https://doi.org/10.1016/S0021-9258(17)32770-9
A testable model for protein folding
FEBS Letters 63 (1) 10 (1976) https://doi.org/10.1016/0014-5793(76)80184-6
Protein-folding dynamics
Martin Karplus and David L. Weaver Nature 260 (5550) 404 (1976) https://doi.org/10.1038/260404a0
Randomly reoxidised soybean trypsin inhibitor and the possibility of conformational barriers to disulphide isomerization in proteins
Hilary C. Hawkins and Robert B. Freedman FEBS Letters 58 (1-2) 7 (1975) https://doi.org/10.1016/0014-5793(75)80213-4
A model of myoglobin self-organization
O.B. Ptitsyn and A.A. Rashin Biophysical Chemistry 3 (1) 1 (1975) https://doi.org/10.1016/0301-4622(75)80033-0
Advances in Protein Chemistry Volume 29
C.B. Anfinsen and H.A. Scheraga Advances in Protein Chemistry, Advances in Protein Chemistry Volume 29 29 205 (1975) https://doi.org/10.1016/S0065-3233(08)60413-1
MECHANISM OF GLUTATHIONE REGENERATION OF REDUCED PANCREATIC RIBONUCLEASE A
Stephen W. Schaffer International Journal of Peptide and Protein Research 7 (2) 179 (1975) https://doi.org/10.1111/j.1399-3011.1975.tb02430.x
Analysis of the conformation of polypeptides : the combined use of energy computations and nuclear magnetic resonance studies
George Némethy Biochimie 57 (4) 471 (1975) https://doi.org/10.1016/S0300-9084(75)80334-8
The two-disulphide intermediates and the folding pathway of reduced pancreatic trypsin inhibitor
Thomas E. Creighton Journal of Molecular Biology 95 (2) 167 (1975) https://doi.org/10.1016/0022-2836(75)90389-7
Two-Angstrom Crystal Structure of Oxidized Chromatium High Potential Iron Protein
Charles W. Carter, Joseph Kraut, Stephan T. Freer, et al. Journal of Biological Chemistry 249 (13) 4212 (1974) https://doi.org/10.1016/S0021-9258(19)42505-2
Intermediates in the refolding of reduced pancreatic trypsin inhibitor
Thomas E. Creighton Journal of Molecular Biology 87 (3) 579 (1974) https://doi.org/10.1016/0022-2836(74)90105-3
Protein Structure and Stability: Conventional Wisdom and New Perspectives
D. B. WETLAUFER Journal of Food Science 38 (5) 740 (1973) https://doi.org/10.1111/j.1365-2621.1973.tb02068.x
Evidence for nucleation in the folding of reduced hen egg lysozyme
Sandra S. Ristow and D.B. Wetlaufer Biochemical and Biophysical Research Communications 50 (2) 544 (1973) https://doi.org/10.1016/0006-291X(73)90874-7
A sequential model of nucleation-dependent protein folding: Kinetic studies of ribonuclease A
Tian Y. Tsong, Robert L. Baldwin, Peter McPhie and Elliot L. Elson Journal of Molecular Biology 63 (3) 453 (1972) https://doi.org/10.1016/0022-2836(72)90440-8
Conformational equilibria in a synthetic copolypeptide
W. B. Gratzer and G. H. Beaven Biopolymers 11 (3) 689 (1972) https://doi.org/10.1002/bip.1972.360110315
Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme
Donald B. Wetlaufer and V. P. Saxena Biochemistry 9 (25) 5015 (1970) https://doi.org/10.1021/bi00827a028
Folding of the polypeptide chain during biosynthesis
J.L. De Coen Journal of Molecular Biology 49 (2) 405 (1970) https://doi.org/10.1016/0022-2836(70)90253-6
Pages:
1001 to 1063 of 1063 articles