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):
1092 articles | Pages:
Protein structure: what is it possible to predict now?
Alexei V Finkelstein Current Opinion in Structural Biology 7 (1) 60 (1997) https://doi.org/10.1016/S0959-440X(97)80008-5
From Levinthal to pathways to funnels
Ken A. Dill and Hue Sun Chan Nature Structural & Molecular Biology 4 (1) 10 (1997) https://doi.org/10.1038/nsb0197-10
Geometrical effects on folding of macromolecules
A. Caliri and M. A. A. da Silva The Journal of Chemical Physics 106 (18) 7856 (1997) https://doi.org/10.1063/1.473744
Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude
Mary Munson, Karen S. Anderson and Lynne Regan Folding and Design 2 (1) 77 (1997) https://doi.org/10.1016/S1359-0278(97)00008-4
Progress in Nucleic Acid Research and Molecular Biology
Peter Bross, Brage S. Andresen and Niels Gregersen Progress in Nucleic Acid Research and Molecular Biology 58 301 (1997) https://doi.org/10.1016/S0079-6603(08)60040-9
Functional rapidly folding proteins from simplified amino acid sequences
David S. Riddle, Jed V. Santiago, Susan T. Bray-Hall, et al. Nature Structural Biology 4 (10) 805 (1997) https://doi.org/10.1038/nsb1097-805
A heteropolymer model study for the mechanism of protein folding
Masataka Fukugita, David Lancaster and Mark G. Mitchard Biopolymers 41 (3) 239 (1997) https://doi.org/10.1002/(SICI)1097-0282(199703)41:3<239::AID-BIP1>3.0.CO;2-T
Consistency in structural energetics of protein folding and peptide recognition
Chao Zhang, James L. Cornette and Charles Delisi Protein Science 6 (5) 1057 (1997) https://doi.org/10.1002/pro.5560060512
The application of circular dichroism to studies of protein folding and unfolding
Sharon M Kelly and Nicholas C Price Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1338 (2) 161 (1997) https://doi.org/10.1016/S0167-4838(96)00190-2
Evolution of the folding ability of proteins through functional selection
Seiji Saito, Masaki Sasai and Tetsuya Yomo Proceedings of the National Academy of Sciences 94 (21) 11324 (1997) https://doi.org/10.1073/pnas.94.21.11324
Relaxational Dynamics of a Random Heteropolymer
Christine Villeneuve, Hong Guo and Martin J. Zuckermann Macromolecules 30 (10) 3066 (1997) https://doi.org/10.1021/ma961162b
"New View" of Protein Folding Reconciled with the Old Through Multiple Unfolding Simulations
Themis Lazaridis and Martin Karplus Science 278 (5345) 1928 (1997) https://doi.org/10.1126/science.278.5345.1928
Characteristic temperatures of folding of a small peptide
Ulrich H. E. Hansmann, Masato Masuya and Yuko Okamoto Proceedings of the National Academy of Sciences 94 (20) 10652 (1997) https://doi.org/10.1073/pnas.94.20.10652
Fluorescence Spectral Changes During the Folding of Intestinal Fatty Acid Binding Protein
Ira J. Ropson and Paula M. Dalessio Biochemistry 36 (28) 8594 (1997) https://doi.org/10.1021/bi962983b
Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold
Alexei V Finkelstein and Azat Ya Badretdinov Folding and Design 2 (2) 115 (1997) https://doi.org/10.1016/S1359-0278(97)00016-3
Dynamics of polyglutamic acids in α-helical and coil states. Comparison with dynamics of some globular proteins. Rayleigh scattering of Mössbauer radiation (RSMR) data
Yu. F. Krupyanskii, I. V. Kurinov, S. A. Kuznetsov, G. V. Eshenko and F. Parak Il Nuovo Cimento D 18 (2-3) 365 (1996) https://doi.org/10.1007/BF02458919
RNA tectonics: towards RNA design
Eric Westhof, Benoît Masquida and Luc Jaeger Folding and Design 1 (4) R78 (1996) https://doi.org/10.1016/S1359-0278(96)00037-5
How do proteins acquire their three-dimensional structure and stability?
Rainer Jaenicke Naturwissenschaften 83 (12) 544 (1996) https://doi.org/10.1007/BF01141979
Progress in Nucleic Acid Research and Molecular Biology
N.A. Kolchanov, I.I. Titov, I.E. Vlassova and V.V. Vlassov Progress in Nucleic Acid Research and Molecular Biology 53 131 (1996) https://doi.org/10.1016/S0079-6603(08)60144-0
The problem of protein folding and dynamics: time-resolved dynamic nonradiative excitation energy transfer measurements
E. Haas IEEE Journal of Selected Topics in Quantum Electronics 2 (4) 1088 (1996) https://doi.org/10.1109/2944.577340
Contact interactions method: A new algorithm for protein folding simulations
Lucio Toma and Salvatore Toma Protein Science 5 (1) 147 (1996) https://doi.org/10.1002/pro.5560050118
Universality and diversity of the protein folding scenarios:a comprehensive analysis with the aid of a lattice model
Leonid A Mirny, Victor Abkevich and Eugene I Shakhnovich Folding and Design 1 (2) 103 (1996) https://doi.org/10.1016/S1359-0278(96)00019-3
Thermodynamic Cycles as Probes of Structure in Unfolded Proteins,
William A. McGee, Frederico I. Rosell, John R. Liggins, et al. Biochemistry 35 (6) 1995 (1996) https://doi.org/10.1021/bi951228f
Protein Folding Dynamics: Application of the Diffusion-Collision Model to the Folding of a Four-Helix Bundle
Kanthi K. Yapa and David L. Weaver The Journal of Physical Chemistry 100 (7) 2498 (1996) https://doi.org/10.1021/jp952543e
Bioinformatics
Erich Bornberg-Bauer Lecture Notes in Computer Science, Bioinformatics 1278 125 (1996) https://doi.org/10.1007/BFb0033211
A Monte Carlo simulation study on the collapse transition of model polymers: Possible solvent effect and relevance to protein folding
Srikanta Sen The Journal of Chemical Physics 104 (13) 5304 (1996) https://doi.org/10.1063/1.471259
Refolding of Thermally and Urea-Denatured Ribonuclease A Monitored by Time-Resolved FTIR Spectroscopy
Diane Reinstädler, Heinz Fabian, Jan Backmann and Dieter Naumann Biochemistry 35 (49) 15822 (1996) https://doi.org/10.1021/bi961810j
Magnesium-aided folding of group I ribozymes with a minimal loss of entropy
Ariel Fernández and Gustavo Appignanesi Biophysical Chemistry 61 (1) 51 (1996) https://doi.org/10.1016/0301-4622(96)02190-4
Circular Dichroism and the Conformational Analysis of Biomolecules
Robert W. Woody and A. Keith Dunker Circular Dichroism and the Conformational Analysis of Biomolecules 109 (1996) https://doi.org/10.1007/978-1-4757-2508-7_4
Molecular collapse: The rate-limiting step in two-state cytochrome c folding
Tobin R. Sosnick, Leland Mayne and S. Water Englander Proteins: Structure, Function, and Genetics 24 (4) 413 (1996) https://doi.org/10.1002/(SICI)1097-0134(199604)24:4<413::AID-PROT1>3.0.CO;2-F
Protein folding for realists: A timeless phenomenon
David Shortle, Yi Wang, Joel R. Gillespie and James O. Wrabl Protein Science 5 (6) 991 (1996) https://doi.org/10.1002/pro.5560050602
34 209 (1996) https://doi.org/10.1016/S0070-2137(96)80008-2
Different folding transition states may result in the same native structure
Ana Rosa Viguera, Luis Serrano and Matthias Wilmanns Nature Structural & Molecular Biology 3 (10) 874 (1996) https://doi.org/10.1038/nsb1096-874
Changing the Transition State for Protein (Un)folding
Donald F. Doyle, Jennifer C. Waldner, Sudip Parikh, Luis Alcazar-Roman and Gary J. Pielak Biochemistry 35 (23) 7403 (1996) https://doi.org/10.1021/bi960409u
Catalysis of a protein folding reaction: Mechanistic implications of the 2.0 .ANG. structure of the subtilisin-prodomain complex
Philip Bryan, Lan Wang, Joel Hoskins, Sergei Ruvinov, Susan Strausberg, Patrick Alexander, Orna Almog, Gary Gilliland and Travis Gallagher Biochemistry 34 (32) 10310 (1995) https://doi.org/10.1021/bi00032a026
The complexity and accuracy of discrete state models of protein structure
Britt H. Park and Michael Levitt Journal of Molecular Biology 249 (2) 493 (1995) https://doi.org/10.1006/jmbi.1995.0311
Protein Folding Intermediates: Native-State Hydrogen Exchange
Yawen Bai, Tobin R. Sosnick, Leland Mayne and S. Walter Englander Science 269 (5221) 192 (1995) https://doi.org/10.1126/science.7618079
Finding the right fold
Christopher M. Dobson Nature Structural Biology 2 (7) 513 (1995) https://doi.org/10.1038/nsb0795-513
Template-Directed Protein Folding into a Metastable State of Increased Activity
Peter Flecker European Journal of Biochemistry 232 (2) 528 (1995) https://doi.org/10.1111/j.1432-1033.1995.tb20840.x
LINUS: A hierarchic procedure to predict the fold of a protein
Rajgopal Srinivasan and George D. Rose Proteins: Structure, Function, and Bioinformatics 22 (2) 81 (1995) https://doi.org/10.1002/prot.340220202
Simulation of protein-folding pathways: lost in (conformational) space?
David A. Hinds and Michael Levitt Trends in Biotechnology 13 (1) 23 (1995) https://doi.org/10.1016/S0167-7799(00)88897-6
Determination of the conformation of folding initiation sites in proteins by computer simulation
Franc Avbelj and John Moult Proteins: Structure, Function, and Bioinformatics 23 (2) 129 (1995) https://doi.org/10.1002/prot.340230203
Bipartite structure of the α-lactalbumin molten globule
Lawren C. Wu, Zheng-yu Peng and Peter S. Kim Nature Structural & Molecular Biology 2 (4) 281 (1995) https://doi.org/10.1038/nsb0495-281
Principles of protein folding — A perspective from simple exact models
Ken A. Dill, Sarina Bromberg, Kaizhi Yue, Hue Sun Chan, Klaus M. Fiebig, David P. Yee and Paul D. Thomas Protein Science 4 (4) 561 (1995) https://doi.org/10.1002/pro.5560040401
Nonlocal Interactions Stabilize Long Range Loops in the Initial Folding Intermediates of Reduced Bovine Pancreatic Trypsin Inhibitor
Varda Ittah and Elisha Haas Biochemistry 34 (13) 4493 (1995) https://doi.org/10.1021/bi00013a042
Template-Directed Protein Folding into a Metastable State of Increased Activity
Peter Flecker European Journal of Biochemistry 232 (2) 528 (1995) https://doi.org/10.1111/j.1432-1033.1995.528zz.x
Ab initio structure prediction for small polypeptides and protein fragments using genetic algorithms
Jan T. Pedersen and John Moult Proteins: Structure, Function, and Bioinformatics 23 (3) 454 (1995) https://doi.org/10.1002/prot.340230319
Investigation of the folding pathway of the TEM‐1 β‐lactamase
Marc Vanhove, Xavier Raquet and Jean‐Marie Frère Proteins: Structure, Function, and Bioinformatics 22 (2) 110 (1995) https://doi.org/10.1002/prot.340220204
Kinetic Characterization of the Chemotactic Protein from Escherichia coli, CheY. Kinetic Analysis of the Inverse Hydrophobic Effect
Victor Munoz, Eva M. Lopez, Markus Jager and Luis Serrano Biochemistry 33 (19) 5858 (1994) https://doi.org/10.1021/bi00185a025
Phase transitions in heteropolymers with ‘‘secondary structure’’
G. Z. Archontis and E. I. Shakhnovich Physical Review E 49 (4) 3109 (1994) https://doi.org/10.1103/PhysRevE.49.3109
Exploring conformational space with a simple lattice model for protein structure
David A. Hinds and Michael Levitt Journal of Molecular Biology 243 (4) 668 (1994) https://doi.org/10.1016/0022-2836(94)90040-X
Kinetics versus Thermodynamics in Protein Folding
David Baker and David A. Agard Biochemistry 33 (24) 7505 (1994) https://doi.org/10.1021/bi00190a002
Molten globular characteristics of the native state of apomyoglobin
Laura Lin, Rachel J. Pinker, Kirk Forde, George D. Rose and Neville R. Kallenbach Nature Structural & Molecular Biology 1 (7) 447 (1994) https://doi.org/10.1038/nsb0794-447
Transition states and folding dynamics of proteins and heteropolymers
Hue Sun Chan and Ken A. Dill The Journal of Chemical Physics 100 (12) 9238 (1994) https://doi.org/10.1063/1.466677
Implications of the random characteristics of protein sequences for their three-dimensional structure
Alexei V. Finkelstein Current Opinion in Structural Biology 4 (3) 422 (1994) https://doi.org/10.1016/S0959-440X(94)90112-0
Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
Luke M. Rice and Axel T. BrüNger Proteins: Structure, Function, and Bioinformatics 19 (4) 277 (1994) https://doi.org/10.1002/prot.340190403
J. Thomas Ngo, Joe Marks and Martin Karplus 433 (1994) https://doi.org/10.1007/978-1-4684-6831-1_14
A measure on the space of polymer folding pathways: Preliminaries for a new scheme of statistical inference
Ariel Fernández Journal of Statistical Physics 77 (5-6) 1079 (1994) https://doi.org/10.1007/BF02183153
Structure–Function Properties of Food Proteins
Structure–Function Properties of Food Proteins 251 (1994) https://doi.org/10.1016/B978-0-12-554360-6.50018-8
Solvent‐induced organization: A physical model of folding myoglobin
David J. E. Callaway Proteins: Structure, Function, and Bioinformatics 20 (2) 124 (1994) https://doi.org/10.1002/prot.340200203
Protein folding dynamics: The diffusion‐collision model and experimental data
Martin Karplus and David L. Weaver Protein Science 3 (4) 650 (1994) https://doi.org/10.1002/pro.5560030413
Understanding how proteins fold: the lysozyme story so far
Christopher M. Dobson, Philip A. Evans and Sheena E. Radford Trends in Biochemical Sciences 19 (1) 31 (1994) https://doi.org/10.1016/0968-0004(94)90171-6
Monte carlo simulations of protein folding. I. Lattice model and interaction scheme
Andrzej Kolinski and Jeffrey Skolnick Proteins: Structure, Function, and Bioinformatics 18 (4) 338 (1994) https://doi.org/10.1002/prot.340180405
Ascribing weights to folding histories: explaining the expediency of biopolymer folding
A Fernandez Journal of Physics A: Mathematical and General 27 (18) 6039 (1994) https://doi.org/10.1088/0305-4470/27/18/014
Matching speed and stability
Robert L. Baldwin Nature 369 (6477) 183 (1994) https://doi.org/10.1038/369183a0
Protein Folding: Solid evidence for molten globules
Christopher M. Dobson Current Biology 4 (7) 636 (1994) https://doi.org/10.1016/S0960-9822(00)00141-X
Statistical Mechanics, Protein Structure, and Protein Substrate Interactions
Robert L. Baldwin NATO ASI Series, Statistical Mechanics, Protein Structure, and Protein Substrate Interactions 325 1 (1994) https://doi.org/10.1007/978-1-4899-1349-4_1
Finding intermediates in protein folding
Robert L. Baldwin BioEssays 16 (3) 207 (1994) https://doi.org/10.1002/bies.950160312
NMR Solution Structure of the C-Terminal Fragment 255-316 of Thermolysin: A Dimer Formed by Subunits Having the Native Structure
Manuel Rico, M. Angeles Jimenez, Carlos Gonzalez, Vincenzo De Filippis and Angelo Fontana Biochemistry 33 (49) 14834 (1994) https://doi.org/10.1021/bi00253a023
Three-State Thermodynamic Analysis of the Denaturation of Staphylococcal Nuclease Mutants
John H. Carra, Elizabeth A. Anderson and Peter L. Privalov Biochemistry 33 (35) 10842 (1994) https://doi.org/10.1021/bi00201a035
Structural argument for N‐terminal initiation of protein folding
Nickolai Alexandrov Protein Science 2 (11) 1989 (1993) https://doi.org/10.1002/pro.5560021121
Folding of subtilisin BPN': characterization of a folding intermediate
Jorg Eder, Michael Rheinnecker and Alan R. Fersht Biochemistry 32 (1) 18 (1993) https://doi.org/10.1021/bi00052a004
1H‐ and 15N‐NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein
Marta BRUIX, Jaime PASCUAL, Jorge SANTORO, Jesús PRIETO, Luis SERRANO and Manuel RICO European Journal of Biochemistry 215 (3) 573 (1993) https://doi.org/10.1111/j.1432-1033.1993.tb18068.x
Towards protein folding by global energy optimization
Ruben A. Abagyan FEBS Letters 325 (1-2) 17 (1993) https://doi.org/10.1016/0014-5793(93)81406-P
Cold denaturation of yeast phosphoglycerate kinase: Kinetics of changes in secondary structure and compactness on unfolding and refolding
Klaus Gast, Gregor Damaschun, Hilde Damaschun, Rolf Misselwitz and Dietrich Zirwer Biochemistry 32 (30) 7747 (1993) https://doi.org/10.1021/bi00081a020
Fluorescence study of conformational flexibility of RNase S-peptide: Distance-distribution, end-to-end diffusion, and anisotropy decays
B. P. Maliwal, J. R. Lakowicz, G. Kupryszewski and P. Rekowski Biochemistry 32 (46) 12337 (1993) https://doi.org/10.1021/bi00097a009
Thermodynamic analysis of the chemotactic protein from Escherichia coli, CheY
Vladimir V. Filimonov, Jesus Prieto, Jose C. Martinez, Marta Bruix, Pedro L. Mateo and Luis Serrano Biochemistry 32 (47) 12906 (1993) https://doi.org/10.1021/bi00210a045
Rationally designing the accumulation of a folding intermediate of barnase by protein engineering
Jesus M. Sanz and Alan R. Fersht Biochemistry 32 (49) 13584 (1993) https://doi.org/10.1021/bi00212a026
The Protein Folding Problem
Hue Sun Chan and Ken A. Dill Physics Today 46 (2) 24 (1993) https://doi.org/10.1063/1.881371
Structural energetics of the molten globule state
Donald T. Haynie and Ernesto Freire Proteins: Structure, Function, and Bioinformatics 16 (2) 115 (1993) https://doi.org/10.1002/prot.340160202
Protein core assembly processes
Klaus M. Fiebig and Ken A. Dill The Journal of Chemical Physics 98 (4) 3475 (1993) https://doi.org/10.1063/1.464068
Protein folding: Structure prediction and statistical mechanics
Masataka Fukugita Nuclear Physics B - Proceedings Supplements 30 159 (1993) https://doi.org/10.1016/0920-5632(93)90185-9
Computational challenges for macromolecular structure determination by X-ray crystallography and solution NMRspectroscopy
Axel T. Brünger and Michael Nilges Quarterly Reviews of Biophysics 26 (1) 49 (1993) https://doi.org/10.1017/S0033583500003966
Detection of intermediate protein conformations by room temperature tryptophan phosphorescence spectroscopy during denaturation of Escherichia coli alkaline phosphatase
Joseph V. Mersol, Duncan G. Steel and Ari Gafni Biophysical Chemistry 48 (2) 281 (1993) https://doi.org/10.1016/0301-4622(93)85015-A
Folding proteins: finding a needle in a haystack
Ken A. Dill Current Opinion in Structural Biology 3 (1) 99 (1993) https://doi.org/10.1016/0959-440X(93)90208-3
Structural relationships of homologous proteins as a fundamental principle in homology modeling
Martina Hilbert, Gerald Böhm and Rainer Jaenicke Proteins: Structure, Function, and Bioinformatics 17 (2) 138 (1993) https://doi.org/10.1002/prot.340170204
Comparison of the hemocyanin β‐barrel with other greek key β‐barrels: Possible importance of the “β‐zipper” in protein structure and folding
Bart Hazes and Wim G. J. Hol Proteins: Structure, Function, and Bioinformatics 12 (3) 278 (1992) https://doi.org/10.1002/prot.340120306
The folding of an enzyme
Andreas Matouschek, Luis Serrano and Alan R. Fersht Journal of Molecular Biology 224 (3) 819 (1992) https://doi.org/10.1016/0022-2836(92)90564-Z
The dead-end elimination theorem and its use in protein side-chain positioning
Johan Desmet, Marc De Maeyer, Bart Hazes and Ignace Lasters Nature 356 (6369) 539 (1992) https://doi.org/10.1038/356539a0
Up the kinetic pathway
T. E. Creighton Nature 356 (6366) 194 (1992) https://doi.org/10.1038/356194a0
Structural comparison of apomyoglobin and metaquomyoglobin: pH titration of histidines by NMR spectroscopy
Melanie J. Cocco, Yung Hsiang Kao, Allen T. Phillips and Juliette T. J. Lecomte Biochemistry 31 (28) 6481 (1992) https://doi.org/10.1021/bi00143a018
The folding of an enzyme
Luis Serrano, Andreas Matouschek and Alan R. Fersht Journal of Molecular Biology 224 (3) 847 (1992) https://doi.org/10.1016/0022-2836(92)90566-3
Folding kinetics of proteins and copolymers
Robert Miller, Craig A. Danko, Michael J. Fasolka, Anna C. Balazs, Hue Sun Chan and Ken A. Dill The Journal of Chemical Physics 96 (1) 768 (1992) https://doi.org/10.1063/1.462462
The nature of folded states of globular proteins
J. D. Honeycutt and D. Thirumalai Biopolymers 32 (6) 695 (1992) https://doi.org/10.1002/bip.360320610
Protein folding bottlenecks: A lattice Monte Carlo simulation
E. Shakhnovich, G. Farztdinov, A. M. Gutin and M. Karplus Physical Review Letters 67 (12) 1665 (1991) https://doi.org/10.1103/PhysRevLett.67.1665
The Energy Landscapes and Motions of Proteins
Hans Frauenfelder, Stephen G. Sligar and Peter G. Wolynes Science 254 (5038) 1598 (1991) https://doi.org/10.1126/science.1749933
Stable submolecular folding units in a non-compact form of cytochrome c
Mei-Fen Jeng and S.Walter Englander Journal of Molecular Biology 221 (3) 1045 (1991) https://doi.org/10.1016/0022-2836(91)80191-V
Protein stability and molecular adaptation to extreme conditons
Rainer JAENICKE European Journal of Biochemistry 202 (3) 715 (1991) https://doi.org/10.1111/j.1432-1033.1991.tb16426.x
EJB Reviews 1991
Rainer Jaenicke EJB Reviews 1991 291 (1991) https://doi.org/10.1007/978-3-642-77200-9_22
Mapping transition states of protein unfolding by protein engineering of ligand-binding sites
Javier Sancho, Elizabeth M. Meiering and Alan R. Fersht Journal of Molecular Biology 221 (3) 1007 (1991) https://doi.org/10.1016/0022-2836(91)80188-Z
Pages:
901 to 1000 of 1092 articles