Are there pathways for protein folding?
J. Chim. Phys., 65 (1968) 44-45
Published online: 2017-05-28
Articles citing this article
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:
This article has been cited by the following article(s):
The Role of Chemistry Across Disciplines From Humanities to Life Sciences in Understanding Complexity and Emergence
Harald Schwalbe, Josef Wachtveitl, Alexander Heckel, Florian Buhr, Sabrina Toews and Thomas M. SchimmerAngewandte Chemie 138 (17) (2026)
https://doi.org/10.1002/ange.202523427
1496 161 (2026)
https://doi.org/10.1007/978-3-032-07511-6_6
The Role of Chemistry Across Disciplines From Humanities to Life Sciences in Understanding Complexity and Emergence
Harald Schwalbe, Josef Wachtveitl, Alexander Heckel, Florian Buhr, Sabrina Toews and Thomas M. SchimmerAngewandte Chemie International Edition 65 (17) (2026)
https://doi.org/10.1002/anie.202523427
2981 119 (2026)
https://doi.org/10.1007/978-1-0716-4836-0_7
(2026)
https://doi.org/10.64898/2026.02.03.703498
Complex cooperativity in DNA origami revealed via design-dependent defectivity
Jacob M Majikes, Amna Hasni, Shankar Haridas, Joseph W F Robertson, Adam L Pintar, Michael Zwolak and J Alexander LiddleNucleic Acids Research 54 (4) (2026)
https://doi.org/10.1093/nar/gkag052
1496 3 (2026)
https://doi.org/10.1007/978-3-032-07511-6_1
Efficient and Accelerated Protein Free Energy Landscape Reconstruction via Conditional Variational Autoencoders
Ruizhe Shen, Miaomiao Zhao, Wei Wang and Hao DongThe Journal of Physical Chemistry Letters (2026)
https://doi.org/10.1021/acs.jpclett.6c00485
1496 51 (2026)
https://doi.org/10.1007/978-3-032-07511-6_2
Decoding How Proteins Fold
Jorge A. VilaBiophysica 6 (2) 36 (2026)
https://doi.org/10.3390/biophysica6020036
Exploring the sequence and structural determinants of the energy landscape from thermodynamically stable and kinetically trapped subtilisins: ISP1 and SbtE
Miriam R. Hood and Susan MarquseeProtein Science 34 (9) (2025)
https://doi.org/10.1002/pro.70264
(2025)
https://doi.org/10.1016/B978-0-443-27380-3.00033-6
Analysis for the Science Librarians of the 2024 Nobel Prize in Chemistry: Computational Protein Design and Protein Structure Prediction
Mary C. Schlembach and Donna T. WrublewskiScience & Technology Libraries 44 (3) 211 (2025)
https://doi.org/10.1080/0194262X.2025.2468333
Single-molecule magnetic tweezers to unravel protein folding dynamics under force
Rafael Tapia-RojoBiophysical Reviews 17 (1) 25 (2025)
https://doi.org/10.1007/s12551-025-01274-1
Efficient quantum algorithm for lattice protein folding
Youle Wang and Xiangzhen ZhouQuantum Science and Technology 10 (1) 015056 (2025)
https://doi.org/10.1088/2058-9565/ada08e
220 (2025)
https://doi.org/10.1109/DSN-W65791.2025.00065
31 (2025)
https://doi.org/10.1016/B978-0-443-21809-5.00017-X
Finite-Time Thermodynamics and Complex Energy Landscapes: A Perspective
Johann Christian SchönEntropy 27 (8) 819 (2025)
https://doi.org/10.3390/e27080819
Topological Analysis Reveals Multiple Pathways in Molecular Dynamics
Luca Donati, Surahit Chewle, Dominik St Pierre, Vijay Natarajan and Marcus WeberJournal of Chemical Theory and Computation 21 (20) 10385 (2025)
https://doi.org/10.1021/acs.jctc.5c00819
Quantum walk and fast protein-folding time
Fei Wan, Li-Hua Lu and You-Quan LiAIP Advances 15 (12) (2025)
https://doi.org/10.1063/5.0293423
(2025)
https://doi.org/10.1101/2025.06.25.661590
Computational complexity, algorithmic scope, and evolution
Leonhard Sidl, Maximilian Faissner, Manuel Uhlir, Cristian A Velandia-Huerto, Maria Waldl, Hua-Ting Yao, Ivo L Hofacker and Peter F StadlerJournal of Physics: Complexity 6 (1) 015013 (2025)
https://doi.org/10.1088/2632-072X/adb928
How proteins manage to fold and how chaperones manage to assist the folding
Sergiy O. Garbuzynskiy, Victor V. Marchenkov, Natalia Y. Marchenko, Gennady V. Semisotnov and Alexei V. FinkelsteinPhysics of Life Reviews 52 66 (2025)
https://doi.org/10.1016/j.plrev.2024.12.006
The Arch from the Stones: Understanding Protein Folding Energy Landscapes via Bioinspired Collective Variables
Valerio Rizzi, Margaux Héritier, Nicola Piasentin, Simone Aureli and Francesco Luigi GervasioThe Journal of Physical Chemistry Letters 16 (37) 9636 (2025)
https://doi.org/10.1021/acs.jpclett.5c02079
315 (2025)
https://doi.org/10.1016/B978-0-443-21809-5.00009-0
Pioneer in Molecular Biology: Conformational Ensembles in Molecular Recognition, Allostery, and Cell Function
Ruth NussinovJournal of Molecular Biology 437 (11) 169044 (2025)
https://doi.org/10.1016/j.jmb.2025.169044
Information optimality and the geometry of chromatin
Subhash KakBiophysical Reviews (2025)
https://doi.org/10.1007/s12551-025-01374-y
Structural Biology in the AlphaFold Era: How Far Is Artificial Intelligence from Deciphering the Protein Folding Code?
Nicole Balasco, Luciana Esposito and Luigi VitaglianoBiomolecules 15 (5) 674 (2025)
https://doi.org/10.3390/biom15050674
Predicting Protein Folding Pathways With Quadratic Constraints on Rates of Entropy Change: A Nonlinear Optimization-Based Control Approach
Alireza Mohammadi and Mark W. SpongJournal of Dynamic Systems, Measurement, and Control 147 (5) (2025)
https://doi.org/10.1115/1.4068504
Partition Function Zeros and Heat Capacity Decomposition Reveal HP Protein Foldability
Sing-Shuo Huang and Chi-Ning ChenPolymers 17 (21) 2956 (2025)
https://doi.org/10.3390/polym17212956
Enhanced Methodology for Peptide Tertiary Structure Prediction Using GRSA and Bio-Inspired Algorithm
Diego A. Soto-Monterrubio, Hernán Peraza-Vázquez, Adrián F. Peña-Delgado and José G. González-HernándezInternational Journal of Molecular Sciences 26 (15) 7484 (2025)
https://doi.org/10.3390/ijms26157484
Quantum mechanics paradox in protein structure prediction: Intrinsically linked to sequence yet independent of it
Sarfaraz K. NiaziComputational and Structural Biotechnology Reports 2 100039 (2025)
https://doi.org/10.1016/j.csbr.2025.100039
https://doi.org/10.1016/bs.apcsb.2024.09.010
1 (2025)
https://doi.org/10.1016/B978-0-443-21809-5.00001-6
Visualizing dynamic tubulin folding in chaperonin TRiC from nonnative nucleus to final native state
Yanyan Zhao, Michael F. Schmid and Wah ChiuNature Communications 16 (1) (2025)
https://doi.org/10.1038/s41467-025-63016-x
Amide Nitrogen Pyramidalization via N–H/N Interactions that Stabilize the δ/α Conformations in Turns, Loops, and 310- and α-Helices
Noah J. Daniecki, Glenn P. A. Yap and Neal J. ZondloACS Chemical Biology 20 (11) 2617 (2025)
https://doi.org/10.1021/acschembio.5c00451
Critical assessment of AI-based protein structure prediction: Fundamental challenges and future directions in drug discovery
Sarfaraz K. NiaziComputational and Structural Biotechnology Reports 2 100064 (2025)
https://doi.org/10.1016/j.csbr.2025.100064
97 (2025)
https://doi.org/10.1016/B978-0-443-15964-0.00001-3
Clearing the protein clutter in human cells: the role of protein disaggregases
Niels Alberts-Visscher, Paolo De Los Rios, Harm H. Kampinga and Nadinath B. NillegodaTransactions of the Royal Society of South Africa 80 (1) 27 (2025)
https://doi.org/10.1080/0035919X.2025.2515392
Resurgence of magnetic resonance techniques in the era of AlphaFold
Caitlin E. Skinner, Bethany A. Haynes and Rivka L. IsaacsonBiophysical Reviews 17 (4) 981 (2025)
https://doi.org/10.1007/s12551-025-01329-3
213 (2025)
https://doi.org/10.1016/B978-0-443-21809-5.00012-0
Proteome-wide determinants of co-translational chaperone binding in bacteria
Carla Verónica Galmozzi, Frank Tippmann, Florian Wruck, Josef Johannes Auburger, Ilia Kats, Manuel Guennigmann, Katharina Till, Edward P. O´Brien, Sander J. Tans, Günter Kramer and Bernd BukauNature Communications 16 (1) (2025)
https://doi.org/10.1038/s41467-025-59067-9
(2025)
https://doi.org/10.1016/B978-0-323-99507-8.00025-1
Conserved structural topologies in RNase A-like and trypsin-like serine proteases: a sequence-based folding analysis
K. M. Ahsanul Kabir, Takuya Takahashi and Takeshi KikuchiBMC Molecular and Cell Biology 26 (1) (2025)
https://doi.org/10.1186/s12860-025-00542-y
(2025)
https://doi.org/10.1101/2025.04.23.650292
Protein structure prediction via deep learning: an in-depth review
Yajie Meng, Zhuang Zhang, Chang Zhou, Xianfang Tang, Xinrong Hu, Geng Tian, Jialiang Yang and Yuhua YaoFrontiers in Pharmacology 16 (2025)
https://doi.org/10.3389/fphar.2025.1498662
2952 39 (2025)
https://doi.org/10.1007/978-1-0716-4690-8_3
Rapid estimation of protein folding pathways from sequence alone using AlphaFold2
Liwei Chang and Alberto PerezNature Communications 17 (1) (2025)
https://doi.org/10.1038/s41467-025-66870-x
Nobel Prize in Chemistry 2024
Tarak KarmakarResonance 30 (5) 649 (2025)
https://doi.org/10.1007/s12045-025-1804-3
Leveraging Artificial Intelligence to Expedite Antibody Design and Enhance Antibody–Antigen Interactions
Doo Nam Kim, Andrew D. McNaughton and Neeraj KumarBioengineering 11 (2) 185 (2024)
https://doi.org/10.3390/bioengineering11020185
(2024)
https://doi.org/10.1101/2024.08.25.609581
Probing Aromatic Side Chains Reveals the Site-Specific Melting in the SUMO1 Molten Globule
Simran Arora and Sri Rama Koti AinavarapuBiochemistry 63 (23) 3090 (2024)
https://doi.org/10.1021/acs.biochem.4c00366
(2024)
https://doi.org/10.1101/2024.09.08.611919
https://doi.org/10.1002/9781394276639.refs
Recent Advances in Protein Folding Pathway Prediction through Computational Methods
Kailong Zhao, Fang Liang, Yuhao Xia, Minghua Hou and Guijun ZhangCurrent Medicinal Chemistry 31 (26) 4111 (2024)
https://doi.org/10.2174/0109298673265249231004193520
Resource analysis of quantum algorithms for coarse-grained protein folding models
Hanna Linn, Isak Lyngfelt, Laura García-Álvarez and Göran JohanssonPhysical Review Research 6 (3) (2024)
https://doi.org/10.1103/PhysRevResearch.6.033112
https://doi.org/10.1021/acsinfocus.7e7032
Energy landscapes—Past, present, and future: A perspective
J. C. SchönThe Journal of Chemical Physics 161 (5) (2024)
https://doi.org/10.1063/5.0212867
(2024)
https://doi.org/10.1101/2024.12.17.628912
35 109 (2024)
https://doi.org/10.1007/978-3-031-46917-6_6
Prediction of protein structure and AI
Shiho Ohno, Noriyoshi Manabe and Yoshiki YamaguchiJournal of Human Genetics 69 (10) 477 (2024)
https://doi.org/10.1038/s10038-023-01215-4
In the Beginning: Let Hydration Be Coded in Proteins for Manifestation and Modulation by Salts and Adenosine Triphosphate
Jianxing SongInternational Journal of Molecular Sciences 25 (23) 12817 (2024)
https://doi.org/10.3390/ijms252312817
(2024)
https://doi.org/10.2139/ssrn.5034578
Magnesium induced structural reorganization in the active site of adenylate kinase
Kwangho Nam, Abdul Raafik Arattu Thodika, Sonja Tischlik, Chanrith Phoeurk, Tamás Milán Nagy, Léon Schierholz, Jörgen Ådén, Per Rogne, Malte Drescher, A. Elisabeth Sauer-Eriksson and Magnus Wolf-WatzScience Advances 10 (32) (2024)
https://doi.org/10.1126/sciadv.ado5504
Sparks of function by de novo protein design
Alexander E. Chu, Tianyu Lu and Po-Ssu HuangNature Biotechnology 42 (2) 203 (2024)
https://doi.org/10.1038/s41587-024-02133-2
Protein Design by Integrating Machine Learning and Quantum-Encoded Optimization
Veronica Panizza, Philipp Hauke, Cristian Micheletti and Pietro FaccioliPRX Life 2 (4) (2024)
https://doi.org/10.1103/PRXLife.2.043012
Entropy associated with conformational and solvent-density fluctuations in biomolecular solutions
Fumio HirataJournal of Molecular Liquids 409 125359 (2024)
https://doi.org/10.1016/j.molliq.2024.125359
A Study on How Conformation Entropy of Attached Macromolecules Drives Polymeric Collapse and Protein Folding
Ionel PopaMacromolecular Theory and Simulations 33 (4) (2024)
https://doi.org/10.1002/mats.202400004
What Is life? Rethinking Biology in Light of Fundamental Parameters
Jacques Fantini, Mélanie Matveeva, Marine Lefebvre and Henri ChahinianLife 14 (3) 280 (2024)
https://doi.org/10.3390/life14030280
A Stochastic Landscape Approach for Protein Folding State Classification
Michael Faran, Dhiman Ray, Shubhadeep Nag, Umberto Raucci, Michele Parrinello and Gili BiskerJournal of Chemical Theory and Computation 20 (13) 5428 (2024)
https://doi.org/10.1021/acs.jctc.4c00464
(2024)
https://doi.org/10.1101/2024.05.06.592702
(2024)
https://doi.org/10.5772/intechopen.1006957
Comprehensive Perspective Towards the Management of Proteinopathies by Elucidating Protein Misfolding and Aggregation
Ishfaq Ahmad Ahanger, Ghulam Md. Ashraf, Anurag Sharma and Asimul IslamCNS & Neurological Disorders - Drug Targets 23 (2) 153 (2024)
https://doi.org/10.2174/1871527322666230306085937
Metadynamics for Transition Paths in Irreversible Dynamics
Tobias Grafke and Alessandro LaioMultiscale Modeling & Simulation 22 (1) 125 (2024)
https://doi.org/10.1137/23M1563025
1 (2024)
https://doi.org/10.4018/979-8-3693-3192-7.ch001
137 (2024)
https://doi.org/10.4018/979-8-3693-3192-7.ch005
Solvation Thermodynamics and Its Applications
Arieh Ben-NaimEntropy 26 (2) 174 (2024)
https://doi.org/10.3390/e26020174
Data-Efficient Generation of Protein Conformational Ensembles with Backbone-to-Side-Chain Transformers
Shriram Chennakesavalu and Grant M. RotskoffThe Journal of Physical Chemistry B 128 (9) 2114 (2024)
https://doi.org/10.1021/acs.jpcb.3c08195
Protein Structure Prediction with High Degrees of Freedom in a Gate-Based Quantum Computer
Jaya Vasavi Pamidimukkala, Soham Bopardikar, Avinash Dakshinamoorthy, Ashwini Kannan, Kalyan Dasgupta and Sanjib SenapatiJournal of Chemical Theory and Computation 20 (22) 10223 (2024)
https://doi.org/10.1021/acs.jctc.4c00848
Modulation of Aggregation and Immunogenicity of a Protein: Based on the Study of Hen Lysozyme
Tadashi UedaYAKUGAKU ZASSHI 144 (3) 299 (2024)
https://doi.org/10.1248/yakushi.23-00192
A Monist Proposal: Against Integrative Pluralism About Protein Structure
Agnes BolinskaErkenntnis 89 (4) 1711 (2024)
https://doi.org/10.1007/s10670-022-00601-2
Fluctuation-driven morphological patterning: An unconventional approach to morphogenesis
Oded Agam and Erez BraunPhysical Review Research 6 (4) (2024)
https://doi.org/10.1103/PhysRevResearch.6.043027
Easy Or Hard? Basic Questions in Computational Complexity Theory
Noa Segev and Avi WigdersonFrontiers for Young Minds 11 (2024)
https://doi.org/10.3389/frym.2023.1284284
Opportunities and challenges in design and optimization of protein function
Dina Listov, Casper A. Goverde, Bruno E. Correia and Sarel Jacob FleishmanNature Reviews Molecular Cell Biology 25 (8) 639 (2024)
https://doi.org/10.1038/s41580-024-00718-y
55 (2024)
https://doi.org/10.1007/978-981-97-6001-5_4
https://doi.org/10.1016/bs.pmbts.2024.03.010
605 (2024)
https://doi.org/10.1016/B978-0-323-90800-9.00263-8
(2024)
https://doi.org/10.1101/2024.10.13.618036
Base Pairing Promoted the Self-Organization of Genetic Coding, Catalysis, and Free-Energy Transduction
Charles W. CarterLife 14 (2) 199 (2024)
https://doi.org/10.3390/life14020199
From covalent transition states in chemistry to noncovalent in biology: from β- to Φ-value analysis of protein folding
Alan R. FershtQuarterly Reviews of Biophysics 57 (2024)
https://doi.org/10.1017/S0033583523000045
Amino Acid Residue-Specific Ramachandran Distributions Derived from a Simple Mean Field Potential
Brian AndrewsACS Physical Chemistry Au 4 (6) 707 (2024)
https://doi.org/10.1021/acsphyschemau.4c00064
Protein Folding Dynamics and Stability
Santanu Sasidharan, Rohit Shukla, Timir Tripathi and Prakash SaudagarProtein Folding Dynamics and Stability 203 (2023)
https://doi.org/10.1007/978-981-99-2079-2_11
Detecting Molecular Folding from Noise Measurements
Marc Rico-Pasto and Felix RitortBiophysica 3 (3) 539 (2023)
https://doi.org/10.3390/biophysica3030036
23 (2023)
https://doi.org/10.5772/intechopen.108545
357 (2023)
https://doi.org/10.1016/B978-0-323-99127-8.00008-8
How Does a Biopolymer (Protein) Fold into a Unique 3D Structure?
K. V. ShaitanMoscow University Biological Sciences Bulletin 78 (S1) S5 (2023)
https://doi.org/10.3103/S009639252370013X
199 (2023)
https://doi.org/10.1016/B978-0-323-99533-7.00007-8
Intelligent Systems and Applications
Alexandre Almeida and Telma Woerle de LimaLecture Notes in Networks and Systems, Intelligent Systems and Applications 543 568 (2023)
https://doi.org/10.1007/978-3-031-16078-3_39
Protein Folding Dynamics and Stability
Santanu Sasidharan, Vijayakumar Gosu, Timir Tripathi and Prakash SaudagarProtein Folding Dynamics and Stability 107 (2023)
https://doi.org/10.1007/978-981-99-2079-2_6
Mechanisms and pathology of protein misfolding and aggregation
Nikolaos Louros, Joost Schymkowitz and Frederic RousseauNature Reviews Molecular Cell Biology 24 (12) 912 (2023)
https://doi.org/10.1038/s41580-023-00647-2