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:

Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases

Vladimir I. Muronetz, Sofia S. Kudryavtseva, Evgeniia V. Leisi, Lidia P. Kurochkina, Kseniya V. Barinova and Elena V. Schmalhausen
International Journal of Molecular Sciences 23 (5) 2747 (2022)
https://doi.org/10.3390/ijms23052747

Protein folding problem: enigma, paradox, solution

Alexei V. Finkelstein, Natalya S. Bogatyreva, Dmitry N. Ivankov and Sergiy O. Garbuzynskiy
Biophysical Reviews 14 (6) 1255 (2022)
https://doi.org/10.1007/s12551-022-01000-1

Dry Molten Globule-Like Intermediates in Protein Folding, Function, and Disease

Nirbhik Acharya and Santosh Kumar Jha
The Journal of Physical Chemistry B 126 (43) 8614 (2022)
https://doi.org/10.1021/acs.jpcb.2c04991

Molten globule–like transition state of protein barnase measured with calorimetric force spectroscopy

Marc Rico-Pasto, Annamaria Zaltron, Sebastian J. Davis, Silvia Frutos and Felix Ritort
Proceedings of the National Academy of Sciences 119 (11) (2022)
https://doi.org/10.1073/pnas.2112382119

DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science

Kunihiro Kuwajima, Maho Yagi-Utsumi, Saeko Yanaka and Koichi Kato
Molecules 27 (12) 3748 (2022)
https://doi.org/10.3390/molecules27123748

The Energy Landscape Perspective: Encoding Structure and Function for Biomolecules

Konstantin Röder and David J. Wales
Frontiers in Molecular Biosciences 9 (2022)
https://doi.org/10.3389/fmolb.2022.820792

A Peptides Prediction Methodology with Fragments and CNN for Tertiary Structure Based on GRSA2

Juan Sánchez-Hernández, Juan Frausto-Solís, Diego Soto-Monterrubio, Juan González-Barbosa and Edgar Roman-Rangel
Axioms 11 (12) 729 (2022)
https://doi.org/10.3390/axioms11120729

Computer Simulations of Aggregation of Proteins and Peptides

Nguyen Truong Co, Mai Suan Li and Pawel Krupa
Methods in Molecular Biology, Computer Simulations of Aggregation of Proteins and Peptides 2340 51 (2022)
https://doi.org/10.1007/978-1-0716-1546-1_4

AlphaFold 2 and NMR Spectroscopy: Partners to Understand Protein Structure, Dynamics and Function

Douglas V. Laurents
Frontiers in Molecular Biosciences 9 (2022)
https://doi.org/10.3389/fmolb.2022.906437

Machine learning/molecular dynamic protein structure prediction approach to investigate the protein conformational ensemble

Martina Audagnotto, Werngard Czechtizky, Leonardo De Maria, et al.
Scientific Reports 12 (1) (2022)
https://doi.org/10.1038/s41598-022-13714-z

Soft interactions versus hard core repulsions: A journey of cytochrome c from acid-induced denaturation to native protein via pre-molten globule and molten globule conformations exploiting dextran and its monomer glucose

Daraksha Yameen, Seerat Siraj, Zahoor Ahmad Parray, Mohammad Masood, Asimul Islam and Mohammad Mahfuzul Haque
Journal of Molecular Liquids 366 120257 (2022)
https://doi.org/10.1016/j.molliq.2022.120257

Chaperones and Catalysts: How Antigen Presentation Pathways Cope With Biological Necessity

David H. Margulies, Daniel K. Taylor, Jiansheng Jiang, et al.
Frontiers in Immunology 13 (2022)
https://doi.org/10.3389/fimmu.2022.859782

Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?

Irina Sorokina, Arcady R. Mushegian and Eugene V. Koonin
International Journal of Molecular Sciences 23 (1) 521 (2022)
https://doi.org/10.3390/ijms23010521

The native state conformational heterogeneity in the energy landscape of protein folding

Prajna Mishra and Santosh Kumar Jha
Biophysical Chemistry 283 106761 (2022)
https://doi.org/10.1016/j.bpc.2022.106761

Critical assessment of methods of protein structure prediction (CASP)—Round XIV

Andriy Kryshtafovych, Torsten Schwede, Maya Topf, Krzysztof Fidelis and John Moult
Proteins: Structure, Function, and Bioinformatics 89 (12) 1607 (2021)
https://doi.org/10.1002/prot.26237

The functions and regulation of heat shock proteins; key orchestrators of proteostasis and the heat shock response

Benjamin J. Lang, Martin E. Guerrero, Thomas L. Prince, et al.
Archives of Toxicology 95 (6) 1943 (2021)
https://doi.org/10.1007/s00204-021-03070-8

Resource-efficient quantum algorithm for protein folding

Anton Robert, Panagiotis Kl. Barkoutsos, Stefan Woerner and Ivano Tavernelli
npj Quantum Information 7 (1) (2021)
https://doi.org/10.1038/s41534-021-00368-4

Protein structure prediction by AlphaFold2: are attention and symmetries all you need?

Nazim Bouatta, Peter Sorger and Mohammed AlQuraishi
Acta Crystallographica Section D Structural Biology 77 (8) 982 (2021)
https://doi.org/10.1107/S2059798321007531

RosettaCM for antibodies with very long HCDR3s and low template availability

Pranav Kodali, Clara T. Schoeder, Samuel Schmitz, James E. Crowe and Jens Meiler
Proteins: Structure, Function, and Bioinformatics 89 (11) 1458 (2021)
https://doi.org/10.1002/prot.26166

Unraveling protein’s structural dynamics: from configurational dynamics to ensemble switching guides functional mesoscale assemblies

Exequiel Medina, Danielle R. Latham and Hugo Sanabria
Current Opinion in Structural Biology 66 129 (2021)
https://doi.org/10.1016/j.sbi.2020.10.016

Molecular Recognition and Self-Organization in Life Phenomena Studied by a Statistical Mechanics of Molecular Liquids, the RISM/3D-RISM Theory

Masatake Sugita, Itaru Onishi, Masayuki Irisa, Norio Yoshida and Fumio Hirata
Molecules 26 (2) 271 (2021)
https://doi.org/10.3390/molecules26020271

Evolution as a Guide to Designing xeno Amino Acid Alphabets

Christopher Mayer-Bacon, Neyiasuo Agboha, Mickey Muscalli and Stephen Freeland
International Journal of Molecular Sciences 22 (6) 2787 (2021)
https://doi.org/10.3390/ijms22062787

Protein dynamics implications of the low- and high-temperature denaturation of myoglobin

Ramzi R. Khuri, Trung V. Phan and Robert H. Austin
Physical Review E 104 (3) (2021)
https://doi.org/10.1103/PhysRevE.104.034414

Understanding Conformational Entropy in Small Molecules

Lucian Chan, Garrett M. Morris and Geoffrey R. Hutchison
Journal of Chemical Theory and Computation 17 (4) 2099 (2021)
https://doi.org/10.1021/acs.jctc.0c01213

The Protein Folding Problem: The Role of Theory

Roy Nassar, Gregory L. Dignon, Rostam M. Razban and Ken A. Dill
Journal of Molecular Biology 433 (20) 167126 (2021)
https://doi.org/10.1016/j.jmb.2021.167126

Flexible Folding: Disulfide-Containing Peptides and Proteins Choose the Pathway Depending on the Environments

Kenta Arai and Michio Iwaoka
Molecules 26 (1) 195 (2021)
https://doi.org/10.3390/molecules26010195

A Peptides Prediction Methodology for Tertiary Structure Based on Simulated Annealing

Juan P. Sánchez-Hernández, Juan Frausto-Solís, Juan J. González-Barbosa, Diego A. Soto-Monterrubio, Fanny G. Maldonado-Nava and Guadalupe Castilla-Valdez
Mathematical and Computational Applications 26 (2) 39 (2021)
https://doi.org/10.3390/mca26020039

Fuzziness and Frustration in the Energy Landscape of Protein Folding, Function, and Assembly

Stefano Gianni, María Inés Freiberger, Per Jemth, et al.
Accounts of Chemical Research 54 (5) 1251 (2021)
https://doi.org/10.1021/acs.accounts.0c00813

Implementation of the Freely Jointed Chain Model to Assess Kinetics and Thermodynamics of Thermosensitive Coil–Globule Transition by Markov States

Patrick K. Quoika, Monica L. Fernández-Quintero, Maren Podewitz, Florian Hofer and Klaus R. Liedl
The Journal of Physical Chemistry B 125 (18) 4898 (2021)
https://doi.org/10.1021/acs.jpcb.1c01946

Entropy-Enthalpy Compensations Fold Proteins in Precise Ways

Jiacheng Li, Chengyu Hou, Xiaoliang Ma, Shuai Guo, Hongchi Zhang, Liping Shi, Chenchen Liao, Bing Zheng, Lin Ye, Lin Yang and Xiaodong He
International Journal of Molecular Sciences 22 (17) 9653 (2021)
https://doi.org/10.3390/ijms22179653

Protein-Folding Analysis Using Features Obtained by Persistent Homology

Takashi Ichinomiya, Ippei Obayashi and Yasuaki Hiraoka
Biophysical Journal 118 (12) 2926 (2020)
https://doi.org/10.1016/j.bpj.2020.04.032

Effects of natural mutations (L94I and L94V) on the stability and mechanism of folding of horse cytochrome c: A combined in vitro and molecular dynamics simulations approach

Sabab Hasan Khan, Amresh Prakash, Preeti Pandey, et al.
International Journal of Biological Macromolecules 159 976 (2020)
https://doi.org/10.1016/j.ijbiomac.2020.05.059

Enhancing fragment-based protein structure prediction by customising fragment cardinality according to local secondary structure

Jad Abbass and Jean-Christophe Nebel
BMC Bioinformatics 21 (1) (2020)
https://doi.org/10.1186/s12859-020-3491-0

Funneled energy landscape unifies principles of protein binding and evolution

Zhiqiang Yan and Jin Wang
Proceedings of the National Academy of Sciences 117 (44) 27218 (2020)
https://doi.org/10.1073/pnas.2013822117

Identification of on- and off-pathway oligomers in amyloid fibril formation

Alexander J. Dear, Georg Meisl, Anđela Šarić, et al.
Chemical Science 11 (24) 6236 (2020)
https://doi.org/10.1039/C9SC06501F

Protein unfolding by SDS: the microscopic mechanisms and the properties of the SDS-protein assembly

David Winogradoff, Shalini John and Aleksei Aksimentiev
Nanoscale 12 (9) 5422 (2020)
https://doi.org/10.1039/C9NR09135A

Solution of Levinthal’s Paradox and a Physical Theory of Protein Folding Times

Dmitry N. Ivankov and Alexei V. Finkelstein
Biomolecules 10 (2) 250 (2020)
https://doi.org/10.3390/biom10020250

Innovative Smart Healthcare and Bio-Medical Systems

Mohamad Yousef, Tamer Abdelkader and Khaled El-Bahnasy
Innovative Smart Healthcare and Bio-Medical Systems 87 (2020)
https://doi.org/10.1201/9781003044291-4

Biological physics by high-speed atomic force microscopy

Ignacio Casuso, Lorena Redondo-Morata and Felix Rico
Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 378 (2186) 20190604 (2020)
https://doi.org/10.1098/rsta.2019.0604

Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications

Xiaoran Roger Liu, Mengru Mira Zhang and Michael L. Gross
Chemical Reviews 120 (10) 4355 (2020)
https://doi.org/10.1021/acs.chemrev.9b00815

Innovative Smart Healthcare and Bio-Medical Systems

Mohamad Yousef, Tamer Abdelkader and Khaled El-Bahnasy
Innovative Smart Healthcare and Bio-Medical Systems 87 (2020)
https://doi.org/10.4324/9781003044291-4

What limits the primary sequence space of natural proteins?

Aditya Mittal, Anandkumar Madhavjibhai Changani and Sakshi Taparia
Journal of Biomolecular Structure and Dynamics 38 (15) 4579 (2020)
https://doi.org/10.1080/07391102.2019.1682051

Heat Shock Proteins in Inflammatory Diseases

Dipankar J. Dutta, Kazue Hashimoto-Torii and Masaaki Torii
Heat Shock Proteins, Heat Shock Proteins in Inflammatory Diseases 22 213 (2020)
https://doi.org/10.1007/7515_2020_10

Root of the Tree: The Significance, Evolution, and Origins of the Ribosome

Jessica C. Bowman, Anton S. Petrov, Moran Frenkel-Pinter, Petar I. Penev and Loren Dean Williams
Chemical Reviews 120 (11) 4848 (2020)
https://doi.org/10.1021/acs.chemrev.9b00742

Alternative Hydrophobic Core in Proteins—The Effect of Specific Synergy

Piotr Fabian, Katarzyna Stapor, Mateusz Banach, Magdalena Ptak-Kaczor, Leszek Konieczny and Irena Roterman
Symmetry 12 (2) 273 (2020)
https://doi.org/10.3390/sym12020273

Basic Epithelial Ion Transport Principles and Function

Aiping Zheng, Sophie C. Frizzell, Solomon M. Klombers and Patrick H. Thibodeau
Physiology in Health and Disease, Basic Epithelial Ion Transport Principles and Function 159 (2020)
https://doi.org/10.1007/978-3-030-52780-8_6

The Amyloid as a Ribbon-Like Micelle in Contrast to Spherical Micelles Represented by Globular Proteins

Mateusz Banach, Leszek Konieczny and Irena Roterman
Molecules 24 (23) 4395 (2019)
https://doi.org/10.3390/molecules24234395

Computational Methods to Study the Structure and Dynamics of Biomolecules and Biomolecular Processes

Dorota Latek, Bartosz Trzaskowski, Szymon Niewieczerzał, et al.
Springer Series on Bio- and Neurosystems, Computational Methods to Study the Structure and Dynamics of Biomolecules and Biomolecular Processes 8 371 (2019)
https://doi.org/10.1007/978-3-319-95843-9_12

Performance of ACE-Reaction on 26 Organic Reactions for Fully Automated Reaction Network Construction and Microkinetic Analysis

Jin Woo Kim, Yeonjoon Kim, Kyung Yup Baek, Kyunghoon Lee and Woo Youn Kim
The Journal of Physical Chemistry A 123 (22) 4796 (2019)
https://doi.org/10.1021/acs.jpca.9b02161

Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis

Justin T. Marinko, Hui Huang, Wesley D. Penn, et al.
Chemical Reviews 119 (9) 5537 (2019)
https://doi.org/10.1021/acs.chemrev.8b00532

Protein Misfolding Diseases and Therapeutic Approaches

Kusum Yadav, Anurag Yadav, Priyanka Vashistha, Veda P. Pandey and Upendra N. Dwivedi
Current Protein & Peptide Science 20 (12) 1226 (2019)
https://doi.org/10.2174/1389203720666190610092840

Automatically obtaining a cellular automaton scheme for modeling protein folding using the FCC model

Daniel Varela and José Santos
Natural Computing 18 (2) 275 (2019)
https://doi.org/10.1007/s11047-018-9705-y

Autonomous Sequences in Myoglobin Emerging from X-ray Structure of Holomyoglobin

Mitsuaki Narita, Masakuni Narita, Yasuko Itsuno and Shinichi Itsuno
ACS Omega 4 (1) 992 (2019)
https://doi.org/10.1021/acsomega.8b03218

Energy Landscapes for Proteins: From Single Funnels to Multifunctional Systems

Konstantin Röder, Jerelle A. Joseph, Brooke E. Husic and David J. Wales
Advanced Theory and Simulations 2 (4) (2019)
https://doi.org/10.1002/adts.201800175