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).
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
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
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
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
De novo protein folding on computers. Benefits and challenges
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
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
Current trends in protein-surfactant interactions: A review
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
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
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
Mariana H. Moreira, Fabio C. L. Almeida, Tatiana Domitrovic and Fernando L. Palhano (2021) https://doi.org/10.1101/2021.03.30.437752
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
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
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
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
An Effective Cumulative Torsion Angles Model for Prediction of Protein Folding Rates
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
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
Role of (single/double chain surfactant) micelles on the protein aggregation
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
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