Hood M, Marqusee S
bioRxiv. 2024; .
PMID: 39314365
PMC: 11419036.
DOI: 10.1101/2024.09.08.611919.
Woodbury B, Newcomer R, Alexandrescu A, Teschke C
bioRxiv. 2024; .
PMID: 39282432
PMC: 11398494.
DOI: 10.1101/2024.09.08.611893.
Bharmoria P, Tietze A, Mondal D, Kang T, Kumar A, Freire M
Chem Rev. 2024; 124(6):3037-3084.
PMID: 38437627
PMC: 10979405.
DOI: 10.1021/acs.chemrev.3c00551.
de La Bourdonnaye G, Ghazalova T, Fojtik P, Kutalkova K, Bednar D, Damborsky J
Comput Struct Biotechnol J. 2024; 23:942-951.
PMID: 38379823
PMC: 10877085.
DOI: 10.1016/j.csbj.2024.02.001.
Lipskij A, Arbeitman C, Rojas P, Ojeda-May P, Garcia M
Viruses. 2023; 15(12).
PMID: 38140646
PMC: 10748067.
DOI: 10.3390/v15122405.
The Effects of Codon Usage on Protein Structure and Folding.
Moss M, Chamness L, Clark P
Annu Rev Biophys. 2023; 53(1):87-108.
PMID: 38134335
PMC: 11227313.
DOI: 10.1146/annurev-biophys-030722-020555.
ATP induces folding of ALS-causing C71G-hPFN1 and nascent hSOD1.
Kang J, Lim L, Song J
Commun Chem. 2023; 6(1):186.
PMID: 37670116
PMC: 10480188.
DOI: 10.1038/s42004-023-00997-0.
Effects of External Perturbations on Protein Systems: A Microscopic View.
Dutta P, Roy P, Sengupta N
ACS Omega. 2022; 7(49):44556-44572.
PMID: 36530249
PMC: 9753117.
DOI: 10.1021/acsomega.2c06199.
Non-Equilibrium Protein Folding and Activation by ATP-Driven Chaperones.
Xu H
Biomolecules. 2022; 12(6).
PMID: 35740957
PMC: 9221429.
DOI: 10.3390/biom12060832.
Algorithmic assessment of missense mutation severity in the Von-Hippel Lindau protein.
Fields F, Suresh N, Hiller M, Freed S, Haldar K, Lee S
PLoS One. 2020; 15(11):e0234100.
PMID: 33151962
PMC: 7644048.
DOI: 10.1371/journal.pone.0234100.
Base-pair ambiguity and the kinetics of RNA folding.
Zhou G, Loper J, Geman S
BMC Bioinformatics. 2019; 20(1):666.
PMID: 31830902
PMC: 6909616.
DOI: 10.1186/s12859-019-3303-6.
Facile measurement of protein stability and folding kinetics using a nano differential scanning fluorimeter.
Chattopadhyay G, Varadarajan R
Protein Sci. 2019; 28(6):1127-1134.
PMID: 30993730
PMC: 6511731.
DOI: 10.1002/pro.3622.
Assessment of Conformational State Transitions of Class B GPCRs Using Molecular Dynamics.
Liao C, May V, Li J
Methods Mol Biol. 2019; 1947:3-19.
PMID: 30969408
PMC: 6571028.
DOI: 10.1007/978-1-4939-9121-1_1.
Computational Estimation of Microsecond to Second Atomistic Folding Times.
Adhikari U, Mostofian B, Copperman J, Subramanian S, Petersen A, Zuckerman D
J Am Chem Soc. 2019; 141(16):6519-6526.
PMID: 30892023
PMC: 6660137.
DOI: 10.1021/jacs.8b10735.
Phosphorylation Induces Conformational Rigidity at the C-Terminal Domain of AMPA Receptors.
Chatterjee S, Ade C, Nurik C, Carrejo N, Dutta C, Jayaraman V
J Phys Chem B. 2018; 123(1):130-137.
PMID: 30537817
PMC: 6465090.
DOI: 10.1021/acs.jpcb.8b10749.
Solution pH jump during antibody and Fc-fusion protein thaw leads to increased aggregation.
Kent K, Schroeder C, Sharma C
J Pharm Anal. 2018; 8(5):302-306.
PMID: 30345143
PMC: 6191964.
DOI: 10.1016/j.jpha.2017.09.002.
An iterative computational design approach to increase the thermal endurance of a mesophilic enzyme.
Sammond D, Kastelowitz N, Donohoe B, Alahuhta M, Lunin V, Chung D
Biotechnol Biofuels. 2018; 11:189.
PMID: 30002729
PMC: 6036693.
DOI: 10.1186/s13068-018-1178-9.
Transmembrane β-barrels: Evolution, folding and energetics.
Chaturvedi D, Mahalakshmi R
Biochim Biophys Acta Biomembr. 2017; 1859(12):2467-2482.
PMID: 28943271
PMC: 7115949.
DOI: 10.1016/j.bbamem.2017.09.020.
Enzyme Efficiency but Not Thermostability Drives Cefotaxime Resistance Evolution in TEM-1 β-Lactamase.
Knies J, Cai F, Weinreich D
Mol Biol Evol. 2017; 34(5):1040-1054.
PMID: 28087769
PMC: 5400381.
DOI: 10.1093/molbev/msx053.
Deep Mutational Scans as a Guide to Engineering High Affinity T Cell Receptor Interactions with Peptide-bound Major Histocompatibility Complex.
Harris D, Wang N, Riley T, Anderson S, Singh N, Procko E
J Biol Chem. 2016; 291(47):24566-24578.
PMID: 27681597
PMC: 5114409.
DOI: 10.1074/jbc.M116.748681.