Singh A, Miranda Bedate A, von Richthofen H, Vijver S, van der Vlist M, Kuhn R
Elife. 2024; 13.
PMID: 39377459
PMC: 11460946.
DOI: 10.7554/eLife.92870.
Vollmers L, Zacharias M
Biophys J. 2024; 123(19):3463-3477.
PMID: 39210596
PMC: 11480772.
DOI: 10.1016/j.bpj.2024.08.022.
Kulkarni P, Leite V, Roy S, Bhattacharyya S, Mohanty A, Achuthan S
Biophys Rev (Melville). 2024; 3(1):011306.
PMID: 38505224
PMC: 10903413.
DOI: 10.1063/5.0080512.
Madhurima K, Nandi B, Munshi S, Naganathan A, Sekhar A
Sci Adv. 2023; 9(26):eadh4591.
PMID: 37379390
PMC: 10306299.
DOI: 10.1126/sciadv.adh4591.
Elkjaer S, Due A, Christensen L, Theisen F, Staby L, Kragelund B
Commun Biol. 2023; 6(1):63.
PMID: 36653471
PMC: 9849366.
DOI: 10.1038/s42003-023-04445-6.
Flexible Target Recognition of the Intrinsically Disordered DNA-Binding Domain of CytR Monitored by Single-Molecule Fluorescence Spectroscopy.
Mitra S, Oikawa H, Rajendran D, Kowada T, Mizukami S, Naganathan A
J Phys Chem B. 2022; 126(33):6136-6147.
PMID: 35969476
PMC: 9422980.
DOI: 10.1021/acs.jpcb.2c02791.
NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins.
Camacho-Zarco A, Schnapka V, Guseva S, Abyzov A, Adamski W, Milles S
Chem Rev. 2022; 122(10):9331-9356.
PMID: 35446534
PMC: 9136928.
DOI: 10.1021/acs.chemrev.1c01023.
Structural-Energetic Basis for Coupling between Equilibrium Fluctuations and Phosphorylation in a Protein Native Ensemble.
Golla H, Kannan A, Gopi S, Murugan S, Perumalsamy L, Naganathan A
ACS Cent Sci. 2022; 8(2):282-293.
PMID: 35233459
PMC: 8880421.
DOI: 10.1021/acscentsci.1c01548.
Molecular Simulations of Intrinsically Disordered Proteins and Their Binding Mechanisms.
Chu X, Nagpal S, Munoz V
Methods Mol Biol. 2021; 2376:343-362.
PMID: 34845619
DOI: 10.1007/978-1-0716-1716-8_19.
Interpreting a black box predictor to gain insights into early folding mechanisms.
Grau I, Nowe A, Vranken W
Comput Struct Biotechnol J. 2021; 19:4919-4930.
PMID: 34527196
PMC: 8433119.
DOI: 10.1016/j.csbj.2021.08.041.
Insights into the Binding of Intrinsically Disordered Proteins from Molecular Dynamics Simulation.
Baker C, Best R
Wiley Interdiscip Rev Comput Mol Sci. 2021; 4(3):182-198.
PMID: 34354764
PMC: 8336759.
DOI: 10.1002/wcms.1167.
A disordered encounter complex is central to the yeast Abp1p SH3 domain binding pathway.
Gerlach G, Carrock R, Stix R, Stollar E, Ball K
PLoS Comput Biol. 2020; 16(9):e1007815.
PMID: 32925900
PMC: 7514057.
DOI: 10.1371/journal.pcbi.1007815.
Measuring and Analyzing Binding Kinetics of Coupled Folding and Binding Reactions Under Pseudo-First-Order Conditions.
Steen Jensen K
Methods Mol Biol. 2020; 2141:629-650.
PMID: 32696381
DOI: 10.1007/978-1-0716-0524-0_32.
Revealing the Dynamical Role of Co-solvents in the Coupled Folding and Dimerization of Insulin.
Zhang X, Tokmakoff A
J Phys Chem Lett. 2020; 11(11):4353-4358.
PMID: 32401513
PMC: 7850624.
DOI: 10.1021/acs.jpclett.0c00982.
Investigation into Early Steps of Actin Recognition by the Intrinsically Disordered N-WASP Domain V.
Chan-Yao-Chong M, Durand D, Ha-Duong T
Int J Mol Sci. 2019; 20(18).
PMID: 31514372
PMC: 6770570.
DOI: 10.3390/ijms20184493.
Structural Characterization of N-WASP Domain V Using MD Simulations with NMR and SAXS Data.
Chan-Yao-Chong M, Deville C, Pinet L, van Heijenoort C, Durand D, Ha-Duong T
Biophys J. 2019; 116(7):1216-1227.
PMID: 30878202
PMC: 6451034.
DOI: 10.1016/j.bpj.2019.02.015.
Kinetic and thermodynamic effects of phosphorylation on p53 binding to MDM2.
Yadahalli S, Neira J, Johnson C, Sing Tan Y, Rowling P, Chattopadhyay A
Sci Rep. 2019; 9(1):693.
PMID: 30679555
PMC: 6345774.
DOI: 10.1038/s41598-018-36589-5.
Structural metamorphism and polymorphism in proteins on the brink of thermodynamic stability.
Kulkarni P, Solomon T, He Y, Chen Y, Bryan P, Orban J
Protein Sci. 2018; 27(9):1557-1567.
PMID: 30144197
PMC: 6194243.
DOI: 10.1002/pro.3458.
A proline switch explains kinetic heterogeneity in a coupled folding and binding reaction.
Zosel F, Mercadante D, Nettels D, Schuler B
Nat Commun. 2018; 9(1):3332.
PMID: 30127362
PMC: 6102232.
DOI: 10.1038/s41467-018-05725-0.
Tunable order-disorder continuum in protein-DNA interactions.
Munshi S, Gopi S, Asampille G, Subramanian S, Campos L, Atreya H
Nucleic Acids Res. 2018; 46(17):8700-8709.
PMID: 30107436
PMC: 6158747.
DOI: 10.1093/nar/gky732.