Why do disordered and structured proteins behave differently in phase separation?
10.1016/j.tibs.2018.03.007 · doi-reference
Competition between native topology and nonnative interactions in simple and complex folding kinetics of natural and designed proteins
10.1073/pnas.0911844107 · doi-reference
Toward accurate simulation of coupling between protein secondary structure and phase separation
10.1021/jacs.3c09195 · doi-reference
Postsynaptic protein assembly in three and two dimensions studied by mesoscopic simulations
10.1016/j.bpj.2023.07.015 · doi-reference
A new coarse-grained force field for membrane–peptide simulations
10.1021/ct200593t · doi-reference
Driving force for the association of hydrophobic peptides: The importance of electrostatic interactions in coarse-grained water models
10.1021/jz2006622 · doi-reference
Awsem-idp: a coarse-grained force field for intrinsically disordered proteins
10.1021/acs.jpcb.8b05791 · doi-reference
Structural and functional relevance of charge-based transient interactions inside intrinsically disordered proteins
10.1021/acsphyschemau.5c00005 · doi-reference
Dual specificity kinase dyrk3 couples stress granule condensation/dissolution to mtorc1 signaling
10.1016/j.cell.2013.01.033 · doi-reference
Analytical formulation and field-theoretic simulation of sequence-specific phase separation of protein-like heteropolymers with short-and long-spatial-range interactions
10.1021/acs.jpcb.2c06181 · doi-reference
Phase behaviour of disordered proteins underlying low density and high permeability of liquid organelles
10.1038/nchem.2803 · doi-reference
Diffusion of intrinsically disordered proteins within protein condensates
10.1103/jsdl-chm9 · doi-reference
Prediction of phase-separation propensities of disordered proteins from sequence
10.1073/pnas.2417920122 · doi-reference
Classification of intrinsically disordered regions and proteins
10.1021/cr400525m · doi-reference
Modeling concentration-dependent phase separation processes involving peptides and rna via residue-based coarse-graining
10.1021/acs.jctc.2c00856 · doi-reference
Intrinsically disordered proteins as crucial constituents of cellular aqueous two phase systems and coacervates
10.1016/j.febslet.2014.11.028 · doi-reference
Conformational ensembles of the human intrinsically disordered proteome
10.1038/s41586-023-07004-5 · doi-reference
Accurate model of liquid–liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties
10.1073/pnas.2111696118 · doi-reference
Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range
10.12688/openreseurope.14967.2 · doi-reference
Time-dependent material properties of aging biomolecular condensates from different viscoelasticity measurements in molecular dynamics simulations
10.1021/acs.jpcb.3c01292 · doi-reference
Dynamics of asp23-lys28 salt-bridge formation in aβ10-35 monomers
10.1021/ja064872y · doi-reference
Viscoelastic phase separation
10.1088/0953-8984/12/15/201 · doi-reference
Phase separation of signaling molecules promotes t cell receptor signal transduction
10.1126/science.aad9964 · doi-reference
Phase separation drives heterochromatin domain formation
10.1038/nature22989 · doi-reference
Martini 3: a general purpose force field for coarse-grained molecular dynamics
10.1038/s41592-021-01098-3 · doi-reference
Liquid phase condensation in cell physiology and disease
10.1126/science.aaf4382 · doi-reference
Effects of high temperature on desolvation costs of salt bridges across protein binding interfaces: similarities and differences between implicit and explicit solvent models
10.1021/jp210172b · doi-reference
Ligand effects on phase separation of multivalent macromolecules
10.1073/pnas.2017184118 · doi-reference
Stress-triggered phase separation is an adaptive, evolutionarily tuned response
10.1016/j.cell.2017.02.027 · doi-reference
Improved coarse-grained model for studying sequence dependent phase separation of disordered proteins
10.1002/pro.4094 · doi-reference
A liquid-to-solid phase transition of the als protein fus accelerated by disease mutation
10.1016/j.cell.2015.07.047 · doi-reference
Polymorphic transitions in single crystals: A new molecular dynamics method
10.1063/1.328693 · doi-reference
Experimental parameterization of an energy function for the simulation of unfolded proteins
10.1529/biophysj.107.108241 · doi-reference
Thermodynamic forces from protein and water govern condensate formation of an intrinsically disordered protein domain
10.1038/s41467-023-41586-y · doi-reference
Entropy tug-of-war determines solvent effects in the liquid–liquid phase separation of a globular protein
10.1021/acs.jpclett.3c03421 · doi-reference
The role of nuclear bodies in gene expression and disease
10.3390/biology2030976 · doi-reference
Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization
10.1016/j.cell.2015.09.015 · doi-reference
Anomalous diffusion models and their properties: non-stationarity, non-ergodicity, and ageing at the centenary of single particle tracking
10.1039/c4cp03465a · doi-reference
Complete phase diagram for liquid–liquid phase separation of intrinsically disordered proteins
10.1021/acs.jpclett.9b00099 · doi-reference
Growth of long-range correlations after a quench in conserved-order-parameter systems
10.1103/physrevlett.73.182 · doi-reference
