Research graph
References from Role of desolvation on biomolecular liquid-liquid phase separation. Local targets link to admitted publications; unresolved targets remain external evidence.
Hoomd-blue: A python package for high-performance molecular dynamics and hard particle monte carlo simulations
10.1016/j.commatsci.2019.109363 · 2020 · External reference
Disprot in 2024: improving function annotation of intrinsically disordered proteins
10.1093/nar/gkad928 · 2024 · External reference
Sequence effects on size, shape, and structural heterogeneity in intrinsically disordered proteins
10.1021/acs.jpcb.9b02575 · 2019 · External reference
Simulation of fus protein condensates with an adapted coarse-grained model
10.1021/acs.jctc.0c01064 · 2020 · External reference
Nuclear stress bodies
10.1101/cshperspect.a000695 · 2010 · External reference
Fusion dynamics and size-dependence of droplet microstructure in ssdna-mediated protein phase separation
10.1021/jacsau.4c00690 · 2024 · External reference
Molecular drivers of aging in biomolecular condensates: Desolvation, rigidification, and sticker lifetimes
10.1103/prxlife.2.023011 · 2024 · External reference
Vapor-liquid interfacial properties of fully flexible lennard-jones chains
10.1063/1.2989115 · 2008 · External reference
Protein phase separation: a new phase in cell biology
10.1016/j.tcb.2018.02.004 · 2018 · External reference
Residue-by-residue view of in vitro fus granules that bind the c-terminal domain of rna polymerase ii
10.1016/j.molcel.2015.09.006 · 2015 · External reference
On spinodal decomposition
10.1016/0001-6160(61)90182-1 · 1961 · External reference
Free energy of a nonuniform system. i. interfacial free energy
10.1063/1.1744102 · 1958 · External reference
Towards a structural biology of the hydrophobic effect in protein folding
10.1038/srep28285 · 2016 · External reference
Accurate prediction of thermoresponsive phase behavior of disordered proteins
10.1002/pro.70284 · 2025 · External reference
Effects of desolvation barriers and sidechains on local–nonlocal coupling and chevron behaviors in coarse-grained models of protein folding
10.1039/c3cp54866j · 2014 · External reference
Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse
10.1073/pnas.022387699 · 2002 · External reference
Lassi: A lattice model for simulating phase transitions of multivalent proteins
10.1371/journal.pcbi.1007028 · 2019 · External reference
Pressure-induced dissolution and reentrant formation of condensed, liquid–liquid phase-separated elastomeric α-elastin
10.1002/chem.201801643 · 2018 · External reference
Temperature, hydrostatic pressure, and osmolyte effects on liquid–liquid phase separation in protein condensates: physical chemistry and biological implications
10.1002/chem.201902210 · 2019 · External reference
Als mutations disrupt phase separation mediated by α-helical structure in the tdp-43 low-complexity c-terminal domain
10.1016/j.str.2016.07.007 · 2016 · External reference
A data-driven hydrophobicity scale for predicting liquid–liquid phase separation of proteins
10.1021/acs.jpcb.0c11479 · 2021 · External reference
Sirah: a structurally unbiased coarse-grained force field for proteins with aqueous solvation and long-range electrostatics
10.1021/ct5007746 · 2015 · External reference
Comparative roles of charge, π, and hydrophobic interactions in sequence-dependent phase separation of intrinsically disordered proteins
10.1073/pnas.2008122117 · 2020 · External reference
Xxxvi. on some applications of the law of the rectilinear diameter
10.1080/14786440908637343 · 1912 · External reference
Awsem-md: protein structure prediction using coarse-grained physical potentials and bioinformatically based local structure biasing
10.1021/jp212541y · 2012 · External reference
Improved parameters for the martini coarse-grained protein force field
10.1021/ct300646g · 2013 · External reference
Evaluating the strength of salt bridges: a comparison of current biomolecular force fields
10.1021/jp500958r · 2014 · External reference
De la theorie des electrolytes. i. abaissement du point de congelation et phenomenes associes
1923 · External reference
Pressure-dependent properties of elementary hydrophobic interactions: ramifications for activation properties of protein folding
10.1021/jp501935f · 2014 · External reference
Biomolecular phase separation: from molecular driving forces to macroscopic properties
10.1146/annurev-physchem-071819-113553 · 2020 · External reference
Relation between single-molecule properties and phase behavior of intrinsically disordered proteins
10.1073/pnas.1804177115 · External reference
Sequence determinants of protein phase behavior from a coarse-grained model
10.1371/journal.pcbi.1005941 · External reference
Temperature-controlled liquid–liquid phase separation of disordered proteins
10.1021/acscentsci.9b00102 · 2019 · External reference
Unresolved reference
1988 · External reference
Openmm 8: molecular dynamics simulation with machine learning potentials
10.1021/acs.jpcb.3c06662 · 2023 · External reference
The disordered p granule protein laf-1 drives phase separation into droplets with tunable viscosity and dynamics
10.1073/pnas.1504822112 · 2015 · External reference
Liquid network connectivity regulates the stability and composition of biomolecular condensates with many components
10.1073/pnas.1917569117 · 2020 · External reference
Desolvation barrier effects are a likely contributor to the remarkable diversity in the folding rates of small proteins
10.1016/j.jmb.2009.04.011 · 2009 · External reference
Coexisting liquid phases underlie nucleolar subcompartments
10.1016/j.cell.2016.04.047 · 2016 · External reference
Thermodynamics of high polymer solutions
10.1063/1.1723621 · 1942 · External reference
Unresolved reference
1953 · External reference
A tale of two desolvation potentials: An investigation of protein behavior under high hydrostatic pressure
10.1021/acs.jpcb.9b10734 · 2020 · External reference
Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins
10.7554/elife.30294 · 2017 · External reference
Biophysics of phase separation of disordered proteins is governed by balance between short-and long-range interactions
10.1021/acs.jpcb.0c09975 · 2021 · External reference
A phase separation model for transcriptional control
10.1016/j.cell.2017.02.007 · 2017 · External reference
Solutions of long chain compounds
10.1063/1.1750930 · 1941 · External reference
Some properties of solutions of long-chain compounds
10.1021/j150415a018 · 1942 · External reference
Physics-driven coarse-grained model for biomolecular phase separation with near-quantitative accuracy
10.1038/s43588-021-00155-3 · 2021 · External reference
Cocomo2: A coarse-grained model for interacting folded and disordered proteins
10.1021/acs.jctc.4c01460 · 2025 · External reference
A simple atomic-level hydrophobicity scale reveals protein interfacial structure
10.1016/j.jmb.2013.09.039 · 2014 · External reference
The origins of asymmetry in the folding transition states of protein l and protein g
10.1110/ps.0205402 · 2002 · External reference
Maximum entropy optimized force field for intrinsically disordered proteins
10.1021/acs.jctc.9b00932 · 2019 · External reference
Consistent force field captures homologue-resolved hp1 phase separation
10.1021/acs.jctc.0c01220 · 2021 · External reference
Crosslink-induced conformation change of intrinsically disordered proteins have a nontrivial effect on phase separation dynamics and thermodynamics
10.1021/acs.jpcb.3c01728 · 2023 · External reference
Energy landscape views for interplays among folding, binding, and allostery of calmodulin domains
10.1073/pnas.1402768111 · 2014 · External reference
Phase separation and single-chain compactness of charged disordered proteins are strongly correlated
10.1016/j.bpj.2017.04.021 · 2017 · External reference
Random-phase-approximation theory for sequence-dependent, biologically functional liquid-liquid phase separation of intrinsically disordered proteins
10.1016/j.molliq.2016.09.090 · 2017 · External reference
Solvation and desolvation effects in protein folding: native flexibility, kinetic cooperativity and enthalpic barriers under isostability conditions
10.1088/1478-3975/2/4/s01 · 2005 · External reference
Hydrophobic association of α-helices, steric dewetting, and enthalpic barriers to protein folding
10.1073/pnas.0605859104 · 2007 · External reference
On the relative roles of free volume and activation energy in the viscosity of liquids
10.1063/1.1695683 · 1965 · External reference
Growth of long-range correlations after a quench in conserved-order-parameter systems
10.1103/physrevlett.73.182 · 1994 · External reference
Complete phase diagram for liquid–liquid phase separation of intrinsically disordered proteins
10.1021/acs.jpclett.9b00099 · 2019 · External reference
Anomalous diffusion models and their properties: non-stationarity, non-ergodicity, and ageing at the centenary of single particle tracking
10.1039/c4cp03465a · 2014 · External reference
Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization
10.1016/j.cell.2015.09.015 · 2015 · External reference
The role of nuclear bodies in gene expression and disease
10.3390/biology2030976 · 2013 · External reference
Entropy tug-of-war determines solvent effects in the liquid–liquid phase separation of a globular protein
10.1021/acs.jpclett.3c03421 · 2024 · External reference
Thermodynamic forces from protein and water govern condensate formation of an intrinsically disordered protein domain
10.1038/s41467-023-41586-y · 2023 · External reference
Experimental parameterization of an energy function for the simulation of unfolded proteins
10.1529/biophysj.107.108241 · 2008 · External reference
Structural diversity of p63 and p73 isoforms
10.1038/s41418-022-00975-4 · 2022 · External reference
Polymorphic transitions in single crystals: A new molecular dynamics method
10.1063/1.328693 · 1981 · External reference
A liquid-to-solid phase transition of the als protein fus accelerated by disease mutation
10.1016/j.cell.2015.07.047 · 2015 · External reference
Improved coarse-grained model for studying sequence dependent phase separation of disordered proteins
10.1002/pro.4094 · 2021 · External reference
Stress-triggered phase separation is an adaptive, evolutionarily tuned response
10.1016/j.cell.2017.02.027 · 2017 · External reference
Unresolved reference
2013 · External reference
Ligand effects on phase separation of multivalent macromolecules
10.1073/pnas.2017184118 · 2021 · External 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 · 2012 · External reference
Liquid phase condensation in cell physiology and disease
10.1126/science.aaf4382 · 2017 · External reference
Martini 3: a general purpose force field for coarse-grained molecular dynamics
10.1038/s41592-021-01098-3 · 2021 · External reference
Phase separation drives heterochromatin domain formation
10.1038/nature22989 · 2017 · External reference
Phase separation of signaling molecules promotes t cell receptor signal transduction
10.1126/science.aad9964 · 2016 · External reference
Viscoelastic phase separation
10.1088/0953-8984/12/15/201 · 2000 · External reference
Dynamics of asp23-lys28 salt-bridge formation in aβ10-35 monomers
10.1021/ja064872y · 2006 · External reference
Time-dependent material properties of aging biomolecular condensates from different viscoelasticity measurements in molecular dynamics simulations
10.1021/acs.jpcb.3c01292 · 2023 · External reference
Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range
10.12688/openreseurope.14967.2 · 2022 · External reference
Accurate model of liquid–liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties
10.1073/pnas.2111696118 · 2021 · External reference
Conformational ensembles of the human intrinsically disordered proteome
10.1038/s41586-023-07004-5 · 2024 · External reference
Intrinsically disordered proteins as crucial constituents of cellular aqueous two phase systems and coacervates
10.1016/j.febslet.2014.11.028 · 2015 · External reference
Modeling concentration-dependent phase separation processes involving peptides and rna via residue-based coarse-graining
10.1021/acs.jctc.2c00856 · 2023 · External reference
Classification of intrinsically disordered regions and proteins
10.1021/cr400525m · 2014 · External reference
Prediction of phase-separation propensities of disordered proteins from sequence
10.1073/pnas.2417920122 · 2025 · External reference
Diffusion of intrinsically disordered proteins within protein condensates
10.1103/jsdl-chm9 · 2025 · External reference
Phase behaviour of disordered proteins underlying low density and high permeability of liquid organelles
10.1038/nchem.2803 · 2017 · External 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 · 2022 · External reference
Dual specificity kinase dyrk3 couples stress granule condensation/dissolution to mtorc1 signaling
10.1016/j.cell.2013.01.033 · 2013 · External reference
Structural and functional relevance of charge-based transient interactions inside intrinsically disordered proteins
10.1021/acsphyschemau.5c00005 · 2025 · External reference
Awsem-idp: a coarse-grained force field for intrinsically disordered proteins
10.1021/acs.jpcb.8b05791 · 2018 · External reference
Driving force for the association of hydrophobic peptides: The importance of electrostatic interactions in coarse-grained water models
10.1021/jz2006622 · External reference
A new coarse-grained force field for membrane–peptide simulations
10.1021/ct200593t · External reference
Postsynaptic protein assembly in three and two dimensions studied by mesoscopic simulations
10.1016/j.bpj.2023.07.015 · 2023 · External reference
Toward accurate simulation of coupling between protein secondary structure and phase separation
10.1021/jacs.3c09195 · 2023 · External reference
Competition between native topology and nonnative interactions in simple and complex folding kinetics of natural and designed proteins
10.1073/pnas.0911844107 · 2010 · External reference
Why do disordered and structured proteins behave differently in phase separation?
10.1016/j.tibs.2018.03.007 · 2018 · External reference
Pressure-induced dissolution and reentrant formation of condensed, liquid–liquid phase-separated elastomeric α-elastin
10.1002/chem.201801643 · ExternalCitation · doi-reference
Temperature, hydrostatic pressure, and osmolyte effects on liquid–liquid phase separation in protein condensates: physical chemistry and biological implications
10.1002/chem.201902210 · ExternalCitation · doi-reference
Improved coarse-grained model for studying sequence dependent phase separation of disordered proteins
10.1002/pro.4094 · ExternalCitation · doi-reference
Accurate prediction of thermoresponsive phase behavior of disordered proteins
10.1002/pro.70284 · ExternalCitation · doi-reference
On spinodal decomposition
10.1016/0001-6160(61)90182-1 · ExternalCitation · doi-reference
Phase separation and single-chain compactness of charged disordered proteins are strongly correlated
10.1016/j.bpj.2017.04.021 · ExternalCitation · doi-reference
Postsynaptic protein assembly in three and two dimensions studied by mesoscopic simulations
10.1016/j.bpj.2023.07.015 · ExternalCitation · doi-reference
Dual specificity kinase dyrk3 couples stress granule condensation/dissolution to mtorc1 signaling
10.1016/j.cell.2013.01.033 · ExternalCitation · doi-reference
A liquid-to-solid phase transition of the als protein fus accelerated by disease mutation
10.1016/j.cell.2015.07.047 · ExternalCitation · doi-reference
Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization
10.1016/j.cell.2015.09.015 · ExternalCitation · doi-reference
Coexisting liquid phases underlie nucleolar subcompartments
10.1016/j.cell.2016.04.047 · ExternalCitation · doi-reference
A phase separation model for transcriptional control
10.1016/j.cell.2017.02.007 · ExternalCitation · doi-reference
Stress-triggered phase separation is an adaptive, evolutionarily tuned response
10.1016/j.cell.2017.02.027 · ExternalCitation · doi-reference
Hoomd-blue: A python package for high-performance molecular dynamics and hard particle monte carlo simulations
10.1016/j.commatsci.2019.109363 · ExternalCitation · doi-reference
Intrinsically disordered proteins as crucial constituents of cellular aqueous two phase systems and coacervates
10.1016/j.febslet.2014.11.028 · ExternalCitation · doi-reference
Desolvation barrier effects are a likely contributor to the remarkable diversity in the folding rates of small proteins
10.1016/j.jmb.2009.04.011 · ExternalCitation · doi-reference
A simple atomic-level hydrophobicity scale reveals protein interfacial structure
10.1016/j.jmb.2013.09.039 · ExternalCitation · doi-reference
Residue-by-residue view of in vitro fus granules that bind the c-terminal domain of rna polymerase ii
10.1016/j.molcel.2015.09.006 · ExternalCitation · doi-reference
Random-phase-approximation theory for sequence-dependent, biologically functional liquid-liquid phase separation of intrinsically disordered proteins
10.1016/j.molliq.2016.09.090 · ExternalCitation · doi-reference
Als mutations disrupt phase separation mediated by α-helical structure in the tdp-43 low-complexity c-terminal domain
10.1016/j.str.2016.07.007 · ExternalCitation · doi-reference
Protein phase separation: a new phase in cell biology
10.1016/j.tcb.2018.02.004 · ExternalCitation · doi-reference
Why do disordered and structured proteins behave differently in phase separation?
10.1016/j.tibs.2018.03.007 · ExternalCitation · doi-reference
Simulation of fus protein condensates with an adapted coarse-grained model
10.1021/acs.jctc.0c01064 · ExternalCitation · doi-reference
Consistent force field captures homologue-resolved hp1 phase separation
10.1021/acs.jctc.0c01220 · ExternalCitation · doi-reference
Modeling concentration-dependent phase separation processes involving peptides and rna via residue-based coarse-graining
10.1021/acs.jctc.2c00856 · ExternalCitation · doi-reference
Cocomo2: A coarse-grained model for interacting folded and disordered proteins
10.1021/acs.jctc.4c01460 · ExternalCitation · doi-reference
Maximum entropy optimized force field for intrinsically disordered proteins
10.1021/acs.jctc.9b00932 · ExternalCitation · doi-reference
Biophysics of phase separation of disordered proteins is governed by balance between short-and long-range interactions
10.1021/acs.jpcb.0c09975 · ExternalCitation · doi-reference
A data-driven hydrophobicity scale for predicting liquid–liquid phase separation of proteins
10.1021/acs.jpcb.0c11479 · ExternalCitation · 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 · ExternalCitation · doi-reference
Time-dependent material properties of aging biomolecular condensates from different viscoelasticity measurements in molecular dynamics simulations
10.1021/acs.jpcb.3c01292 · ExternalCitation · doi-reference
Crosslink-induced conformation change of intrinsically disordered proteins have a nontrivial effect on phase separation dynamics and thermodynamics
10.1021/acs.jpcb.3c01728 · ExternalCitation · doi-reference
Openmm 8: molecular dynamics simulation with machine learning potentials
10.1021/acs.jpcb.3c06662 · ExternalCitation · doi-reference
Awsem-idp: a coarse-grained force field for intrinsically disordered proteins
10.1021/acs.jpcb.8b05791 · ExternalCitation · doi-reference
Sequence effects on size, shape, and structural heterogeneity in intrinsically disordered proteins
10.1021/acs.jpcb.9b02575 · ExternalCitation · doi-reference
A tale of two desolvation potentials: An investigation of protein behavior under high hydrostatic pressure
10.1021/acs.jpcb.9b10734 · ExternalCitation · doi-reference
Entropy tug-of-war determines solvent effects in the liquid–liquid phase separation of a globular protein
10.1021/acs.jpclett.3c03421 · ExternalCitation · doi-reference
Complete phase diagram for liquid–liquid phase separation of intrinsically disordered proteins
10.1021/acs.jpclett.9b00099 · ExternalCitation · doi-reference
Temperature-controlled liquid–liquid phase separation of disordered proteins
10.1021/acscentsci.9b00102 · ExternalCitation · doi-reference
Structural and functional relevance of charge-based transient interactions inside intrinsically disordered proteins
10.1021/acsphyschemau.5c00005 · ExternalCitation · doi-reference
Classification of intrinsically disordered regions and proteins
10.1021/cr400525m · ExternalCitation · doi-reference
A new coarse-grained force field for membrane–peptide simulations
10.1021/ct200593t · ExternalCitation · doi-reference
Improved parameters for the martini coarse-grained protein force field
10.1021/ct300646g · ExternalCitation · doi-reference
Sirah: a structurally unbiased coarse-grained force field for proteins with aqueous solvation and long-range electrostatics
10.1021/ct5007746 · ExternalCitation · doi-reference
Some properties of solutions of long-chain compounds
10.1021/j150415a018 · ExternalCitation · doi-reference
Dynamics of asp23-lys28 salt-bridge formation in aβ10-35 monomers
10.1021/ja064872y · ExternalCitation · doi-reference
Toward accurate simulation of coupling between protein secondary structure and phase separation
10.1021/jacs.3c09195 · ExternalCitation · doi-reference
Fusion dynamics and size-dependence of droplet microstructure in ssdna-mediated protein phase separation
10.1021/jacsau.4c00690 · ExternalCitation · 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 · ExternalCitation · doi-reference
Awsem-md: protein structure prediction using coarse-grained physical potentials and bioinformatically based local structure biasing
10.1021/jp212541y · ExternalCitation · doi-reference
Evaluating the strength of salt bridges: a comparison of current biomolecular force fields
10.1021/jp500958r · ExternalCitation · doi-reference
Pressure-dependent properties of elementary hydrophobic interactions: ramifications for activation properties of protein folding
10.1021/jp501935f · ExternalCitation · doi-reference
Driving force for the association of hydrophobic peptides: The importance of electrostatic interactions in coarse-grained water models
10.1021/jz2006622 · ExternalCitation · doi-reference
Phase separation drives heterochromatin domain formation
10.1038/nature22989 · ExternalCitation · doi-reference
Phase behaviour of disordered proteins underlying low density and high permeability of liquid organelles
10.1038/nchem.2803 · ExternalCitation · doi-reference
Structural diversity of p63 and p73 isoforms
10.1038/s41418-022-00975-4 · ExternalCitation · doi-reference
Thermodynamic forces from protein and water govern condensate formation of an intrinsically disordered protein domain
10.1038/s41467-023-41586-y · ExternalCitation · doi-reference
Conformational ensembles of the human intrinsically disordered proteome
10.1038/s41586-023-07004-5 · ExternalCitation · doi-reference
Martini 3: a general purpose force field for coarse-grained molecular dynamics
10.1038/s41592-021-01098-3 · ExternalCitation · doi-reference
Physics-driven coarse-grained model for biomolecular phase separation with near-quantitative accuracy
10.1038/s43588-021-00155-3 · ExternalCitation · doi-reference
Towards a structural biology of the hydrophobic effect in protein folding
10.1038/srep28285 · ExternalCitation · doi-reference
Effects of desolvation barriers and sidechains on local–nonlocal coupling and chevron behaviors in coarse-grained models of protein folding
10.1039/c3cp54866j · ExternalCitation · doi-reference
Anomalous diffusion models and their properties: non-stationarity, non-ergodicity, and ageing at the centenary of single particle tracking
10.1039/c4cp03465a · ExternalCitation · doi-reference
On the relative roles of free volume and activation energy in the viscosity of liquids
10.1063/1.1695683 · ExternalCitation · doi-reference
Thermodynamics of high polymer solutions
10.1063/1.1723621 · ExternalCitation · doi-reference
Free energy of a nonuniform system. i. interfacial free energy
10.1063/1.1744102 · ExternalCitation · doi-reference
Solutions of long chain compounds
10.1063/1.1750930 · ExternalCitation · doi-reference
Vapor-liquid interfacial properties of fully flexible lennard-jones chains
10.1063/1.2989115 · ExternalCitation · doi-reference
Polymorphic transitions in single crystals: A new molecular dynamics method
10.1063/1.328693 · ExternalCitation · doi-reference
Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse
10.1073/pnas.022387699 · ExternalCitation · doi-reference
Hydrophobic association of α-helices, steric dewetting, and enthalpic barriers to protein folding
10.1073/pnas.0605859104 · ExternalCitation · doi-reference
Competition between native topology and nonnative interactions in simple and complex folding kinetics of natural and designed proteins
10.1073/pnas.0911844107 · ExternalCitation · doi-reference
Energy landscape views for interplays among folding, binding, and allostery of calmodulin domains
10.1073/pnas.1402768111 · ExternalCitation · doi-reference
The disordered p granule protein laf-1 drives phase separation into droplets with tunable viscosity and dynamics
10.1073/pnas.1504822112 · ExternalCitation · doi-reference
Relation between single-molecule properties and phase behavior of intrinsically disordered proteins
10.1073/pnas.1804177115 · ExternalCitation · doi-reference
Liquid network connectivity regulates the stability and composition of biomolecular condensates with many components
10.1073/pnas.1917569117 · ExternalCitation · doi-reference
Comparative roles of charge, π, and hydrophobic interactions in sequence-dependent phase separation of intrinsically disordered proteins
10.1073/pnas.2008122117 · ExternalCitation · doi-reference
Ligand effects on phase separation of multivalent macromolecules
10.1073/pnas.2017184118 · ExternalCitation · doi-reference
Accurate model of liquid–liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties
10.1073/pnas.2111696118 · ExternalCitation · doi-reference
Prediction of phase-separation propensities of disordered proteins from sequence
10.1073/pnas.2417920122 · ExternalCitation · doi-reference
Xxxvi. on some applications of the law of the rectilinear diameter
10.1080/14786440908637343 · ExternalCitation · doi-reference
Viscoelastic phase separation
10.1088/0953-8984/12/15/201 · ExternalCitation · doi-reference
Solvation and desolvation effects in protein folding: native flexibility, kinetic cooperativity and enthalpic barriers under isostability conditions
10.1088/1478-3975/2/4/s01 · ExternalCitation · doi-reference
Disprot in 2024: improving function annotation of intrinsically disordered proteins
10.1093/nar/gkad928 · ExternalCitation · doi-reference
Nuclear stress bodies
10.1101/cshperspect.a000695 · ExternalCitation · doi-reference
Diffusion of intrinsically disordered proteins within protein condensates
10.1103/jsdl-chm9 · ExternalCitation · doi-reference
Growth of long-range correlations after a quench in conserved-order-parameter systems
10.1103/physrevlett.73.182 · ExternalCitation · doi-reference
Molecular drivers of aging in biomolecular condensates: Desolvation, rigidification, and sticker lifetimes
10.1103/prxlife.2.023011 · ExternalCitation · doi-reference
The origins of asymmetry in the folding transition states of protein l and protein g
10.1110/ps.0205402 · ExternalCitation · doi-reference
Phase separation of signaling molecules promotes t cell receptor signal transduction
10.1126/science.aad9964 · ExternalCitation · doi-reference
Liquid phase condensation in cell physiology and disease
10.1126/science.aaf4382 · ExternalCitation · doi-reference
Biomolecular phase separation: from molecular driving forces to macroscopic properties
10.1146/annurev-physchem-071819-113553 · ExternalCitation · doi-reference
Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range
10.12688/openreseurope.14967.2 · ExternalCitation · doi-reference
Sequence determinants of protein phase behavior from a coarse-grained model
10.1371/journal.pcbi.1005941 · ExternalCitation · doi-reference
Lassi: A lattice model for simulating phase transitions of multivalent proteins
10.1371/journal.pcbi.1007028 · ExternalCitation · doi-reference
Experimental parameterization of an energy function for the simulation of unfolded proteins
10.1529/biophysj.107.108241 · ExternalCitation · doi-reference
The role of nuclear bodies in gene expression and disease
10.3390/biology2030976 · ExternalCitation · doi-reference
Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins
10.7554/elife.30294 · ExternalCitation · doi-reference