On the public citation graph

Expanding the Realm of Ultrafast Protein Folding: gpW, a Midsize Natural Single-Domain with α+β Topology that Folds Downhill

0 signed · 127 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/jcc.20924openalex-snapshot
Energy minimizations with a combination of two knowledge‐based potentials for protein folding
inferredcites →https://doi.org/10.1002/prot.10108openalex-snapshot
Anti‐cooperativity and cooperativity in hydrophobic interactions: Three‐body free energy landscapes and comparison with implicit‐solvent potential functions for proteins
inferredcites →https://doi.org/10.1002/prot.20172openalex-snapshot
The nature of the free energy barriers to two‐state folding
inferredcites →https://doi.org/10.1002/prot.21342openalex-snapshot
Probe‐dependent and nonexponential relaxation kinetics: Unreliable signatures of downhill protein folding
inferredcites →https://doi.org/10.1002/prot.340210302openalex-snapshot
Funnels, pathways, and the energy landscape of protein folding: A synthesis
inferredcites →https://doi.org/10.1002/qua.10384openalex-snapshot
Thermodynamics and kinetics of downhill protein folding investigated with a simple statistical mechanical model
inferredcites →https://doi.org/10.1006/jmbi.1998.1645openalex-snapshot
Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. Wright
inferredcites →https://doi.org/10.1006/jmbi.2000.3665openalex-snapshot
Mapping the transition state of the WW domain β-sheet
inferredcites →https://doi.org/10.1006/jmbi.2001.4582openalex-snapshot
The solution structure of bacteriophage λ protein W, a small morphogenetic protein possessing a novel fold11Edited by P. E. Wright
inferredcites →https://doi.org/10.1016/j.jmb.2004.02.055openalex-snapshot
Characterization of the Folding Energy Landscapes of Computer Generated Proteins Suggests High Folding Free Energy Barriers and Cooperativity may be Consequences of Natural Selection
inferredcites →https://doi.org/10.1016/j.jmb.2004.09.069openalex-snapshot
One-state Downhill versus Conventional Protein Folding
inferredcites →https://doi.org/10.1016/j.sbi.2004.01.013openalex-snapshot
The protein folding ‘speed limit’
inferredcites →https://doi.org/10.1016/j.sbi.2007.12.003openalex-snapshot
Protein folding studied by single-molecule FRET
inferredcites →https://doi.org/10.1016/s0022-2836(03)00513-8openalex-snapshot
Energetic Evidence for Formation of a pH-dependent Hydrophobic Cluster in the Denatured State of Thermus thermophilus Ribonuclease H
inferredcites →https://doi.org/10.1016/s0959-440x(97)80003-6openalex-snapshot
Submillisecond kinetics of protein folding
inferredcites →https://doi.org/10.1016/s1359-0278(98)00033-9openalex-snapshot
How do small single-domain proteins fold?
inferredcites →https://doi.org/10.1021/ar970343aopenalex-snapshot
Infrared Studies of Fast Events in Protein Folding
inferredcites →https://doi.org/10.1021/bi00174a022openalex-snapshot
Thermodynamic and Kinetic Analysis of the SH3 Domain of Spectrin Shows a Two-State Folding Transition
inferredcites →https://doi.org/10.1021/bi050118yopenalex-snapshot
Robustness of Downhill Folding: Guidelines for the Analysis of Equilibrium Folding Experiments on Small Proteins
inferredcites →https://doi.org/10.1021/bi060643copenalex-snapshot
Dynamics, Energetics, and Structure in Protein Folding
inferredcites →https://doi.org/10.1021/cr040430yopenalex-snapshot
Early Events in Protein Folding Explored by Rapid Mixing Methods
inferredcites →https://doi.org/10.1021/ja044449uopenalex-snapshot
Scaling of Folding Times with Protein Size
inferredcites →https://doi.org/10.1021/ja048309wopenalex-snapshot
A Simple Thermodynamic Test To Discriminate between Two-State and Downhill Folding
inferredcites →https://doi.org/10.1021/ja055996yopenalex-snapshot
Direct Measurement of Barrier Heights in Protein Folding
inferredcites →https://doi.org/10.1021/ja0689740openalex-snapshot
Protein Folding Kinetics: Barrier Effects in Chemical and Thermal Denaturation Experiments
inferredcites →https://doi.org/10.1021/jp053770bopenalex-snapshot
Effect of Finite Size on Cooperativity and Rates of Protein Folding
inferredcites →https://doi.org/10.1021/jp0757715openalex-snapshot
Estimating Free-Energy Barrier Heights for an Ultrafast Folding Protein from Calorimetric and Kinetic Data
inferredcites →https://doi.org/10.1038/nature01609openalex-snapshot
Folding at the speed limit
inferredcites →https://doi.org/10.1038/nature04859openalex-snapshot
Atom-by-atom analysis of global downhill protein folding
inferredcites →https://doi.org/10.1038/nature05645openalex-snapshot
Analysis of 'downhill' protein folding; Analysis of protein-folding cooperativity (Reply)
inferredcites →https://doi.org/10.1038/nsb0497-305openalex-snapshot
The energy landscape of a fast-folding protein mapped by Ala→Gly Substitutions
inferredcites →https://doi.org/10.1038/nsb0694-399openalex-snapshot
Elucidating the folding problem of helical peptides using empirical parameters
inferredcites →https://doi.org/10.1073/pnas.0403486101openalex-snapshot
Three-body interactions improve the prediction of rate and mechanism in protein folding models
inferredcites →https://doi.org/10.1073/pnas.0405829101openalex-snapshot
Exploring protein-folding ensembles: A variable-barrier model for the analysis of equilibrium unfolding experiments
inferredcites →https://doi.org/10.1073/pnas.052700099openalex-snapshot
Helix formation via conformation diffusion search
inferredcites →https://doi.org/10.1073/pnas.0538054100openalex-snapshot
Tuning the free-energy landscape of a WW domain by temperature, mutation, and truncation
inferredcites →https://doi.org/10.1073/pnas.0609717104openalex-snapshot
Distinguishing between cooperative and unimodal downhill protein folding
inferredcites →https://doi.org/10.1073/pnas.0708480105openalex-snapshot
Cooperative folding kinetics of BBL protein and peripheral subunit-binding domain homologues
inferredcites →https://doi.org/10.1073/pnas.0709376104openalex-snapshot
Origins of barriers and barrierless folding in BBL
inferredcites →https://doi.org/10.1073/pnas.221467198openalex-snapshot
Ultrafast folding of WW domains without structured aromatic clusters in the denatured state
inferredcites →https://doi.org/10.1126/science.1077809openalex-snapshot
Experimental Identification of Downhill Protein Folding
inferredcites →https://doi.org/10.1146/annurev.biophys.36.040306.132608openalex-snapshot
Conformational Dynamics and Ensembles in Protein Folding
inferredcites →https://doi.org/10.1146/annurev.physchem.48.1.545openalex-snapshot
THEORY OF PROTEIN FOLDING: The Energy Landscape Perspective
inferredcites →https://doi.org/10.1146/annurev.physchem.50.1.485openalex-snapshot
T HE F AST P ROTEIN F OLDING P ROBLEM
inferredcites →https://doi.org/10.1385/0896033015openalex-snapshot
Protein Stability and Folding

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4841883openalex-extracted
Dierential Scanning Calorimetry of Proteins and Zimm-Bragg Model in Water
inferred← citeshttps://doi.org/10.1002/9781118935682.ch14openalex-snapshot
Protein Characterization by Thermal Property Measurement
inferred← citeshttps://doi.org/10.1002/jccs.201300173openalex-snapshot
Molecular Dynamics Insight into the Diverse Thermodynamic Behavior of a Beta‐Hairpin Peptide
inferred← citeshttps://doi.org/10.1002/pro.3015openalex-snapshot
How cooperative are protein folding and unfolding transitions?
inferred← citeshttps://doi.org/10.1002/pro.70705openalex-snapshot
Physics‐based prediction of protein folding and unfolding rates: Examining the roles of fold topology and core packing
inferred← citeshttps://doi.org/10.1002/qua.22272openalex-snapshot
Interplaying roles of native topology and chain length in marginally cooperative and noncooperative folding of small protein fragments
inferred← citeshttps://doi.org/10.1007/978-1-0716-1716-8_10openalex-snapshot
NMR Analysis of Protein Folding Interaction Networks
inferred← citeshttps://doi.org/10.1007/978-1-0716-1716-8_21openalex-snapshot
Predicting and Simulating Mutational Effects on Protein Folding Kinetics
inferred← citeshttps://doi.org/10.1007/978-1-62703-065-6_13openalex-snapshot
Protein Folding at Atomic Resolution: Analysis of Autonomously Folding Supersecondary Structure Motifs by Nuclear Magnetic Resonance
inferred← citeshttps://doi.org/10.1007/s10858-017-0155-0openalex-snapshot
Simultaneous determination of fast and slow dynamics in molecules using extreme CPMG relaxation dispersion experiments
inferred← citeshttps://doi.org/10.1007/s10867-012-9271-yopenalex-snapshot
Thermodynamics of protein folding using a modified Wako-Saitô-Muñoz-Eaton model
inferred← citeshttps://doi.org/10.1016/b978-0-443-21809-5.00009-0openalex-snapshot
Frustration and fuzziness in the three functional states of proteins
inferred← citeshttps://doi.org/10.1016/bs.mie.2015.08.027openalex-snapshot
Modern Analysis of Protein Folding by Differential Scanning Calorimetry
inferred← citeshttps://doi.org/10.1016/bs.mie.2016.09.011openalex-snapshot
Single-Molecule Fluorescence Studies of Fast Protein Folding
inferred← citeshttps://doi.org/10.1016/j.abb.2012.09.008openalex-snapshot
Differential scanning calorimetry as a tool for protein folding and stability
inferred← citeshttps://doi.org/10.1016/j.abb.2024.110132openalex-snapshot
Differential scanning calorimetry of proteins and Zimm–Bragg model in water
inferred← citeshttps://doi.org/10.1016/j.bbapap.2010.09.013openalex-snapshot
Dynamics of protein folding: Probing the kinetic network of folding–unfolding transitions with experiment and theory
inferred← citeshttps://doi.org/10.1016/j.bpc.2010.02.004openalex-snapshot
Protein kinetic stability
inferred← citeshttps://doi.org/10.1016/j.bpj.2008.11.004openalex-snapshot
Native Topology of the Designed Protein Top7 is Not Conducive to Cooperative Folding
inferred← citeshttps://doi.org/10.1016/j.bpj.2011.08.017openalex-snapshot
Improvement of Structure-Based Potentials for Protein Folding by Native and Nonnative Hydrogen Bonds
inferred← citeshttps://doi.org/10.1016/j.bpj.2012.05.021openalex-snapshot
Equilibrium Unfolding of the PDZ Domain of β2-Syntrophin
inferred← citeshttps://doi.org/10.1016/j.bpr.2021.100037openalex-snapshot
Molecular understanding of calorimetric protein unfolding experiments
inferred← citeshttps://doi.org/10.1016/j.jasms.2008.11.007openalex-snapshot
A simple model for the disintegration of highly charged solvent droplets during electrospray ionization
inferred← citeshttps://doi.org/10.1016/j.jmb.2008.09.023openalex-snapshot
Probing Possible Downhill Folding: Native Contact Topology Likely Places a Significant Constraint on the Folding Cooperativity of Proteins with ∼40 Residues
inferred← citeshttps://doi.org/10.1016/j.jmb.2008.10.056openalex-snapshot
Between-Species Variation in the Kinetic Stability of TIM Proteins Linked to Solvation-Barrier Free Energies
inferred← citeshttps://doi.org/10.1016/j.jmb.2010.01.071openalex-snapshot
A Survey of λ Repressor Fragments from Two-State to Downhill Folding
inferred← citeshttps://doi.org/10.1016/j.jmb.2021.167325openalex-snapshot
Folding Intermediates, Heterogeneous Native Ensembles and Protein Function
inferred← citeshttps://doi.org/10.1016/j.sbi.2015.12.001openalex-snapshot
Limited cooperativity in protein folding
inferred← citeshttps://doi.org/10.1017/s003358351400002xopenalex-snapshot
Fast protein folding kinetics
inferred← citeshttps://doi.org/10.1021/acs.accounts.0c00322openalex-snapshot
Lessons about Protein Folding and Binding from Archetypal Folds
inferred← citeshttps://doi.org/10.1021/acs.biochem.6b00573openalex-snapshot
Activation Barrier-Limited Folding and Conformational Sampling of a Dynamic Protein Domain
inferred← citeshttps://doi.org/10.1021/acs.biochem.9b00089openalex-snapshot
Thermally versus Chemically Denatured Protein States
inferred← citeshttps://doi.org/10.1021/acs.chemrev.1c00704openalex-snapshot
Heterogeneity in Protein Folding and Unfolding Reactions
inferred← citeshttps://doi.org/10.1021/acs.jpcb.0c01230openalex-snapshot
Curvature and Torsion of Protein Main Chain as Local Order Parameters of Protein Unfolding
inferred← citeshttps://doi.org/10.1021/acs.jpcb.0c05976openalex-snapshot
Slow Folding of a Helical Protein: Large Barriers, Strong Internal Friction, or a Shallow, Bumpy Landscape?
inferred← citeshttps://doi.org/10.1021/acs.jpcb.1c05401openalex-snapshot
Protein Folding Dynamics as Diffusion on a Free Energy Surface: Rate Equation Terms, Transition Paths, and Analysis of Single-Molecule Photon Trajectories
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b11351openalex-snapshot
Analysis of Fluorescence Lifetime and Energy Transfer Efficiency in Single-Molecule Photon Trajectories of Fast-Folding Proteins
inferred← citeshttps://doi.org/10.1021/acs.jpcb.8b05198openalex-snapshot
Protein Folding Cooperativity and Thermodynamic Barriers of the Simplest β-Sheet Fold: A Survey of WW Domains
inferred← citeshttps://doi.org/10.1021/acs.jpcb.8b05975openalex-snapshot
Instrumental Effects in the Dynamics of an Ultrafast Folding Protein under Mechanical Force
inferred← citeshttps://doi.org/10.1021/acs.jpclett.0c01848openalex-snapshot
A Disordered Loop Mediates Heterogeneous Unfolding of an Ordered Protein by Altering the Native Ensemble
inferred← citeshttps://doi.org/10.1021/acsomega.5c05567openalex-snapshot
FitFoldData: A Web-Based Toolkit for Circular Dichroism and Differential Scanning Calorimetry Data Analysis of Protein Thermal Denaturation
inferred← citeshttps://doi.org/10.1021/acssynbio.0c00190openalex-snapshot
Downhill (Un)Folding Coupled to Binding as a Mechanism for Engineering Broadband Protein Conformational Transducers
inferred← citeshttps://doi.org/10.1021/bi9007758openalex-snapshot
Thermodynamic Characterization of the Folding Equilibrium of the Human Nedd4-WW4 Domain: At the Frontiers of Cooperative Folding
inferred← citeshttps://doi.org/10.1021/ct100313aopenalex-snapshot
PACE Force Field for Protein Simulations. 2. Folding Simulations of Peptides
inferred← citeshttps://doi.org/10.1021/ct300676wopenalex-snapshot
Predictions from an Ising-like Statistical Mechanical Model on the Dynamic and Thermodynamic Effects of Protein Surface Electrostatics
inferred← citeshttps://doi.org/10.1021/ja1031503openalex-snapshot
Evidence, from Simulations, of a Single State with Residual Native Structure at the Thermal Denaturation Midpoint of a Small Globular Protein
inferred← citeshttps://doi.org/10.1021/ja103612qopenalex-snapshot
Navigating the Downhill Protein Folding Regime via Structural Homologues
inferred← citeshttps://doi.org/10.1021/ja110884mopenalex-snapshot
Quantitative Prediction of Protein Folding Behaviors from a Simple Statistical Model
inferred← citeshttps://doi.org/10.1021/ja204053nopenalex-snapshot
The Native Ensemble and Folding of a Protein Molten-Globule: Functional Consequence of Downhill Folding
inferred← citeshttps://doi.org/10.1021/ja4009562openalex-snapshot
Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins
inferred← citeshttps://doi.org/10.1021/ja502705yopenalex-snapshot
Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR
inferred← citeshttps://doi.org/10.1021/jacs.5b02324openalex-snapshot
Interaction Networks in Protein Folding via Atomic-Resolution Experiments and Long-Time-Scale Molecular Dynamics Simulations
inferred← citeshttps://doi.org/10.1021/jacs.6b10608openalex-snapshot
Graded Structural Polymorphism in a Bacterial Thermosensor Protein
inferred← citeshttps://doi.org/10.1021/jp212132vopenalex-snapshot
Configuration-Dependent Diffusion Dynamics of Downhill and Two-State Protein Folding
inferred← citeshttps://doi.org/10.1021/jp501879sopenalex-snapshot
Free Energy Landscape of Lysozyme: Multiple Near-Native Conformational States and Rollover in the Urea Dependence of Folding Energy
inferred← citeshttps://doi.org/10.1021/jp504261gopenalex-snapshot
Thermodynamics of Downhill Folding: Multi-Probe Analysis of PDD, a Protein that Folds Over a Marginal Free Energy Barrier
inferred← citeshttps://doi.org/10.1038/ncomms11777openalex-snapshot
A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution
inferred← citeshttps://doi.org/10.1038/nsmb.1592openalex-snapshot
An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms
inferred← citeshttps://doi.org/10.1038/s41598-020-78008-8openalex-snapshot
The change of conditions does not affect Ros87 downhill folding mechanism
inferred← citeshttps://doi.org/10.1038/s42004-018-0060-9openalex-snapshot
Reversible two-state folding of the ultrafast protein gpW under mechanical force
inferred← citeshttps://doi.org/10.1039/b925033fopenalex-snapshot
A natural missing link between activated and downhill protein folding scenarios
inferred← citeshttps://doi.org/10.1039/c1cp20156eopenalex-snapshot
Estimation of protein folding free energy barriers from calorimetric data by multi-model Bayesian analysis
inferred← citeshttps://doi.org/10.1039/c1cp20402eopenalex-snapshot
Integrated prediction of protein folding and unfolding rates from only size and structural class
inferred← citeshttps://doi.org/10.1039/c1cp20964gopenalex-snapshot
The protein folding transition-state ensemble from a Gō-like model
inferred← citeshttps://doi.org/10.1039/c2fd20009kopenalex-snapshot
Crowding effects on the small, fast-folding protein λ6–85
inferred← citeshttps://doi.org/10.1039/c5sc03886copenalex-snapshot
Atomistic picture of conformational exchange in a T4 lysozyme cavity mutant: an experiment-guided molecular dynamics study
inferred← citeshttps://doi.org/10.1039/c7cp03011hopenalex-snapshot
Toward a quantitative description of microscopic pathway heterogeneity in protein folding
inferred← citeshttps://doi.org/10.1039/d5sc06411bopenalex-snapshot
Local entropy in proteins
inferred← citeshttps://doi.org/10.1042/bcj20160107openalex-snapshot
When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches
inferred← citeshttps://doi.org/10.1063/1.3077008openalex-snapshot
A one-dimensional free energy surface does not account for two-probe folding kinetics of protein α3D
inferred← citeshttps://doi.org/10.1073/pnas.1506309112openalex-snapshot
Sequence, structure, and cooperativity in folding of elementary protein structural motifs
inferred← citeshttps://doi.org/10.1073/pnas.1900203116openalex-snapshot
Ultrafast folding kinetics of WW domains reveal how the amino acid sequence determines the speed limit to protein folding
inferred← citeshttps://doi.org/10.1088/1674-1056/ab8dafopenalex-snapshot
Different potential of mean force of two-state protein GB1 and downhill protein gpW revealed by molecular dynamics simulation*
inferred← citeshttps://doi.org/10.1111/febs.13503openalex-snapshot
The prokaryotic zinc‐finger: structure, function and comparison with the eukaryotic counterpart
inferred← citeshttps://doi.org/10.1111/febs.16246openalex-snapshot
Structural characterization of the thermal unfolding pathway of human VEGFR1 D2 domain
inferred← citeshttps://doi.org/10.1146/annurev-physchem-032210-103504openalex-snapshot
Probing Free-Energy Surfaces with Differential Scanning Calorimetry
inferred← citeshttps://doi.org/10.1371/journal.pone.0026409openalex-snapshot
Revisiting the NMR Structure of the Ultrafast Downhill Folding Protein gpW from Bacteriophage λ
inferred← citeshttps://doi.org/10.1371/journal.pone.0078044openalex-snapshot
Slow Proton Transfer Coupled to Unfolding Explains the Puzzling Results of Single-Molecule Experiments on BBL, a Paradigmatic Downhill Folding Protein
inferred← citeshttps://doi.org/10.2976/1.2988030openalex-snapshot
Exploiting the downhill folding regime via experiment
inferred← citeshttps://doi.org/10.3390/biophysica4020016openalex-snapshot
Differential Scanning Calorimetry of Proteins and the Two-State Model: Comparison of Two Formulas
inferred← citeshttps://doi.org/10.70675/d8ca4e5cz8936z455fzbe69zfa8cefdf6495openalex-snapshot
Simulation des mécanismes de reconnaissance ligand-récepteur des glutathion transférases humaines par calcul du paysage d’énergie libre : Applications à la science du goût et au cancer.
inferred← citeshttps://doi.org/10.7498/aps.72.20230533openalex-snapshot
Single molecule magnetic tweezers for unfolding dynamics of Acyl-CoA binding protein
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.