On the public citation graph

Navigating the Folding Routes

0 signed · 1170 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 See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.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/bip.360350114openalex-snapshot
Nucleation mechanism for protein folding and theoretical predictions for hydrogen‐exchange labeling experiments
inferredcites →https://doi.org/10.1002/prot.340210302openalex-snapshot
Funnels, pathways, and the energy landscape of protein folding: A synthesis
inferredcites →https://doi.org/10.1006/jmbi.1994.1110openalex-snapshot
Kinetics of Protein Folding
inferredcites →https://doi.org/10.1021/bi00188a023openalex-snapshot
Kinetic Mechanism of Cytochrome c Folding: Involvement of the Heme and Its Ligands
inferredcites →https://doi.org/10.1038/nsb0394-149openalex-snapshot
The barriers in protein folding
inferredcites →https://doi.org/10.1063/1.462462openalex-snapshot
Folding kinetics of proteins and copolymers
inferredcites →https://doi.org/10.1073/pnas.87.9.3526openalex-snapshot
Metastability of the folded states of globular proteins.
inferredcites →https://doi.org/10.1073/pnas.89.11.4918openalex-snapshot
Optimal protein-folding codes from spin-glass theory.
inferredcites →https://doi.org/10.1073/pnas.90.13.6369openalex-snapshot
Kinetics and thermodynamics of folding in model proteins.
inferredcites →https://doi.org/10.1073/pnas.90.24.11860openalex-snapshot
Fast events in protein folding initiated by nanosecond laser photolysis.
inferredcites →https://doi.org/10.1073/pnas.91.22.10422openalex-snapshot
Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.
inferredcites →https://doi.org/10.1073/pnas.92.8.3626openalex-snapshot
Toward an outline of the topography of a realistic protein-folding funnel.
inferredcites →https://doi.org/10.1146/annurev.bb.23.060194.001443openalex-snapshot
High-Pressure NMR Spectroscopy of Proteins and Membranes

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.4135355openalex-extracted
inferred← citeshttps://doi.org/10.1002/(sici)1097-0134(199602)24:2<145::aid-prot1>3.0.co;2-iopenalex-snapshot
Future directions in folding: The multi-state nature of protein structure
inferred← citeshttps://doi.org/10.1002/(sici)1097-0134(199612)26:4<411::aid-prot4>3.0.co;2-eopenalex-snapshot
Factors governing the foldability of proteins
inferred← citeshttps://doi.org/10.1002/(sici)1097-0134(199702)27:2<171::aid-prot3>3.0.co;2-jopenalex-snapshot
Predicting the equilibrium protein folding pathway: Structure-based analysis of staphylococcal nuclease
inferred← citeshttps://doi.org/10.1002/(sici)1097-0134(19980101)30:1<2::aid-prot2>3.0.co;2-ropenalex-snapshot
Protein folding in the landscape perspective: Chevron plots and non-arrhenius kinetics
inferred← citeshttps://doi.org/10.1002/(sici)1097-0134(19980215)30:3<295::aid-prot9>3.0.co;2-jopenalex-snapshot
Two structural subdomains of barstar detected by rapid mixing NMR measurement of amide hydrogen exchange
inferred← citeshttps://doi.org/10.1002/(sici)1097-0134(19980515)31:3<299::aid-prot6>3.0.co;2-eopenalex-snapshot
Extracting contact energies from protein structures: A study using a simplified model
inferred← citeshttps://doi.org/10.1002/(sici)1097-0134(19980701)32:1<52::aid-prot7>3.0.co;2-gopenalex-snapshot
Testing a new Monte Carlo algorithm for protein folding
inferred← citeshttps://doi.org/10.1002/(sici)1097-0134(19991201)37:4<544::aid-prot5>3.0.co;2-7openalex-snapshot
Folding Lennard-Jones proteins by a contact potential
inferred← citeshttps://doi.org/10.1002/(sici)1097-0282(199610)39:4<591::aid-bip9>3.0.co;2-sopenalex-snapshot
Extensive molecular dynamics simulations of a β-hairpin-forming peptide
inferred← citeshttps://doi.org/10.1002/(sici)1097-0282(199712)42:7<745::aid-bip1>3.0.co;2-topenalex-snapshot
Thermodynamics of protein folding: A statistical mechanical study of a small all-β protein
inferred← citeshttps://doi.org/10.1002/(sici)1099-0526(199903/04)4:4<61::aid-cplx8>3.0.co;2-nopenalex-snapshot
A parameterization of RNA sequence space
inferred← citeshttps://doi.org/10.1002/0470845015.cca022mopenalex-snapshot
Conformational Search: Proteins
inferred← citeshttps://doi.org/10.1002/0470845015.cpa027openalex-snapshot
Protein Folding and Optimization Algorithms
inferred← citeshttps://doi.org/10.1002/0471440264.pst302openalex-snapshot
Protein Folding
inferred← citeshttps://doi.org/10.1002/1097-0134(20000901)40:4<543::aid-prot20>3.0.co;2-oopenalex-snapshot
Modeling protein density of states: Additive hydrophobic effects are insufficient for calorimetric two-state cooperativity
inferred← citeshttps://doi.org/10.1002/1097-0134(20000901)40:4<637::aid-prot80>3.0.co;2-4openalex-snapshot
Polymer principles of protein calorimetric two-state cooperativity
inferred← citeshttps://doi.org/10.1002/1097-0134(20000901)40:4<637::aid-prot80>3.3.co;2-wopenalex-snapshot
Polymer principles of protein calorimetric two‐state cooperativity
inferred← citeshttps://doi.org/10.1002/1097-0134(20001115)41:3<288::aid-prot20>3.0.co;2-copenalex-snapshot
Mechanism of protein folding
inferred← citeshttps://doi.org/10.1002/1097-0134(20010215)42:3<345::aid-prot50>3.0.co;2-hopenalex-snapshot
Exploring the energy landscape of a ? hairpin in explicit solvent
inferred← citeshttps://doi.org/10.1002/1097-0134(20010215)42:3<422::aid-prot120>3.0.co;2-2openalex-snapshot
Learning effective amino acid interactions through iterative stochastic techniques
inferred← citeshttps://doi.org/10.1002/1097-0134(20010301)42:4<433::aid-prot10>3.0.co;2-sopenalex-snapshot
Computational approach to the protein-folding problem
inferred← citeshttps://doi.org/10.1002/1097-0282(200101)58:1<46::aid-bip50>3.0.co;2-qopenalex-snapshot
Effective protein folding in simple random search
inferred← citeshttps://doi.org/10.1002/1521-3757(20011119)113:22<4378::aid-ange4378>3.0.co;2-gopenalex-snapshot
Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovineα-Lactalbumin
inferred← citeshttps://doi.org/10.1002/1521-3773(20011119)40:22<4248::aid-anie4248>3.0.co;2-iopenalex-snapshot
Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine α-Lactalbumin
inferred← citeshttps://doi.org/10.1002/1522-2683(200107)22:12<2359::aid-elps2359>3.0.co;2-8openalex-snapshot
Folding/unfolding/refolding of proteins: Present methodologies in comparison with capillary zone electrophoresis
inferred← citeshttps://doi.org/10.1002/1522-2683(200109)22:17<3728::aid-elps3728>3.0.co;2-oopenalex-snapshot
Monitoring folding/unfolding transitions of proteins by capillary zone electrophoresis: Measurement ofG and its variation along the pH scale
inferred← citeshttps://doi.org/10.1002/3527600906.mcb.200300050openalex-snapshot
Food Proteins: Interactions and Functionality
inferred← citeshttps://doi.org/10.1002/3527600906.mcb.200300085openalex-snapshot
Aggregation, Protein
inferred← citeshttps://doi.org/10.1002/9780470141649.ch10openalex-snapshot
Simulated Annealing—Optimal Histogram Methods
inferred← citeshttps://doi.org/10.1002/9780470141649.ch9openalex-snapshot
Macrostate Dissection of Thermodynamic Monte Carlo Integrals
inferred← citeshttps://doi.org/10.1002/9780470141748.ch1openalex-snapshot
Energy Landscapes: From Clusters to Biomolecules
inferred← citeshttps://doi.org/10.1002/9780470939932.ch13openalex-snapshot
Refolding of Inclusion Body Proteins fromE. coli
inferred← citeshttps://doi.org/10.1002/9781119162254.ch02openalex-snapshot
Scoring Functions for Predicting Structure and Binding of Proteins
inferred← citeshttps://doi.org/10.1002/9783527612949.ch06openalex-snapshot
Protein Folding and Beyond
inferred← citeshttps://doi.org/10.1002/9783527619498.ch12bopenalex-snapshot
Characterization of Protein Folding Barriers with Rate Equilibrium Free Energy Relationships
inferred← citeshttps://doi.org/10.1002/9783527626137.ch13openalex-snapshot
Force‐clamp Spectroscopy of Single Proteins
inferred← citeshttps://doi.org/10.1002/9783527654185.ch9openalex-snapshot
Sequence‐Based Prediction of Protein Behavior
inferred← citeshttps://doi.org/10.1002/adts.201800175openalex-snapshot
Energy Landscapes for Proteins: From Single Funnels to Multifunctional Systems
inferred← citeshttps://doi.org/10.1002/advs.76023openalex-snapshot
AI‐Physics‐Experiment Trinity for Integrated Protein Dynamics Modeling
inferred← citeshttps://doi.org/10.1002/ange.200802644openalex-snapshot
Kohärente mehrdimensionale Schwingungsspektroskopie von Biomolekülen: Konzepte, Simulationen und Herausforderungen
inferred← citeshttps://doi.org/10.1002/ange.201308512openalex-snapshot
An Off‐Pathway Folding Intermediate of an Acyl Carrier Protein Domain Coexists with the Folded and Unfolded States under Native Conditions
inferred← citeshttps://doi.org/10.1002/anie.200802644openalex-snapshot
Coherent Multidimensional Vibrational Spectroscopy of Biomolecules: Concepts, Simulations, and Challenges
inferred← citeshttps://doi.org/10.1002/anie.201308512openalex-snapshot
An Off‐Pathway Folding Intermediate of an Acyl Carrier Protein Domain Coexists with the Folded and Unfolded States under Native Conditions
inferred← citeshttps://doi.org/10.1002/app.32786openalex-snapshot
Synthesis and comparative solution properties of a cationic polyelectrolyte and its corresponding polyzwitterion from 1,1‐diallyl‐4‐methoxycarbonylpiperidinium chloride
inferred← citeshttps://doi.org/10.1002/bip.20388openalex-snapshot
Removal of kinetic traps and enhanced protein folding by strategic substitution of amino acids in a model α‐helical hairpin peptide
inferred← citeshttps://doi.org/10.1002/bip.20866openalex-snapshot
Structural insights into cold inactivation of tryptophanase and cold adaptation of subtilisin S41
inferred← citeshttps://doi.org/10.1002/chem.201000619openalex-snapshot
A Self‐Powered and Reusable Biocomputing Security Keypad Lock System Based on Biofuel Cells
inferred← citeshttps://doi.org/10.1002/cphc.200400024openalex-snapshot
Biofunctionalized Polymer Surfaces Exhibiting Minimal Interaction towards Immobilized Proteins
inferred← citeshttps://doi.org/10.1002/cphc.200700662openalex-snapshot
From Valleys to Ridges: Exploring the Dynamic Energy Landscape of Single Membrane Proteins
inferred← citeshttps://doi.org/10.1002/cphc.201500700openalex-snapshot
Reduction of the Search Space for the Folding of Proteins at the Level of Formation and Assembly of Secondary Structures: A New View on the Solution of Levinthal′s Paradox
inferred← citeshttps://doi.org/10.1002/cphc.201501125openalex-snapshot
Stochastic Resonance in Protein Folding Dynamics
inferred← citeshttps://doi.org/10.1002/cplx.10052openalex-snapshot
Networks in molecular evolution
inferred← citeshttps://doi.org/10.1002/ijch.201400012openalex-snapshot
Simulating Biomolecular Folding and Function by Native‐Structure‐Based/Go‐Type Models
inferred← citeshttps://doi.org/10.1002/ijch.201400022openalex-snapshot
Coarse‐Grained and Atomistic MD Simulations of RNA and DNA Folding
inferred← citeshttps://doi.org/10.1002/ijch.201400030openalex-snapshot
Structural Heterogeneity and Dynamics of the Unfolded Ensemble
inferred← citeshttps://doi.org/10.1002/ijch.201400074openalex-snapshot
Significance of Molecular Dynamics Simulations for Life Sciences
inferred← citeshttps://doi.org/10.1002/iub.223openalex-snapshot
Protein folding simulations: From coarse‐grained model to all‐atom model
inferred← citeshttps://doi.org/10.1002/jcc.27060openalex-snapshot
Evolutionary conservation of amino acids contributing to the protein folding transition state
inferred← citeshttps://doi.org/10.1002/jccs.200000141openalex-snapshot
Protein Folding and β‐Sheet Proteins
inferred← citeshttps://doi.org/10.1002/jccs.200400163openalex-snapshot
Modular Assembly Revealed by Tryptophan and Other Optical Probes in Staphylococcal Nuclease Folding
inferred← citeshttps://doi.org/10.1002/jccs.202400396openalex-snapshot
How simple models explain complex protein folding behaviors
inferred← citeshttps://doi.org/10.1002/mabi.200600158openalex-snapshot
Exploring Protein Structure and Dynamics under Denaturing Conditions by Single‐Molecule FRET Analysis
inferred← citeshttps://doi.org/10.1002/mats.201900036openalex-snapshot
Network Topology of the States Probed by a Glassy Polymer during Physical Aging
inferred← citeshttps://doi.org/10.1002/nadc.19960440209openalex-snapshot
Biochemie und Molekulargenetik 1995
inferred← citeshttps://doi.org/10.1002/nadc.19990470211openalex-snapshot
Biochemie und Molekulargenetik 1998
inferred← citeshttps://doi.org/10.1002/pi.2176openalex-snapshot
Study of structure and scaling behavior of chemically unfolded β‐casein by means of small‐angle neutron scattering
inferred← citeshttps://doi.org/10.1002/pmic.201000241openalex-snapshot
Dual energy landscape: The functional state of the β‐barrel outer membrane protein G molds its unfolding energy landscape
inferred← citeshttps://doi.org/10.1002/pmic.201800059openalex-snapshot
Formation of Heterotypic Amyloids: α‐Synuclein in Co‐Aggregation
inferred← citeshttps://doi.org/10.1002/pola.10336openalex-snapshot
Synthesis of a new amino acid/sulfur dioxide copolymer and its use in aqueous two‐phase polymer systems
inferred← citeshttps://doi.org/10.1002/pola.10565openalex-snapshot
Synthesis and solution properties of a new pH‐responsive polymer containing amino propanesulfonic acid residues
inferred← citeshttps://doi.org/10.1002/pro.2256openalex-snapshot
Ensemble‐based characterization of unbound and bound states on protein energy landscape
inferred← citeshttps://doi.org/10.1002/pro.296openalex-snapshot
β‐strand interactions at the domain interface critical for the stability of human lens γD‐crystallin
inferred← citeshttps://doi.org/10.1002/pro.339openalex-snapshot
Amino acid interaction preferences in proteins
inferred← citeshttps://doi.org/10.1002/pro.4096openalex-snapshot
Protein folding ‐ seeing is deceiving
inferred← citeshttps://doi.org/10.1002/pro.4332openalex-snapshot
Characterization of early and late transition states of the folding pathway of a SH2 domain
inferred← citeshttps://doi.org/10.1002/pro.444openalex-snapshot
Interaction of an ionic complementary peptide with a hydrophobic graphite surface
inferred← citeshttps://doi.org/10.1002/pro.5560040921openalex-snapshot
A statistical mechanical model for hydrogen exchange in globular proteins
inferred← citeshttps://doi.org/10.1002/pro.5560051015openalex-snapshot
In vitro renaturation of bovine β‐lactoglobulin A leads to a biologically active but incompletely refolded state
inferred← citeshttps://doi.org/10.1002/pro.5560060210openalex-snapshot
A desolvation barrier to hydrophobic cluster formation may contribute to the rate‐limiting step in protein folding
inferred← citeshttps://doi.org/10.1002/pro.5560060709openalex-snapshot
Absence of a stable intermediate on the folding pathway of protein A
inferred← citeshttps://doi.org/10.1002/pro.5560060713openalex-snapshot
Temperature control for kinetic refolding of heat‐denatured ovalbumin
inferred← citeshttps://doi.org/10.1002/pro.5560060719openalex-snapshot
Mutational analysis of the BPTI folding pathway: I. Effects of aromatic → leucine substitutions on the distribution of folding intermediates
inferred← citeshttps://doi.org/10.1002/pro.5560061210openalex-snapshot
Lack of coupling between secondary structure formation and collapse in a model polypeptide that mimics early folding intermediates, the F2 fragment of the Escherichia coli tryptophan‐synthase β chain
inferred← citeshttps://doi.org/10.1002/pro.5560070415openalex-snapshot
Conformational diversity of acid‐denatured cytochrome c studied by a matrix analysis of far‐UV CD spectra
inferred← citeshttps://doi.org/10.1002/pro.619openalex-snapshot
Constraining local structure can speed up folding by promoting structural polarization of the folding pathway
inferred← citeshttps://doi.org/10.1002/prot.10185openalex-snapshot
Effects of a helix substitution on the folding mechanism of bovine α‐lactalbumin
inferred← citeshttps://doi.org/10.1002/prot.10342openalex-snapshot
Prediction of folding rates and transition‐state placement from native‐state geometry
inferred← citeshttps://doi.org/10.1002/prot.1039openalex-snapshot
Population analyses of kinetic partitioning in protein folding
inferred← citeshttps://doi.org/10.1002/prot.1049openalex-snapshot
Molecular dynamics studies on HIV‐1 protease: Drug resistance and folding pathways
inferred← citeshttps://doi.org/10.1002/prot.10563openalex-snapshot
Funnel‐like organization in sequence space determines the distributions of protein stability and folding rate preferred by evolution
inferred← citeshttps://doi.org/10.1002/prot.10583openalex-snapshot
Squeezed exponential kinetics to describe a nonglassy downhill folding as observed in a lattice protein model
inferred← citeshttps://doi.org/10.1002/prot.1107openalex-snapshot
Structured disorder and conformational selection
inferred← citeshttps://doi.org/10.1002/prot.20094openalex-snapshot
Recognition of coarse‐grained protein tertiary structure
inferred← citeshttps://doi.org/10.1002/prot.20175openalex-snapshot
Transition states for folding of circular‐permuted proteins
inferred← citeshttps://doi.org/10.1002/prot.20247openalex-snapshot
Exploring peptide energy landscapes: A test of force fields and implicit solvent models
inferred← citeshttps://doi.org/10.1002/prot.20313openalex-snapshot
Study of the Villin headpiece folding dynamics by combining coarse‐grained Monte Carlo evolution and all‐atom molecular dynamics
inferred← citeshttps://doi.org/10.1002/prot.20585openalex-snapshot
Atomically detailed potentials to recognize native and approximate protein structures
inferred← citeshttps://doi.org/10.1002/prot.20714openalex-snapshot
Computational characterization of the sequence landscape in simple protein alphabets
inferred← citeshttps://doi.org/10.1002/prot.20782openalex-snapshot
Effect of ethanol on folding of hen egg‐white lysozyme under acidic condition
inferred← citeshttps://doi.org/10.1002/prot.21069openalex-snapshot
Transition state of a SH3 domain detected with principle component analysis and a charge‐neutralized all‐atom protein model
inferred← citeshttps://doi.org/10.1002/prot.21185openalex-snapshot
Complexity of free energy landscapes of peptides revealed by nonlinear principal component analysis
inferred← citeshttps://doi.org/10.1002/prot.21317openalex-snapshot
Conformational states and folding pathways of peptides revealed by principal‐independent component analyses
inferred← citeshttps://doi.org/10.1002/prot.21345openalex-snapshot
Can molecular dynamics simulations provide high‐resolution refinement of protein structure?
inferred← citeshttps://doi.org/10.1002/prot.21830openalex-snapshot
Distant homology detection using a LEngth and STructure‐based sequence Alignment Tool (LESTAT)
inferred← citeshttps://doi.org/10.1002/prot.22099openalex-snapshot
How general is the nucleation–condensation mechanism?
inferred← citeshttps://doi.org/10.1002/prot.22626openalex-snapshot
Predicting protein complex geometries with a neural network
inferred← citeshttps://doi.org/10.1002/prot.23074openalex-snapshot
Mechanistic insight of photo‐induced aggregation of chicken egg white lysozyme: The interplay between hydrophobic interactions and formation of intermolecular disulfide bonds
inferred← citeshttps://doi.org/10.1002/prot.24309openalex-snapshot
Analyzing the effect of homogeneous frustration in protein folding
inferred← citeshttps://doi.org/10.1002/prot.24460openalex-snapshot
Molecular dynamics study of HIV‐1 RT‐DNA‐nevirapine complexes explains NNRTI inhibition and resistance by connection mutations
inferred← citeshttps://doi.org/10.1002/prot.24980openalex-snapshot
Identification of putative unfolding intermediates of the mutant His‐107‐tyr of human carbonic anhydrase II in a multidimensional property space
inferred← citeshttps://doi.org/10.1002/prot.26062openalex-snapshot
Investigating the folding mechanism of the N‐terminal domain of ribosomal protein L9
inferred← citeshttps://doi.org/10.1002/prot.26349openalex-snapshot
Multi‐layer sequential network analysis improves protein 3D structural classification
inferred← citeshttps://doi.org/10.1002/prot.26566openalex-snapshot
II . Geometrical framework for thinking about globular proteins: The power of poking
inferred← citeshttps://doi.org/10.1002/prot.26567openalex-snapshot
A geometrical framework for thinking about proteins
inferred← citeshttps://doi.org/10.1002/qua.22347openalex-snapshot
Structural alignment using the generalized Euclidean distance between conformations
inferred← citeshttps://doi.org/10.1002/qua.26089openalex-snapshot
Moment expansion approach to the time dynamics of genetic evolution
inferred← citeshttps://doi.org/10.1002/wcms.1130openalex-snapshot
Proteins in the gas phase
inferred← citeshttps://doi.org/10.1006/jmbi.1996.0156openalex-snapshot
Local Conformational Signals and the Statistical Thermodynamics of Collapsed Helical Proteins
inferred← citeshttps://doi.org/10.1006/jmbi.1996.0793openalex-snapshot
Folding kinetics of Che Y mutants with enhanced native α-helix propensities 1 1Edited by A. R. Fersht
inferred← citeshttps://doi.org/10.1006/jmbi.1997.0960openalex-snapshot
Folding of the disulfide-bonded β-sheet protein tendamistat: rapid two-state folding without hydrophobic collapse 1 1Edited by A. R. Fersht
inferred← citeshttps://doi.org/10.1006/jmbi.1997.0996openalex-snapshot
Structural characterisation and comparison of the native and A-states of equine lysozyme
inferred← citeshttps://doi.org/10.1006/jmbi.1997.1284openalex-snapshot
Torsion angle dynamics for NMR structure calculation with the new program Dyana
inferred← citeshttps://doi.org/10.1006/jmbi.1998.1997openalex-snapshot
Lattice models for proteins reveal multiple folding nuclei for nucleation-collapse mechanism 1 1Edited by A. R. Fersht
inferred← citeshttps://doi.org/10.1006/jmbi.1998.2588openalex-snapshot
The greek key protein apo-pseudoazurin folds through an obligate on-pathway intermediate 1 1Edited by A. R. Fersht
inferred← citeshttps://doi.org/10.1006/jmbi.1999.2612openalex-snapshot
Exploring structures in protein folding funnels with free energy functionals: the denatured ensemble
inferred← citeshttps://doi.org/10.1006/jmbi.1999.2613openalex-snapshot
Exploring structures in protein folding funnels with free energy functionals: the transition state ensemble
inferred← citeshttps://doi.org/10.1006/jmbi.1999.2843openalex-snapshot
Analysis methods for comparison of multiple molecular dynamics trajectories: applications to protein unfolding pathways and denatured ensembles 1 1Edited by A. R. Fersht
inferred← citeshttps://doi.org/10.1006/jmbi.1999.2924openalex-snapshot
Experimental study of the protein folding landscape: unfolding reactions in cytochrome c
inferred← citeshttps://doi.org/10.1006/jmbi.1999.3006openalex-snapshot
Protein folding: from the levinthal paradox to structure prediction
inferred← citeshttps://doi.org/10.1006/jmbi.2000.3922openalex-snapshot
A statistical appraisal of native state hydrogen exchange data: evidence for a burst phase continuum?11Edited by P. E. Wright
inferred← citeshttps://doi.org/10.1006/jmbi.2000.4314openalex-snapshot
A kinetic folding intermediate probed by native state hydrogen exchange11Edited by A. R. Fersht
inferred← citeshttps://doi.org/10.1006/jmbi.2000.4399openalex-snapshot
Apparent two-state tendamistat folding is a sequential process along a defined route11Edited by A. R. Fersht
inferred← citeshttps://doi.org/10.1006/jmbi.2001.4436openalex-snapshot
Native hydrogen bonds in a molten globule: the apoflavodoxin thermal intermediate
inferred← citeshttps://doi.org/10.1006/jmbi.2001.4804openalex-snapshot
Origin of apparent fast and non-exponential kinetics of lysozyme folding measured in pulsed hydrogen exchange experiments
inferred← citeshttps://doi.org/10.1007/0-306-48628-8_5openalex-snapshot
Hairpin Formation in Polynucleotides: A Simple Folding Problem?
inferred← citeshttps://doi.org/10.1007/0-387-25919-8_2openalex-snapshot
The Generic Nature of Protein Folding and Misfolding
inferred← citeshttps://doi.org/10.1007/1-4020-4814-9_4openalex-snapshot
The Necessity Of Biosemiotics: Matter-Symbol Complementarity
inferred← citeshttps://doi.org/10.1007/3-540-27004-3_10openalex-snapshot
Protein Dynamics and Protein Folding Dynamics Revealed by Time-Resolved Fluorescence
inferred← citeshttps://doi.org/10.1007/3-540-45621-x_10openalex-snapshot
Energy Landscapes
inferred← citeshttps://doi.org/10.1007/978-0-387-30379-6_10openalex-snapshot
Protein Folding
inferred← citeshttps://doi.org/10.1007/978-0-387-68372-0_3openalex-snapshot
Knowledge-Based Energy Functions for Computational Studies of Proteins
inferred← citeshttps://doi.org/10.1007/978-0-387-76497-9_16openalex-snapshot
Probing Single Membrane Proteins by Atomic Force Microscopy
inferred← citeshttps://doi.org/10.1007/978-1-4020-9394-4_15openalex-snapshot
Systems-Level Analysis of Protein Quality in Inclusion Body-Forming Escherichia coli Cells
inferred← citeshttps://doi.org/10.1007/978-1-4020-9650-1_17openalex-snapshot
The Physics and Metaphysics of Biosemiotics
inferred← citeshttps://doi.org/10.1007/978-1-4419-6351-2_6openalex-snapshot
Topics in Nucleic Acids Structure: DNA Interactions and Folding
inferred← citeshttps://doi.org/10.1007/978-1-4419-6889-0_6openalex-snapshot
Statistical Contact Potentials in Protein Coarse-Grained Modeling: From Pair to Multi-body Potentials
inferred← citeshttps://doi.org/10.1007/978-1-4612-4066-2_13openalex-snapshot
Pursuing Laplace’s Vision on Modern Computers
inferred← citeshttps://doi.org/10.1007/978-1-4613-0279-7_8openalex-snapshot
Global Minimization and Parameter Estimation in Computational Biology
inferred← citeshttps://doi.org/10.1007/978-1-4614-2152-8_11openalex-snapshot
Subcellular Systems
inferred← citeshttps://doi.org/10.1007/978-1-4615-5903-0_17openalex-snapshot
Picturing the Working Protein
inferred← citeshttps://doi.org/10.1007/978-1-4757-3218-4_3openalex-snapshot
Energy Landscape Projections of Molecular Potential Functions
inferred← citeshttps://doi.org/10.1007/978-1-4757-5284-7_1openalex-snapshot
Convex Global Underestimation for Molecular Structure Prediction
inferred← citeshttps://doi.org/10.1007/978-1-59259-322-4_23openalex-snapshot
Protein Models
inferred← citeshttps://doi.org/10.1007/978-1-59745-367-7_13openalex-snapshot
Single-Molecule Fluorescence Studies of Protein Folding
inferred← citeshttps://doi.org/10.1007/978-3-030-04598-2_2openalex-snapshot
Science as a Social Self-organizing Extended Cognitive System. Coherence and Flexibility of Scientific Explanatory Patterns
inferred← citeshttps://doi.org/10.1007/978-3-030-28303-2_2openalex-snapshot
The Amino Acid Sequences of Proteins Determine Folding and Non-folding
inferred← citeshttps://doi.org/10.1007/978-3-0348-0651-0_2openalex-snapshot
Studying Protein Interior with Fractal Dimension
inferred← citeshttps://doi.org/10.1007/978-3-319-02970-2_8openalex-snapshot
Simulating Protein Folding in Different Environmental Conditions
inferred← citeshttps://doi.org/10.1007/978-3-319-23449-6_4openalex-snapshot
Managing the Adaptive Proteostatic Landscape: Restoring Resilience in Alpha-1 Antitrypsin Deficiency
inferred← citeshttps://doi.org/10.1007/978-3-319-50688-3_10openalex-snapshot
Molecular Dynamics Simulations of Biocorona Formation
inferred← citeshttps://doi.org/10.1007/978-3-319-91092-5_27openalex-snapshot
Two Views on the Protein Folding Puzzle
inferred← citeshttps://doi.org/10.1007/978-3-319-95843-9_3openalex-snapshot
Protein Dynamics Simulations Using Coarse-Grained Models
inferred← citeshttps://doi.org/10.1007/978-3-540-39668-0_6openalex-snapshot
Information Complexity and Biology
inferred← citeshttps://doi.org/10.1007/978-3-540-88787-4_13openalex-snapshot
Protein Misfolding Diseases and the Key Role Played by the Interactions of Polypeptides with Water
inferred← citeshttps://doi.org/10.1007/978-3-642-01228-0_9openalex-snapshot
Formation of the Functional Structure of Enzymes: Co- and Post-Translational Events
inferred← citeshttps://doi.org/10.1007/978-3-642-28554-7_3openalex-snapshot
Coarse-Grained Modeling of Protein Dynamics
inferred← citeshttps://doi.org/10.1007/978-3-642-28882-1_6openalex-snapshot
Self-Evolvability for Biosystems
inferred← citeshttps://doi.org/10.1007/978-3-642-33206-7_3openalex-snapshot
Rugged and Elementary Landscapes
inferred← citeshttps://doi.org/10.1007/978-3-642-59542-4_4openalex-snapshot
Strain-Dependent Fluorescence Correlation Spectroscopy: Proposing a New Measurement for Conformational Fluctuations of Biological Macromolecules
inferred← citeshttps://doi.org/10.1007/978-3-642-60854-4_49openalex-snapshot
Surveying a potential energy surface by eigenvector-following
inferred← citeshttps://doi.org/10.1007/978-3-7091-0670-9_11openalex-snapshot
Interplay Between Phase Separation and Polymer Crystallization
inferred← citeshttps://doi.org/10.1007/978-94-007-5161-3_18openalex-snapshot
The Necessity of Biosemiotics: Matter-Symbol Complementarity
inferred← citeshttps://doi.org/10.1007/978-94-007-6546-7_19openalex-snapshot
Habitability on Kepler Worlds: Are Moons Relevant?
inferred← citeshttps://doi.org/10.1007/978-981-10-4651-3_10openalex-snapshot
Evolution of Multiple Chaperonins: Innovation of Evolutionary Capacitors
inferred← citeshttps://doi.org/10.1007/978-981-15-9144-0_5openalex-snapshot
Modeling and Analysis of Large-Scale Networks
inferred← citeshttps://doi.org/10.1007/978-981-96-2088-3_12openalex-snapshot
Force Spectroscopy Tools for Probing the Mechanochemistry of Protein Folding/Unfolding
inferred← citeshttps://doi.org/10.1007/978-981-97-2987-6_1openalex-snapshot
Introduction
inferred← citeshttps://doi.org/10.1007/bf02738169openalex-snapshot
Folding funnels and conformational transitions via hinge-bending motions
inferred← citeshttps://doi.org/10.1007/bf02897477openalex-snapshot
A symmetry-related sequence-structure relation of proteins
inferred← citeshttps://doi.org/10.1007/bf02932892openalex-snapshot
What is the role of thermodynamics on protein stability?
inferred← citeshttps://doi.org/10.1007/bfb0105008openalex-snapshot
Scaling laws for protein folding
inferred← citeshttps://doi.org/10.1007/s00018-016-2340-9openalex-snapshot
Expanding role of molecular chaperones in regulating α-synuclein misfolding; implications in Parkinson’s disease
inferred← citeshttps://doi.org/10.1007/s000180050042openalex-snapshot
Recent insights on RNA folding mechanisms from catalytic RNA
inferred← citeshttps://doi.org/10.1007/s000180050072openalex-snapshot
Protein folding: concepts and perspectives
inferred← citeshttps://doi.org/10.1007/s00214-005-0026-8openalex-snapshot
Protein Folding Simulations: Combining Coarse-grained Models and All-atom Molecular Dynamics
inferred← citeshttps://doi.org/10.1007/s00232-019-00069-2openalex-snapshot
The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins
inferred← citeshttps://doi.org/10.1007/s002490050033openalex-snapshot
Stopped-flow dynamic light scattering as a method to monitor compaction during protein folding
inferred← citeshttps://doi.org/10.1007/s00396-015-3713-6openalex-snapshot
The fragile-to-strong dynamical crossover and the system viscoelasticity in attractive glass forming colloids
inferred← citeshttps://doi.org/10.1007/s00396-015-3770-xopenalex-snapshot
Erratum to: The fragile-to-strong dynamical crossover and the system viscoelasticity in attractive glass forming colloids
inferred← citeshttps://doi.org/10.1007/s00449-022-02696-xopenalex-snapshot
Chemical modification for improving catalytic performance of lipase B from Candida antarctica with hydrophobic proline ionic liquid
inferred← citeshttps://doi.org/10.1007/s00453-007-0178-0openalex-snapshot
Sampling Conformation Space to Model Equilibrium Fluctuations in Proteins
inferred← citeshttps://doi.org/10.1007/s004600050192openalex-snapshot
Surveying a potential energy surface by eigenvector-following
inferred← citeshttps://doi.org/10.1007/s10710-022-09427-xopenalex-snapshot
Evolving cellular automata schemes for protein folding modeling using the Rosetta atomic representation
inferred← citeshttps://doi.org/10.1007/s10930-013-9497-yopenalex-snapshot
Two Global Conformation States of a Novel NAD(P) Reductase Like Protein of the Thermogenic Appendix of the Sauromatum guttatum Inflorescence
inferred← citeshttps://doi.org/10.1007/s10955-011-0148-4openalex-snapshot
Simple Model Study of Phase Transition Properties of Isolated and Aggregated Protein
inferred← citeshttps://doi.org/10.1007/s10955-012-0456-3openalex-snapshot
Protein Sequence and Structure: Is One More Fundamental than the Other?
inferred← citeshttps://doi.org/10.1007/s11071-021-06239-zopenalex-snapshot
Deterministic and stochastic dynamics in a gene regulatory network mediated by miRNA
inferred← citeshttps://doi.org/10.1007/s11427-014-4617-2openalex-snapshot
Physicochemical bases for protein folding, dynamics, and protein-ligand binding
inferred← citeshttps://doi.org/10.1007/s11427-014-4728-9openalex-snapshot
Statistical analyses of protein folding rates from the view of quantum transition
showing the first 200 of 1157 · page through all 1157
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.