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Thermodynamics of ubiquitin unfolding
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Determination of stability of the DNA double helix in an aqueous medium
inferredcites →https://doi.org/10.1002/bip.360100713openalex-snapshot
Correction of light‐scattering errors in spectrophotometric protein determinations
inferredcites →https://doi.org/10.1002/bip.360230813openalex-snapshot
Buried surface area, conformational entropy, and protein stability
inferredcites →https://doi.org/10.1002/bip.360301102openalex-snapshot
Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range
inferredcites →https://doi.org/10.1002/pro.5560021204openalex-snapshot
Thermodynamics of bpti folding
inferredcites →https://doi.org/10.1006/jmbi.1993.1049openalex-snapshot
Protein Folding in the Absence of the Solvent Ordering Contribution to the Hydrophobic Interaction
inferredcites →https://doi.org/10.1006/jmbi.1993.1416openalex-snapshot
Contribution of Hydration to Protein Folding Thermodynamics
inferredcites →https://doi.org/10.1006/jmbi.1993.1417openalex-snapshot
Contribution of Hydration to Protein Folding Thermodynamics
inferredcites →https://doi.org/10.1016/0003-2697(89)90602-7openalex-snapshot
Calculation of protein extinction coefficients from amino acid sequence data
inferredcites →https://doi.org/10.1016/0003-9861(86)90741-1openalex-snapshot
Alcohol-induced conformational changes of ubiquitin
inferredcites →https://doi.org/10.1016/0005-2795(77)90140-4openalex-snapshot
Nuclear magnetic resonance studies of the denaturation of ubiquitin
inferredcites →https://doi.org/10.1016/0022-2836(73)90011-9openalex-snapshot
Environment and exposure to solvent of protein atoms. Lysozyme and insulin
inferredcites →https://doi.org/10.1016/0022-2836(74)90188-0openalex-snapshot
A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
inferredcites →https://doi.org/10.1016/0022-2836(76)90191-1openalex-snapshot
The nature of the accessible and buried surfaces in proteins
inferredcites →https://doi.org/10.1016/0022-2836(87)90038-6openalex-snapshot
Interior and surface of monomeric proteins
inferredcites →https://doi.org/10.1016/0022-2836(87)90679-6openalex-snapshot
Structure of ubiquitin refined at 1.8 Å resolution
inferredcites →https://doi.org/10.1016/0022-2836(89)90318-5openalex-snapshot
Heat capacity and conformation of proteins in the denatured state
inferredcites →https://doi.org/10.1016/0022-2836(92)90555-xopenalex-snapshot
Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding
inferredcites →https://doi.org/10.1016/0022-2836(92)90988-vopenalex-snapshot
Thermodynamics of unfolding of the α-amylase inhibitor tendamistat
inferredcites →https://doi.org/10.1016/0022-2836(92)91058-wopenalex-snapshot
Hydrogen bonding in globular proteins
inferredcites →https://doi.org/10.1016/0076-6879(86)31033-4openalex-snapshot
[2]Scanning microcalorimetry in studying temperature-induced changes in proteins
inferredcites →https://doi.org/10.1016/0079-6107(84)90007-5openalex-snapshot
Hydrogen bonding in globular proteins
inferredcites →https://doi.org/10.1016/s0022-2836(05)80197-4openalex-snapshot
Heat capacity of proteins
inferredcites →https://doi.org/10.1016/s0022-2836(05)80198-6openalex-snapshot
Heat capacity of proteins
inferredcites →https://doi.org/10.1016/s0022-2836(77)80200-3openalex-snapshot
The protein data bank: A computer-based archival file for macromolecular structures
inferredcites →https://doi.org/10.1016/s0065-3233(08)60460-xopenalex-snapshot
Stability of Proteins Small Globular Proteins
inferredcites →https://doi.org/10.1021/bi00161a019openalex-snapshot
Hydrogen exchange in native and alcohol forms of ubiquitin
inferredcites →https://doi.org/10.1021/bi00226a020openalex-snapshot
Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitin
inferredcites →https://doi.org/10.1021/bi00397a013openalex-snapshot
Sequential proton NMR assignments and secondary structure identification of human ubiquitin
inferredcites →https://doi.org/10.1038/nbt0390-209openalex-snapshot
New Perspectives on the Structure and Function of Ubiquitin
inferredcites →https://doi.org/10.1073/pnas.89.6.2017openalex-snapshot
Early hydrogen-bonding events in the folding reaction of ubiquitin.
inferredcites →https://doi.org/10.13018/bmr68openalex-snapshot
Sequential 1H NMR Assignments and Secondary Structure Identification of Human Ubiquitin
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Dramatic Increase in Unfolding Rate of Ubiquitin at High Sds Concentrations: A Threshold Value for Sds Penetration?
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Energetic Basis of Protein Structure
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The immunosuppressive activity and solution structures of ubiquitin fragments
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A Universal Expression Tag for Structural and Functional Studies of Proteins
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Zinc(II) Complexes of Ubiquitin: Speciation, Affinity and Binding Features
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Two‐Distinct Polymer Ubiquitin Conjugates by Photochemical Grafting‐From
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THE IMS PARADOX: A PERSPECTIVE ON STRUCTURAL ION MOBILITY‐MASS SPECTROMETRY
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Thermal coefficients of the methyl groups within ubiquitin
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Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR
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Thermodynamics of bpti folding
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Localized solution structure refinement of an F45W variant of ubiquitin using stochastic boundary molecular dynamics and NMR distance restraints
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Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
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On the entropy of protein folding
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Anion binding to the ubiquitin molecule
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Thermal versus mechanical unfolding of ubiquitin
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Temperature-induced unfolding behavior of proteins studied by tensorial elastic network model
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Thermal unfolding of proteins probed by laser spray mass spectrometry
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Thermal Unfolding of the DNA-binding Protein Sso7d from the HyperthermophileSulfolobus solfataricus
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Linkage of protonation and anion binding to the folding of Sac7d
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Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2 and Sa3 1 1Edited by P. E. Wright
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Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima 1 1Edited by A. R. Fersht
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[L29M] substitution in the interface of subunit-subunit interactions enhances Escherichia coli RecA protein properties important for its recombinogenic activity 1 1Edited by J. Karn
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Thermodynamics of protein folding: methodology, data analysis and interpretation of data
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Molecular dynamics simulation of the effect of temperature on the conformation of ubiquitin protein
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Role of electrostatics in the thermal stability of ubiquitin
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[6] Thermal denaturation methods in the study of protein folding
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Hydration effects in protein unfolding
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CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases
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Thermal unfolding of the archaeal DNA and RNA binding protein Ssh10
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Microcalorimetry of biological macromolecules
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Nonadditivity in Conformational Entropy upon Molecular Rigidification Reveals a Universal Mechanism Affecting Folding Cooperativity
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Probing multimodal ligand binding regions on ubiquitin using nuclear magnetic resonance, chromatography, and molecular dynamics simulations
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Combining size-exclusion chromatography with differential hydrogen–deuterium exchange to study protein conformational changes
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Alzheimer’s disease-associated ubiquitin mutant Ubb+1: Properties of the carboxy-terminal domain and its influence on biomolecular interactions
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Analyses of the Effects of All Ubiquitin Point Mutants on Yeast Growth Rate
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Alanine Scan of Core Positions in Ubiquitin Reveals Links between Dynamics, Stability, and Function
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Core Structures of Ubiquitin Dictate Its Dynamics and Function
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A Highly Diverse and Functional Naïve Ubiquitin Variant Library for Generation of Intracellular Affinity Reagents
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Electrostatic interaction-induced inclusion body formation of glucagon-like peptide-1 fused with ubiquitin and cationic tag
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Role of Hydration Water in Protein Unfolding
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AS‐48: a circular protein with an extremely stable globular structure
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Allosteric Switching by Mutually Exclusive Folding of Protein Domains
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Enthalpic Contribution to Protein Stability: Insights from Atom-Based Calculations and Statistical Mechanics
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Energetics of Protein Structure
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Chapter 7 A Computational Approach for the Rational Design of Stable Proteins and Enzymes
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Cold denaturation of ubiquitin
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Calculation of the standard molal thermodynamic properties of aqueous biomolecules at elevated temperatures and pressures II. Unfolded proteins
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Heat capacities of protein functional groups
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An alternative approach in the structure-based predictions of the thermodynamics of protein unfolding
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Heat capacities of amino acids, peptides and proteins
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Characterizing cosolvent effects on protein stability: cold-denaturation of ubiquitin in the presence of guanidine
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Mass Spectrometry-Based Thermal Shift Assay for Protein−Ligand Binding Analysis
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Electrothermal Supercharging of Proteins in Native Electrospray Ionization
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Sample Flow Rate Scan in Electrospray Ionization Mass Spectrometry Reveals Alterations in Protein Charge State Distribution
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Variable-Temperature Electrospray Ionization for Temperature-Dependent Folding/Refolding Reactions of Proteins and Ligand Binding
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Protein Unfolding in Freeze Frames: Intermediate States are Revealed by Variable-Temperature Ion Mobility–Mass Spectrometry
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Laser-Induced Denaturation of Cytochrome c in Electrospray Droplets
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New High Resolution Ion Mobility Mass Spectrometer Capable of Measurements of Collision Cross Sections from 150 to 520 K
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Slow Conformational Exchange between Partially Folded and Near-Native States of Ubiquitin: Evidence for a Multistate Folding Model
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Hydrophobic Collapse of Ubiquitin Generates Rapid Protein–Water Motions
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Extending the Experimentally Accessible Range of Spin Dipole–Dipole Spectral Densities for Protein–Cosolute Interactions by Temperature-Dependent Solvent Paramagnetic Relaxation Enhancement Measurements
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Temperature-Dependent Trimethylamine N -Oxide Induced the Formation of Substance P Dimers
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Statistical-Mechanics Analyses on Thermodynamics of Protein Folding Constructed by Privalov and Co-Workers
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Dissecting Ubiquitin Folding Using the Self-Organized Polymer Model
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Protein Transfer Free Energy Obeys Entropy-Enthalpy Compensation
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Collapse Precedes Folding in Denaturant-Dependent Assembly of Ubiquitin
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The Sensitivity of Computational Protein Folding to Contact Map Perturbations: The Case of Ubiquitin Folding and Function
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Ionic Liquid-Induced Modulation of Ubiquitin Stability: The Dominant Role of Hydrophobic Interactions
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Single Molecule Force Spectroscopy and Molecular Dynamics Simulations as a Combined Platform for Probing Protein Face-Specific Binding
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Modulated Scanning Fluorimetry Can Quickly Assess Thermal Protein Unfolding Reversibility in Microvolume Samples
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Dissecting the Thermodynamics of ATP Binding to GroEL One Nucleotide at a Time
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Dynamics of the Myoglobin/Heme Complex: A Limited Proteolysis Perspective
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Robust Design of Effective Allosteric Activators for Rsp5 E3 Ligase Using the Machine Learning Tool ProteinMPNN
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Thermodynamics of Unfolding of the All .beta.-Sheet Protein Interleukin-1.beta.
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Electrostatic Interactions in Ubiquitin: Stabilization of Carboxylates by Lysine Amino Groups
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Characterizing Substrate Selectivity of Ubiquitin C-Terminal Hydrolase-L3 Using Engineered α-Linked Ubiquitin Substrates
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PowerBorn: A Barnes–Hut Tree Implementation for Accurate and Efficient Born Radii Computation
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Detailed Unfolding and Folding of Gaseous Ubiquitin Ions Characterized by Electron Capture Dissociation
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Analyzing Protein Folding Cooperativity by Differential Scanning Calorimetry and NMR Spectroscopy
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Macromolecular Crowding and Protein Stability
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Protein Stabilization by Macromolecular Crowding through Enthalpy Rather Than Entropy
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Protein Cold Denaturation as Seen From the Solvent
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Hydrogen Bond Geometry and 2H/1H Fractionation in Proteins
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Rational Design of Protein-Specific Folding Modifiers
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Melting Proteins: Evidence for Multiple Stable Structures upon Thermal Denaturation of Native Ubiquitin from Ion Mobility Spectrometry-Mass Spectrometry Measurements
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Protons Are Fast and Smart; Proteins Are Slow and Dumb: On the Relationship of Electrospray Ionization Charge States and Conformations
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Effects of Hydrogen/Deuterium Exchange on Protein Stability in Solution and in the Gas Phase
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Thermal Unfolding Kinetics of Ubiquitin in the Microsecond-to-Second Time Range Probed by Tyr-59 Fluorescence
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A Statistical Model for Translocation of Structured Polypeptide Chains through Nanopores
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Effects of Urea on Selectivity and Protein–Ligand Interactions in Multimodal Cation Exchange Chromatography
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Investigation into the Molecular and Thermodynamic Basis of Protein Interactions in Multimodal Chromatography Using Functionalized Nanoparticles
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On the Thermal Unfolding Character of Globular Proteins
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Conformational analysis of [Met5]-enkephalin: Solvation and ionization considerations
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A cryptic protease couples deubiquitination and degradation by the proteasome
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The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates
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Proteasomes and their kin: proteases in the machine age
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Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
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Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation
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Breakdown of supersaturation barrier links protein folding to amyloid formation
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Ubiquitin: a small protein folding paradigm
inferred← citeshttps://doi.org/10.1039/b819365gopenalex-snapshot
Enhancing the fluorescence of tyr-59 in ubiquitin by blocking proton transfer
inferred← citeshttps://doi.org/10.1039/c7cc09829dopenalex-snapshot
Melting proteins confined in nanodroplets with 10.6 μm light provides clues about early steps of denaturation
inferred← citeshttps://doi.org/10.1039/d0cp01910kopenalex-snapshot
Why small proteins tend to have high denaturation temperatures
inferred← citeshttps://doi.org/10.1039/d3dt01815fopenalex-snapshot
Stretching the chains: the destabilizing impact of Cu 2+ and Zn 2+ ions on K48-linked diubiquitin
inferred← citeshttps://doi.org/10.1046/j.1432-1327.2000.01037.xopenalex-snapshot
Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A
inferred← citeshttps://doi.org/10.1046/j.1432-1327.2000.01638.xopenalex-snapshot
Thermodynamic analysis of helix‐engineered forms of the activation domain of human procarboxypeptidase A2
inferred← citeshttps://doi.org/10.1063/1.3556671openalex-snapshot
Power-law dependence of the melting temperature of ubiquitin on the volume fraction of macromolecular crowders
inferred← citeshttps://doi.org/10.1063/1.5019410openalex-snapshot
Probabilistic analysis for identifying the driving force of protein folding
inferred← citeshttps://doi.org/10.1073/pnas.1218321110openalex-snapshot
Atomic-level description of ubiquitin folding
inferred← citeshttps://doi.org/10.1074/jbc.ra120.013396openalex-snapshot
Quantitating denaturation by formic acid: imperfect repeats are essential to the stability of the functional amyloid protein FapC
inferred← citeshttps://doi.org/10.1080/07391102.2006.10507117openalex-snapshot
Side Chain Dynamics and Alternative Hydrogen Bonding in the Mechanism of Protein Thermostabilization
inferred← citeshttps://doi.org/10.1080/13102818.2015.1008192openalex-snapshot
An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes
inferred← citeshttps://doi.org/10.1080/23328940.2014.1000702openalex-snapshot
Species-specific temperature sensitivity of TRPA1
inferred← citeshttps://doi.org/10.1093/emboj/18.14.3877openalex-snapshot
Structural basis for the specificity of ubiquitin C‐terminal hydrolases
inferred← citeshttps://doi.org/10.1103/physreve.91.022708openalex-snapshot
Protein unfolding from free-energy calculations: Integration of the Gaussian network model with bond binding energies
inferred← citeshttps://doi.org/10.1110/ps.062383807openalex-snapshot
BPPred: A Web‐based computational tool for predicting biophysical parameters of proteins
inferred← citeshttps://doi.org/10.1110/ps.370101openalex-snapshot
Heat capacity changes upon burial of polar and nonpolar groups in proteins
inferred← citeshttps://doi.org/10.1110/ps.9.2.387openalex-snapshot
Contribution of proton linkage to the thermodynamic stability of the major cold‐shock protein of Escherichia coli CspA
inferred← citeshttps://doi.org/10.1111/febs.14264openalex-snapshot
Structural insight into a partially unfolded state preceding aggregation in an intracellular lipid‐binding protein
inferred← citeshttps://doi.org/10.1111/j.1432-1033.2004.04392.xopenalex-snapshot
Context‐dependent effects of proline residues on the stability and folding pathway of ubiquitin
inferred← citeshttps://doi.org/10.1139/o02-081openalex-snapshot
The elusive structural role of ubiquitinated histones
inferred← citeshttps://doi.org/10.1155/2010/794318openalex-snapshot
Translocation process of structured polypeptides across nanopores
inferred← citeshttps://doi.org/10.1201/9781439822548.ch7openalex-snapshot
Denaturation of Globular Proteins in Relation to Their Functional Properties
inferred← citeshttps://doi.org/10.1201/b20161-17openalex-snapshot
Protein Stability in Crowded Environments
inferred← citeshttps://doi.org/10.13028/m2g027openalex-snapshot
Analyses of All Possible Point Mutations within a Protein Reveals Relationships between Function and Experimental Fitness: A Dissertation
inferred← citeshttps://doi.org/10.13140/rg.2.1.1732.4965openalex-snapshot
Protein Dynamics: Aggregation and Mechanical Unfolding
inferred← citeshttps://doi.org/10.1351/pac200779081445openalex-snapshot
Thermodynamic problems in structural molecular biology
inferred← citeshttps://doi.org/10.1371/journal.pone.0019425openalex-snapshot
Rational Design of Protein Stability: Effect of (2S,4R)-4-Fluoroproline on the Stability and Folding Pathway of Ubiquitin
inferred← citeshttps://doi.org/10.14288/1.0221256openalex-snapshot
Protein-solvent interactions and classical density functional theory
inferred← citeshttps://doi.org/10.1515/bmc-2016-0009openalex-snapshot
The evolving world of ubiquitin: transformed polyubiquitin chains
inferred← citeshttps://doi.org/10.1515/bmc.2010.002openalex-snapshot
Ubiquitin fragments: their known biological activities and putative roles
inferred← citeshttps://doi.org/10.1529/biophysj.104.046466openalex-snapshot
Unfolding of Ubiquitin Studied by Picosecond Time-Resolved Fluorescence of the Tyrosine Residue
inferred← citeshttps://doi.org/10.1529/biophysj.104.048496openalex-snapshot
Elucidating Protein Thermodynamics from the Three-Dimensional Structure of the Native State Using Network Rigidity
inferred← citeshttps://doi.org/10.1534/genetics.114.168351openalex-snapshot
Viewing Protein Fitness Landscapes Through a Next-Gen Lens
inferred← citeshttps://doi.org/10.17615/d9ga-p250openalex-snapshot
Macromolecular crowding and protein chemistry: views from inside and outside cells
inferred← citeshttps://doi.org/10.26434/chemrxiv.11888958openalex-snapshot
Protein Unfolding in Freeze Frames: Intermediates of Ubiquitin and Lysozyme Revealed by Variable Temperature Ion Mobility-Mass Spectrometry
inferred← citeshttps://doi.org/10.26508/lsa.202201760openalex-snapshot
The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro but not in cellulo
inferred← citeshttps://doi.org/10.33774/chemrxiv-2021-4g8w7-v3openalex-snapshot
Protein unfolding in freeze frames: intermediate states are revealed by variable temperature ion mobility-mass spectrometry.
inferred← citeshttps://doi.org/10.3389/fcomp.2024.1415648openalex-snapshot
A lightweight visualization tool for protein unfolding by collision detection and elimination
inferred← citeshttps://doi.org/10.3390/molecules29132950openalex-snapshot
The Temperature Dependence of Hydrogen Bonds Is More Uniform in Stable Proteins: An Analysis of NMR h3JNC′ Couplings in Four Different Protein Structures
inferred← citeshttps://doi.org/10.5012/bkcs.2009.30.7.1567openalex-snapshot
Partially Folded States of Mutant Ubiquitin in Mild Denaturing Conditions
inferred← citeshttps://doi.org/10.5012/jkcs.2014.58.6.560openalex-snapshot
Contribution of Electrostatic Interactions to Protein Folding Reaction
inferred← citeshttps://doi.org/10.53846/goediss-4118openalex-snapshot
Thermal coefficients of methyl groups within ubiquitin and metabolic coupling of NAA and lactate in cortical neurons
inferred← citeshttps://doi.org/10.5772/intechopen.112091openalex-snapshot
Ubiquitin: Structure and Function
inferred← citeshttps://doi.org/10.5772/intechopen.97318openalex-snapshot
Modifications in Biomacromolecules
inferred← citeshttps://doi.org/10.7554/elife.15802openalex-snapshot
Determination of ubiquitin fitness landscapes under different chemical stresses in a classroom setting
inferred← citeshttps://doi.org/10.7554/elife.91122openalex-snapshot
Plasticity of the proteasome-targeting signal Fat10 enhances substrate degradation
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