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Reversible pressure-temperature denaturation of chymotrypsinogen
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Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/bip.1966.360040808openalex-snapshot
Validity of the “two‐state” hypothesis for conformational transitions of proteins
inferredcites →https://doi.org/10.1016/s0021-9258(17)41299-3openalex-snapshot
PRESSURE AND PROTEIN DENATURATION
inferredcites →https://doi.org/10.1016/s0021-9258(18)88287-4openalex-snapshot
THE COAGULATION OF ALBUMEN BY PRESSURE
inferredcites →https://doi.org/10.1021/bi00806a045openalex-snapshot
Thermodynamics of protein denaturation. Effect of pressure on the denaturation on ribonuclease A
inferredcites →https://doi.org/10.1021/bi00813a011openalex-snapshot
Thermodynamics of protein denaturation. Calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation
inferredcites →https://doi.org/10.1021/j100801a021openalex-snapshot
THE REVERSIBLE THERMAL DENATURATION OF CHYMOTRYPSINOGEN.1 I. EXPERIMENTAL CHARACTERIZATION
inferredcites →https://doi.org/10.1021/j100816a041openalex-snapshot
ULTRACENTRIFUGAL AND VISCOMETRIC STUDIES OF THE REVERSIBLE THERMAL DENATURATION OF RIBONUCLEASE1,2a
inferredcites →https://doi.org/10.1021/j100889a013openalex-snapshot
Influence of Pressure on the Reversible Unfolding of Ribonuclease and Poly-γ-benzyl-L-glutamate1
inferredcites →https://doi.org/10.1021/ja00995a002openalex-snapshot
Thermodynamics of protein denaturation. III. Denaturation of ribonuclease in water and in aqueous urea and aqueous ethanol mixtures
inferredcites →https://doi.org/10.1021/ja01074a013openalex-snapshot
The Thermodynamics of Protein Denaturation. I. The Denaturation of Chymotrypsinogen
inferredcites →https://doi.org/10.1063/1.1684575openalex-snapshot
A High Pressure Optical Vessel for Corrosive or Sensitive Liquid Samples
inferredcites →https://doi.org/10.1063/1.1720742openalex-snapshot
Differential Calorimetry of Thermally Induced Processes in Solution
inferredcites →https://doi.org/10.1063/1.1744074openalex-snapshot
Chemical Determination of the Oscillator Strength of F Centers
inferredcites →https://doi.org/10.1121/1.1910740openalex-snapshot
Specific Volumes of Water at High Pressures, Obtained from Ultrasonic-Propagation Measurements
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Dierential Scanning Calorimetry of Proteins and Zimm-Bragg Model in Water
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Molecular mechanisms of pressure induced conformational changes in BPTI
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Pressure–temperature stability of DNA in neutral salt solutions
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Heat capacity changes and partial molal heat capacities of some di‐ and tripeptides in water
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Specific volume and adiabatic compressibility measurements of native and aggregated recombinant human interleukin‐1 receptor antagonist: Density differences enable pressure‐modulated refolding
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Pressure—A Gateway to Fundamental Insights into Protein Solvation, Dynamics, and Function
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inferred← citeshttps://doi.org/10.1002/hlca.200590037openalex-snapshot
Extending the Pressure–Temperature State Diagram of Myoglobin
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inferred← citeshttps://doi.org/10.1002/pro.4905openalex-snapshot
Energy, water, and protein folding: A molecular dynamics‐based quantitative inventory of molecular interactions and forces that make proteins stable
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Probing the contribution of internal cavities to the volume change of protein unfolding under pressure
inferred← citeshttps://doi.org/10.1002/prot.1083openalex-snapshot
Pressure effect on denaturant‐induced unfolding of hen egg white lysozyme
inferred← citeshttps://doi.org/10.1002/prot.20925openalex-snapshot
Comment on “Phenomenological similarities between protein denaturation and small‐molecule dissolution: Insights into the mechanism driving the thermal resistance of globular proteins” (Proteins 2004;54:323–332)
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Molecular dynamics of the structural changes of helical peptides induced by pressure
inferred← citeshttps://doi.org/10.1002/prot.24875openalex-snapshot
Thermodynamics of Aβ16–21 dissociation from a fibril: Enthalpy, entropy, and volumetric properties
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Pressure‐induced conformational switch of an interfacial protein
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Determination of the Volumetric Properties of Proteins and Other Solutes Using Pressure Perturbation Calorimetry
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Destruction of Salmonella enteritidis inoculated in liquid whole egg by high hydrostatic pressure: comparative study in selective and non-selective media
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The native and the heat-induced denatured states of α-chymotrypsinogen A: thermodynamic and spectroscopic studies
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Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy 1 1Edited by P. E. Wright
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The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by 1H NMR
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Structure and Hydrophobic Bonding: Concepts and Applications to Anesthesia
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The Effects of High Pressure on Biomaterials
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Effects of High Pressure on Enzymes Related to Food Quality
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High Pressure Effects on Protein Structure
inferred← citeshttps://doi.org/10.1007/978-1-4899-0664-9_42openalex-snapshot
Flexibility of Globular Proteins in Water as Revealed by Compressibility
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Effects of High Pressure on Food Proteins
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Effects of High Pressure on Enzymes
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High-Pressure Fluorescence Applications
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Change in Volume Upon Inhibitor Binding to Carbonic Anhydrases by Fluorescent Pressure Shift Assay
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Water Contribution to the Protein Folding and Its Relevance in Protein Design and Protein Aggregation
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Multi-Scale Approach for Self-Assembly and Protein Folding
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Volumetric Properties of Proteins and the Role of Solvent in Conformational Dynamics
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The Behaviour of Proteins Under Pressure
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inferred← citeshttps://doi.org/10.1007/978-94-017-9918-8_4openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/978-94-017-9918-8_5openalex-snapshot
Volume and Compressibility of Proteins
inferred← citeshttps://doi.org/10.1007/978-981-10-5966-7_1openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/bf00180369openalex-snapshot
Fourth derivative UV-spectroscopy of proteins under high pressure II. Application to reversible structural changes
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Fast-folding proteins under stress
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inferred← citeshttps://doi.org/10.1007/s00253-011-3854-6openalex-snapshot
Pressure to kill or pressure to boost: a review on the various effects and applications of hydrostatic pressure in bacterial biotechnology
inferred← citeshttps://doi.org/10.1007/s00253-012-4162-5openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s00396-005-1270-0openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s00397-007-0170-2openalex-snapshot
Influence of high pressure processing on the linear viscoelastic properties of egg yolk dispersions
inferred← citeshttps://doi.org/10.1007/s00449-005-0417-1openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s10867-011-9235-7openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s10973-005-6963-6openalex-snapshot
Modelling of a high pressure calorimeter
inferred← citeshttps://doi.org/10.1007/s11947-013-1140-6openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s12393-014-9075-xopenalex-snapshot
High-pressure Processing: Kinetic Models for Microbial and Enzyme Inactivation
inferred← citeshttps://doi.org/10.1007/s12393-016-9153-3openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s12551-019-00537-yopenalex-snapshot
Molecular simulations by generalized-ensemble algorithms in isothermal–isobaric ensemble
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Pressure effects on lipid-protein interactions in (Na+ + K+)-ATPase
inferred← citeshttps://doi.org/10.1016/0005-2795(73)90219-5openalex-snapshot
Electrophoretic separation of conformational states of α-chymotrypsinogen A at high pressures
inferred← citeshttps://doi.org/10.1016/0005-2795(78)90521-4openalex-snapshot
A contribution to the debate about hydrophobic effects
inferred← citeshttps://doi.org/10.1016/0009-2614(85)85275-1openalex-snapshot
Pressure effects on the Raman spectra of proteins: Pressure-induced changes in the conformation of lysozyme in aqueous solutions
inferred← citeshttps://doi.org/10.1016/0022-2836(76)90223-0openalex-snapshot
Electrophoretic separation of molecular species associated with the thermal transition of chymotrypsinogen A
inferred← citeshttps://doi.org/10.1016/0022-2836(86)90017-3openalex-snapshot
Cold denaturation of myoglobin
inferred← citeshttps://doi.org/10.1016/0022-5193(75)90035-1openalex-snapshot
A discussion of pressure-volume effects in aqueous protein solutions
inferred← citeshttps://doi.org/10.1016/0065-227x(94)90012-4openalex-snapshot
Thermodynamics of protein folding: Effects of hydration and electrostatic interactions
inferred← citeshttps://doi.org/10.1016/0079-6107(81)90011-0openalex-snapshot
The fluidity of cell membranes and its regulation
inferred← citeshttps://doi.org/10.1016/0079-6700(93)90009-2openalex-snapshot
Modification of biopolymer functions by high pressure
inferred← citeshttps://doi.org/10.1016/0141-8130(95)01053-xopenalex-snapshot
Effect of pressure on the deuterium exchange reaction of α-lactalbumin and β-lactoglobulin
inferred← citeshttps://doi.org/10.1016/0141-8130(95)01084-xopenalex-snapshot
Pressure-induced change in proteins studied through chemical modifications
inferred← citeshttps://doi.org/10.1016/0141-8130(95)98152-oopenalex-snapshot
The liquid amide transfer model and the unfolding thermodynamics of small globular proteins
inferred← citeshttps://doi.org/10.1016/0144-8617(82)90046-7openalex-snapshot
Effect of hydrostatic pressure on starch gelatinisation
inferred← citeshttps://doi.org/10.1016/0144-8617(82)90055-8openalex-snapshot
Effect of hydrostatic pressure on starch gelatinisation, as determined by DTA
inferred← citeshttps://doi.org/10.1016/0165-9936(81)80048-9openalex-snapshot
Reversed-phase chromatography
inferred← citeshttps://doi.org/10.1016/0167-4838(86)90018-xopenalex-snapshot
Adiabatic compressibility of myoglobin. Effect of axial ligand and denaturation
inferred← citeshttps://doi.org/10.1016/0167-4838(86)90145-7openalex-snapshot
Kinetics of pressure-induced inactivation of bovine liver glutamate dehydrogenase
inferred← citeshttps://doi.org/10.1016/0167-4838(88)90291-9openalex-snapshot
Pressure effects on protein secondary structure and hydrogen deuterium exchange in chymotrypsinogen: a Fourier transform infrared spectroscopic study
inferred← citeshttps://doi.org/10.1016/0167-4838(89)90252-5openalex-snapshot
Pressure effects on thermal inactivation of Taka-amylase A
inferred← citeshttps://doi.org/10.1016/0167-4838(94)90154-6openalex-snapshot
Determination of hydrophobic hydration in protein unfolding by an intrinsic reference state
inferred← citeshttps://doi.org/10.1016/0167-4838(95)00196-4openalex-snapshot
Pressure-induced inactivation of E. coli β-galactosidase: influence of pH and temperatur
inferred← citeshttps://doi.org/10.1016/0167-7799(90)90200-hopenalex-snapshot
Biochemical reactions in supercritical fluids
inferred← citeshttps://doi.org/10.1016/0167-7799(94)90057-4openalex-snapshot
Exploiting the effects of high hydrostatic pressure in biotechnological applications
inferred← citeshttps://doi.org/10.1016/0168-1605(95)00057-7openalex-snapshot
Understanding physical inactivation processes: combined preservation opportunities using heat, ultrasound and pressure
inferred← citeshttps://doi.org/10.1016/0301-4622(79)85032-2openalex-snapshot
Thermodynamic compensation process in interacting protein systems: Definition of thermodynamic compensatory temperature, 〈Tc〉
inferred← citeshttps://doi.org/10.1016/0301-4622(88)85052-xopenalex-snapshot
Temperature-induced phase transitions in proteins and lipids
inferred← citeshttps://doi.org/10.1016/0378-3812(92)85079-nopenalex-snapshot
Application of high pressure and thermophysical properties of water to biotechnology
inferred← citeshttps://doi.org/10.1016/0378-4363(86)90718-7openalex-snapshot
Pressure effects on heme proteins
inferred← citeshttps://doi.org/10.1016/b978-0-08-024938-4.50029-xopenalex-snapshot
PRESSURE EFFECTS ON BIOCHEMICAL SYSTEMS
inferred← citeshttps://doi.org/10.1016/b978-0-12-312202-5.50009-9openalex-snapshot
REVERSED-PHASE CHROMATOGRAPHY
inferred← citeshttps://doi.org/10.1016/b978-0-12-823872-1.00005-3openalex-snapshot
Introduction to high pressure thermal processing and pressure assisted thermal sterilization
inferred← citeshttps://doi.org/10.1016/b978-0-323-98386-0.00005-1openalex-snapshot
Effects of high pressure on protein stability, structure, and function—Theory and applications
inferred← citeshttps://doi.org/10.1016/b978-0-323-98386-0.00014-2openalex-snapshot
Effect of high-pressure processing on the kinetic parameters of enzymes
inferred← citeshttps://doi.org/10.1016/b978-0-443-15437-9.00002-1openalex-snapshot
Enzymes at high hydrostatic pressure
inferred← citeshttps://doi.org/10.1016/b978-0-444-63743-7.00001-9openalex-snapshot
Biotransformation Using Liquid and Supercritical CO 2
inferred← citeshttps://doi.org/10.1016/b978-0-444-81946-8.50014-7openalex-snapshot
Pressure denaturation mechanism for proteins
inferred← citeshttps://doi.org/10.1016/b978-0-444-89372-7.50045-2openalex-snapshot
Pressure effect on the stability of Lipoxygenase: FTIR studies with the diamond anvil cell
inferred← citeshttps://doi.org/10.1016/b978-012530990-5/50010-9openalex-snapshot
The Equilibrium Condition Applied to Chemical Processes
inferred← citeshttps://doi.org/10.1016/b978-044451766-1/50001-9openalex-snapshot
Pressure – Temperature Effects on Protein Conformational States
inferred← citeshttps://doi.org/10.1016/b978-044451766-1/50002-0openalex-snapshot
High Pressure Effects in Molecular Bioscience
inferred← citeshttps://doi.org/10.1016/j.ab.2011.02.019openalex-snapshot
Determination of the volume changes induced by ligand binding to heat shock protein 90 using high-pressure denaturation
inferred← citeshttps://doi.org/10.1016/j.bbagen.2005.05.003openalex-snapshot
Linear and non-linear pressure dependence of enzyme catalytic parameters
inferred← citeshttps://doi.org/10.1016/j.bbapap.2004.06.012openalex-snapshot
Effect of hydrostatic pressure on conformational changes of canine milk lysozyme between the native, molten globule, and unfolded states
inferred← citeshttps://doi.org/10.1016/j.bbapap.2005.03.002openalex-snapshot
Stability of proteins: Temperature, pressure and the role of the solvent
inferred← citeshttps://doi.org/10.1016/j.bbapap.2005.10.004openalex-snapshot
What lies in the future of high-pressure bioscience?
inferred← citeshttps://doi.org/10.1016/j.bbapap.2005.11.011openalex-snapshot
Pressure as a tool to study protein-unfolding/refolding processes: The case of ribonuclease A
inferred← citeshttps://doi.org/10.1016/j.bbapap.2005.11.019openalex-snapshot
Protein stability and dynamics in the pressure–temperature plane
inferred← citeshttps://doi.org/10.1016/j.bbapap.2005.12.019openalex-snapshot
Folding studies of two hydrostatic pressure sensitive proteins
inferred← citeshttps://doi.org/10.1016/j.bbapap.2006.01.015openalex-snapshot
The pressure effect on the structure and functions of protein disulfide isomerase
inferred← citeshttps://doi.org/10.1016/j.bbapap.2006.01.016openalex-snapshot
Refolding studies using pressure: The folding landscape of lysozyme in the pressure–temperature plane
inferred← citeshttps://doi.org/10.1016/j.bbapap.2006.01.017openalex-snapshot
High pressure application for food biopolymers
inferred← citeshttps://doi.org/10.1016/j.bbapap.2007.03.013openalex-snapshot
Pressure effects on the structure and function of human thioredoxin
inferred← citeshttps://doi.org/10.1016/j.bbapap.2009.04.005openalex-snapshot
High pressure stabilization of collagen structure
inferred← citeshttps://doi.org/10.1016/j.bbapap.2009.10.003openalex-snapshot
Effect of pressure on the secondary structure of coiled coil peptide GCN4-p1
inferred← citeshttps://doi.org/10.1016/j.bbapap.2012.10.001openalex-snapshot
Different pressure–temperature behavior of the structured and unstructured regions of titin
inferred← citeshttps://doi.org/10.1016/j.bpc.2013.06.005openalex-snapshot
Temperature and pressure dependence of azurin stability as monitored by tryptophan fluorescence and phosphorescence. The case of F29A mutant
inferred← citeshttps://doi.org/10.1016/j.bpc.2019.106211openalex-snapshot
Thermodynamic properties of aqueous osmolyte solutions at high-pressure conditions
inferred← citeshttps://doi.org/10.1016/j.bpc.2019.106222openalex-snapshot
Density variations of TMAO solutions in the kilobar range: Experiments, PC-SAFT predictions, and molecular dynamics simulations
inferred← citeshttps://doi.org/10.1016/j.bpc.2023.107167openalex-snapshot
Atomistic simulations of RNA duplex thermal denaturation: Sequence- and forcefield-dependence
inferred← citeshttps://doi.org/10.1016/j.bpj.2009.12.4298openalex-snapshot
The Behavior of the Hydrophobic Effect under Pressure and Protein Denaturation
inferred← citeshttps://doi.org/10.1016/j.bpj.2010.02.044openalex-snapshot
Unique Features of the Folding Landscape of a Repeat Protein Revealed by Pressure Perturbation
inferred← citeshttps://doi.org/10.1016/j.bpj.2010.11.087openalex-snapshot
An Effective Solvent Theory Connecting the Underlying Mechanisms of Osmolytes and Denaturants for Protein Stability
inferred← citeshttps://doi.org/10.1016/j.bpj.2011.11.2484openalex-snapshot
Direct Characterization of Hydrophobic Hydration during Cold and Pressure Denaturation
inferred← citeshttps://doi.org/10.1016/j.bpj.2013.11.3718openalex-snapshot
Volume of Hsp90 Ligand Binding and the Unfolding Phase Diagram as a Function of Pressure and Temperature
inferred← citeshttps://doi.org/10.1016/j.bpj.2017.07.012openalex-snapshot
Putting the Piezolyte Hypothesis under Pressure
inferred← citeshttps://doi.org/10.1016/j.bpj.2022.03.010openalex-snapshot
Heat and cold denaturation of yeast frataxin: The effect of pressure
inferred← citeshttps://doi.org/10.1016/j.bpr.2022.100098openalex-snapshot
Pressure, motion, and conformational entropy in molecular recognition by proteins
inferred← citeshttps://doi.org/10.1016/j.carbpol.2009.05.005openalex-snapshot
Supercritical carbon dioxide (scCO2) induced gelatinization of potato starch
inferred← citeshttps://doi.org/10.1016/j.chemphys.2012.09.014openalex-snapshot
Effect of pressure on the solution structure and hydrogen bond properties of aqueous N-methylacetamide
inferred← citeshttps://doi.org/10.1016/j.chroma.2011.10.034openalex-snapshot
Technology trends in antibody purification
inferred← citeshttps://doi.org/10.1016/j.cocis.2011.04.008openalex-snapshot
Protein hydration and volumetric properties
inferred← citeshttps://doi.org/10.1016/j.cocis.2019.05.001openalex-snapshot
High-pressure small-angle neutron scattering for food studies
inferred← citeshttps://doi.org/10.1016/j.cplett.2008.12.063openalex-snapshot
Piezotropic unfolding of lysozyme in pure D2O at the outer edge of excess hydration
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