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Applications of isothermal titration calorimetry - the research and technical developments from 2011 to 2015

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inferredcites →https://doi.org/10.1002/aic.14221openalex-snapshot
Molecular and thermodynamic basis for EGCG‐Keratin interaction‐part II: Experimental investigation
inferredcites →https://doi.org/10.1002/anie.201208561openalex-snapshot
Dissecting the Hydrophobic Effect on the Molecular Level: The Role of Water, Enthalpy, and Entropy in Ligand Binding to Thermolysin
inferredcites →https://doi.org/10.1002/anie.201209858openalex-snapshot
Cover Picture: Champagne and Fireworks: Angewandte Chemie Celebrates Its Birthday (Angew. Chem. Int. Ed. 1/2013)
inferredcites →https://doi.org/10.1002/cbic.201200521openalex-snapshot
Using a Fragment‐Based Approach To Target Protein–Protein Interactions
inferredcites →https://doi.org/10.1002/chem.201002105openalex-snapshot
Induction‐Driven Stabilization of the Anion–π Interaction in Electron‐Rich Aromatics as the Key to Fluoride Inclusion in Imidazolium‐Cage Receptors
inferredcites →https://doi.org/10.1002/chem.201002635openalex-snapshot
Selectivity among Two Lectins: Probing the Effect of Topology, Multivalency and Flexibility of “Clicked” Multivalent Glycoclusters
inferredcites →https://doi.org/10.1002/chem.201003402openalex-snapshot
Combining Glycomimetic and Multivalent Strategies toward Designing Potent Bacterial Lectin Inhibitors
inferredcites →https://doi.org/10.1002/chem.201003411openalex-snapshot
Urea‐, Squaramide‐, and Sulfonamide‐Based Anion Receptors: A Thermodynamic Study
inferredcites →https://doi.org/10.1002/chem.201101861openalex-snapshot
Cycloalkane and Alicyclic Heterocycle Complexation by New Switchable Resorcin[4]arene‐Based Container Molecules: NMR and ITC Binding Studies
inferredcites →https://doi.org/10.1002/chem.201102034openalex-snapshot
Multivalent Gold Glycoclusters: High Affinity Molecular Recognition by Bacterial Lectin PA‐IL
inferredcites →https://doi.org/10.1002/chem.201200010openalex-snapshot
Rational Design and Synthesis of Optimized Glycoclusters for Multivalent Lectin–Carbohydrate Interactions: Influence of the Linker Arm
inferredcites →https://doi.org/10.1002/chem.201202584openalex-snapshot
Supramolecular Polymerization of C 3 ‐Symmetric Organogelators: Cooperativity, Solvent, and Gelation Relationship
inferredcites →https://doi.org/10.1002/chem.201300989openalex-snapshot
Osteopontin: A Uranium Phosphorylated Binding‐Site Characterization
inferredcites →https://doi.org/10.1002/chem.201302365openalex-snapshot
The “True” Affinities of Metal Cations to p ‐Sulfonatocalix[4]arene: A Thermodynamic Study at Neutral pH Reveals a Pitfall Due to Salt Effects in Microcalorimetry
inferredcites →https://doi.org/10.1002/chem.201502043openalex-snapshot
Multiple Multidentate Halogen Bonding in Solution, in the Solid State, and in the (Calculated) Gas Phase
inferredcites →https://doi.org/10.1002/chir.22473openalex-snapshot
Isothermal Titration Calorimetry of Chiral Polymeric Nanoparticles
inferredcites →https://doi.org/10.1002/cmdc.201200206openalex-snapshot
Water Makes the Difference: Rearrangement of Water Solvation Layer Triggers Non‐additivity of Functional Group Contributions in Protein–Ligand Binding
inferredcites →https://doi.org/10.1002/cmdc.201400013openalex-snapshot
Methyl, Ethyl, Propyl, Butyl: Futile But Not for Water, as the Correlation of Structure and Thermodynamic Signature Shows in a Congeneric Series of Thermolysin Inhibitors
inferredcites →https://doi.org/10.1002/jmr.1025openalex-snapshot
Survey of the year 2008: applications of isothermal titration calorimetry
inferredcites →https://doi.org/10.1002/jmr.1073openalex-snapshot
Survey of the year 2009: applications of isothermal titration calorimetry
inferredcites →https://doi.org/10.1002/jmr.1142openalex-snapshot
Label‐free detection of enhanced saccharide binding at pH 7.4 to nanoparticulate benzoboroxole based receptor units
inferredcites →https://doi.org/10.1002/jmr.1167openalex-snapshot
Applications of isothermal titration calorimetry in pure and applied research—survey of the literature from 2010
inferredcites →https://doi.org/10.1002/jmr.2330openalex-snapshot
Label-free characterization of carbonic anhydrase-novel inhibitor interactions using surface plasmon resonance, isothermal titration calorimetry and fluorescence-based thermal shift assays
inferredcites →https://doi.org/10.1002/jmr.648openalex-snapshot
A survey of the year 2002 literature on applications of isothermal titration calorimetry
inferredcites →https://doi.org/10.1002/jmr.714openalex-snapshot
A survey of the year 2003 literature on applications of isothermal titration calorimetry
inferredcites →https://doi.org/10.1002/jmr.750openalex-snapshot
Survey of the year 2004: literature on applications of isothermal titration calorimetry
inferredcites →https://doi.org/10.1002/jmr.803openalex-snapshot
Survey of the year 2005: literature on applications of isothermal titration calorimetry
inferredcites →https://doi.org/10.1002/jmr.859openalex-snapshot
A survey of the year 2006 literature on applications of isothermal titration calorimetry
inferredcites →https://doi.org/10.1002/jmr.909openalex-snapshot
A survey of the year 2007 literature on applications of isothermal titration calorimetry
inferredcites →https://doi.org/10.1002/jps.24630openalex-snapshot
Modulation of the Hydration Water Around Monoclonal Antibodies on Addition of Excipients Detected by Terahertz Time-Domain Spectroscopy
inferredcites →https://doi.org/10.1002/mabi.201000395openalex-snapshot
BSA Adsorption on Differently Charged Polystyrene Nanoparticles using Isothermal Titration Calorimetry and the Influence on Cellular Uptake
inferredcites →https://doi.org/10.1002/open.201402017openalex-snapshot
The Thermochemistry of London Dispersion‐Driven Transition Metal Reactions: Getting the ‘Right Answer for the Right Reason’
inferredcites →https://doi.org/10.1002/pro.692openalex-snapshot
Extent of enthalpy–entropy compensation in protein–ligand interactions
inferredcites →https://doi.org/10.1006/abio.1999.4402openalex-snapshot
Exact Analysis of Competition Ligand Binding by Displacement Isothermal Titration Calorimetry
inferredcites →https://doi.org/10.1006/abio.2001.5218openalex-snapshot
Enzyme Kinetics Determined Using Calorimetry: A General Assay for Enzyme Activity?
inferredcites →https://doi.org/10.1007/978-1-62703-293-3_2openalex-snapshot
Determining Enzyme Kinetics via Isothermal Titration Calorimetry
inferredcites →https://doi.org/10.1007/s00216-012-6565-7openalex-snapshot
Conditions for calibration of an isothermal titration calorimeter using chemical reactions
inferredcites →https://doi.org/10.1007/s00775-011-0824-5openalex-snapshot
Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine
inferredcites →https://doi.org/10.1007/s00775-012-0874-3openalex-snapshot
Calorimetric investigation of copper(II) binding to Aβ peptides: thermodynamics of coordination plasticity
inferredcites →https://doi.org/10.1007/s10822-015-9867-yopenalex-snapshot
Thermodynamics of protein–ligand interactions as a reference for computational analysis: how to assess accuracy, reliability and relevance of experimental data
inferredcites →https://doi.org/10.1007/s10973-011-1426-8openalex-snapshot
Investigation of copper(II) complexation by glycylglycine using isothermal titration calorimetry
inferredcites →https://doi.org/10.1007/s10973-011-2014-7openalex-snapshot
Binding mechanisms of nano-baskets toward alkali metals
inferredcites →https://doi.org/10.1007/s10973-012-2251-4openalex-snapshot
Isothermal titration calorimetry (ITC) study of natural cyclodextrins inclusion complexes with drugs
inferredcites →https://doi.org/10.1007/s10973-012-2593-yopenalex-snapshot
Investigation of metal–buffer interactions using isothermal titration calorimetry
inferredcites →https://doi.org/10.1007/s10973-015-4775-xopenalex-snapshot
Geometric features of the Wiseman isotherm in isothermal titration calorimetry
inferredcites →https://doi.org/10.1007/s11010-013-1735-2openalex-snapshot
Kinetic regulation of the binding of prothrombin to phospholipid membranes
inferredcites →https://doi.org/10.1007/s13361-013-0751-5openalex-snapshot
Measuring Positive Cooperativity Using the Direct ESI-MS Assay. Cholera Toxin B Subunit Homopentamer Binding to GM1 Pentasaccharide
inferredcites →https://doi.org/10.1016/0003-2697(89)90213-3openalex-snapshot
Rapid measurement of binding constants and heats of binding using a new titration calorimeter
inferredcites →https://doi.org/10.1016/0307-4412(75)90040-0openalex-snapshot
Physical Chemistry of the Life Sciences
inferredcites →https://doi.org/10.1016/j.ab.2004.03.022openalex-snapshot
The development of a continuous isothermal titration calorimetric method for equilibrium studies
inferredcites →https://doi.org/10.1016/j.ab.2010.11.002openalex-snapshot
Simultaneous determination of equilibrium constants and enthalpy changes by titration calorimetry: Methods, instruments, and uncertainties
inferredcites →https://doi.org/10.1016/j.ab.2011.03.024openalex-snapshot
Systematic errors in isothermal titration calorimetry: Concentrations and baselines
inferredcites →https://doi.org/10.1016/j.ab.2011.12.035openalex-snapshot
Designing isothermal titration calorimetry experiments for the study of 1:1 binding: Problems with the “standard protocol”
inferredcites →https://doi.org/10.1016/j.ab.2012.11.030openalex-snapshot
Modeling complex equilibria in isothermal titration calorimetry experiments: Thermodynamic parameters estimation for a three-binding-site model
inferredcites →https://doi.org/10.1016/j.ab.2014.11.010openalex-snapshot
Misuse of thermodynamics in the interpretation of isothermal titration calorimetry data for ligand binding to proteins
inferredcites →https://doi.org/10.1016/j.ab.2015.03.014openalex-snapshot
Isothermal titration calorimetry determination of individual rate constants of trypsin catalytic activity
inferredcites →https://doi.org/10.1016/j.ab.2015.06.027openalex-snapshot
Kinetics of trypsin-catalyzed hydrolysis determined by isothermal titration calorimetry
inferredcites →https://doi.org/10.1016/j.bbagen.2014.04.018openalex-snapshot
Impact of protein and ligand impurities on ITC-derived protein–ligand thermodynamics
inferredcites →https://doi.org/10.1016/j.bbagen.2014.12.007openalex-snapshot
Thermodynamic signatures of fragment binding: Validation of direct versus displacement ITC titrations
inferredcites →https://doi.org/10.1016/j.bbagrm.2014.04.014openalex-snapshot
Global analysis of riboswitches by small-angle X-ray scattering and calorimetry
inferredcites →https://doi.org/10.1016/j.bbamem.2010.09.009openalex-snapshot
Different membrane behaviour and cellular uptake of three basic arginine-rich peptides
inferredcites →https://doi.org/10.1016/j.bbamem.2012.03.001openalex-snapshot
Binding of cationic pentapeptides with modified side chain lengths to negatively charged lipid membranes: Complex interplay of electrostatic and hydrophobic interactions
inferredcites →https://doi.org/10.1016/j.bbamem.2013.05.023openalex-snapshot
Isothermal titration calorimetry of membrane proteins — Progress and challenges
inferredcites →https://doi.org/10.1016/j.bbapap.2015.04.031openalex-snapshot
Insights into the Hendra virus N TAIL –XD complex: Evidence for a parallel organization of the helical MoRE at the XD surface stabilized by a combination of hydrophobic and polar interactions
inferredcites →https://doi.org/10.1016/j.bbrc.2015.10.124openalex-snapshot
Thermodynamic and NMR analyses of NADPH binding to lipocalin-type prostaglandin D synthase
inferredcites →https://doi.org/10.1016/j.biochi.2011.04.005openalex-snapshot
Binding properties of human telomeric quadruplex multimers: A new route for drug design
inferredcites →https://doi.org/10.1016/j.biochi.2011.05.021openalex-snapshot
A more detailed picture of the interactions between virtual screening-derived hits and the DNA G-quadruplex: NMR, molecular modelling and ITC studies
inferredcites →https://doi.org/10.1016/j.biochi.2012.02.012openalex-snapshot
Kinetic and thermodynamic characterization of the functional properties of a hybrid versatile peroxidase using isothermal titration calorimetry: Insight into manganese peroxidase activation and lignin peroxidase inhibition
inferredcites →https://doi.org/10.1016/j.bmc.2013.09.029openalex-snapshot
Benzenesulfonamides with pyrimidine moiety as inhibitors of human carbonic anhydrases I, II, VI, VII, XII, and XIII
inferredcites →https://doi.org/10.1016/j.bpj.2014.11.641openalex-snapshot
Desolvation Energy: A Rationale for Changes in Binding Affinity as Measured by ITC
inferredcites →https://doi.org/10.1016/j.colsurfb.2010.08.013openalex-snapshot
The influence of chitosan valence on the complexation and transfection of DNA: The weaker the DNA–chitosan binding the higher the transfection efficiency
inferredcites →https://doi.org/10.1016/j.colsurfb.2011.07.032openalex-snapshot
Studies of the binding mechanism between aptamers and thrombin by circular dichroism, surface plasmon resonance and isothermal titration calorimetry
inferredcites →https://doi.org/10.1016/j.colsurfb.2013.01.019openalex-snapshot
Exploring DNA binding properties and biological activities of dihydropyrimidinones derivatives
inferredcites →https://doi.org/10.1016/j.enzmictec.2011.06.015openalex-snapshot
Effects of non-ionic surfactants on the interactions between cellulases and tannic acid: A model system for cellulase–poly-phenol interactions
inferredcites →https://doi.org/10.1016/j.enzmictec.2012.01.005openalex-snapshot
Laccase catalysed oxidation of syringic acid: Calorimetric determination of kinetic parameters
inferredcites →https://doi.org/10.1016/j.febslet.2015.10.024openalex-snapshot
Kinetic analysis of gluconate phosphorylation by human gluconokinase using isothermal titration calorimetry
inferredcites →https://doi.org/10.1016/j.fob.2013.04.003openalex-snapshot
Isothermal titration calorimetry with micelles: Thermodynamics of inhibitor binding to carnitine palmitoyltransferase 2 membrane protein
inferredcites →https://doi.org/10.1016/j.ijbiomac.2013.03.021openalex-snapshot
Binding of 18-carbon unsaturated fatty acids to bovine β-lactoglobulin—Structural and thermodynamic studies
inferredcites →https://doi.org/10.1016/j.ijbiomac.2015.03.036openalex-snapshot
Spectroscopic and molecular docking studies on the interaction of troxerutin with DNA
inferredcites →https://doi.org/10.1016/j.ijpharm.2015.03.051openalex-snapshot
Controlling protein stability: Mechanisms revealed using formulations of arginine, glycine and guanidinium HCl with three globular proteins
inferredcites →https://doi.org/10.1016/j.jcis.2010.11.075openalex-snapshot
Copolymers sensitive to temperature and pH in water and in water+oil mixtures: A DSC, ITC and volumetric study
inferredcites →https://doi.org/10.1016/j.jcis.2011.05.059openalex-snapshot
Micellisation of triblock copolymers of ethylene oxide and 1,2-butylene oxide: Effect of B-block length
inferredcites →https://doi.org/10.1016/j.jcis.2014.09.016openalex-snapshot
Isothermal titration calorimetric analysis on solubilization of an octane oil-in-water emulsion in surfactant micelles and surfactant–anionic polymer complexes
inferredcites →https://doi.org/10.1016/j.jconrel.2011.08.023openalex-snapshot
Biophysical properties of chitosan/siRNA polyplexes: Profiling the polymer/siRNA interactions and bioactivity
inferredcites →https://doi.org/10.1016/j.jct.2010.12.001openalex-snapshot
A calorimetric study of carbamate formation
inferredcites →https://doi.org/10.1016/j.jct.2010.12.024openalex-snapshot
Thermodynamic studies on the interaction of folic acid with bovine serum albumin
inferredcites →https://doi.org/10.1016/j.jct.2011.05.015openalex-snapshot
Influence of the alkyl chain length, temperature, and added salt on the thermodynamics of micellization: Alkyltrimethylammonium chlorides in NaCl aqueous solutions
inferredcites →https://doi.org/10.1016/j.jct.2013.08.027openalex-snapshot
An improved method for analyzing isothermal titration calorimetry data from oppositely charged surfactant polyelectrolyte mixtures
inferredcites →https://doi.org/10.1016/j.jct.2015.08.002openalex-snapshot
Heat of adsorption of surfactants and its role on nanoparticle stabilization
inferredcites →https://doi.org/10.1016/j.jinorgbio.2010.09.005openalex-snapshot
Interactions of arene–Ru(II)–chloroquine complexes of known antimalarial and antitumor activity with human serum albumin (HSA) and transferrin
inferredcites →https://doi.org/10.1016/j.jmb.2011.12.057openalex-snapshot
Metal Binding Dictates Conformation and Function of the Amyloid Precursor Protein (APP) E2 Domain
inferredcites →https://doi.org/10.1016/j.jmb.2013.05.019openalex-snapshot
Chaperone-Interacting TPR Proteins in Caenorhabditis elegans
inferredcites →https://doi.org/10.1016/j.jmb.2013.07.001openalex-snapshot
Subtle Interplay between Synaptotagmin and Complexin Binding to the SNARE Complex
inferredcites →https://doi.org/10.1016/j.jmb.2013.07.030openalex-snapshot
Blind Prediction of Charged Ligand Binding Affinities in a Model Binding Site
inferredcites →https://doi.org/10.1016/j.jsb.2013.06.005openalex-snapshot
Bidirectional binding property of high glycine–tyrosine keratin-associated protein contributes to the mechanical strength and shape of hair
inferredcites →https://doi.org/10.1016/j.mce.2014.09.001openalex-snapshot
A multi-step, dynamic allosteric model of testosterone's binding to sex hormone binding globulin
inferredcites →https://doi.org/10.1016/j.molcel.2011.02.012openalex-snapshot
U1 snRNA Directly Interacts with Polypyrimidine Tract-Binding Protein during Splicing Repression
inferredcites →https://doi.org/10.1016/j.molcel.2012.09.001openalex-snapshot
Interdomain Allostery Promotes Assembly of the Poly(A) mRNA Complex with PABP and eIF4G
inferredcites →https://doi.org/10.1016/j.saa.2011.07.044openalex-snapshot
Study on the interaction of amino phosphine ester derivatives with DNA by spectroscopy, modeling and calorimetry
inferredcites →https://doi.org/10.1016/j.saa.2012.11.060openalex-snapshot
Exploring the binding mechanism of phosphoramidate derivative with DNA: Spectroscopy, calorimetry and modeling
inferredcites →https://doi.org/10.1016/j.str.2015.04.019openalex-snapshot
GTP-Dependent K-Ras Dimerization
inferredcites →https://doi.org/10.1016/j.tca.2006.06.019openalex-snapshot
Applications of isothermal titration calorimetry to measure enzyme kinetics and activity in complex solutions
inferredcites →https://doi.org/10.1016/j.watres.2012.10.037openalex-snapshot
Thermodynamic analysis on the binding of heavy metals onto extracellular polymeric substances (EPS) of activated sludge
inferredcites →https://doi.org/10.1016/j.ymeth.2012.12.003openalex-snapshot
Simultaneous addition of two ligands: A potential strategy for estimating divalent ion affinities in EF-hand proteins by isothermal titration calorimetry
inferredcites →https://doi.org/10.1016/j.ymeth.2014.09.010openalex-snapshot
A unified framework based on the binding polynomial for characterizing biological systems by isothermal titration calorimetry
inferredcites →https://doi.org/10.1016/j.ymeth.2014.10.034openalex-snapshot
Single-experiment displacement assay for quantifying high-affinity binding by isothermal titration calorimetry
inferredcites →https://doi.org/10.1016/j.ymeth.2014.11.012openalex-snapshot
SEDPHAT – A platform for global ITC analysis and global multi-method analysis of molecular interactions
inferredcites →https://doi.org/10.1016/j.ymeth.2014.11.018openalex-snapshot
Fitting two- and three-site binding models to isothermal titration calorimetric data
inferredcites →https://doi.org/10.1016/j.ymeth.2014.11.024openalex-snapshot
High-precision, automated integration of multiple isothermal titration calorimetric thermograms: New features of NITPIC
inferredcites →https://doi.org/10.1016/j.ymeth.2014.12.003openalex-snapshot
Enzyme kinetics determined by single-injection isothermal titration calorimetry
inferredcites →https://doi.org/10.1016/j.ymeth.2014.12.018openalex-snapshot
Global ITC fitting methods in studies of protein allostery
inferredcites →https://doi.org/10.1016/j.ymeth.2015.01.012openalex-snapshot
Isothermal titration calorimetry of ion-coupled membrane transporters
inferredcites →https://doi.org/10.1021/ac00217a002openalex-snapshot
Isothermal titration calorimetry
inferredcites →https://doi.org/10.1021/ac3007522openalex-snapshot
High-Precision Isothermal Titration Calorimetry with Automated Peak-Shape Analysis
inferredcites →https://doi.org/10.1021/ac3025575openalex-snapshot
Quantifying High-Affinity Binding of Hydrophobic Ligands by Isothermal Titration Calorimetry
inferredcites →https://doi.org/10.1021/acs.biochem.5b00722openalex-snapshot
Vascular Endothelial Growth Factor Peptide Ligands Explored by Competition Assay and Isothermal Titration Calorimetry
inferredcites →https://doi.org/10.1021/acs.jafc.5b00758openalex-snapshot
Ethanol Concentration Influences the Mechanisms of Wine Tannin Interactions with Poly( l -proline) in Model Wine
inferredcites →https://doi.org/10.1021/acs.jafc.5b04843openalex-snapshot
Binding of an Oligomeric Ellagitannin Series to Bovine Serum Albumin (BSA): Analysis by Isothermal Titration Calorimetry (ITC)
inferredcites →https://doi.org/10.1021/acs.jcim.5b00514openalex-snapshot
Energetics, Thermodynamics, and Molecular Recognition of Piperine with DNA
inferredcites →https://doi.org/10.1021/acs.jpcb.5b01708openalex-snapshot
Thermodynamic Profiles of Salt Effects on a Host–Guest System: New Insight into the Hofmeister Effect
inferredcites →https://doi.org/10.1021/acs.jpcb.5b03817openalex-snapshot
Thermodynamic Relationships with Processivity in Serratia marcescens Family 18 Chitinases
inferredcites →https://doi.org/10.1021/acs.langmuir.5b02299openalex-snapshot
Binding of Folic Acid Induces Specific Self-Aggregation of Lactoferrin: Thermodynamic Characterization
inferredcites →https://doi.org/10.1021/bi201134uopenalex-snapshot
The Second Ca2+-Binding Domain of NCX1 Binds Mg2+ with High Affinity
inferredcites →https://doi.org/10.1021/bi201674dopenalex-snapshot
Thermodynamics of Coupled Folding in the Interaction of Archaeal RNase P Proteins RPP21 and RPP29
inferredcites →https://doi.org/10.1021/bi4006946openalex-snapshot
P450cin Active Site Water: Implications for Substrate Binding and Solvent Accessibility
inferredcites →https://doi.org/10.1021/bi4009374openalex-snapshot
The Hydrophobic Region of the DmsA Twin-Arginine Leader Peptide Determines Specificity with Chaperone DmsD
inferredcites →https://doi.org/10.1021/bm101341sopenalex-snapshot
Binding of Pentagalloyl Glucose to Two Globular Proteins Occurs via Multiple Surface Sites
inferredcites →https://doi.org/10.1021/bm200954jopenalex-snapshot
Adsorption of RNase A on Cationic Polyelectrolyte Brushes: A Study by Isothermal Titration Calorimetry
inferredcites →https://doi.org/10.1021/bm300810topenalex-snapshot
Binding Specificity and Thermodynamics of Cellulose-Binding Modules from Trichoderma reesei Cel7A and Cel6A
inferredcites →https://doi.org/10.1021/bm301865gopenalex-snapshot
Binding between Proteins and Cationic Spherical Polyelectrolyte Brushes: Effect of pH, Ionic Strength, and Stoichiometry
inferredcites →https://doi.org/10.1021/bm401077bopenalex-snapshot
Toward a Mechanistic Understanding of Ionic Self-Complementary Peptide Self-Assembly: Role of Water Molecules and Ions
inferredcites →https://doi.org/10.1021/bm500041aopenalex-snapshot
Protein-Selective Coacervation with Hyaluronic Acid
inferredcites →https://doi.org/10.1021/bm5007954openalex-snapshot
Structure of Chitosan Determines Its Interactions with Mucin
inferredcites →https://doi.org/10.1021/ci200608bopenalex-snapshot
Thermodynamics of Fragment Binding
inferredcites →https://doi.org/10.1021/cm504080dopenalex-snapshot
A General Approach To Study the Thermodynamics of Ligand Adsorption to Colloidal Surfaces Demonstrated by Means of Catechols Binding to Zinc Oxide Quantum Dots
inferredcites →https://doi.org/10.1021/ic502425eopenalex-snapshot
Ion Exchange in Hydroxyapatite with Lanthanides
inferredcites →https://doi.org/10.1021/ja108118vopenalex-snapshot
Neomycin−Neomycin Dimer: An All-Carbohydrate Scaffold with High Affinity for AT-Rich DNA Duplexes
inferredcites →https://doi.org/10.1021/ja110571ropenalex-snapshot
Fragment Growing Induces Conformational Changes in Acetylcholine-Binding Protein: A Structural and Thermodynamic Analysis
inferredcites →https://doi.org/10.1021/ja2045293openalex-snapshot
Fluoroalkyl and Alkyl Chains Have Similar Hydrophobicities in Binding to the “Hydrophobic Wall” of Carbonic Anhydrase
inferredcites →https://doi.org/10.1021/ja207565mopenalex-snapshot
Molecular Structure Encodes Nanoscale Assemblies: Understanding Driving Forces in Electrostatic Self-Assembly
inferredcites →https://doi.org/10.1021/ja209057dopenalex-snapshot
kinITC: A New Method for Obtaining Joint Thermodynamic and Kinetic Data by Isothermal Titration Calorimetry
inferredcites →https://doi.org/10.1021/ja209959topenalex-snapshot
Synthetic Polymer Nanoparticle–Polysaccharide Interactions: A Systematic Study
inferredcites →https://doi.org/10.1021/ja210475aopenalex-snapshot
Measurement and Theory of Hydrogen Bonding Contribution to Isosteric DNA Base Pairs
inferredcites →https://doi.org/10.1021/ja210567kopenalex-snapshot
Nanomechanical Recognition ofN-Methylammonium Salts
inferredcites →https://doi.org/10.1021/ja211417gopenalex-snapshot
Thermodynamics of Zn2+Binding to Cys2His2and Cys2HisCys Zinc Fingers and a Cys4Transcription Factor Site
inferredcites →https://doi.org/10.1021/ja300605nopenalex-snapshot
Energetic Basis of Human Telomeric DNA Folding into G-Quadruplex Structures
inferredcites →https://doi.org/10.1021/ja303309eopenalex-snapshot
Release of High-Energy Water as an Essential Driving Force for the High-Affinity Binding of Cucurbit[n]urils
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inferred← citeshttps://doi.org/10.7287/peerj.4068v0.1/reviews/1openalex-snapshot
Peer Review #1 of "An update on anticancer drug development and delivery targeting carbonic anhydrase IX (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.4068v0.1/reviews/2openalex-snapshot
Peer Review #2 of "An update on anticancer drug development and delivery targeting carbonic anhydrase IX (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.4068v0.1/reviews/3openalex-snapshot
Peer Review #3 of "An update on anticancer drug development and delivery targeting carbonic anhydrase IX (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.4068v0.1/reviews/4openalex-snapshot
Peer Review #4 of "An update on anticancer drug development and delivery targeting carbonic anhydrase IX (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.4068v0.2/reviews/2openalex-snapshot
Peer Review #2 of "An update on anticancer drug development and delivery targeting carbonic anhydrase IX (v0.2)"
inferred← citeshttps://doi.org/10.7287/peerj.4412v0.1/reviews/1openalex-snapshot
Peer Review #1 of "Crystal structure correlations with the intrinsic thermodynamics of human carbonic anhydrase inhibitor binding (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.4412v0.1/reviews/2openalex-snapshot
Peer Review #2 of "Crystal structure correlations with the intrinsic thermodynamics of human carbonic anhydrase inhibitor binding (v0.1)"
inferred← citeshttps://doi.org/10.7717/peerj.4068openalex-snapshot
An update on anticancer drug development and delivery targeting carbonic anhydrase IX
inferred← citeshttps://doi.org/10.7717/peerj.4412openalex-snapshot
Crystal structure correlations with the intrinsic thermodynamics of human carbonic anhydrase inhibitor binding
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