About: Structural energetics of peptide recognition: Angiotensin II/antibody binding

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scholarly article by Kenneth P. Murphy published in February 1993

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в лютому 1993 (uk) article scientifique publié en 1993 (fr) im Februar 1993 veröffentlichter wissenschaftlicher Artikel (de) scholarly article by Kenneth P. Murphy published in February 1993 (en)
publication date	wds:Q57206223-5FA1C072-A4DE-433A-B7D3-31F30B02F4F0
publication date	1993-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57206223-9F430E34-6F00-4D18-BF7B-2220E5D3C6D5
language of work or name	English
author name string	wds:Q57206223-1CF46E68-681C-4428-B675-8700A64AC360 wds:Q57206223-716F6488-846B-4E4D-88AE-2BA4A9AC235E wds:Q57206223-857A893C-711B-40A9-B5D2-8BBDDFA55C86 wds:Q57206223-8E1DE226-0137-4D20-AC49-AA2D5D2D6ED0
author name string	Ernesto Freire Dong Xie K. Christopher Garcia Kenneth P. Murphy
rdfs:label	Structural energetics of peptide recognition: Angiotensin II/antibody binding (en) Structural energetics of peptide recognition: Angiotensin II/antibody binding (nl)
skos:prefLabel	Structural energetics of peptide recognition: Angiotensin II/antibody binding (en) Structural energetics of peptide recognition: Angiotensin II/antibody binding (nl)
name	Structural energetics of peptide recognition: Angiotensin II/antibody binding (en) Structural energetics of peptide recognition: Angiotensin II/antibody binding (nl)
author	wds:Q57206223-86842E22-DF90-43FC-A24B-A3A05832E022
author	L. Mario Amzel
title	wds:Q57206223-0C3F9272-BD8C-4916-A2F2-54B105A91D52
title	Structural energetics of peptide recognition: Angiotensin II/antibody binding (en)
page(s)	wds:Q57206223-CC4D1C5A-63C7-469D-9DE9-D2053D09B4A0
page(s)	113-120
instance of	wds:Q57206223-24F70138-13C7-4A42-A47D-0D2756899DB0
instance of	scholarly article
main subject	wds:Q57206223-1833FD55-272B-4B22-B5E1-5B90048D9C06 wds:Q57206223-E4880173-B7D4-4A0C-8C11-B3FA42BDD67B wds:Q57206223-F45A1F77-2691-4EE0-88EE-EAC1025B0DD5
main subject	antibody molecular biology structural biology
PubMed ID	wds:Q57206223-1A596C23-9DBE-480B-9435-DA11DD393279
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8441749
PubMed ID	8441749
published in	wds:Q57206223-3B19E1E9-87DC-4355-AE2C-4EF80AD31EC1
published in	Proteins
issue	wds:Q57206223-509925A9-3489-4510-94DE-227D683074AC
volume	wds:Q57206223-D4AF66E5-EED4-4966-BD44-377757C3724E
issue	2
volume	15
DOI	wds:Q57206223-B633A8DB-E95A-428C-8995-23D59C7ABB43
DOI	http://dx.doi.org/10.1002/PROT.340150203
DOI	10.1002/PROT.340150203
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57206223
is cites work of	Two different proteins that compete for binding to thrombin have opposite kinetic and thermodynamic profiles The affinity maturation of anti-4-hydroxy-3-nitrophenylacetyl mouse monoclonal antibody. A calorimetric study of the antigen-antibody interaction Thermodynamic analysis of the interaction between the 0.5beta Fv fragment and the RP135 peptide antigen derived from the V3 loop of HIV-1 gp120 Structure-based drug design Dimethyl sulfoxide at 2.5% (v/v) alters the structural cooperativity and unfolding mechanism of dimeric bacterial NAD+ synthetase Thermodynamic analyses reveal role of water release in epitope recognition by a monoclonal antibody against the human guanylyl cyclase C receptor Thermodynamic characterization of the interaction of human cyclophilin 18 with cyclosporin A. The statistical-thermodynamic basis for computation of binding affinities: a critical review Aspartate transcarbamylase from Escherichia coli: activity and regulation Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation Thermodynamics of T cell receptor binding to peptide-MHC: evidence for a general mechanism of molecular scanning Prediction of binding energetics from structure using empirical parameterization Studying multisite binary and ternary protein interactions by global analysis of isothermal titration calorimetry data in SEDPHAT: application to adaptor protein complexes in cell signaling Recognition between flexible protein molecules: induced and assisted folding Protonation and pK changes in protein-ligand binding. On the entropy of protein folding Large-scale expression and thermodynamic characterization of a glutamate receptor agonist-binding domain Thermodynamics of protein-ligand interactions: history, presence, and future aspects Statistical thermodynamic analysis of differential scanning calorimetry data: structural deconvolution of heat capacity function of proteins A structural and energetics analysis of the binding of a series of N-acetylneuraminic-acid-based inhibitors to influenza virus sialidase Identification of ligands for RNA targets via structure-based virtual screening: HIV-1 TAR. Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry Kinetic analysis of interaction of BRCA1 tandem breast cancer c-terminal domains with phosphorylated peptides reveals two binding conformations Measurement of protein interaction bioenergetics: application to structural variants of anti-sCD4 antibody Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin-biotin system Structure-based prediction of binding affinities and molecular design of peptide ligands. Involvement of water molecules in the association of monoclonal antibody HyHEL-5 with bobwhite quail lysozyme Recognition of the intrinsically flexible addiction antidote MazE by a dromedary single domain antibody fragment. Structure, thermodynamics of binding, stability, and influence on interactions with DNA. Synthetic peptide vaccine and antibody therapeutic development: prevention and treatment of Pseudomonas aeruginosa A novel method reveals that solvent water favors polyproline II over beta-strand conformation in peptides and unfolded proteins: conditional hydrophobic accessible surface area (CHASA). Bound water molecules and conformational stabilization help mediate an antigen-antibody association Antidotes, antibody-mediated immunity and the future of pharmaceutical product development. Consistency in structural energetics of protein folding and peptide recognition Structural Insight into the Kinetics and Cp of Interactions between TEM-1 -Lactamase and -Lactamase Inhibitory Protein (BLIP) Thermodynamics of interactions of urea and guanidinium salts with protein surface: relationship between solute effects on protein processes and changes in water-accessible surface area Characterization of ligand binding of a soluble human insulin-like growth factor I receptor variant suggests a ligand-induced conformational change Effector-repressor interactions, binding of a single effector molecule to the operator-bound TtgR homodimer mediates derepression. The structural basis for the allosteric regulation of ribonucleotide reductase Contribution of translational and rotational motions to molecular association in aqueous solution Thermodynamic characterization of interleukin-8 monomer binding to CXCR1 receptor N-terminal domain Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization Structures of Aβ-Related Peptide−Monoclonal Antibody Complexes , Thermodynamic analysis of the binding of component enzymes in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Biophysical characterization of the interaction between hepatic glucokinase and its regulatory protein: impact of physiological and pharmacological effectors Predicting binding energetics from structure: looking beyond DeltaG degrees. Membrane partitioning of the pore-forming domain of colicin A. Role of the hydrophobic helical hairpin Interaction of a designed interleukin-10 epitope mimic with an antibody studied by isothermal titration microcalorimetry Tight ligand binding affinities determined from thermodynamic linkage to temperature by titration calorimetry. Kinetics and energetics of specific intermolecular interactions

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