Mapping protein-protein interactions by affinity-directed mass spectrometry.
about
Modification-specific proteomics: strategies for characterization of post-translational modifications using enrichment techniquesThe use of bioreactive probes in protein characterization.Advances in surface plasmon resonance biomolecular interaction analysis mass spectrometry (BIA/MS).Use of nitrocellulose films for affinity-directed mass spectrometry for the analysis of antibody/antigen interactions.Efficient identification of photolabelled amino acid residues by combining immunoaffinity purification with MS: revealing the semotiadil-binding site and its relevance to binding sites for myristates in domain III of human serum albumin.Mass spectrometry and non-covalent protein-ligand complexes: confirmation of binding sites and changes in tertiary structure.Characterization of the Streptococcus mutans P1 epitope recognized by immunomodulatory monoclonal antibody 6-11A.Epitope mapping of monoclonal antibodies by mass spectrometry: identification of protein antigens in complex biological systems.Matrix-assisted laser desorption ionization/mass spectrometry mapping of human immunodeficiency virus-gp120 epitopes recognized by a limited polyclonal antibody.Detection of immune complexes by matrix-assisted laser desorption/ionization mass spectrometry.CLPM: a cross-linked peptide mapping algorithm for mass spectrometric analysisEpitope mapping factor VIII A2 domain by affinity-directed mass spectrometry: residues 497-510 and 584-593 comprise a discontinuous epitope for the monoclonal antibody R8B12.Instrumental biosensors: new perspectives for the analysis of biomolecular interactions.Epitope structure of the carbohydrate recognition domain of asialoglycoprotein receptor to a monoclonal antibody revealed by high-resolution proteolytic excision mass spectrometry.Contributions of mass spectrometry to structural immunology.Direct antigen detection from immunoprecipitated beads using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry; a new method for immunobeads-mass spectrometry (iMS).Biomedical applications of protein chips.Combinatorial and Computational Approaches to Identify Interactions of Macrophage Colony-stimulating Factor (M-CSF) and Its Receptor c-FMS.Determination of protein-derived epitopes by mass spectrometry.Characterization of an anti-Borrelia burgdorferi OspA conformational epitope by limited proteolysis of monoclonal antibody-bound antigen and mass spectrometric peptide mapping.Brian Chait: master of mass spectrometry. Interview by Ruth Williams.Mass spectrometry-based immunoassays for the next phase of clinical applications.Quantitation of target proteins and post-translational modifications in affinity-based proteomics approaches.Cryo-EM visualization of an exposed RGD epitope on adenovirus that escapes antibody neutralization.
P2860
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P2860
Mapping protein-protein interactions by affinity-directed mass spectrometry.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on April 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Mapping protein-protein interactions by affinity-directed mass spectrometry.
@en
Mapping protein-protein interactions by affinity-directed mass spectrometry.
@nl
type
label
Mapping protein-protein interactions by affinity-directed mass spectrometry.
@en
Mapping protein-protein interactions by affinity-directed mass spectrometry.
@nl
prefLabel
Mapping protein-protein interactions by affinity-directed mass spectrometry.
@en
Mapping protein-protein interactions by affinity-directed mass spectrometry.
@nl
P2093
P2860
P356
P1476
Mapping protein-protein interactions by affinity-directed mass spectrometry.
@en
P2093
P2860
P304
P356
10.1073/PNAS.93.9.4020
P407
P577
1996-04-01T00:00:00Z