Unbinding forces of single antibody-antigen complexes correlate with their thermal dissociation rates.
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Molecular immunolabeling with recombinant single-chain variable fragment (scFv) antibodies designed with metal-binding domainsElectrophilic affibodies forming covalent bonds to protein targetsIn vitro evolution of single-chain antibodies using mRNA displaySurface-anchored monomeric agonist pMHCs alone trigger TCR with high sensitivityStructural insight into M-band assembly and mechanics from the titin-obscurin-like-1 complexThree-dimensional structure, binding, and spectroscopic characteristics of the monoclonal antibody 43.1 directed to the carboxyphenyl moiety of fluoresceinRare cell isolation and analysis in microfluidics.Molecular force balance measurements reveal that double-stranded DNA unbinds under force in rate-dependent pathwaysTethering forces of secretory granules measured with optical tweezers.Dynamics of the interaction between a fibronectin molecule and a living bacterium under mechanical force.Measurement of adhesive forces between S. epidermidis and fibronectin-coated surfaces using optical tweezers.Dynamic force spectroscopy: optimized data analysis.Interactions between synaptic vesicle fusion proteins explored by atomic force microscopy.Tailoring in vitro evolution for protein affinity or stability.The elasticity of single kettin molecules using a two-bead laser-tweezers assay.Refined procedure of evaluating experimental single-molecule force spectroscopy data.Multi-step fibrinogen binding to the integrin (alpha)IIb(beta)3 detected using force spectroscopy.A mutation designed to alter crystal packing permits structural analysis of a tight-binding fluorescein-scFv complex.Single molecule mechanical probing of the SNARE protein interactions.Elastic properties of the cell surface and trafficking of single AMPA receptors in living hippocampal neurons.Affinity-matured recombinant antibody fragments analyzed by single-molecule force spectroscopyExploring transferrin-receptor interactions at the single-molecule level.T cell receptor triggering by force.Single Molecule Measurements of Interaction Free Energies Between the Proteins Within Binary and Ternary SNARE ComplexesSingle Molecule Probing of Exocytotic Protein Interactions Using Force Spectroscopy.Force-induced lysozyme--HyHEL5 antibody dissociation and its analysis by means of a cooperative binding model.Design Considerations for CMOS-Integrated Hall-Effect Magnetic Bead Detectors for Biosensor Applications.Antibody responses during hepatitis B viral infection.A bifunctional converter: fluorescein quenching scFv/fluorogen activating protein for photostability and improved signal to noise in fluorescence experiments.A label-free immunosensor array using single-chain antibody fragments.Real-time measurement of spontaneous antigen-antibody dissociation.Temperature dependence of unbinding forces between complementary DNA strandsForce spectroscopy with a small dithering of AFM tip: a method of direct and continuous measurement of the spring constant of single molecules and molecular complexes.Simultaneous topography and recognition imaging using force microscopy.Enforced detachment of red blood cells adhering to surfaces: statics and dynamics.A tactile response in Staphylococcus aureus.Single-molecule force spectroscopy of the Aplysia cell adhesion molecule reveals two homophilic bondsAtomic force microscope based biomolecular force-clamp measurements using a micromachined electrostatic actuator.A force-activated trip switch triggers rapid dissociation of a colicin from its immunity protein.Minimal encounter time and separation determine ligand-receptor binding in cell adhesion
P2860
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P2860
Unbinding forces of single antibody-antigen complexes correlate with their thermal dissociation rates.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on August 2000
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Unbinding forces of single ant ...... ir thermal dissociation rates.
@en
Unbinding forces of single ant ...... ir thermal dissociation rates.
@nl
type
label
Unbinding forces of single ant ...... ir thermal dissociation rates.
@en
Unbinding forces of single ant ...... ir thermal dissociation rates.
@nl
prefLabel
Unbinding forces of single ant ...... ir thermal dissociation rates.
@en
Unbinding forces of single ant ...... ir thermal dissociation rates.
@nl
P2093
P2860
P356
P1476
Unbinding forces of single ant ...... ir thermal dissociation rates.
@en
P2093
A Honegger
A Pluckthun
D Anselmetti
F Schwesinger
H J Güntherodt
L Jermutus
L Tiefenauer
P2860
P304
P356
10.1073/PNAS.97.18.9972
P407
P577
2000-08-01T00:00:00Z