The solution to the streptavidin-biotin paradox: the influence of history on the strength of single molecular bonds.
about
Regulation of catch bonds by rate of force applicationCharacterization of enhanced monovalent and bivalent thrombin DNA aptamer binding using single molecule force spectroscopy.Force measurements of TCR/pMHC recognition at T cell surfaceBFPTool: a software tool for analysis of Biomembrane Force Probe experiments.Effects of multiple-bond ruptures on kinetic parameters extracted from force spectroscopy measurements: revisiting biotin-streptavidin interactions.Single-molecule bonds characterized by solid-state nanopore force spectroscopy.Monitoring ligand-receptor interactions by photonic force microscopy.Reconsideration of dynamic force spectroscopy analysis of streptavidin-biotin interactions.Quantitative modeling assesses the contribution of bond strengthening, rebinding and force sharing to the avidity of biomolecule interactions.The role of flexible tethers in multiple ligand-receptor bond formation between curved surfaces.Minimal encounter time and separation determine ligand-receptor binding in cell adhesionAtomic force microscopy reveals a role for endothelial cell ICAM-1 expression in bladder cancer cell adherence.A simple bioconjugate attachment protocol for use in single molecule force spectroscopy experiments based on mixed self-assembled monolayers.Extending Bell's model: how force transducer stiffness alters measured unbinding forces and kinetics of molecular complexes.Biophysical description of multiple events contributing blood leukocyte arrest on endotheliumTuning the formation and rupture of single ligand-receptor bonds by hyaluronan-induced repulsion.Integrin-generated forces lead to streptavidin-biotin unbinding in cellular adhesions.How Cells feel their environment: a focus on early dynamic events.Studying Molecular Interactions at the Single Bond Level with a Laminar Flow Chamber.Predicting the rupture probabilities of molecular bonds in series.The adhesion mediated by the P-selectin P-selectin glycoprotein ligand-1 (PSGL-1) couple is stronger for shorter PSGL-1 variants.Kinetics and mechanics of two-dimensional interactions between T cell receptors and different activating ligandsAn RNA toolbox for single-molecule force spectroscopy studies.Force measurement enabling precise analysis by dynamic force spectroscopy.Energy landscape of chelated uranyl: antibody interactions by dynamic force spectroscopy.Electrical detection of fast reaction kinetics in nanochannels with an induced flow.Characterizing cell adhesion by using micropipette aspirationSingle-molecule pulling experiments: when the stiffness of the pulling device matters.Single-molecule unfolding force distributions reveal a funnel-shaped energy landscape.Single and multiple bonds in (strept)avidin-biotin interactions.Axon zippering in neuronal cell culture and its biophysical modeling.Fatigue failure and molecular machine design.Micropipette force probe to quantify single-cell force generation: application to T-cell activation.A high throughput molecular force assay for protein-DNA interactions.Analyzing single-bond experiments: influence of the shape of the energy landscape and universal law between the width, depth, and force spectrum of the bond.Force spectroscopy of a single artificial biomolecule bond: the Kramers' high-barrier limit holds close to the critical forceDirect immobilization of avidin protein on AFM tip functionalized by acrylic acid vapor at RF plasmaDissection of structural dynamics of chromatin fibers by single-molecule magnetic tweezersInvestigating the binding behaviour of two avidin-based testosterone binders using molecular recognition force spectroscopypH-Dependent Deformations of the Energy Landscape of Avidin-like Proteins Investigated by Single Molecule Force Spectroscopy
P2860
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P2860
The solution to the streptavidin-biotin paradox: the influence of history on the strength of single molecular bonds.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
The solution to the streptavid ...... gth of single molecular bonds.
@en
The solution to the streptavid ...... gth of single molecular bonds.
@nl
type
label
The solution to the streptavid ...... gth of single molecular bonds.
@en
The solution to the streptavid ...... gth of single molecular bonds.
@nl
prefLabel
The solution to the streptavid ...... gth of single molecular bonds.
@en
The solution to the streptavid ...... gth of single molecular bonds.
@nl
P2860
P1433
P1476
The solution to the streptavid ...... ngth of single molecular bonds
@en
P2860
P304
P356
10.1529/BIOPHYSJ.105.067769
P407
P577
2005-09-16T00:00:00Z