about
Directly interrogating single quantum dot labelled UvrA2 molecules on DNA tightropes using an optically trapped nanoprobe.Investigation of bacterial nucleotide excision repair using single-molecule techniques.Load and Pi control flux through the branched kinetic cycle of myosin V.A mutant heterodimeric myosin with one inactive head generates maximal displacement.TRF1 and TRF2 use different mechanisms to find telomeric DNA but share a novel mechanism to search for protein partners at telomeres.Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single- molecule imaging of quantum-dot-labeled proteins.Single molecule techniques in DNA repair: a primerFunctional interplay between SA1 and TRF1 in telomeric DNA binding and DNA-DNA pairingSingle-myosin crossbridge interactions with actin filaments regulated by troponin-tropomyosin.Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin.Combining intracellular selection with protein-fragment complementation to derive Aβ interacting peptides.Retro-inversal of intracellular selected β-amyloid-interacting peptides: implications for a novel Alzheimer's disease treatment.Intracellular selection of peptide inhibitors that target disulphide-bridged Aβ42 oligomersSingle Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNAIntracellular screening of a peptide library to derive a potent peptide inhibitor of α-synuclein aggregation.Direct Measurements of Local Coupling between Myosin Molecules Are Consistent with a Model of Muscle Activation.DNA-Protein Interactions Studied Directly Using Single Molecule Fluorescence Imaging of Quantum Dot Tagged Proteins Moving on DNA Tightropes.A branched kinetic scheme describes the mechanochemical coupling of Myosin Va processivity in response to substrate.Integrating Optical Tweezers, DNA Tightropes, and Single-Molecule Fluorescence Imaging: Pitfalls and Traps.Real-time single-molecule imaging reveals a direct interaction between UvrC and UvrB on DNA tightropes.Dynamics of lesion processing by bacterial nucleotide excision repair proteinsA kinetic analysis of the nucleotide-induced allosteric transitions of GroEL.DNA repair: Clamping down on copy errorsSingle-Molecule Imaging Reveals that Rad4 Employs a Dynamic DNA Damage Recognition ProcessSingle-Molecule Methods for Nucleotide Excision Repair: Building a System to Watch Repair in Real Time.Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings.Using fluorescent myosin to directly visualize cooperative activation of thin filaments.Beta(2)-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro.Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro.Recruitment of UvrBC complexes to UV-induced damage in the absence of UvrA increases cell survival.Hierarchical assembly of beta2-microglobulin amyloid in vitro revealed by atomic force microscopy.Amyloid-forming peptides from beta2-microglobulin-Insights into the mechanism of fibril formation in vitro.PrefaceRevealing the mechanism of how cardiac myosin-binding protein C N-terminal fragments sensitize thin filaments for myosin bindingSingle-cell mutagenic responses and cell death revealed in real timeUnderstanding the coupling between DNA damage detection and UvrA's ATPase using bulk and single molecule kineticsMyBP-C: one protein to govern them all
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Neil M Kad
@ast
Neil M Kad
@en
Neil M Kad
@es
Neil M Kad
@sl
type
label
Neil M Kad
@ast
Neil M Kad
@en
Neil M Kad
@es
Neil M Kad
@sl
prefLabel
Neil M Kad
@ast
Neil M Kad
@en
Neil M Kad
@es
Neil M Kad
@sl
P106
P21
P31
P496
0000-0002-3491-8595