about
Mass-selective soft-landing of protein assemblies with controlled landing energies.EM∩IM: software for relating ion mobility mass spectrometry and electron microscopy data.Mass spectrometry: come of age for structural and dynamical biology.Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallinThe quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated.Small heat shock protein activity is regulated by variable oligomeric substructure.Detergent-free mass spectrometry of membrane protein complexes.Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry.Dynamical structure of αB-crystallin.Real-time monitoring of protein complexes reveals their quaternary organization and dynamics.Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity.C-terminal interactions mediate the quaternary dynamics of αB-crystallin.Mimicking phosphorylation of alphaB-crystallin affects its chaperone activityCollision cross sections for structural proteomics.Bayesian deconvolution of mass and ion mobility spectra: from binary interactions to polydisperse ensembles.Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1†Electronic supplementary information (ESI) available: Procedures for protein expression and purification, 19F-labelling, crystallisation, data collection, and structure deAll three chaperonin genes in the archaeon Haloferax volcanii are individually dispensable.The small heat-shock proteins HSPB2 and HSPB3 form well-defined heterooligomers in a unique 3 to 1 subunit ratio.Quadrupole-time-of-flight mass spectrometer modified for higher-energy dissociation reduces protein assemblies to peptide fragments.Separating and visualising protein assemblies by means of preparative mass spectrometry and microscopy.Dodecameric structure of the small heat shock protein Acr1 from Mycobacterium tuberculosis.Discovery of a Highly Selective Cell-Active Inhibitor of the Histone Lysine Demethylases KDM2/7.Probing dynamic conformations of the high-molecular-weight αB-crystallin heat shock protein ensemble by NMR spectroscopy.Coupling microdroplet microreactors with mass spectrometry: reading the contents of single droplets online.Quantitative mass imaging of single biological macromolecules.The unusual mycobacterial chaperonins: evidence for in vivo oligomerization and specialization of function.The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPasesPublisher Correction: The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPasesIt takes a dimer to tango: Oligomeric small heat shock proteins dissociate to capture substrateEjection of structural zinc leads to inhibition of γ-butyrobetaine hydroxylaseDehydrated but unharmedStructural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions.Combining tandem mass spectrometry with ion mobility separation to determine the architecture of polydisperse proteinsTandem Mass Spectrometry Reveals the Quaternary Organization of Macromolecular AssembliesThermal Dissociation of Multimeric Protein Complexes by Using Nanoelectrospray Mass SpectrometrySubunit Exchange of Multimeric Protein ComplexesA Monte Carlo approach for assessing the specificity of protein oligomers observed in nano-electrospray mass spectraIon mobility–mass spectrometry analysis of large protein complexesLocal unfolding of the HSP27 monomer regulates chaperone activityHspB1 phosphorylation regulates its intramolecular dynamics and mechanosensitive molecular chaperone interaction with filamin C
P50
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P50
description
onderzoeker
@nl
researcher, ORCID id # 0000-0002-1507-3742
@en
name
Justin L.P. Benesch
@ast
Justin L.P. Benesch
@en
Justin L.P. Benesch
@es
Justin L.P. Benesch
@nl
type
label
Justin L.P. Benesch
@ast
Justin L.P. Benesch
@en
Justin L.P. Benesch
@es
Justin L.P. Benesch
@nl
prefLabel
Justin L.P. Benesch
@ast
Justin L.P. Benesch
@en
Justin L.P. Benesch
@es
Justin L.P. Benesch
@nl
P106
P31
P496
0000-0002-1507-3742