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Justin L. P. Benesch

Justin L. P. Benesch

D-Index & Metrics

Chemistry

D-Index
60
Citations
14251
World Ranking
9617
National Ranking
545

Overview

Justin L. P. Benesch is a researcher affiliated with the University of Oxford in the United Kingdom. Their primary field of study encompasses Biochemistry, Genetics, and Molecular Biology with a focus on Molecular Biology, Spectroscopy, Materials Chemistry, Cell Biology, and Computational Mechanics as subfields.

Benesch's research prominently addresses areas such as Protein Structure and Dynamics, Enzyme Structure and Function, Mass Spectrometry Techniques and Applications, Heat Shock Proteins research, Ion-surface interactions and analysis, Advanced Electron Microscopy Techniques and Applications, and Endoplasmic Reticulum Stress and Disease.

Recent publications by Benesch include:

  • Quantifying the heterogeneity of macromolecular machines by mass photometry (2020, Nature Communications)
  • Origin of complexity in haemoglobin evolution (2020, Nature)
  • Quantifying Protein-Protein Interactions by Molecular Counting with Mass Photometry (2020, Angewandte Chemie International Edition)
  • Hyperphosphorylated tau self-assembles into amorphous aggregates eliciting TLR4-dependent responses (2022, Nature Communications)
  • Small heat-shock proteins and their role in mechanical stress (2020, Cell Stress and Chaperones)

Benesch has collaborated frequently with several researchers including Philipp Kukura, Weston B. Struwe, Dominik Šaman, Carol V. Robinson, and Matteo T. Degiacomi.

Publications appear predominantly in venues such as bioRxiv (Cold Spring Harbor Laboratory), Biophysical Journal, Nature Communications, Nature, and Proceedings of the National Academy of Sciences.

Best Publications

  • Ion mobility-mass spectrometry analysis of large protein complexes.

    Brandon T. Ruotolo;Justin L.P. Benesch;Alan M. Sandercock;Suk Joon Hyung

  • Bayesian deconvolution of mass and ion mobility spectra: from binary interactions to polydisperse ensembles.

    Michael T. Marty;Andrew J. Baldwin;Erik G. Marklund;Georg K. A. Hochberg

  • Quantitative mass imaging of single biological macromolecules

    Gavin Young;Nikolas Hundt;Daniel Cole;Adam Fineberg

  • Protein complexes in the gas phase: technology for structural genomics and proteomics.

    Justin L. P. Benesch;Brandon T. Ruotolo;Douglas A. Simmons;Carol V. Robinson

  • Recommendations for reporting ion mobility Mass Spectrometry measurements

    Valérie Gabelica;Alexandre A. Shvartsburg;Carlos Afonso;Perdita Barran

  • Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function.

    Arthur Laganowsky;Justin L. P. Benesch;Justin L. P. Benesch;Meytal Landau;Meytal Landau;Linlin Ding

  • Mass spectrometry: come of age for structural and dynamical biology

    Justin L P Benesch;Brandon T Ruotolo

  • Collision cross sections for structural proteomics.

    Erik G. Marklund;Matteo T. Degiacomi;Carol V. Robinson;Andrew J. Baldwin

  • Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin.

    J. Andrew Aquilina;Justin L. P. Benesch;Orval A. Bateman;Christine Slingsby

  • Quaternary dynamics and plasticity underlie small heat shock protein chaperone function

    Florian Stengel;Andrew J. Baldwin;Alexander J. Painter;Nomalie Jaya

  • Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies.

    Justin L.P. Benesch;J. Andrew Aquilina;Brandon T. Ruotolo;Frank Sobott

  • Coupling microdroplet microreactors with mass spectrometry: reading the contents of single droplets online.

    Luis M Fidalgo;Graeme Whyte;Brandon T Ruotolo;Justin L P Benesch

  • Mass spectrometry of macromolecular assemblies: preservation and dissociation.

    Justin L. P. Benesch;Carol V. Robinson

  • Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry.

    Frank Sobott;Justin L.P. Benesch;Elizabeth Vierling;Carol V. Robinson

  • Collisional Activation of Protein Complexes: Picking Up the Pieces

    Justin L. P. Benesch

  • The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity

    Georg K. A. Hochberg;Heath Ecroyd;Heath Ecroyd;Cong Liu;Cong Liu;Cong Liu;Dezerae Cox;Dezerae Cox

  • Quantifying the heterogeneity of macromolecular machines by mass photometry.

    Adar Sonn-Segev;Katarina Belacic;Tatyana Bodrug;Gavin Young

  • Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity

    Heath Ecroyd;Sarah Meehan;Joseph Horwitz;J. Andrew Aquilina

  • Thermal dissociation of multimeric protein complexes by using nanoelectrospray mass spectrometry.

    Justin L. P. Benesch;Frank Sobott;Carol V. Robinson

  • Phosphorylation of αB-Crystallin Alters Chaperone Function through Loss of Dimeric Substructure *

    J. Andrew Aquilina;Justin L.P. Benesch;Lin Lin Ding;Orna Yaron

  • Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry.

    Gillian R. Hilton;Justin L. P. Benesch

Frequent Co-Authors

Carol V. Robinson
Carol V. Robinson University of Oxford
Andrew J. Baldwin
Andrew J. Baldwin University of Oxford
Heath Ecroyd
Heath Ecroyd University of Wollongong
Elizabeth Vierling
Elizabeth Vierling University of Massachusetts Amherst
Frank Sobott
Frank Sobott University of Leeds
Brandon T. Ruotolo
Brandon T. Ruotolo University of Michigan–Ann Arbor
John A. Carver
John A. Carver Australian National University
Philipp Kukura
Philipp Kukura University of Oxford
Duilio Cascio
Duilio Cascio University of California, Los Angeles
Wilbert C. Boelens
Wilbert C. Boelens Radboud University

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