Výsledky vyhledávání - "Gillian R. Hilton"

Terminal Regions Confer Plasticity to the Tetrameric Assembly of Human HspB2 and HspB3

Autor: Wilbert C. Boelens, Frances D.L. Kondrat, Nicholas J. Ray, Nicholas H. Keep, Ambrose R. Cole, Gillian R. Hilton, Christine Slingsby, Wilma Vree Egberts, Alice R. Clark, John A. Carver, Justin L. P. Benesch

Publikováno v: Journal of Molecular Biology, 430, 3297-3310
'Journal of Molecular Biology ', vol: 430, pages: 3297-3310 (2018)
Journal of Molecular Biology
Journal of Molecular Biology, 430, 18, pp. 3297-3310

Heterogeneity in small heat shock proteins (sHsps) spans multiple spatiotemporal regimes—from fast fluctuations of part of the protein, to conformational variability of tertiary structure, plasticity of the interfaces, and polydispersity of the int

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7eb6bb4ad1717ba7769b716c6c542818
https://doi.org/10.1016/j.jmb.2018.06.047

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Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach

Autor: Justin L. P. Benesch, Andrew Baldwin, Gillian R. Hilton, Elizabeth Vierling, Matthew F. Bush, Florian Stengel, Eman Basha, Hadi Lioe, Nomalie Jaya

Small Heat-Shock Proteins (sHSPs) are a family of molecular chaperones that help prevent irreversible aggregation through binding non-native target proteins to form large and heterogeneous complexes. These sHSP:target complexes are an integral part o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cb33b384b190e0a8cd9acd2b4affa3d
https://ora.ox.ac.uk/objects/uuid:70135646-cbeb-4748-99c4-15fbee5e2e98

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Probing Dynamic Conformations of the High-Molecular-Weight αB-Crystallin Heat Shock Protein Ensemble by NMR Spectroscopy

Autor: Patrick Walsh, Simon Sharpe, Andrew Baldwin, Justin L. P. Benesch, Gillian R. Hilton, Lewis E. Kay, D. Flemming Hansen

Publikováno v: Journal of the American Chemical Society. 134:15343-15350

Solution- and solid-state nuclear magnetic resonance (NMR) spectroscopy are highly complementary techniques for studying supra-molecular structure. Here they are employed for investigating the molecular chaperone αB-crystallin, a polydisperse ensemb

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44781c107ee31ce86845c6950ab731f3
https://doi.org/10.1021/ja307874r

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

Autor: Justin L. P. Benesch, Gillian R. Hilton

Publikováno v: Journal of the Royal Society Interface

Mass spectrometry (MS) is a recognized approach for characterizing proteins and the complexes they assemble into. This application of a long-established physico-chemical tool to the frontiers of structural biology has stemmed from experiments perform

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5598dcb974a89fda8f5dc0a29ba4e59f
https://doi.org/10.1098/rsif.2011.0823

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The Polydispersity of αB-Crystallin Is Rationalized by an Interconverting Polyhedral Architecture

Autor: John L. Rubinstein, Lindsay A. Baker, Andrew Baldwin, Justin L. P. Benesch, Hadi Lioe, Lewis E. Kay, Gillian R. Hilton

Publikováno v: Structure. 19:1855-1863

SummaryWe report structural models for the most abundant oligomers populated by the polydisperse molecular chaperone αB-crystallin. Subunit connectivity is determined by using restraints obtained from nuclear magnetic resonance spectroscopy and mass

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a81b997090c3f4b4c20b6caf2211c792
https://doi.org/10.1016/j.str.2011.09.015

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Characterization of Phosphorylated Peptides Using Traveling Wave-Based and Drift Cell Ion Mobility Mass Spectrometry

Autor: Konstantinos Thalassinos, James H. Scrivens, Gillian R. Hilton, Megan Grabenauer, Susan E. Slade, Michael T. Bowers

Publikováno v: Analytical Chemistry. 81:248-254

Phosphorylation is one the most studied and important post translational modifications. Nano electrospray mass spectrometry coupled with traveling wave (T-Wave)-based ion mobility has been used to filter for phosphorylated peptides in tryptic protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c9bad5e9c0d470768dd80ebbafc6a79
https://doi.org/10.1021/ac801916h

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C-terminal interactions mediate the quaternary dynamics of alphaB-crystallin

Autor: Georg K. A. Hochberg, Scott I. McGinnigle, Andrew Baldwin, Arthur Laganowsky, Gillian R. Hilton, Justin L. P. Benesch

Publikováno v: Philos Trans R Soc Lond B Biol Sci
Philosophical Transactions of the Royal Society B: Biological Sciences

αB-crystallin is a highly dynamic, polydisperse small heat-shock protein that can form oligomers ranging in mass from 200 to 800 kDa. Here we use a multifaceted mass spectrometry approach to assess the role of the C-terminal tail in the self-assembl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6a038aada13885fa8fca8d7bddfcd0e
https://hdl.handle.net/21.11116/0000-000A-7687-9

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Small heat-shock proteins: paramedics of the cell

Autor: Gillian R, Hilton, Hadi, Lioe, Florian, Stengel, Andrew J, Baldwin, Justin L P, Benesch

Publikováno v: Topics in current chemistry. 328

The small heat-shock proteins (sHSPs) comprise a family of molecular chaperones which are widespread but poorly understood. Despite considerable effort, comparatively few high-resolution structures have been determined for the sHSPs, a likely consequ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ec30b48e3d7f1b6234ace7d66abcd145
https://pubmed.ncbi.nlm.nih.gov/22576357

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