C
Carol V. Robinson
Researcher at University of Oxford
Publications - 710
Citations - 58493
Carol V. Robinson is an academic researcher from University of Oxford. The author has contributed to research in topics: Mass spectrometry & Protein structure. The author has an hindex of 123, co-authored 670 publications receiving 51896 citations. Previous affiliations of Carol V. Robinson include Cardiff University & University of East Anglia.
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Journal ArticleDOI
Mechanism of auxin perception by the TIR1 ubiquitin ligase
Xu Tan,Luz Irina A. Calderon-Villalobos,Michal Sharon,Changxue Zheng,Carol V. Robinson,Mark Estelle,Ning Zheng +6 more
TL;DR: These structures show that the leucine-rich repeat domain of TIR1 contains an unexpected inositol hexakisphosphate co-factor and recognizes auxin and the Aux/IAA polypeptide substrate through a single surface pocket, establishing the first structural model of a plant hormone receptor.
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Climate change and marine plankton
TL;DR: The interactions between climate change and plankton communities are reviewed, focusing on systematic changes in plankton community structure, abundance, distribution and phenology over recent decades, to consider the potential socioeconomic impacts.
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Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
David R. Booth,Margaret Sunde,Vittorio Bellotti,Vittorio Bellotti,Carol V. Robinson,Winston L. Hutchinson,Paul E. Fraser,Philip N. Hawkins,Christopher M. Dobson,Sheena E. Radford,Sheena E. Radford,Colin C.F. Blake,Mark B. Pepys +12 more
TL;DR: Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.
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Ion mobility-mass spectrometry analysis of large protein complexes.
TL;DR: Within this protocol, general approaches to data interpretation, methods of predicting whether specific model structures for a given protein assembly can be separated by ion mobility, and generalized strategies for data normalization and modeling are covered.
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Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
Summer L. Bernstein,Nicholas F. Dupuis,Noel D. Lazo,Thomas Wyttenbach,Margaret M. Condron,Gal Bitan,David B. Teplow,Joan-Emma Shea,Brandon T. Ruotolo,Carol V. Robinson,Michael T. Bowers +10 more
TL;DR: This work presents a new analysis method, ion mobility coupled with mass spectrometry, for determination of in vitro oligomer distributions and the qualitative structure of each of the aggregates, which provides a candidate in the Aβ42 dodecamer for the primary toxic species in Alzheimer's disease.