Elspeth F. Garman
University of Oxford
204 Papers
1.8K Citations
Elspeth F. Garman is an academic researcher from University of Oxford. The author has contributed to research in topics: Chemistry & Neuraminidase. The author has an hindex of 55, co-authored 187 publications. Previous affiliations of Elspeth F. Garman include University of British Columbia & University of Washington.
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Papers
Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product
David J. Owen,Martin E.M. Noble,Elspeth F. Garman,Anastassios C. Papageorgiou,Louise N. Johnson +4 more
TL;DR: The overall structure of Phk gamma trnc is similar to that of the catalytic core of other protein kinases, and the interactions between the enzyme and the nucleotide product of its activity, Mg2+/ADP, explain the inhibitory properties of the nucleotides that are observed in kinetic studies.
HDAC6–p97/VCP controlled polyubiquitin chain turnover
Cyril Boyault,Benoit Gilquin,Yu Zhang,Vladimir Rybin,Elspeth F. Garman,Wolfram Meyer-Klaucke,Patrick Matthias,Christoph W. Müller,Saadi Khochbin +8 more
TL;DR: It is proposed that a finely tuned balance of HDAC6 and p97/VCP concentrations determines the fate of ubiquitinated misfolded proteins: p97 /VCP would promote protein degradation and ubiquitin turnover, whereasHDAC6 would favour the accumulation of ubiquITinated protein aggregates and inclusion body formation.
Crystal structure of a bacterial photoactivated adenylate cyclase determined at room temperature by serial femtosecond crystallography
S. M. Kapetanaki,Nicolas Coquelle,David von Stetten,Martin Byrdin,R. Rios-Santacruz,Richard Bean,Johan Bielecki,Mohamed Boudjelida,Z. Fekete,Geoff W. Grime,H. Han,Caitlin E. Hatton,Sravya Mounika Kantamneni,Konstantin Kharitonov,M. Kloos,F. Koua,Iñaki de Diego Martinez,Diogo V. M. Melo,Lukas Rane,A. Round,Ekaterina Round,A. Sarma,Robin Schubert,Joachim Schulz,M. Sikorski,M. Vakili,J. Valerio,Jovana Vitas,R. De Wijn,Agnieszka Wrona,Ninon Zala,Arwen Pearson,Katerina Dörner,G. Schirò,Elspeth F. Garman,A. Lukács,Martin Weik +36 more
TL;DR: These structures of the wild-type enzyme in combination with the cryo MX synchrotron structure of a light-sensor domain mutant provide insight into the hydrogen bond network rearrangement upon blue-light illumination and pave the way for the determination of structural intermediates of the enzyme by time-resolved SX.
The topology, structure and PE interaction of LITAF underpin a Charcot-Marie-Tooth disease type 1C
Anita K. Ho,Jane L. Wagstaff,Paul T. Manna,Lena Wartosch,Seema Qamar,Elspeth F. Garman,Stefan M.V. Freund,Rhys C. Roberts +7 more
TL;DR: It is proposed that an aberrant LITAF-PE interaction on the surface of intracellular membranes contributes to the molecular pathogenesis that underlies this currently incurable disease.