M
Matthew J. Sanders
Researcher at National Institute for Medical Research
Publications - 12
Citations - 3526
Matthew J. Sanders is an academic researcher from National Institute for Medical Research. The author has contributed to research in topics: AMP-activated protein kinase & AMPK. The author has an hindex of 9, co-authored 9 publications receiving 3184 citations. Previous affiliations of Matthew J. Sanders include Hammersmith Hospital & Imperial College London.
Papers
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Journal ArticleDOI
Structure of mammalian AMPK and its regulation by ADP
Bing Xiao,Matthew J. Sanders,Matthew J. Sanders,Elizabeth Underwood,Richard Heath,Faith V. Mayer,David Carmena,Chun-Xia Jing,Philip A. Walker,John F. Eccleston,Lesley F. Haire,Peter Saiu,Steven Howell,Rein Aasland,Stephen R. Martin,David Carling,Steven J. Gamblin +16 more
TL;DR: It is shown that ADP binding to just one of the two exchangeable AXP (AMP/ADP/ATP) binding sites on the regulatory domain protects the enzyme from dephosphorylation, although it does not lead to allosteric activation.
Journal ArticleDOI
Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade
TL;DR: It is demonstrated that AMP activates AMPK via two mechanisms: by direct allosteric activation and by protecting Thr172 from dephosphorylation, and a simple model for the regulation of AMPK in mammalian cells by LKB1 and CaMKKbeta is proposed.
Journal ArticleDOI
Structural Basis of Ampk Regulation by Small Molecule Activators.
Bing Xiao,Matthew J. Sanders,David Carmena,Nicola J. Bright,Lesley F. Haire,Elizabeth Underwood,Bhakti R. Patel,Richard Heath,Philip A. Walker,Stefan Hallén,Fabrizio Giordanetto,Stephen R. Martin,David Carling,Steven J. Gamblin +13 more
TL;DR: The crystal structure of human AMPK in complex with a small molecule activator that binds at a site between the kinase domain and the carbohydrate-binding module, stabilising the interaction between these two components and suggesting the involvement of an additional metabolite in the physiological regulation of AMPK.
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AMP-activated protein kinase: nature's energy sensor.
TL;DR: The role of AMPK as an energy sensor is reviewed and the recent finding that ADP, as well as AMP, causes activation of mammalian AMPK is considered, which provides a mechanism for the regulation of AM PK in which AMP and ADP protect it against dephosphorylation.
Journal ArticleDOI
AMP-activated protein kinase: new regulation, new roles?
TL;DR: The present review examines the recent progress aimed at understanding the regulation of AMPK and discusses some of the latest developments that have emerged in key areas of human physiology where AMPK is thought to play an important role.