Matthew R. Pratt

Oct 8, 2024 | sharecast.com | Steven Boyes |Mike Scott |Matthew R. Pratt |David Thomas

BARRATT REDROW PLC(the 'Company')Notification and public disclosure of transactions by persons discharging managerial responsibilities ('PDMRs') and persons closely associated ('PCAs') with them.

Oct 8, 2024 | sharesmagazine.co.uk | Steven Boyes |Mike Scott |Matthew R. Pratt |David Thomas

BARRATT REDROW PLC (the 'Company') Notification and public disclosure of transactions by persons discharging managerial responsibilities ('PDMRs') and persons closely associated ('PCAs') with them.

May 3, 2024 | cell.com | Binyou Wang |Matthew R. Pratt

Small heat shock proteins (sHSPs) play key roles in cellular stress and several human diseases. The direct effects of some post-translational modifications (PTMs) on certain sHSPs have been characterized, raising the possibility that small molecules could be used to modulate these modifications and indirectly up- or downregulate sHSP activity.

Oct 30, 2023 | jbc.org | Byrne M.D |Matthew R. Pratt |David J. Vocadlo |Simon FRASER

AbstractO-GlcNAc is a common modification found on nuclear and cytoplasmic proteins. Determining the catalytic mechanism of the enzyme O-GlcNAcase (OGA), which removes O-GlcNAc from proteins, enabled the creation of potent and selective inhibitors of this regulatory enzyme. Such inhibitors have served as important tools in helping to uncover the cellular and organismal physiological roles of this modification.

Feb 22, 2023 | nature.com | Matthew R. Pratt

O-GlcNAc is a widespread form of intracellular glycosylation that is added to thousands of substrates by one enzyme, O-GlcNAc transferase (OGT), and removed by one other enzyme, O-GlcNAcase (OGA); the generality of this biochemistry has made it extremely challenging to alter the levels of O-GlcNAc on selected proteins to investigate the consequences of specific modifications. In a recent Cell paper, Zhu et al.