User profiles for Matthew R. Pratt

Matthew Pratt

Professor, University of Southern California
Verified email at usc.edu
Cited by 5020

O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's disease

…, BW Zaro, MT Roth, DB Arnold, R Langen, MR Pratt - Nature …, 2015 - nature.com
Several aggregation-prone proteins associated with neurodegenerative diseases can be
modified by O-linked N-acetyl-glucosamine (O-GlcNAc) in vivo. One of these proteins, α-…

[PDF][PDF] Click chemistry in proteomic investigations

CG Parker, MR Pratt - Cell, 2020 - cell.com
Despite advances in genetic and proteomic techniques, a complete portrait of the proteome
and its complement of dynamic interactions and modifications remains a lofty, and as of yet, …

Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1

…, YY Yang, HC Hang, MR Pratt - Proceedings of the …, 2011 - National Acad Sciences
The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine
(GlcNAc) continues to emerge as an important regulator of many biological …

Synthetic glycopeptides and glycoproteins as tools for biology

MR Pratt, CR Bertozzi - Chemical Society Reviews, 2005 - pubs.rsc.org
Investigations into the roles of protein glycosylation have revealed functions such as modulating
protein structure and localization, cell–cell recognition, and signaling in multicellular …

The E3 ligase adapter cereblon targets the C-terminal cyclic imide degron

…, N Vallavoju, HC Lloyd, B Wang, D Shen, MR Pratt… - Nature, 2022 - nature.com
The ubiquitin E3 ligase substrate adapter cereblon (CRBN) is a target of thalidomide and
lenalidomide 1 , therapeutic agents used in the treatment of haematopoietic malignancies 2 , 3 …

α-Synuclein O-GlcNAcylation alters aggregation and toxicity, revealing certain residues as potential inhibitors of Parkinson's disease

…, CA De Leon, HA Lashuel, MR Pratt - Proceedings of the …, 2019 - National Acad Sciences
A compelling link is emerging between the posttranslational modification O-GlcNAc and
protein aggregation. A prime example is α-synuclein, which forms toxic aggregates that are …

Homogeneous glycopeptides and glycoproteins for biological investigation

MJ Grogan, MR Pratt, LA Marcaurelle… - Annual review of …, 2002 - annualreviews.org
▪ Abstract Protein glycosylation is widely recognized as a modulator of protein structure,
localization, and cell-cell recognition in multicellular systems. Glycoproteins are typically …

Changes in Metabolic Chemical Reporter Structure Yield a Selective Probe of O-GlcNAc Modification

…, BW Zaro, F Piller, V Piller, MR Pratt - Journal of the American …, 2014 - ACS Publications
Metabolic chemical reporters (MCRs) of glycosylation are analogues of monosaccharides
that contain bioorthogonal functionalities and enable the direct visualization and identification …

Semisynthetic, site-specific ubiquitin modification of α-synuclein reveals differential effects on aggregation

…, R Langen, C Chatterjee, MR Pratt - Journal of the …, 2012 - ACS Publications
The process of neurodegeneration in Parkinson’s Disease is intimately associated with the
aggregation of the protein α-synuclein into toxic oligomers and fibrils. Interestingly, many of …

O-GlcNAc modification of small heat shock proteins enhances their anti-amyloid chaperone activity

…, TT Takahashi, CFW Becker, D Baker, MR Pratt - Nature …, 2021 - nature.com
A major role for the intracellular post-translational modification O-GlcNAc appears to be the
inhibition of protein aggregation. Most of the previous studies in this area focused on O-…