Browsing by Author "Boyce, Michael"
Now showing items 1-20 of 26
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A chemical method for labeling lysine methyltransferase substrates.
(Chembiochem : a European journal of chemical biology, 2011-01)Several protein lysine methyltransferases (PKMTs) modify histones to regulate chromatin-dependent cellular processes, such as transcription, DNA replication and DNA damage repair. PKMTs are likely to have many additional ... -
A decade of caspases.
(Oncogene, 2003-11)Caspases are a family of cysteine proteases that play important roles in regulating apoptosis. A decade of research has generated a wealth of information on the signal transduction pathways mediated by caspases, the distinct ... -
A genome-wide RNAi screen reveals multiple regulators of caspase activation.
(The Journal of cell biology, 2007-11-12)Apoptosis is an evolutionally conserved cellular suicide mechanism that can be activated in response to a variety of stressful stimuli. Increasing evidence suggests that apoptotic regulation relies on specialized cell death ... -
A novel glycoproteomics workflow reveals dynamic O-GlcNAcylation of COPγ1 as a candidate regulator of protein trafficking
(Frontiers in Endocrinology, 2018-10-15)Copyright © 2018 Cox, Luo, Smith, Bisnett, Soderblom and Boyce. O-linked ß-N-acetylglucosamine (O-GlcNAc) is an abundant and essential intracellular form of protein glycosylation in animals and plants. In humans, dysregulation ... -
A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress.
(Science (New York, N.Y.), 2005-02)Most protein phosphatases have little intrinsic substrate specificity, making selective pharmacological inhibition of specific dephosphorylation reactions a challenging problem. In a screen for small molecules that protect ... -
A Sweet Embrace: Control of Protein-Protein Interactions by O-Linked β-N-Acetylglucosamine.
(Biochemistry, 2018-01)O-Linked β-N-acetylglucosamine (O-GlcNAc) is a critical post-translational modification (PTM) of thousands of intracellular proteins. Reversible O-GlcNAcylation governs many aspects of cell physiology and is dysregulated ... -
Bringing chemistry to life.
(Nature methods, 2011-07-28) -
Cell surface glycoproteomic analysis of prostate cancer-derived PC-3 cells.
(Bioorganic & medicinal chemistry letters, 2011-09)Most clinically approved biomarkers of cancer are glycoproteins, and those residing on the cell surface are of particular interest in biotherapeutics. We report a method for selective labeling, affinity enrichment, ... -
Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury.
(Nature chemical biology, 2005-07)The mechanism of apoptosis has been extensively characterized over the past decade, but little is known about alternative forms of regulated cell death. Although stimulation of the Fas/TNFR receptor family triggers a canonical ... -
Directing Traffic: Regulation of COPI Transport by Post-translational Modifications
(Frontiers in Cell and Developmental Biology, 2019-09-11)© Copyright © 2019 Luo and Boyce. The coat protein complex I (COPI) is an essential, highly conserved pathway that traffics proteins and lipids between the endoplasmic reticulum (ER) and the Golgi. Many aspects of the COPI ... -
Dynamic Glycosylation Governs the Vertebrate COPII Protein Trafficking Pathway.
(Biochemistry, 2018-01)The COPII coat complex, which mediates secretory cargo trafficking from the endoplasmic reticulum, is a key control point for subcellular protein targeting. Because misdirected proteins cannot function, protein sorting by ... -
Esterified Trehalose Analogues Protect Mammalian Cells from Heat Shock.
(Chembiochem : a European journal of chemical biology, 2017-09)Trehalose is a disaccharide produced by many organisms to better enable them to survive environmental stresses, including heat, cold, desiccation, and reactive oxygen species. Mammalian cells do not naturally biosynthesize ... -
Functional crosstalk among oxidative stress and O-GlcNAc signaling pathways.
(Glycobiology, 2018-08)In metazoans, thousands of intracellular proteins are modified with O-linked β-N-acetylglucosamine (O-GlcNAc) in response to a wide range of stimuli and stresses. In particular, a complex and evolutionarily conserved interplay ... -
Glycosylation of gigaxonin regulates intermediate filaments: Novel molecular insights into giant axonal neuropathy: supplemental information
(2019-01-26)Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins. Mutations in human gigaxonin cause the fatal neurodegenerative disease ... -
Glycosylation of KEAP1 links nutrient sensing to redox stress signaling.
(The EMBO journal, 2017-08)O-GlcNAcylation is an essential, nutrient-sensitive post-translational modification, but its biochemical and phenotypic effects remain incompletely understood. To address this question, we investigated the global transcriptional ... -
KEAP1 has a sweet spot: A new connection between intracellular glycosylation and redox stress signaling in cancer cells.
(Molecular & cellular oncology, 2017-01)The KEAP1/NRF2 pathway is a master regulator of the redox stress response and is dysregulated in numerous human tumors. We discovered that NRF2 signaling is controlled by the site-specific glycosylation of KEAP1, revealing ... -
Life and death in paradise.
(Nature cell biology, 2002-06)Over 500 researchers participated in a recent American Association for Cancer Research special conference, entitled "Apoptosis and Cancer: Basic Mechanisms and Therapeutic Opportunities in the Post-Genomic Era" (February ... -
Life is sweet: the cell biology of glycoconjugates.
(Molecular biology of the cell, 2019-03)Cells are dazzling in their diversity, both within and across organisms. And yet, throughout this variety runs at least one common thread: sugars. All cells on Earth, in all domains of life, are literally covered in glycans, ... -
Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.
(Proceedings of the National Academy of Sciences of the United States of America, 2011-02-07)Hundreds of mammalian nuclear and cytoplasmic proteins are reversibly glycosylated by O-linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and stability. Despite its broad functional significance, ... -
Metabolic labeling enables selective photocrosslinking of O-GlcNAc-modified proteins to their binding partners.
(Proceedings of the National Academy of Sciences of the United States of America, 2012-03-12)O-linked β-N-acetylglucosamine (O-GlcNAc) is a reversible posttranslational modification found on hundreds of nuclear and cytoplasmic proteins in higher eukaryotes. Despite its ubiquity and essentiality in mammals, functional ...
