Global Proteome and Ubiquitinome Changes in the Soluble and Insoluble Fractions of Q175 Huntington Mice Brains*
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Summary
The authors' data sheds light on putative novel proteins involved in different cellular processes as well as their ubiquitinated status in Huntington's disease, which forms the basis for further mechanistic studies to understand the role of differential ubiquitination of huntingtin and ubiquitin-regulated processes in Huntington’s disease.
- Type
- article
- Published
- 2019-05-28
- Cited by
- 28
- References
- 71
- Access
- Open access
- OpenAlex
- https://openalex.org/W2947192474
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:169033487
Keywords
Proteome, Huntington's disease, Proteomics, Chemistry, Computational biology
References
- The role of post-translational modifications of huntingtin in the pathogenesis of Huntington’s disease
- A Role for Huntington Disease Protein in Dendritic RNA Granules*
- Proteomic Analysis of Wild-type and Mutant Huntingtin-associated Proteins in Mouse Brains Identifies Unique Interactions and Involvement in Protein Synthesis*
- Huntingtin Functions as a Scaffold for Selective Macroautophagy
- Inhibition of the Striatal Specific Phosphodiesterase PDE10A Ameliorates Striatal and Cortical Pathology in R6/2 Mouse Model of Huntington's Disease
- IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome
- Cellular and subcellular localization of PDE10A, a striatum-enriched phosphodiesterase.
- Unbiased Screen Reveals Ubiquilin-1 and -2 Highly Associated with Huntingtin Inclusions
- Mutant Huntingtin N-terminal Fragments of Specific Size Mediate Aggregation and Toxicity in Neuronal Cells*
- Ubiquitin ligase ITCH recruitment suppresses the aggregation and cellular toxicity of cytoplasmic misfolded proteins
- Differential ubiquitination and degradation of huntingtin fragments modulated by ubiquitin-protein ligase E3A
- E6-AP Promotes Misfolded Polyglutamine Proteins for Proteasomal Degradation and Suppresses Polyglutamine Protein Aggregation and Toxicity*
- Detection of ubiquitinated huntingtin species in intracellular aggregates
- Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin.
- p53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease.
- Evidence for degenerative and regenerative changes in neostriatal spiny neurons in Huntington's disease.
- Phosphorylation of Threonine 3
- The phosphodiesterase 10 positron emission tomography tracer, [18F]MNI-659, as a novel biomarker for early Huntington disease.
- Ubiquitin-conjugating enzyme E2-25K increases aggregate formation and cell death in polyglutamine diseases.
- Huntingtin as an Essential Integrator of Intracellular Vesicular Trafficking
Cited by
- How Do Post-Translational Modifications Influence the Pathomechanistic Landscape of Huntington’s Disease? A Comprehensive Review
- Strategies to Investigate Ubiquitination in Huntington's Disease
- Ubiquilin-2 differentially regulates polyglutamine disease proteins.
- Site-specific ubiquitination of pathogenic huntingtin attenuates its deleterious effects
- Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties
- A possible non-proteolytic role of ubiquitin conjugation in alleviating the pathology of Huntingtin’s aggregation
- Ubiquitin signaling in neurodegenerative diseases: an autophagy and proteasome perspective
- Mutant Huntingtin stalls ribosomes and represses protein synthesis in a cellular model of Huntington disease
- Neuroproteomics of the Synapse: Subcellular Quantification of Protein Networks and Signaling Dynamics
- Identification of Full-Length Wild-Type and Mutant Huntingtin Interacting Proteins by Crosslinking Immunoprecipitation in Mice Brain Cortex
- Juvenile Huntington’s Disease and Other PolyQ Diseases, Update on Neurodevelopmental Character and Comparative Bioinformatic Review of Transcriptomic and Proteomic Data
- CPLM 4.0: an updated database with rich annotations for protein lysine modifications
- Dietary Plant Polyphenols as the Potential Drugs in Neurodegenerative Diseases: Current Evidence, Advances, and Opportunities
- Ribotoxic collisions on CAG expansions disrupt proteostasis and stress responses in Huntington’s Disease
- Shift of the insoluble content of the proteome in aging mouse brain
- Ubiquitin-modifying enzymes in Huntington’s disease
- Autophagy preferentially degrades non-fibrillar polyQ aggregates
- Abnormal protein post-translational modifications induces aggregation and abnormal deposition of protein, mediating neurodegenerative diseases
- Ubiquitinome Analysis Uncovers Alterations in Synaptic Proteins and Glucose Metabolism Enzymes in the Hippocampi of Adolescent Mice Following Cold Exposure
- Polyglutamine-mediated ribotoxicity disrupts proteostasis and stress responses in Huntington’s disease
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