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Vibhuti Joshi

Researcher at Indian Institute of Technology, Jodhpur

Publications -  17
Citations -  336

Vibhuti Joshi is an academic researcher from Indian Institute of Technology, Jodhpur. The author has contributed to research in topics: Ubiquitin ligase & Ubiquitin. The author has an hindex of 10, co-authored 16 publications receiving 242 citations.

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E3 Ubiquitin Ligases Neurobiological Mechanisms: Development to Degeneration

TL;DR: To understand how few E3 ubiquitin ligases sense major molecular events, which are crucial for human brain development from its early embryonic stages to throughout adolescence period, is explained.
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A Decade of Boon or Burden: What Has the CHIP Ever Done for Cellular Protein Quality Control Mechanism Implicated in Neurodegeneration and Aging?

TL;DR: A wide range of functionality of CHIP inside cells is explored by a detailed presentation of its co-chaperone, E3 and E4 enzyme like functions, with central focus on its protein quality control roles in neurodegenerative diseases.
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Gp78 E3 Ubiquitin Ligase: Essential Functions and Contributions in Proteostasis.

TL;DR: The current findings of Gp78 are comprehensively represented, which shows its PQC roles in different physiological functions and diseases; and novel opportunities to better understand the unsolved questions for therapeutic interventions linked with different protein misfolding disorders are proposed.
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Polyphenolic flavonoid (Myricetin) upregulated proteasomal degradation mechanisms: Eliminates neurodegenerative proteins aggregation.

TL;DR: It is shown that Myricetin, a flavonoid, can eliminate various abnormal proteins from the cellular environment via modulating endogenous levels of Hsp70 chaperone and quality control (QC)‐E3 ubiquitin ligase E6‐AP and reduce the misfolded proteins inclusions, which further alleviates cytotoxicity.
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Ubiquitin ligase ITCH recruitment suppresses the aggregation and cellular toxicity of cytoplasmic misfolded proteins

TL;DR: It is demonstrated that the Nedd4-like E3 ubiquitin ligase ITCH specifically interacts with mutant bona fide misfolded proteins and colocalizes with their perinuclear aggregates and overexpression of ITCH alleviates the cytotoxic potential of expanded polyglutamine proteins and reduces aggregation.