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by IQAC KIITKIIT Deemed to be University — Internal Quality Assurance Cell

Publication2022

S‑Nitrosylation of OTUB1 Alters Its Stability and Ubc13 Binding

The record

Type
Publication
Date
18 May 2022
Level
National
Journal
ACS Chemical Neuroscience
Volume
13
Issue
10
Pages
1517-1525
Published
18 May 2022
DOI
10.1021/acschemneuro.1c00855
Scopus ID
85130020690
ISSN
19487193
Authors
5
Open access
No
Citations
13
International co-authorship
No
Co-author countries
IN

Classification

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UN Sustainable Development Goals

  1. 3 Ensure healthy lives and promote well-being for all at all ages

    GoalPrimaryHigh confidenceJudged

    Investigates post-translational modification of OTUB1 protein under oxidative stress, demonstrating impact on protein aggregation directly relevant to Parkinson's disease pathology and neurodegeneration

    High confidence
    The subject matter is a strong and direct inference from the record type, the funding or organising body, or the programme context, even where the title alone is thin. Example: an ICMR-funded project against SDG 3, on the strength of the agency.
    Judged
    Judged against the published classification rubric, under the rubric and prompt versions recorded with the run that produced it.
    Produced by
    claude-haiku-4-5-20251001, under kortex-publication-v1

Viksit Bharat @2047

  1. vb-1.2 Health and well-being

    Sub-themePrimaryHigh confidenceJudged

    Addresses neurodegenerative disease mechanisms and therapeutic understanding for health outcome improvement

    Produced by
    claude-haiku-4-5-20251001, under kortex-publication-v1

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Citing this record

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KIIT Deemed to be University. “S‑Nitrosylation of OTUB1 Alters Its Stability and Ubc13 Binding”. Kortex.

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