Mechanistic view of NMNAT chaperoning different pathological proteins against amyloid aggregation
Ontology highlight
ABSTRACT:
ORGANISM(S): Homo Sapiens
SUBMITTER: 
Dan Li
PROVIDER: PXD031653 | iProX | Fri Feb 11 00:00:00 GMT 2022
REPOSITORIES: iProX
Publications
The mouse nicotinamide mononucleotide adenylyltransferase chaperones diverse pathological amyloid client proteins.
Huang Chengan C Lu Jinxia J Ma Xiaojuan X Qiang Jiali J Wang Chuchu C Liu Cong C Fang Yanshan Y Zhang Yaoyang Y Jiang Lin L Li Dan D Zhang Shengnan S
The Journal of biological chemistry 20220407 5
Molecular chaperones safeguard cellular protein homeostasis and obviate proteotoxicity. In the process of aging, as chaperone networks decline, aberrant protein amyloid aggregation accumulates in a mechanism that underpins neurodegeneration, leading to pathologies such as Alzheimer's disease and Parkinson's disease. Thus, it is important to identify and characterize chaperones for preventing such protein aggregation. In this work, we identified that the NAD<sup>+</sup> synthase-nicotinamide mono ...[more]
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todescribe the production, misfolding, aggregation, transport and
degradation of α-syn that may lead to Parkinson's Disease
(PD). Deregulated α-syn degradation is predicted to be
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What can trigger the onset
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Abstract:
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This model is hosted on
BioModels Database
and identified by:
BIOMD0000000615.
To cite BioModels Database, please use:
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To the extent possible under law, all copyright and related or
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