PTMD 2.0: an updated database of disease-associated post-translational modifications DOI Creative Commons
Xinhe Huang, Zihao Feng, Dan Liu

et al.

Nucleic Acids Research, Journal Year: 2024, Volume and Issue: 53(D1), P. D554 - D563

Published: Sept. 26, 2024

Various post-translational modifications (PTMs) participate in nearly all aspects of biological processes by regulating protein functions, and aberrant states PTMs are frequently associated with human diseases. Here, we present a comprehensive database diseases (PTMD 2.0), including 342 624 PTM-disease associations (PDAs) 15 105 proteins for 93 types 2083 Based on the distinct PTM diseases, classified PDAs into six categories: upregulation (U) or downregulation (D) levels, absence (A) presence (P) PTMs, creation (C) disruption (N) sites. We provided detailed annotations each PDA carefully annotated disease-associated integrating knowledge from 101 additional resources that covered 13 aspects, information, variation mutation, protein-protein interaction, functional annotation, DNA RNA element, structure, chemical-target relationship, mRNA expression, expression/proteomics, subcellular localization, pathway domain annotation physicochemical property. With data volume ∼8 GB, anticipate PTMD 2.0 will serve as fundamental resource further analysing relationships between The online service is freely available at https://ptmd.biocuckoo.cn/.

Language: Английский

Protein modification in neurodegenerative diseases DOI Creative Commons

Shahin Ramazi,

Maedeh Dadzadi,

Mona Darvazi

et al.

MedComm, Journal Year: 2024, Volume and Issue: 5(8)

Published: Aug. 1, 2024

Abstract Posttranslational modifications play a crucial role in governing cellular functions and protein behavior. Researchers have implicated dysregulated posttranslational misfolding, which results cytotoxicity, particularly neurodegenerative diseases such as Alzheimer disease, Parkinson Huntington disease. These aberrant cause proteins to gather certain parts of the brain that are linked development diseases. This leads neuronal dysfunction start disease symptoms. Cognitive decline neurological impairments commonly manifest patients, underscoring urgency comprehending modifications’ impact on function for targeted therapeutic interventions. review elucidates critical link between specific modifications, focusing Tau, APP, α‐synuclein, Huntingtin protein, Parkin, DJ‐1, Drp1. By delineating prominent within underscores significance understanding interplay among these modifications. Emphasizing 10 key abnormal this study aims provide comprehensive framework investigating holistically. The insights presented herein shed light potential avenues aimed at modulating mitigate aggregation retard progression.

Language: Английский

Citations

4
Protein succinylation mechanisms and potential targeted therapies in urinary disease DOI

Y.C. Lou,

Caitao Dong,

Qinhong Jiang

et al.

Cellular Signalling, Journal Year: 2025, Volume and Issue: unknown, P. 111744 - 111744

Published: March 1, 2025

Language: Английский

Citations

0
SIRT5 Alleviates Apoptosis of Vascular Endothelial Cells Under Simulated Microgravity via Desuccinylation of ERO1A DOI Open Access
Yikai Pan, Qian Zhang, Chengfei Li

et al.

International Journal of Molecular Sciences, Journal Year: 2025, Volume and Issue: 26(7), P. 2908 - 2908

Published: March 23, 2025

The adverse effects of weightlessness on the human cardiovascular system greatly hinder process long-term and long-distance space exploration. Succinylation is an important type protein post-translational modification. However, whether succinylation modification able to play a role in altered vascular endothelial cell function under microgravity or simulated has not been reported. This study aims investigate quantitative global proteome changes lysine related proteins, seeking facilitate better understanding deconditioning microgravity. LC-MS/MS combined with bioinformatics analysis were used quantitatively detect perspectives at level. Immunoprecipitation Western blot conducted further verify alterations proteins succinylation. A total 132 differentially expressed 164 sites identified umbilical vein cells (HUVECs). Bioinformatics indicates that may potential energy metabolism. In addition, desuccinylase SIRT5 was downregulated regulated levels HUVECs Notably, overexpression effectively protected from apoptosis induced by And Lys396 ERO1A significantly increased Mechanistically, knockdown found induce through ERO1A. These results can provide new ideas for elucidating molecular mechanism dysfunction environments, key targets scientific protective measures against space.

Language: Английский

Citations

0
Identification of Mitochondrial and Succinylation Modification-Related Gene Signature in Ischemic Stroke DOI Creative Commons
Lixia Wang,

Jishuai Zhao,

Hui Cai

et al.

Molecular Neurobiology, Journal Year: 2025, Volume and Issue: unknown

Published: April 22, 2025

Language: Английский

Citations

0
PTMD 2.0: an updated database of disease-associated post-translational modifications DOI Creative Commons
Xinhe Huang, Zihao Feng, Dan Liu

et al.

Nucleic Acids Research, Journal Year: 2024, Volume and Issue: 53(D1), P. D554 - D563

Published: Sept. 26, 2024

Various post-translational modifications (PTMs) participate in nearly all aspects of biological processes by regulating protein functions, and aberrant states PTMs are frequently associated with human diseases. Here, we present a comprehensive database diseases (PTMD 2.0), including 342 624 PTM-disease associations (PDAs) 15 105 proteins for 93 types 2083 Based on the distinct PTM diseases, classified PDAs into six categories: upregulation (U) or downregulation (D) levels, absence (A) presence (P) PTMs, creation (C) disruption (N) sites. We provided detailed annotations each PDA carefully annotated disease-associated integrating knowledge from 101 additional resources that covered 13 aspects, information, variation mutation, protein-protein interaction, functional annotation, DNA RNA element, structure, chemical-target relationship, mRNA expression, expression/proteomics, subcellular localization, pathway domain annotation physicochemical property. With data volume ∼8 GB, anticipate PTMD 2.0 will serve as fundamental resource further analysing relationships between The online service is freely available at https://ptmd.biocuckoo.cn/.

Language: Английский

Citations

1