PuSH - Publikationsserver des Helmholtz Zentrums München

Chapter 5 – “Parkinson's disease – A role of non-enzymatic posttranslational modifications in disease onset and progression?”.

Mol. Aspects Med. 86:101096 (2022)
Postprint DOI PMC
Open Access Green
Parkinson's disease (PD) is a still incurable neurodegenerative disorder with a highly complex etiology. While about 10% of cases are associated with single-gene mutations, the majority of PD is thought to originate from a combination of factors such as environmental impact, lifestyle and aging. Even though investigations into the genetically caused cases have uncovered major pathomechanisms of the disease there still exists a wide gap concerning the molecular impact of the other risk factors. All of them are known to have a major impact on the oxidative burden of the cell and thus strongly influence the non-enzymatic posttranslational modifications (nePTMs) of proteins. These modifications are by now known to dramatically alter the stability of proteins, their interactomes, and also their functions. However, the knowledge of nePTMs and their possible causative role in the pathoetiology of PD is just starting to emerge again guided by research on PD-associated genes. In this short review, we will thus concentrate on known nePTMs of two PD-associated genes, SCNA and DJ-1, and discuss their role in the pathoetiology of PD. In the future, it will, however, be essential to unravel the complete “environmental proteome” to understand the impact of nePTMs on PD etiology. This might open up new pathways urgently needed to develop new diagnostic and therapeutic tools for this still incurable disease.
Altmetric
Weitere Metriken?
Zusatzinfos bearbeiten [➜Einloggen]
Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Korrespondenzautor
Schlagwörter Dj-1 ; Neurodegenerative Diseases ; Non-enzymatic Ptm ; Parkinson's Disease ; Post-translational Modifications ; Ptms ; α-synuclein; Cysteine-sulfinic Acid; Parkinsons-disease; Alpha-synuclein; Mitochondrial Dysfunction; Oxidative Stress; S-nitrosylation; Protein Dj-1; Nitric-oxide; Glycation; Methylglyoxal
ISSN (print) / ISBN 0098-2997
e-ISSN 0098-2997
Quellenangaben Band: 86, Heft: , Seiten: , Artikelnummer: 101096 Supplement: ,
Verlag Elsevier
Verlagsort Radarweg 29, 1043 Nx Amsterdam, Netherlands
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Förderungen Helmholtz Association
Courant Forschungszentrum Geobiologie, Georg-August-Universität Göttingen
Deutsche Forschungsgemeinschaft
German Science Foundation Collaborative Research Centre