FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2945531011> ?p ?o ?g. }

• W2945531011 endingPage "521" @default.
• W2945531011 startingPage "507" @default.
• W2945531011 abstract "Abstract Parkinson’s disease is the second most common neurodegenerative disorder worldwide. Neurodegeneration in this pathology is characterized by the loss of dopaminergic neurons in the substantia nigra, coupled with cytoplasmic inclusions known as Lewy bodies containing α‐synuclein. The brain is an organ that concentrates metal ions, and there is emerging evidence that a break‐down in metal homeostasis may be a critical factor in a variety of neurodegenerative diseases. α‐synuclein has emerged as an important metal‐binding protein in the brain, whereas these interactions play an important role in its aggregation and might represent a link between protein aggregation, oxidative damage, and neuronal cell loss. Additionally, α‐synuclein undergoes several post‐translational modifications that regulate its structure and physiological function, and may be linked to the aggregation and/or oligomer formation. This review is focused on the interaction of this protein with physiologically relevant metal ions, highlighting the cases where metal‐AS interactions profile as key modulators for its structural, aggregation, and membrane‐binding properties. The impact of α‐synuclein phosphorylation and N‐terminal acetylation in the metal‐binding properties of the protein are also discussed, underscoring a potential interplay between PTMs and metal ion binding in regulating α‐synuclein physiological functions and its role in pathology. image This article is part of the Special Issue “Synuclein”." @default.
• W2945531011 created "2019-05-29" @default.
• W2945531011 creator A5006282765 @default.
• W2945531011 creator A5014020587 @default.
• W2945531011 creator A5022803338 @default.
• W2945531011 creator A5044955482 @default.
• W2945531011 creator A5047542889 @default.
• W2945531011 creator A5068968780 @default.
• W2945531011 creator A5090268707 @default.
• W2945531011 date "2019-07-09" @default.
• W2945531011 modified "2023-10-14" @default.
• W2945531011 title "Effects of alpha‐synuclein post‐translational modifications on metal binding" @default.
• W2945531011 cites W1496790952 @default.
• W2945531011 cites W1527671059 @default.
• W2945531011 cites W1548866259 @default.
• W2945531011 cites W1680110353 @default.
• W2945531011 cites W1844422703 @default.
• W2945531011 cites W1952199403 @default.
• W2945531011 cites W1957955281 @default.
• W2945531011 cites W1966083586 @default.
• W2945531011 cites W1967874097 @default.
• W2945531011 cites W1968428021 @default.
• W2945531011 cites W1969243451 @default.
• W2945531011 cites W1974361709 @default.
• W2945531011 cites W1974906361 @default.
• W2945531011 cites W1975330599 @default.
• W2945531011 cites W1979833383 @default.
• W2945531011 cites W1979944790 @default.
• W2945531011 cites W1980704317 @default.
• W2945531011 cites W1981172305 @default.
• W2945531011 cites W1984688042 @default.
• W2945531011 cites W1984974501 @default.
• W2945531011 cites W1985683279 @default.
• W2945531011 cites W1986921533 @default.
• W2945531011 cites W1989516071 @default.
• W2945531011 cites W1989522802 @default.
• W2945531011 cites W1990004798 @default.
• W2945531011 cites W1990473626 @default.
• W2945531011 cites W1991322550 @default.
• W2945531011 cites W1992922782 @default.
• W2945531011 cites W1994939101 @default.
• W2945531011 cites W1999635723 @default.
• W2945531011 cites W2000299127 @default.
• W2945531011 cites W2002768329 @default.
• W2945531011 cites W2004281689 @default.
• W2945531011 cites W2008612498 @default.
• W2945531011 cites W2009573330 @default.
• W2945531011 cites W2011077381 @default.
• W2945531011 cites W2016974971 @default.
• W2945531011 cites W2018686658 @default.
• W2945531011 cites W2022285303 @default.
• W2945531011 cites W2022790339 @default.
• W2945531011 cites W2026606393 @default.
• W2945531011 cites W2026717532 @default.
• W2945531011 cites W2028680240 @default.
• W2945531011 cites W2029119021 @default.
• W2945531011 cites W2031859221 @default.
• W2945531011 cites W2032980138 @default.
• W2945531011 cites W2033938955 @default.
• W2945531011 cites W2037441494 @default.
• W2945531011 cites W2038286309 @default.
• W2945531011 cites W2039321158 @default.
• W2945531011 cites W2040178046 @default.
• W2945531011 cites W2041134571 @default.
• W2945531011 cites W2045062740 @default.
• W2945531011 cites W2045489211 @default.
• W2945531011 cites W2047206971 @default.
• W2945531011 cites W2048256242 @default.
• W2945531011 cites W2048692457 @default.
• W2945531011 cites W2049048519 @default.
• W2945531011 cites W2049366603 @default.
• W2945531011 cites W2051283118 @default.
• W2945531011 cites W2051609969 @default.
• W2945531011 cites W2054490148 @default.
• W2945531011 cites W2054698767 @default.
• W2945531011 cites W2056626063 @default.
• W2945531011 cites W2057121960 @default.
• W2945531011 cites W2057550343 @default.
• W2945531011 cites W2058827782 @default.
• W2945531011 cites W2058943073 @default.
• W2945531011 cites W2059382925 @default.
• W2945531011 cites W2060495308 @default.
• W2945531011 cites W2066170812 @default.
• W2945531011 cites W2066304458 @default.
• W2945531011 cites W2068118457 @default.
• W2945531011 cites W2070760404 @default.
• W2945531011 cites W2071049093 @default.
• W2945531011 cites W2076592306 @default.
• W2945531011 cites W2076815669 @default.
• W2945531011 cites W2077043544 @default.
• W2945531011 cites W2077044335 @default.
• W2945531011 cites W2077273627 @default.
• W2945531011 cites W2079481706 @default.
• W2945531011 cites W2084146695 @default.
• W2945531011 cites W2084929273 @default.
• W2945531011 cites W2085108920 @default.
• W2945531011 cites W2087575094 @default.
• W2945531011 cites W2089435862 @default.

• next