The hydrolytic stability of the human tubulin α 1A protein fragment – a potential reason for the role of metal ions in the development of neurodegenerative diseases

Essential (Cu( ii )) and toxic (Ni( ii )) metal ions can bind to proteins and, under certain conditions, induce irreversible changes. We investigated these processes in a human tubulin alpha 1A protein fragment under physiological conditions.

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Publication Details

Journal
Inorganic Chemistry Frontiers
Published
2025-01-01
DOI
https://doi.org/10.1039/d4qi03271c
Citations
1
Primary Topic
Microtubule and mitosis dynamics
Type
article
Field-Weighted Citation Impact
1.15

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article

The hydrolytic stability of the human tubulin α 1A protein fragment – a potential reason for the role of metal ions in the development of neurodegenerative diseases

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Microtubule and mitosis dynamics
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article

The hydrolytic stability of the human tubulin α 1A protein fragment – a potential reason for the role of metal ions in the development of neurodegenerative diseases

Katalin Várnagy, Giuseppe Di Natale, Giuseppina Sabatino, Giuseppe Pappalardo, Ágnes Grenács, Gergő Zoltán Sajtos, Balázs Sándor
article en
1 citations

Abstract

Essential (Cu( ii )) and toxic (Ni( ii )) metal ions can bind to proteins and, under certain conditions, induce irreversible changes. We investigated these processes in a human tubulin alpha 1A protein fragment under physiological conditions.

Inorganic Chemistry FrontiersVol. 12(11)
University of Debrecen (HU), Institute of Crystallography (IT)
Consiglio Nazionale delle Ricerche, Debreceni Egyetem, Nemzeti Kutatási, Fejlesztési és Innovaciós Alap
Openalex Percentile: Top 24%
Microtubule and mitosis dynamics
1.15
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