Cited by 33Aluminum toxicity and tolerance in plants and animalsProtein Interaction Studies and Fluorescence AnalysisProtein Structure and Dynamics
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Aluminum's preferential binding site in proteins: sidechain of amino acids versus backbone interactions
Open accessMujika, Jon I., Dalla Torre, Gabriele, Formoso, Elena, Grande-Aztatzi, Rafael, Grabowski, Slawomir J., Exley, Christopher, Lopez, Xabier·2018·Journal of Inorganic Biochemistry
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Protein polypeptides are transformed to secondary structures when aluminium ions interact with them through oxygen-containing amino acids, side chains and protein backbone, leading to ultimate denaturation or conformational or structural alteration as in β-amyloid.
“Protein polypeptides are transformed to secondary structures when Al ions interact with them through oxygen-containing amino acids, side chains and protein backbone leading to ultimate denaturation (Mujika et al., 2018) or conformational or structural alteration (Exley et al., 1993; Zatta et al., 2005; Exley, 2006) as in β-amyloid.”
From Aluminium toxicosis: a review of toxic actions and effects (2019) · cites this paper as Mujika et al., 2018
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Research works printed but not linked: 30
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Cited by
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Aluminium toxicosis: a review of toxic actions and effects
Igbokwe, I. O., Igwenagu, E., & Igbokwe, N. A. (2019) · Interdisciplinary Toxicology · doi:10.2478/intox-2019-0007 · Cited by 395
“Protein polypeptides are transformed to secondary structures when Al ions interact with them through oxygen-containing amino acids, side chains and protein backbone leading to ultimate denaturation (Mujika et al., 2018) or conformational or structural alteration (Exley et al.”
Background
Metadata
- Authors
- Mujika, J. I., Dalla Torre, G., Formoso, E., Grande-Aztatzi, R., Grabowski, S. J., Exley, C., & Lopez, X.
- Affiliations
- University of the Basque Country (ES)
- Ikerbasque (ES)
- Keele University (GB)
- Venue
- Journal of Inorganic Biochemistry
- Publisher
- Elsevier BV
- Published
- 2018-04
- Volume
- 181
- Pages
- 111-116
- ISSN
- 0162-0134 (ISSN-L)
- OpenAlex
- W2767261787
- Cited by
- 33
- References
- 0
- Citations by year
- 2025: 1 · 2024: 4 · 2023: 6 · 2022: 6 · 2021: 5 · 2020: 3 · 2019: 5 · 2018: 3
- FWCI
- 2.96
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Inorganic Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Keele Research Repository (Keele University) (submittedVersion, cc-by)
- Communities in ADDI (University of the Basque Country) (submittedVersion, cc-by-nc-nd)
- Hispana (submittedVersion, cc-by-nc-nd)
- Funders
- UPV/EHU (PES14/35)
- Eusko Jaurlaritza (IT588-13)
- Ministerio de Ciencia e Innovación (CTQ2015-67608-P)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Aluminum toxicity and tolerance in plants and animals
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- aluminum ions, protein denaturation, binding thermodynamics, aspartic acid, carbonyl compounds, secondary structure changes
- MeSH terms
- Aluminum, Aluminum Hydroxide, Binding Sites, Chelating Agents, Computer Simulation, Energy Transfer, Environmental Pollutants, Humans, Kinetics, Ligands, Models, Molecular, Oligopeptides, Peptide Fragments, Phosphorylation, Phosphoserine, Protein Conformation, Quantum Theory, Thermodynamics, Amyloid beta-Peptides, Computational Biology, Amino Acid Motifs, Static Electricity, Coordination Complexes
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