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Copper ion incorporation in α‐synuclein amyloids.
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- Protein Science: A Publication of the Protein Society, 2024, v. 33, n. 4, p. 1, doi. 10.1002/pro.4956
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- Article
Chemical catalysis by biological amyloids.
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- Biochemical Society Transactions, 2023, v. 51, n. 5, p. 1967, doi. 10.1042/BST20230617
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- Article
Amyloids of α-Synuclein Promote Chemical Transformations of Neuronal Cell Metabolites.
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- International Journal of Molecular Sciences, 2023, v. 24, n. 16, p. 12849, doi. 10.3390/ijms241612849
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Comparing lipid remodeling of brown adipose tissue, white adipose tissue, and liver after one‐week high fat diet intervention with quantitative Raman microscopy.
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- Journal of Cellular Biochemistry, 2023, v. 124, n. 3, p. 382, doi. 10.1002/jcb.30372
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Crossroads between copper ions and amyloid formation in Parkinson's disease.
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- Essays in Biochemistry, 2022, v. 66, n. 7, p. 977, doi. 10.1042/EBC20220043
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Evaluation of ATOX1 as a Potential Predictive Biomarker for Tetrathiomolybdate Treatment of Breast Cancer Patients with High Risk of Recurrence.
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- Biomedicines, 2021, v. 9, n. 12, p. 1887, doi. 10.3390/biomedicines9121887
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- Article
Effects of the Toxic Metals Arsenite and Cadmium on α-Synuclein Aggregation In Vitro and in Cells.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 21, p. 11455, doi. 10.3390/ijms222111455
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Impact of crowded environments on binding between protein and single-stranded DNA.
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- Scientific Reports, 2021, v. 11, n. 1, p. 1, doi. 10.1038/s41598-021-97219-1
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- Article
Elever forskar på pollen.
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- Biologen, 2021, n. 3, p. 10
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- Article
ATP7A-Regulated Enzyme Metalation and Trafficking in the Menkes Disease Puzzle.
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- Biomedicines, 2021, v. 9, n. 4, p. 391, doi. 10.3390/biomedicines9040391
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- Article
A large 'discovery' experiment: Gender Initiative for Excellence (Genie) at Chalmers University of Technology.
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- QRB Discovery, 2021, v. 2, p. 1, doi. 10.1017/qrd.2021.3
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Response to crowded conditions reveals compact nucleus for amyloid formation of folded protein.
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- QRB Discovery, 2021, v. 2, p. 1, doi. 10.1017/qrd.2020.17
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Female Faculty: Why So Few and Why Care?
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- Chemistry - A European Journal, 2020, v. 26, n. 38, p. 8319, doi. 10.1002/chem.202002522
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- Article
Differential effects of Cu2+ and Fe3+ ions on in vitro amyloid formation of biologically-relevant α-synuclein variants.
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- BioMetals, 2020, v. 33, n. 2/3, p. 97, doi. 10.1007/s10534-020-00234-4
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- Article
The Caenorhabditis elegans homolog of human copper chaperone Atox1, CUC-1, aids in distal tip cell migration.
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- BioMetals, 2020, v. 33, n. 2/3, p. 147, doi. 10.1007/s10534-020-00239-z
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- Article
Redox-Dependent Copper Ion Modulation of Amyloid-β (1-42) Aggregation In Vitro.
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- Biomolecules (2218-273X), 2020, v. 10, n. 6, p. 924, doi. 10.3390/biom10060924
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Evaluation of copper chaperone ATOX1 as prognostic biomarker in breast cancer.
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- Breast Cancer (13406868), 2020, v. 27, n. 3, p. 505, doi. 10.1007/s12282-019-01044-4
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- Article
My journey in academia: things not on the CV.
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- Pure & Applied Chemistry, 2020, v. 92, n. 5, p. 789, doi. 10.1515/pac-2019-0805
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- Article
Mirror‐Image 5S Ribonucleoprotein Complexes.
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- Angewandte Chemie, 2020, v. 132, n. 9, p. 3753, doi. 10.1002/ange.201914799
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- Article
Mirror‐Image 5S Ribonucleoprotein Complexes.
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- Angewandte Chemie International Edition, 2020, v. 59, n. 9, p. 3724, doi. 10.1002/anie.201914799
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- Article
Wilson disease missense mutations in ATP7B affect metal-binding domain structural dynamics.
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- BioMetals, 2019, v. 32, n. 6, p. 875, doi. 10.1007/s10534-019-00219-y
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Copper relay path through the N-terminus of Wilson disease protein, ATP7B.
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- Metallomics, 2019, v. 11, n. 9, p. 1472, doi. 10.1039/c9mt00147f
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- Article
Synaptic vesicle mimics affect the aggregation of wild-type and A53T α-synuclein variants differently albeit similar membrane affinity.
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- PEDS: Protein Engineering, Design & Selection, 2019, v. 32, n. 2, p. 59, doi. 10.1093/protein/gzz021
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Alpha‐Synuclein Modulates the Physical Properties of DNA.
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- Chemistry - A European Journal, 2018, v. 24, n. 58, p. 15685, doi. 10.1002/chem.201803933
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- Article
Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p.
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- International Journal of Molecular Sciences, 2018, v. 19, n. 1, p. 269, doi. 10.3390/ijms19010269
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- Article
Folding of copper proteins: role of the metal?
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- Quarterly Reviews of Biophysics, 2018, v. 51, p. 1, doi. 10.1017/s0033583518000021
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- Article
Copper chaperone blocks amyloid formation via ternary complex.
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- Quarterly Reviews of Biophysics, 2018, v. 51, p. 1, doi. 10.1017/S0033583518000045
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The six metal binding domains in human copper transporter, ATP7B: molecular biophysics and disease-causing mutations.
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- BioMetals, 2017, v. 30, n. 6, p. 823, doi. 10.1007/s10534-017-0058-2
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- Article
Second harmonic generation for collagen I characterization in rectal cancer patients with and without preoperative radiotherapy.
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- Journal of Biomedical Optics, 2017, v. 22, n. 10, p. 106006-1, doi. 10.1117/1.JBO.22.10.106006
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Effects of small-molecule amyloid modulators on a Drosophila model of Parkinson’s disease.
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- PLoS ONE, 2017, v. 12, n. 9, p. 1, doi. 10.1371/journal.pone.0184117
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Probing functional roles of Wilson disease protein (ATP7B) copper-binding domains in yeast.
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- Metallomics, 2017, v. 9, n. 7, p. 981, doi. 10.1039/c7mt00101k
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- Article
Roles of Copper-Binding Proteins in Breast Cancer.
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- International Journal of Molecular Sciences, 2017, v. 18, n. 4, p. 871, doi. 10.3390/ijms18040871
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- Article
Disease-causing point-mutations in metal-binding domains of Wilson disease protein decrease stability and increase structural dynamics.
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- BioMetals, 2017, v. 30, n. 1, p. 27, doi. 10.1007/s10534-016-9976-7
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A stretched conformation of DNA with a biological role?
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- Quarterly Reviews of Biophysics, 2017, v. 50, p. 1, doi. 10.1017/S0033583517000099
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- Article
Unraveling amyloid formation paths of Parkinson's disease protein α-synuclein triggered by anionic vesicles.
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- Quarterly Reviews of Biophysics, 2017, v. 50, p. 1, doi. 10.1017/S0033583517000026
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- Article
A Copper Story: From Protein Folding and Metal Transport to Cancer.
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- Israel Journal of Chemistry, 2016, v. 56, n. 9/10, p. 671, doi. 10.1002/ijch.201600019
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Extended functional repertoire for human copper chaperones.
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- Biomolecular Concepts, 2016, v. 7, n. 1, p. 29, doi. 10.1515/bmc-2015-0030
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Unresolved questions in human copper pump mechanisms.
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- Quarterly Reviews of Biophysics, 2015, v. 48, n. 4, p. 471, doi. 10.1017/S0033583515000128
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Corrigendum: Direct Correlation Between Ligand-Induced α-Synuclein Oligomers and Amyloid-like Fibril Growth.
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- Scientific Reports, 2015, p. 15692, doi. 10.1038/srep15692
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Bacterial Chaperones CsgE and CsgC Differentially Modulate Human α-Synuclein Amyloid Formation via Transient Contacts.
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- PLoS ONE, 2015, v. 10, n. 10, p. 1, doi. 10.1371/journal.pone.0140194
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Identification of New Potential Interaction Partners for Human Cytoplasmic Copper Chaperone Atox1: Roles in Gene Regulation?
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- International Journal of Molecular Sciences, 2015, v. 16, n. 8, p. 16728, doi. 10.3390/ijms160816728
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- Article
Insulin-degrading enzyme prevents α-synuclein fibril formation in a nonproteolytical manner.
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- Scientific Reports, 2015, p. 12531, doi. 10.1038/srep12531
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- Article
Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro.
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- BioMetals, 2015, v. 28, n. 3, p. 577, doi. 10.1007/s10534-015-9832-1
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- Article
Direct Correlation Between Ligand-Induced α-Synuclein Oligomers and Amyloid-like Fibril Growth.
- Published in:
- Scientific Reports, 2015, p. 10422, doi. 10.1038/srep10422
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- Article
Enthalpy-entropy compensation at play in human copper ion transfer.
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- Scientific Reports, 2015, p. 10518, doi. 10.1038/srep10518
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T versus D in the MTCXXC motif of copper transport proteins plays a role in directional metal transport.
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- Journal of Biological Inorganic Chemistry (JBIC), 2014, v. 19, n. 6, p. 1037, doi. 10.1007/s00775-014-1147-0
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Synthetic crowding agent dextran causes excluded volume interactions exclusively to tracer protein apoazurin.
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- FEBS Letters, 2014, v. 588, n. 5, p. 811, doi. 10.1016/j.febslet.2014.01.043
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Determinants for Simultaneous Binding of Copper and Platinum to Human Chaperone Atox1: <i>Hitchhiking not Hijacking</i>.
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- PLoS ONE, 2013, v. 8, n. 7, p. 1, doi. 10.1371/journal.pone.0070473
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Similar but Different: Thermodynamic and Structural Characterization of a Pair of Enantiomers Binding to Acetylcholinesterase.
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- Angewandte Chemie, 2012, v. 124, n. 51, p. 12888, doi. 10.1002/ange.201205113
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- Article
Similar but Different: Thermodynamic and Structural Characterization of a Pair of Enantiomers Binding to Acetylcholinesterase.
- Published in:
- Angewandte Chemie International Edition, 2012, v. 51, n. 51, p. 12716, doi. 10.1002/anie.201205113
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- Article