Cargando…

Evaluation of ATOX1 as a Potential Predictive Biomarker for Tetrathiomolybdate Treatment of Breast Cancer Patients with High Risk of Recurrence

Copper plays a key role in cancer metastasis, which is the most common cause of cancer death. Copper depletion treatment with tetrathiomolybdate (TM) improved disease-free survival in breast cancer patients with high risk of recurrence in a phase II clinical trial. Because the copper metallochaperon...

Descripción completa

Detalles Bibliográficos
Autores principales:	Blockhuys, Stéphanie, Hildesjö, Camilla, Olsson, Hans, Vahdat, Linda, Wittung-Stafshede, Pernilla
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2021
Materias:	Communication
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8698757/ https://www.ncbi.nlm.nih.gov/pubmed/34944703 http://dx.doi.org/10.3390/biomedicines9121887

Ejemplares similares

Evaluation of copper chaperone ATOX1 as prognostic biomarker in breast cancer
por: Blockhuys, Stéphanie, et al.
Publicado: (2020)

Single-cell tracking demonstrates copper chaperone Atox1 to be required for breast cancer cell migration
por: Blockhuys, Stéphanie, et al.
Publicado: (2020)

Copper Chaperone Atox1 Interacts with Cell Cycle Proteins
por: Matson Dzebo, Maria, et al.
Publicado: (2018)

The Caenorhabditis elegans homolog of human copper chaperone Atox1, CUC-1, aids in distal tip cell migration
por: Zhang, Xiaolu, et al.
Publicado: (2020)

Identification of New Potential Interaction Partners for Human Cytoplasmic Copper Chaperone Atox1: Roles in Gene Regulation?
por: Öhrvik, Helena, et al.
Publicado: (2015)

Roles of Copper-Binding Proteins in Breast Cancer
por: Blockhuys, Stéphanie, et al.
Publicado: (2017)

Memo1 binds reduced copper ions, interacts with copper chaperone Atox1, and protects against copper-mediated redox activity in vitro
por: Zhang, Xiaolu, et al.
Publicado: (2022)

The C-Terminus of Human Copper Importer Ctr1 Acts as a Binding Site and Transfers Copper to Atox1
por: Kahra, Dana, et al.
Publicado: (2016)

Determinants for Simultaneous Binding of Copper and Platinum to Human Chaperone Atox1: Hitchhiking not Hijacking
por: Palm-Espling, Maria E., et al.
Publicado: (2013)

Crossroads between copper ions and amyloid formation in Parkinson’s disease
por: Wittung-Stafshede, Pernilla
Publicado: (2022)

Chemical catalysis by biological amyloids
por: Wittung-Stafshede, Pernilla
Publicado: (2023)

Amyloids of α-Synuclein Promote Chemical Transformations of Neuronal Cell Metabolites
por: Horvath, Istvan, et al.
Publicado: (2023)

ATP7A-Regulated Enzyme Metalation and Trafficking in the Menkes Disease Puzzle
por: Horn, Nina, et al.
Publicado: (2021)

Amyloid Fibers of α-Synuclein Catalyze Chemical Reactions
por: Horvath, Istvan, et al.
Publicado: (2023)

Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches
por: Samiotakis, Antonios, et al.
Publicado: (2009)

The six metal binding domains in human copper transporter, ATP7B: molecular biophysics and disease-causing mutations
por: Ariöz, Candan, et al.
Publicado: (2017)

Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p
por: Sedlák, Erik, et al.
Publicado: (2018)

Crosstalk Between Alpha-Synuclein and Other Human and Non-Human Amyloidogenic Proteins: Consequences for Amyloid Formation in Parkinson’s Disease
por: Werner, Tony, et al.
Publicado: (2020)

Macromolecular crowding modulates α-synuclein amyloid fiber growth
por: Horvath, Istvan, et al.
Publicado: (2021)

A large ‘discovery’ experiment: Gender Initiative for Excellence (Genie) at Chalmers University of Technology
por: Saline, Maria, et al.
Publicado: (2021)

In Vitro Thermodynamic Dissection of Human Copper Transfer from Chaperone to Target Protein
por: Niemiec, Moritz S., et al.
Publicado: (2012)

Tetrathiomolybdate (TM)-associated copper depletion influences collagen remodeling and immune response in the pre-metastatic niche of breast cancer
por: Liu, Ying L., et al.
Publicado: (2021)

Med8, Med18, and Med20 subunits of the Mediator head domain are interdependent upon each other for folding and complex formation
por: Adler, David, et al.
Publicado: (2009)

Enthalpy-entropy compensation at play in human copper ion transfer
por: Niemiec, Moritz S., et al.
Publicado: (2015)

Differential effects of Cu(2+) and Fe(3+) ions on in vitro amyloid formation of biologically-relevant α-synuclein variants
por: Lorentzon, Emma, et al.
Publicado: (2020)

Synaptic vesicle mimics affect the aggregation of wild-type and A53T α-synuclein variants differently albeit similar membrane affinity
por: Rocha, Sandra, et al.
Publicado: (2019)

Impact of crowded environments on binding between protein and single-stranded DNA
por: Köhn, Birgit, et al.
Publicado: (2021)

Orientation of α-Synuclein at Negatively Charged Lipid Vesicles: Linear Dichroism Reveals Time-Dependent Changes in Helix Binding Mode
por: Rocha, Sandra, et al.
Publicado: (2021)

Response to crowded conditions reveals compact nucleus for amyloid formation of folded protein
por: Werner, Tony E.R., et al.
Publicado: (2021)

The Isolation of Atoxic Strains of Bacillus Tetani in Egypt
por: Forsyth, W. Leonard, et al.
Publicado: (1930)

Abundant fish protein inhibits α-synuclein amyloid formation
por: Werner, Tony, et al.
Publicado: (2018)

Ammonium tetrathiomolybdate treatment of copper‐associated hepatopathy in dogs
por: Langlois, Daniel K., et al.
Publicado: (2019)

Probing the interface in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identified
por: Guidry, Jesse J, et al.
Publicado: (2003)

A Luminal Loop of Wilson Disease Protein Binds Copper and Is Required for Protein Activity
por: Köhn, Birgit, et al.
Publicado: (2018)

Redox-Dependent Copper Ion Modulation of Amyloid-β (1-42) Aggregation In Vitro
por: Sasanian, Nima, et al.
Publicado: (2020)

Disease-causing point-mutations in metal-binding domains of Wilson disease protein decrease stability and increase structural dynamics
por: Kumar, Ranjeet, et al.
Publicado: (2016)

Frustration Dynamics and Electron-Transfer Reorganization Energies in Wild-Type and Mutant Azurins
por: Chen, Xun, et al.
Publicado: (2022)

Genomic organization of ATOX1, a human copper chaperone
por: Liu, Po-Ching, et al.
Publicado: (2003)

Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers
por: Werner, Tony E. R., et al.
Publicado: (2020)

Bis-choline tetrathiomolybdate prevents copper-induced blood–brain barrier damage
por: Borchard, Sabine, et al.
Publicado: (2021)

Cannot write session to /tmp/vufind_sessions/sess_7gd435ou1pg3oocrj4p34l9ij5