Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Ariel A. Valiente-Gabioud"'
Autor:
Ariel A. Valiente-Gabioud, Inés Garteizgogeascoa Suñer, Agata Idziak, Arne Fabritius, Jérome Basquin, Julie Angibaud, U. Valentin Nägerl, Sumeet Pal Singh, Oliver Griesbeck
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
Abstract Calcium in interstitial fluids is central to systemic physiology and a crucial ion pool for entry into cells through numerous plasma membrane channels. Its study has been limited by the scarcity of methods that allow monitoring in tight inte
Externí odkaz:
https://doaj.org/article/2e45164c35d54f6283163a236c70892f
Autor:
Ariel A. Valiente-Gabioud, Inés Garteizgogeascoa Suñer, Agata Idziak, Arne Fabritius, Julie Angibaud, Jérome Basquin, U. Valentin Nägerl, Sumeet Pal Singh, Oliver Griesbeck
Calcium in interstitial fluids is central to systemic physiology and a crucial ion pool for entry into cells through numerous plasma membrane channels. Its study has been limited by the lack of methods that allow monitoring in tight inter-cell spaces
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a63f445fa97544aaa4e510216caa31a7
https://doi.org/10.1101/2023.03.23.533956
https://doi.org/10.1101/2023.03.23.533956
Autor:
Manuel Vicente, Jussep Salgado-Almario, Ariel A. Valiente-Gabioud, Michelle M. Collins, Pierre Vincent, Beatriz Domingo, Juan Llopis
Publikováno v:
Journal of molecular and cellular cardiology. 173
The phospholamban mutation Arg 9 to Cys (R9C) has been found to cause a dilated cardiomyopathy in humans and in transgenic mice, with ventricular dilation and premature death. Emerging evidence suggests that phospholamban R9C is a loss-of-function mu
Publikováno v:
The Journal of physiologyReferences.
Calcium in interstitial fluids is a crucial ion pool for entry into cells through a plethora of calcium-permeable channels. It is also sensed actively by dedicated receptors. While the mechanisms of global calcium homeostasis and regulation in body f
Autor:
Timo Strohäker, Ariel A. Valiente-Gabioud, Claudio O. Fernández, Pablo Peralta, Markus Zweckstetter, Filippo Favretto, Diana F. Lázaro, Annekatrin König, Caterina Masaracchia, Tiago F. Outeiro
Publikováno v:
Biochimica et biophysica acta / Proteins and proteomics 1868(1), 140298 (2020). doi:10.1016/j.bbapap.2019.140298
Biochimica et Biophysica Acta-Proteins and Proteomics
Biochimica et Biophysica Acta-Proteins and Proteomics
The misfolding and aggregation of alpha-synuclein (aSyn) are thought to be central events in synucleinopathies. The physiological function of aSyn has been related to vesicle binding and trafficking, but the precise molecular mechanisms leading to aS
Autor:
Ariel A. Valiente-Gabioud, Dietmar Riedel, Christian Griesinger, Claudio O. Fernández, Tiago F. Outeiro, Mauricio Menacho-Márquez
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Biophysical Journal
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Biophysical Journal
The inherent tendency of proteins to convert from their native states into amyloid aggregates is associated with a range of human disorders, including Alzheimer's and Parkinson's diseases. In that sense, the use of small molecules as probes for the s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05c296bf9373da02a8d926e7693778e1
https://www.sciencedirect.com/science/article/pii/S0006349518300663
https://www.sciencedirect.com/science/article/pii/S0006349518300663
Autor:
Marco C. Miotto, Ariel A. Valiente-Gabioud, Maria Eugenia Chesta, Verónica A. Lombardo, Andres Binolfi, Claudio O. Fernández
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
ConspectusThe aggregation of proteins into toxic conformations plays a critical role in the development of different neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD), and Creutzfled-Jakob's disease (CJD). These di
Autor:
Ariel A. Valiente-Gabioud, Markus Zweckstetter, Philipp Selenko, Andres Binolfi, Marco C. Miotto, Giulia Rossetti, Claudio O. Fernández, Christian Griesinger, Paolo Carloni
Publikováno v:
Journal of the American Chemical Society 137(20), 6444-6447 (2015). doi:10.1021/jacs.5b01911
Journal of the American Chemical Society
Journal of the American Chemical Society
Growing evidence supports a link between brain copper homeostasis, the formation of alpha-synuclein (AS)-copper complexes, and the development of Parkinson disease (PD). Recently it was demonstrated that the physiological form of AS is N-terminally a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ea1e23e6758c00649c84f8dfec9579d
https://pubs.acs.org/doi/10.1021/jacs.5b01911
https://pubs.acs.org/doi/10.1021/jacs.5b01911
Autor:
Jesus Landeira-Fernandez, Daphne S. Cukierman, Nicolás A. Rey, Rachel Ann Hauser-Davis, L. V. de Freitas, Ariel A. Valiente-Gabioud, Claudio O. Fernández, Marco C. Miotto, W. S. Cruz
Publikováno v:
Metallomics : integrated biometal science. 7(5)
Disruptions of biometal-Aβ(1-40) interactions by an isoniazid-derived hydrazone, INHHQ, were demonstrated via in vitro NMR titrations. The compound has adequate theoretical BBB absorption properties, assessed by in silico studies. In vivo acute toxi
Autor:
Christian Griesinger, Liliana Quintanar, Markus Zweckstetter, Claudio O. Fernández, Marco C. Miotto, Esaú E. Rodriguez, Andres Binolfi, Ariel A. Valiente-Gabioud, Valentina Torres-Monserrat
Publikováno v:
Inorganic Chemistry
Inorganic chemistry 53(9), 4350-4358 (2014). doi:10.1021/ic4031377
Inorganic chemistry 53(9), 4350-4358 (2014). doi:10.1021/ic4031377
The amyloid aggregation of alpha-synuclein (AS) has been linked to the pathological effects associated to Parkinson´s disease (PD). Cu(II) binds specifically at the N-terminus of AS and triggers its aggregation. Site-specific Cu(I)-catalyzed oxidati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26a33f7a28f09c6f4bba5bd8a4877dd9
https://hdl.handle.net/11858/00-001M-0000-0019-B6EC-311858/00-001M-0000-0019-B6F6-B11858/00-001M-0000-0019-B6F7-9
https://hdl.handle.net/11858/00-001M-0000-0019-B6EC-311858/00-001M-0000-0019-B6F6-B11858/00-001M-0000-0019-B6F7-9