Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Neeleema Seetaloo"'
Autor:
Amberley D. Stephens, Maria Zacharopoulou, Rani Moons, Giuliana Fusco, Neeleema Seetaloo, Anass Chiki, Philippa J. Woodhams, Ioanna Mela, Hilal A. Lashuel, Jonathan J. Phillips, Alfonso De Simone, Frank Sobott, Gabriele S. Kaminski Schierle
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
In Parkinson’s disease (PD) the monomeric protein alpha-synuclein (aSyn) misfolds and aggregates into insoluble fibrils. Here the authors use NMR measurements and hydrogen–deuterium exchange mass spectrometry and find that the more solvent expose
Externí odkaz:
https://doaj.org/article/06df908e29ff4c6a9479ca48a333babb
Publikováno v:
Analytical Chemistry. 94:4557-4564
Hydrogen/deuterium-exchange mass spectrometry (HDX-MS) experiments on protein structures can be performed at three levels: (1) by enzymatically digesting labelled proteins and analyzing the peptides (bottom-up), (2) by further fragmenting peptides fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a480b9e66d0b872ed816bde6316a5688
https://doi.org/10.1021/acs.analchem.1c05339
https://doi.org/10.1021/acs.analchem.1c05339
Publikováno v:
Journal of Visualized Experiments.
Alpha-synuclein (aSyn) is an intrinsically disordered protein whose fibrillar aggregates are abundant in Lewy bodies and neurites, which are the hallmarks of Parkinson's disease. Yet, much of its biological activity, as well as its aggregation, centr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ad93718ff5eed8fab794cde6e0a71dd
https://doi.org/10.3791/64050
https://doi.org/10.3791/64050
Autor:
Neeleema Seetaloo, Maria Zacharopoulou, Amberley D. Stephens, Gabriele S. Kaminski Schierle, Jonathan J. Phillips
In Parkinson’s disease and other synucleinopathies, the intrinsically disordered, presynaptic protein alpha-synuclein misfolds and aggregates. We hypothesise that the exposure of alpha-synuclein to different cellular environments, with different ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9dec3879704754eb81c72774a2801410
https://doi.org/10.1101/2022.02.11.480045
https://doi.org/10.1101/2022.02.11.480045
Autor:
Alfonso De Simone, Ioanna Mela, Giuliana Fusco, Frank Sobott, Rani Moons, Jonathan J. Phillips, Anass Chiki, Philippa J. Woodhams, Maria Zacharopoulou, Neeleema Seetaloo, Gabriele S. Kaminski Schierle, Hilal A. Lashuel, Amberley D. Stephens
Publikováno v:
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Nature communications
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Nature communications
As an intrinsically disordered protein, monomeric alpha-synuclein (aSyn) occupies a large conformational space. Certain conformations lead to aggregation prone and non-aggregation prone intermediates, but identifying these within the dynamic ensemble
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7cebfb0f2cfefb837dabdf877f35541
Autor:
Alfonso De Simone, Rani Moons, Frank Sobott, Ioanna Mela, Neeleema Seetaloo, Amberley D. Stephens, Gabriele S. Kaminski Schierle, Anass Chiki, Hilal A. Lashuel, Jonathan J. Phillips, Maria Zacharopoulou, Philippa J. Hooper, Giuliana Fusco
As an intrinsically disordered protein, monomeric alpha synuclein (aSyn) constantly reconfigures and probes the conformational space. Long-range interactions across the protein maintain its solubility and mediate this dynamic flexibility, but also pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1948a8ace3df713737fdd612233adfa7
https://doi.org/10.1101/740241
https://doi.org/10.1101/740241