Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Emily J, Byrd"'
Autor:
Sabine M. Ulamec, Roberto Maya-Martinez, Emily J. Byrd, Katherine M. Dewison, Yong Xu, Leon F. Willis, Frank Sobott, George R. Heath, Patricija van Oosten Hawle, Vladimir L. Buchman, Sheena E. Radford, David J. Brockwell
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
The authors of this work characterize the effect of amino acid substitution on α-synuclein (α-Syn) aggregation. Residues 38 and 42 (in addition to 39) within the P1 region of α-Syn affect amyloid formation. The effect of substitution at position 3
Externí odkaz:
https://doaj.org/article/795dea3b15b941688aa5f281361c1332
Publikováno v:
Journal of the American Society for Mass Spectrometry. 34:493-504
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fb68a2a4b8c801e32eda2c46770ee780
https://doi.org/10.1021/jasms.2c00379
https://doi.org/10.1021/jasms.2c00379
Autor:
Jaime Santos, Jorge Cuellar, Irantzu Pallarès, Emily J Byrd, Alons Lends, Fernando Moro, Muhammed Bilal Abdul-Shukkoor, Jordi Pujols, Lorea Velasco-Carneros, Frank Sobott, Daniel E Otzen, Antonio N Calabrese, Arturo Muga, Jan Skov Pedersen, Antoine Loquet, Jose María Valpuesta, Sheena E Radford, Salvador Ventura
Oligomeric species populated during α-synuclein aggregation are considered key drivers of neurodegeneration in Parkinson’s disease. However, their structure and the molecular determinants driving their conversion to fibrils remain elusive. In this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cc5124549253e70a4832df8bf77b620a
https://doi.org/10.1101/2023.02.10.527650
https://doi.org/10.1101/2023.02.10.527650
Autor:
Sabine M, Ulamec, Roberto, Maya-Martinez, Emily J, Byrd, Katherine M, Dewison, Yong, Xu, Leon F, Willis, Frank, Sobott, George R, Heath, Patricija, van Oosten Hawle, Vladimir L, Buchman, Sheena E, Radford, David J, Brockwell
Publikováno v:
Nature communications. 13(1)
Alpha-synuclein (αSyn) is a protein involved in neurodegenerative disorders including Parkinson's disease. Amyloid formation of αSyn can be modulated by the 'P1 region' (residues 36-42). Here, mutational studies of P1 reveal that Y39A and S42A exte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::89b1e3ae3e24b7c969295b86ef771ad4
https://pubmed.ncbi.nlm.nih.gov/36008493
https://pubmed.ncbi.nlm.nih.gov/36008493