Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Katherine M Dewison"'
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
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
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 19
International Journal of Molecular Sciences, Vol 22, Iss 10752, p 10752 (2021)
Volume 22
Issue 19
International Journal of Molecular Sciences, Vol 22, Iss 10752, p 10752 (2021)
Aggregation of β2 microglobulin (β2m) into amyloid fibrils is associated with systemic amyloidosis, caused by the deposition of amyloid fibrils containing the wild-type protein and its truncated variant, ΔN6 β2m, in haemo-dialysed patients. A sec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aebd315e24b574a786356dfe80775f62
https://doi.org/10.3390/ijms221910752
https://doi.org/10.3390/ijms221910752