Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Mahmoud B, Maina"'
Autor:
Zaid Muhammad, Phoebe W. Brown, Larema Babazau, Abdulrahman I. Alkhamis, Baba W. Goni, Haruna A. Nggada, Kefas M. Mbaya, Selina Wray, Isa H. Marte, Celeste M. Karch, Louise C. Serpell, Mahmoud B. Maina
Publikováno v:
Stem Cell Research, Vol 80, Iss , Pp 103503- (2024)
Genetic backgrounds influence cellular phenotypes, drug responses, and health outcomes, yet most human iPSC lines are derived from individuals of European descent, with lines from indigenous Africans particularly scarce. Addressing this gap, we gener
Externí odkaz:
https://doaj.org/article/c6d390ba54254cd6a3c68b1584f11a95
Publikováno v:
Frontiers in Neuroscience, Vol 17 (2023)
Oxidative stress is a significant source of damage that accumulates during aging and contributes to Alzheimer’s disease (AD) pathogenesis. Oxidation of proteins can give rise to covalent links between adjacent tyrosines known as dityrosine (DiY) cr
Externí odkaz:
https://doaj.org/article/70a09f36edf04aff9cce76085be19d7f
Autor:
Sebastian S. Oakley, Mahmoud B. Maina, Karen E. Marshall, Youssra K. Al-Hilaly, Charlie R. Harrington, Claude M. Wischik, Louise C. Serpell
Publikováno v:
Frontiers in Neurology, Vol 11 (2020)
Tau plays an important pathological role in a group of neurodegenerative diseases called tauopathies, including Alzheimer's disease, Pick's disease, chronic traumatic encephalopathy and corticobasal degeneration. In each disease, tau self-assembles a
Externí odkaz:
https://doaj.org/article/5b7b64b5eba24b5790a5b05d5ddc4ab8
Autor:
Mahmoud B. Maina, Gunasekhar Burra, Youssra K. Al-Hilaly, Kurtis Mengham, Kate Fennell, Louise C. Serpell
Publikováno v:
iScience, Vol 23, Iss 10, Pp 101537- (2020)
Summary: Dityrosine (DiY), via the cross-linking of tyrosine residues, is a marker of protein oxidation, which increases with aging. Amyloid-β (Aβ) forms DiY in vitro and DiY-cross-linked Aβ is found in the brains of patients with Alzheimer diseas
Externí odkaz:
https://doaj.org/article/4f3367717ded4dfe87b1faeb3c86248f
Autor:
Mahmoud B. Maina, Laura J. Bailey, Sherin Wagih, Luca Biasetti, Saskia J. Pollack, James P. Quinn, Julian R. Thorpe, Aidan J. Doherty, Louise C. Serpell
Publikováno v:
Acta Neuropathologica Communications, Vol 6, Iss 1, Pp 1-13 (2018)
Abstract Tau is known for its pathological role in neurodegenerative diseases, including Alzheimer’s disease (AD) and other tauopathies. Tau is found in many subcellular compartments such as the cytosol and the nucleus. Although its normal role in
Externí odkaz:
https://doaj.org/article/a34deb81486543e3bd80a46007061673
Autor:
Mahmoud B. Maina, Youssra K. Al-Hilaly, Gunasekhar Burra, Janet E. Rickard, Charles R. Harrington, Claude M. Wischik, Louise C. Serpell
Publikováno v:
Cells, Vol 10, Iss 3, p 703 (2021)
The self-assembly of tau into paired helical filaments (PHFs) in neurofibrillary tangles (NFTs) is a significant event in Alzheimer’s disease (AD) pathogenesis. Numerous post-translational modifications enhance or inhibit tau assembly into NFTs. Ox
Externí odkaz:
https://doaj.org/article/8253ab4ebde849ff9bbb23fd6a5f95e4
Publikováno v:
Frontiers in Cellular Neuroscience, Vol 12 (2018)
Alzheimer’s disease (AD) is the most common form of dementia and is distinguished from other dementias by observation of extracellular Amyloid-β (Aβ) plaques and intracellular neurofibrillary tangles, comprised of fibrils of Aβ and tau protein,
Externí odkaz:
https://doaj.org/article/900f80d41ee14dfd87e27493d2b44a8a
Autor:
Kurtis Mengham, Youssra Al-Hilaly, Sebastian Oakley, Kamillia Kasbi, Mahmoud B. Maina, Louise C. Serpell
Publikováno v:
Essays in biochemistry.
Tau is an intrinsically disordered protein that has the ability to self-assemble to form paired helical and straight filaments in Alzheimer’s disease, as well as the ability to form additional distinct tau filaments in other tauopathies. In the pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ea6ec910c1216410f674d92d062b398
https://pubmed.ncbi.nlm.nih.gov/36373666
https://pubmed.ncbi.nlm.nih.gov/36373666
Autor:
Mahmoud B. Maina, Youssra K. Al-Hilaly, Sebastian Oakley, Gunashekar Burra, Tahmida Khanon, Luca Biasetti, Kurtis Mengham, Karen Marshall, Janet E. Rickard, Charles R. Harrington, Claude M. Wischik, Louise C. Serpell
A characteristic hallmark of Alzheimer’s Disease (AD) is the pathological aggregation and deposition of tau into paired helical filaments (PHF) in neurofibrillary tangles (NFTs). Oxidative stress is an early event during AD pathogenesis and is asso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::51fb3a085481601be4853471a36e72a8
https://doi.org/10.1101/2022.05.28.493839
https://doi.org/10.1101/2022.05.28.493839
GNNQQNY sequence offers crucial information about the formation and structure of an amyloid fibril. In this study, we demonstrate a reproducible solubilisation protocol where the reduction of pH to 2.0 resulted in the generation of GNNQQNY monomers.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9a7a6ebd7f13a0ac72b144d133ab7c25
https://doi.org/10.1101/2022.01.01.474692
https://doi.org/10.1101/2022.01.01.474692