Zobrazeno 1 - 10
of 225
pro vyhledávání: '"Mick F Tuite"'
Autor:
Ricardo Marchante, David M Beal, Nadejda Koloteva-Levine, Tracey J Purton, Mick F Tuite, Wei-Feng Xue
Publikováno v:
eLife, Vol 6 (2017)
Transmissible amyloid particles called prions are associated with infectious prion diseases in mammals and inherited phenotypes in yeast. All amyloid aggregates can give rise to potentially infectious seeds that accelerate their growth. Why some amyl
Externí odkaz:
https://doaj.org/article/e9380a6aa4604b23a684d3bbc4418689
Publikováno v:
PLoS Genetics, Vol 13, Iss 4, p e1006708 (2017)
Mammalian and fungal prions arise de novo; however, the mechanism is poorly understood in molecular terms. One strong possibility is that oxidative damage to the non-prion form of a protein may be an important trigger influencing the formation of its
Externí odkaz:
https://doaj.org/article/e13b63ac85914d3db2c3cd4b7bb4a1c5
Autor:
Mick F Tuite
Publikováno v:
eLife, Vol 5 (2016)
Some bacteria use lactic acid to communicate with yeast cells.
Externí odkaz:
https://doaj.org/article/5a28f81b79bd4224bb81b0a914bfd946
Autor:
Johann W Bauer, Clemens Brandl, Olaf Haubenreisser, Bjoern Wimmer, Manuela Weber, Thomas Karl, Alfred Klausegger, Michael Breitenbach, Helmut Hintner, Tobias von der Haar, Mick F Tuite, Lore Breitenbach-Koller
Publikováno v:
PLoS ONE, Vol 8, Iss 7, p e67609 (2013)
Evidence is now accumulating that sub-populations of ribosomes - so-called specialized ribosomes - can favour the translation of subsets of mRNAs. Here we use a large collection of diploid yeast strains, each deficient in one or other copy of the set
Externí odkaz:
https://doaj.org/article/27ed8fd143834101829b818f7233ed4e
Publikováno v:
PLoS ONE, Vol 4, Iss 3, p e4670 (2009)
BACKGROUND:Yeast (Saccharomyces cerevisiae) prions are efficiently propagated and the on-going generation and transmission of prion seeds (propagons) to daughter cells during cell division ensures a high degree of mitotic stability. The reversible in
Externí odkaz:
https://doaj.org/article/191603b2d1474e8d96aa3a0cb7ded9de
Publikováno v:
PLoS Biology, Vol 2, Iss 4, p E86 (2004)
Many proteins can misfold into beta-sheet-rich, self-seeding polymers (amyloids). Prions are exceptional among such aggregates in that they are also infectious. In fungi, prions are not pathogenic but rather act as epigenetic regulators of cell physi
Externí odkaz:
https://doaj.org/article/7b141c458a474820bf10b30edc58f5d2
Autor:
Yajing Wang, Houlu Tian, Na Shi, Chunyan Wu, Yaowei Huang, Yongling Yang, Qiang Ding, Xu Zheng, Qin Zhao, Mick F. Tuite, Hongying Chen, Yuchen Nan
Hepatitis E virus (HEV) is a common causative agent of acute hepatitis. Due to the shortage of efficient in vitro model, the viral assembly and release processes are still poorly understood. In this study, we found that ORF3, an HEV structural protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d247db34de359ba7e7f10b77d4f713a
https://doi.org/10.1101/2023.01.13.523929
https://doi.org/10.1101/2023.01.13.523929
Publikováno v:
Biomolecules; Volume 12; Issue 5; Pages: 630
The division of amyloid fibril particles through fragmentation is implicated in the progression of human neurodegenerative disorders such as Parkinson’s disease. Fragmentation of amyloid fibrils plays a crucial role in the propagation of the amyloi
Publikováno v:
Biomolecular Concepts, Vol 11, Iss 1, Pp 102-115 (2020)
Atomic force microscopy, AFM, is a powerful tool that can produce detailed topographical images of individual nano-structures with a high signal-to-noise ratio without the need for ensemble averaging. However, the application of AFM in structural bio
Autor:
Claude M. Wischik, Liisa Lutter, Wei-Feng Xue, Youssra K. Al-Hilaly, Christopher J. Serpell, Mick F. Tuite, Louise C. Serpell
The presence of amyloid fibrils is a hallmark of more than 50 human disorders, including neurodegenerative diseases and systemic amyloidoses. A key unresolved challenge in understanding the involvement of amyloid in disease is to explain the relation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4c7fc2d0782424ca544d98609b0bc1be
https://doi.org/10.1101/2021.10.19.464873
https://doi.org/10.1101/2021.10.19.464873