Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Liisa, Lutter"'
Autor:
Einav Tayeb-Fligelman, Jeannette T. Bowler, Christen E. Tai, Michael R. Sawaya, Yi Xiao Jiang, Gustavo Garcia, Sarah L. Griner, Xinyi Cheng, Lukasz Salwinski, Liisa Lutter, Paul M. Seidler, Jiahui Lu, Gregory M. Rosenberg, Ke Hou, Romany Abskharon, Hope Pan, Chih-Te Zee, David R. Boyer, Yan Li, Daniel H. Anderson, Kevin A. Murray, Genesis Falcon, Duilio Cascio, Lorena Saelices, Robert Damoiseaux, Vaithilingaraja Arumugaswami, Feng Guo, David S. Eisenberg
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-18 (2023)
Abstract The self-assembly of the Nucleocapsid protein (NCAP) of SARS-CoV-2 is crucial for its function. Computational analysis of the amino acid sequence of NCAP reveals low-complexity domains (LCDs) akin to LCDs in other proteins known to self-asse
Externí odkaz:
https://doaj.org/article/afcfb5ca25ff4981a1a88a2f530c23e4
Autor:
Youssra K, Al-Hilaly, Karen E, Marshall, Liisa, Lutter, Luca, Biasetti, Kurtis, Mengham, Charles R, Harrington, Wei-Feng, Xue, Claude M, Wischik, Louise C, Serpell
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2551
Tau is a natively unfolded protein that contributes to the stability of microtubules. Under pathological conditions such as Alzheimer's disease (AD), tau protein misfolds and self-assembles to form paired helical filaments (PHFs) and straight filamen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d5ebe12eb3fbc8d0128307e019baa14d
https://pubmed.ncbi.nlm.nih.gov/36310203
https://pubmed.ncbi.nlm.nih.gov/36310203
Autor:
Youssra K. Al-Hilaly, Karen E. Marshall, Liisa Lutter, Luca Biasetti, Kurtis Mengham, Charles R. Harrington, Wei-Feng Xue, Claude M. Wischik, Louise C. Serpell
Publikováno v:
Methods in Molecular Biology ISBN: 9781071625965
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dfec2dab062f29bdce33aab424c72ec1
https://doi.org/10.1007/978-1-0716-2597-2_12
https://doi.org/10.1007/978-1-0716-2597-2_12
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e16dba4583b89d0b5b33703f38c5c5fa
https://doi.org/10.1515/bmc-2020-0009
https://doi.org/10.1515/bmc-2020-0009
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
The prediction of highly ordered three-dimensional structures of amyloid protein fibrils from the amino acid sequences of their monomeric self-assembly precursors constitutes a challenging and unresolved aspect of the classical protein folding proble
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cae837c685856c4b627c692259f83db9
Autor:
Liam D. Aubrey, Christopher J. Serpell, Louise C. Serpell, Mick F. Tuite, Wei-Feng Xue, Ben J. F. Blakeman, Liisa Lutter
Publikováno v:
Communications Chemistry, Vol 3, Iss 1, Pp 1-10 (2020)
Amyloid fibrils are highly polymorphic structures formed by many different proteins. They provide biological function but also abnormally accumulate in numerous human diseases. The physicochemical principles of amyloid polymorphism are not understood
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ebfa99466763e50f3b859ebf14dadb6
https://doi.org/10.1038/s42004-020-00372-3
https://doi.org/10.1038/s42004-020-00372-3
Autor:
John Storey, Youssra K. Al-Hilaly, Janet Elizabeth Rickard, Bronwen E Foster, Luca Biasetti, Wei-Feng Xue, Liisa Lutter, Saskia J. Pollack, Claude M. Wischik, Louise C. Serpell, Charles R. Harrington
Publikováno v:
Febs Letters
The constituent paired helical filaments (PHFs) in neurofibrillary tangles are insoluble intracellular deposits central to the development of Alzheimer’s disease (AD) and other tauopathies. Full‐length tau requires the addition of anionic cofacto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a7bc0dac034817aa9c457e1419140a2
https://pubmed.ncbi.nlm.nih.gov/31721178
https://pubmed.ncbi.nlm.nih.gov/31721178
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1867:140257
The formation of a diverse range of amyloid structures from normally soluble proteins and peptides is a hallmark of devastating human disorders as well as biological functions. The current molecular understanding of the amyloid lifecycle reveals four
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cc1422798f6a126c8f331fa8380ac06
https://doi.org/10.1016/j.bbapap.2019.07.010
https://doi.org/10.1016/j.bbapap.2019.07.010