Zobrazeno 1 - 10
of 141
pro vyhledávání: '"Paula J Booth"'
Autor:
Natalie Di Bartolo, Emma L R Compton, Tony Warne, Patricia C Edwards, Christopher G Tate, Gebhard F X Schertler, Paula J Booth
Publikováno v:
PLoS ONE, Vol 11, Iss 3, p e0151582 (2016)
The factors defining the correct folding and stability of integral membrane proteins are poorly understood. Folding of only a few select membrane proteins has been scrutinised, leaving considerable deficiencies in knowledge for large protein families
Externí odkaz:
https://doaj.org/article/0ef8c841adb849ae9f0ed741cb3e29c8
Autor:
Stephen D. Fried, Paula J. Booth
Publikováno v:
Frontiers in molecular biosciences. 9
Autor:
Oscar Ces, Paula J. Booth, Nestor Lopez Mora, Nicholas J. Brooks, Heather E. Findlay, Sowmya Purushothaman
Publikováno v:
Biophysical Journal
Cellular life relies on membranes, which provide a resilient and adaptive cell boundary. Many essential processes depend upon the ease with which the membrane is able to deform and bend, features that can be characterized by the bending rigidity. Qua
Autor:
Nicola J. Harris, Grant A. Pellowe, Laura R. Blackholly, Samuel Gulaidi-Breen, Heather E. Findlay, Paula J. Booth
Publikováno v:
Harris, N J, Pellowe, G A, Blackholly, L R, Gulaidi-Breen, S, Findlay, H E & Booth, P J 2022, ' Methods to study folding of alpha-helical membrane proteins in lipids ', Open Biology, vol. 12, no. 7, 220054 . https://doi.org/10.1098/rsob.220054
How alpha-helical membrane proteins fold correctly in the highly hydrophobic membrane interior is not well understood. Their folding is known to be highly influenced by the lipids within the surrounding bilayer, but the majority of folding studies ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f10b9f8f152674814188ba3229c0266
https://kclpure.kcl.ac.uk/en/publications/d8735ca9-7050-4e7d-8e2a-3aecb1798566
https://kclpure.kcl.ac.uk/en/publications/d8735ca9-7050-4e7d-8e2a-3aecb1798566
Activating mechanosensitive channels embedded in droplet interface bilayers using membrane asymmetry
Autor:
Oscar Ces, Robert V. Law, Robert John Strutt, Paula J. Booth, John D. Harling, Mark S. Friddin, Jordan Gregg, James W. Hindley
Publikováno v:
Chemical Science
Droplet microcompartments linked by lipid bilayers show great promise in the construction of synthetic minimal tissues. Central to controlling the flow of information in these systems are membrane proteins, which can gate in response to specific stim
Autor:
null Nicola J. Harris, null Grant A. Pellowe, null Laura R. Blackholly, null Samuel Gulaidi-Breen, null Heather E. Findlay, null Paula J. Booth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4ad1bc3682d4e0644c27067bb6876f79
https://doi.org/10.1098/rsob.220054/v2/response1
https://doi.org/10.1098/rsob.220054/v2/response1
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
The majority of alpha helical membrane proteins fold co-translationally during their synthesis on the ribosome. In contrast, most mechanistic folding studies address refolding of full-length proteins from artificially induced denatured states that ar
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2433
In order to comprehend the molecular basis of transmembrane protein biogenesis, methods are required that are capable of investigating the co-translational folding of these hydrophobic proteins. Equally, in artificial cell studies, controllable metho
Publikováno v:
Cell-Free Gene Expression ISBN: 9781071619971
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::492b3e04553349652add10a030f23654
https://doi.org/10.1007/978-1-0716-1998-8_17
https://doi.org/10.1007/978-1-0716-1998-8_17
Publikováno v:
Brady, R, Harris, N J, Pellowe, G A, Breen, S G & Booth, P J 2022, ' How lipids affect the energetics of co-translational alpha helical membrane protein folding ', Biochemical Society Transactions, vol. 50, no. 1, pp. 555-567 . https://doi.org/10.1042/BST20201063
Membrane proteins need to fold with precision in order to function correctly, with misfolding potentially leading to disease. The proteins reside within a hydrophobic lipid membrane and must insert into the membrane and fold correctly, generally whil