Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Alice Robson"'
Autor:
Dilem Hizlan, Alice Robson, Sarah Whitehouse, Vicki A. Gold, Janet Vonck, Deryck Mills, Werner Kühlbrandt, Ian Collinson
Publikováno v:
Cell Reports, Vol 1, Iss 1, Pp 21-28 (2012)
The Sec complex forms the core of a conserved machinery coordinating the passage of proteins across or into biological membranes. The bacterial complex SecYEG interacts with the ATPase SecA or translating ribosomes to translocate secretory and membra
Externí odkaz:
https://doaj.org/article/f8f689fa01c44449bd7ff9a31cd7aaa7
Autor:
Jonathan A. Davies, Marisa Till, Thomas D. Ackrill, Alice Robson, Christine L. Willis, Paul R. Race, Kavita Tiwari, Catherine R. Back, Matthew J. Byrne, Asha V. Nair
Publikováno v:
Nair, A V, Robson, A, Ackrill, T D, Till, M, Byrne, M J, Back, C, Tiwari, K, Davies, J, Willis, C L & Race, P R 2020, ' Structure and mechanism of a dehydratase/decarboxylase enzyme couple involved in polyketide β-methyl branch incorporation ', Scientific Reports, vol. 10 (2020), 15323 . https://doi.org/10.1038/s41598-020-71850-w
Scientific Reports, Vol 10, Iss 1, Pp 1-16 (2020)
Scientific Reports
Scientific Reports, Vol 10, Iss 1, Pp 1-16 (2020)
Scientific Reports
Complex polyketides of bacterial origin are biosynthesised by giant assembly-line like megaenzymes of the type 1 modular polyketide synthase (PKS) class. The trans-AT family of modular PKSs, whose biosynthetic frameworks diverge significantly from th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2dbbc44c86bc1a39ec33f8a583dea41
https://research-information.bris.ac.uk/en/publications/2740573e-9c26-441d-a581-c7abbcbe1641
https://research-information.bris.ac.uk/en/publications/2740573e-9c26-441d-a581-c7abbcbe1641
Publikováno v:
Human Reproduction. 28:2332-2342
STUDY QUESTION Can selenium (Se) independent, epididymal-specific glutathione peroxidase 5 (GPX5) protect CHO-K1 cells from oxidative damage and, more specifically, from lipid peroxidation and DNA mutation? SUMMARY ANSWER CHO-K1 cells expressing GPX5
Publikováno v:
Biochemical Journal
The motor ATPase SecA drives protein secretion through the bacterial Sec complex. The PPXD (pre-protein cross-linking domain) of the enzyme has been observed in different positions, effectively opening and closing a clamp for the polypeptide substrat
Autor:
William J. Allen, Ian Collinson, Richard B. Sessions, Vicki A. M. Gold, Alice Robson, Sarah L. Whitehouse
Publikováno v:
The Journal of Cell Biology
Polypeptide translocation in bacteria, once underway, requires only one copy each of SecA and SecYEG and does not require the mobility of the SecA 2-helix-finger.
The bacterial ATPase SecA and protein channel complex SecYEG form the core of an e
The bacterial ATPase SecA and protein channel complex SecYEG form the core of an e
Autor:
Howard F. Jenkinson, Paul R. Race, Richard B. Sessions, Richard J. Lamont, Sara Rego, Alice Robson, Angela H. Nobbs, Marisa Till, Grace R. Pidwill, Timothy J. Heal
Publikováno v:
Rego, S, Heal, T J, Pidwill, G R, Till, M, Robson, A, Lamont, R, Sessions, R B, Jenkinson, H F, Race, P R & Nobbs, A H 2016, ' Structural and Functional Analysis of Cell Wall-Anchored PolypeptideAdhesin BspA in Streptococcus agalactiae ', Journal of Biological Chemistry, vol. 291, no. 31, pp. 15985-16000 . https://doi.org/10.1074/jbc.M116.726562
Streptococcus agalactiae (Group B Streptococcus, GBS) is the predominant cause of early-onset infectious disease in neonates and is responsible for life threatening infections in elderly and immune-compromised individuals. Clinical manifestations of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6b3ee63d456c5c14fd4302428d6fd84
https://europepmc.org/articles/PMC4965550/
https://europepmc.org/articles/PMC4965550/
Autor:
Ian Collinson, Alice Robson, Joanna Komar, Robin A. Corey, William J. Allen, Simonas Masiulis, Sam Menzies
Publikováno v:
Corey, R A, Allen, W J, Komar, J, Masiulis, S, Menzies, S, Robson, A & Collinson, I R 2016, ' Unlocking the bacterial SecY translocon ', Structure, vol. 24, pp. 1-10 . https://doi.org/10.1016/j.str.2016.02.001
Structure(London, England:1993)
Structure(London, England:1993)
Summary The Sec translocon performs protein secretion and membrane protein insertion at the plasma membrane of bacteria and archaea (SecYEG/β), and the endoplasmic reticular membrane of eukaryotes (Sec61). Despite numerous structures of the complex,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef1f058e3622e891de4d2587894a64a5
https://research-information.bris.ac.uk/en/publications/3453f329-c3ca-4366-a47c-1deba82c18d7
https://research-information.bris.ac.uk/en/publications/3453f329-c3ca-4366-a47c-1deba82c18d7
Autor:
Ian Collinson, Vicki A. M. Gold, Sarah L. Whitehouse, Alice Robson, Dilem Hizlan, Werner Kühlbrandt, Janet Vonck, Deryck J. Mills
Publikováno v:
Cell Reports, Vol 1, Iss 1, Pp 21-28 (2012)
Cell Reports
Cell Reports
Summary The Sec complex forms the core of a conserved machinery coordinating the passage of proteins across or into biological membranes. The bacterial complex SecYEG interacts with the ATPase SecA or translating ribosomes to translocate secretory an
Autor:
Ian Collinson, Richard B. Sessions, Vicki A. M. Gold, Sarah L. Whitehouse, Karine Deville, Alice Robson, Stephen A. Baldwin, Sheena E. Radford
Publikováno v:
The Journal of Biological Chemistry
Protein secretion in bacteria is driven through the ubiquitous SecYEG complex by the ATPase SecA. The structure of SecYEG alone or as a complex with SecA in detergent reveal a monomeric heterotrimer enclosing a central protein channel, yet in membran
Publikováno v:
Proceedings of the National Academy of Sciences. 107:10044-10049
Cardiolipin is an ever-present component of the energy-conserving inner membranes of bacteria and mitochondria. Its modulation of the structure and dynamism of the bilayer impacts on the activity of their resident proteins, as a number of studies hav