Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Aline C Simon"'
Autor:
John F Darby, Ewelina M Krysztofinska, Peter J Simpson, Aline C Simon, Pawel Leznicki, Newran Sriskandarajah, David S Bishop, Lisa R Hale, Caterina Alfano, Maria R Conte, Santiago Martínez-Lumbreras, Arjun Thapaliya, Stephen High, Rivka L Isaacson
Publikováno v:
PLoS ONE, Vol 9, Iss 11, p e113281 (2014)
The BAG6 complex resides in the cytosol and acts as a sorting point to target diverse hydrophobic protein substrates along their appropriate paths, including proteasomal degradation and ER membrane insertion. Composed of a trimeric complex of BAG6, T
Externí odkaz:
https://doaj.org/article/8e8a952f4dc54536822cf9d134d1aff8
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-15 (2016)
The cell cycle division protein Cdc45 is required for genome duplication in eukaryotes. Here, the authors determine the crystal structure of human Cdc45 and combine it with functional data to improve our understanding of its role in DNA replication.
Externí odkaz:
https://doaj.org/article/336a490581984f819349c8beafd6bee9
Autor:
Aline C. Simon, Luca Pellegrini, Karim Labib, Lina Dobnikar, Yuteng Wu, Joseph D. Maman, David R. Spring, Fabrizio Villa, Yu Heng Lau
Publikováno v:
Angewandte Chemie International Edition. 56:12866-12872
The exploitation of synthetic lethality by small-molecule targeting of pathways that maintain genomic stability is an attractive chemotherapeutic approach. The Ctf4/AND-1 protein hub, which links DNA replication, repair, and chromosome segregation, r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2d074b026e320423d4280ee9756ef1f
https://doi.org/10.1002/anie.201705611
https://doi.org/10.1002/anie.201705611
Autor:
Karim Labib, Jin C. Zhou, Cecile Evrin, Ludovic Renault, Mairi L. Kilkenny, Luca Pellegrini, Dijana Matak-Vinkovic, Rajika L. Perera, Aline C. Simon, Alessandro Costa, Svend Kjaer, Frederick van Deursen, Marina E. Ivanova
Publikováno v:
Nature
This study shows how the yeast Ctf4 protein couples the DNA helicase, Cdc45–MCM–GINS, to DNA polymerase α — the GINS subunit of the helicase and the polymerase use a similar interaction to bind Ctf4, suggesting that, as Ctf4 is a trimer, two p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e204c49ed82b12f336919a1702db5b8
http://europepmc.org/articles/PMC4059944
http://europepmc.org/articles/PMC4059944
Autor:
Peter Simpson, Stephen High, Rachael M. Goldstone, Aline C. Simon, James W. Murray, Rivka L. Isaacson, Ewelina M. Krysztofinska
Publikováno v:
Proceedings of the National Academy of Sciences. 110:1327-1332
Small, glutamine-rich, tetratricopeptide repeat protein 2 (Sgt2) is the first known port of call for many newly synthesized tail-anchored (TA) proteins released from the ribosome and destined for the GET (Guided Entry of TA proteins) pathway. This le
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb9db10d94646c54c9b3b79129670b73
https://doi.org/10.1073/pnas.1207518110
https://doi.org/10.1073/pnas.1207518110
Publikováno v:
Proceedings of the National Academy of Sciences. 108:7757-7762
The bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP) signaling pathway regulates biofilm formation, virulence, and other processes in many bacterial species and is critical for their survival. Two classes of c-di-GMP-binding riboswit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0347d6c2387cd687ec44d01883f49151
https://doi.org/10.1073/pnas.1018857108
https://doi.org/10.1073/pnas.1018857108
Autor:
Aline C. Simon, Pawel Leznicki, Peter Simpson, Santiago Martínez-Lumbreras, Lisa R. Hale, David S. Bishop, Arjun Thapaliya, John F. Darby, Ewelina M. Krysztofinska, Rivka L. Isaacson, Newran Sriskandarajah, Stephen High, Caterina Alfano, Maria R. Conte
Publikováno v:
Darby, J F, Krysztofinska, E M, Simpson, P J, Simon, A C, Leznicki, P, Sriskandarajah, N, Bishop, D S, Hale, L R, Alfano, C, Conte, M R, Martínez-Lumbreras, S, Thapaliya, A, High, S & Isaacson, R L 2014, ' Solution Structure of the SGTA Dimerisation Domain and Investigation of Its Interactions with the Ubiquitin-Like Domains of BAG6 and UBL4A ', PLOS One, vol. 9, no. 11, e113281 . https://doi.org/10.1371/journal.pone.0113281
PLoS ONE, Vol 9, Iss 11, p e113281 (2014)
PLoS ONE
PLoS ONE, Vol 9, Iss 11, p e113281 (2014)
PLoS ONE
Background The BAG6 complex resides in the cytosol and acts as a sorting point to target diverse hydrophobic protein substrates along their appropriate paths, including proteasomal degradation and ER membrane insertion. Composed of a trimeric complex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7dfb54b6c239d7d45bf64b655e9d102
https://kclpure.kcl.ac.uk/en/publications/00b58205-a08f-41e2-aac3-f41dc79d3e36
https://kclpure.kcl.ac.uk/en/publications/00b58205-a08f-41e2-aac3-f41dc79d3e36
Autor:
Mairi L. Kilkenny, Aline C. Simon, Jack Mainwaring, David Wirthensohn, Sandro Holzer, Luca Pellegrini
Publikováno v:
Open Biology, Vol 7, Iss 11 (2017)
A dynamic multi-protein assembly known as the replisome is responsible for DNA synthesis in eukaryotic cells. In yeast, the hub protein Ctf4 bridges DNA helicase and DNA polymerase and recruits factors with roles in metabolic processes coupled to DNA
Externí odkaz:
https://doaj.org/article/d02f8648c818478099e9295c0dede697