Zobrazeno 1 - 3
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pro vyhledávání: '"Allen T.Y. Lo"'
Autor:
Valerie L. O’Shea, Jacob S. Lewis, Allen T.Y. Lo, Nicholas E. Dixon, Antoine M. van Oijen, James M. Berger, Zhi-Qiang Xu, Enrico Monachino, Slobodan Jergic
Publikováno v:
Mol Cell
Molecular Cell, 79(1), 140-154.e7. CELL PRESS
Molecular Cell, 79(1), 140-154.e7. CELL PRESS
SUMMARYRecent studies of bacterial DNA replication have led to a picture of the replisome as an entity that freely exchanges DNA polymerases and displays intermittent coupling between the helicase and polymerase(s). Challenging the textbook model of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36423d9ef2d1528b5b69492642acaffc
https://doi.org/10.1016/j.molcel.2020.04.037
https://doi.org/10.1016/j.molcel.2020.04.037
Autor:
Allen T.Y. Lo, Aaron J. Oakley, Gottfried Otting, Stephen J. Headey, Nicholas E. Dixon, Zhi-Qiang Xu, Martin J. Scanlon, Zorik Chilingaryan
Publikováno v:
Antibiotics, Vol 7, Iss 1, p 14 (2018)
Antibiotics; Volume 7; Issue 1; Pages: 14
Antibiotics
Antibiotics; Volume 7; Issue 1; Pages: 14
Antibiotics
In bacteria, the DnaG primase is responsible for synthesis of short RNA primers used to initiate chain extension by replicative DNA polymerase(s) during chromosomal replication. Among the proteins with which Escherichia coli DnaG interacts is the sin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e126b93f5427c19050ec4a7d38e068bd
http://www.mdpi.com/2079-6382/7/1/14
http://www.mdpi.com/2079-6382/7/1/14
Autor:
Jennifer L. Beck, Nicholas E. Dixon, Yao Wang, Allen T.Y. Lo, Slobodan Jergic, Claire E. Mason
Publikováno v:
Journal of the American Society for Mass Spectrometry. 24(2)
Single-stranded DNA-binding proteins (SSBs) are ubiquitous oligomeric proteins that bind with very high affinity to single-stranded DNA and have a variety of essential roles in DNA metabolism. Nanoelectrospray ionization mass spectrometry (nanoESI-MS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8aee3bb72ab87af341b19b091811b6e
https://pubmed.ncbi.nlm.nih.gov/23283730
https://pubmed.ncbi.nlm.nih.gov/23283730