Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Tara K. Bartolec"'
Autor:
Sunali Mehta, Michael Algie, Tariq Al-Jabry, Cushla McKinney, Srinivasaraghavan Kannan, Chandra S Verma, Weini Ma, Jessie Zhang, Tara K. Bartolec, V. Pragathi Masamsetti, Kim Parker, Luke Henderson, Maree L Gould, Puja Bhatia, Rhodri Harfoot, Megan Chircop, Torsten Kleffmann, Scott B Cohen, Adele G Woolley, Anthony J Cesare, Antony Braithwaite
Publikováno v:
Cancers, Vol 12, Iss 9, p 2473 (2020)
High levels of the cold shock protein Y-box-binding protein-1, YB-1, are tightly correlated with increased cell proliferation and progression. However, the precise mechanism by which YB-1 regulates proliferation is unknown. Here, we found that YB-1 d
Externí odkaz:
https://doaj.org/article/39b16761981742bf9426cc54ff1ffc53
Autor:
Sunali Mehta, Cushla McKinney, Michael Algie, Chandra S. Verma, Srinivasaraghavan Kannan, Rhodri Harfoot, Tara K. Bartolec, Puja Bhatia, Alistair J. Fisher, Maree L. Gould, Kim Parker, Anthony J. Cesare, Heather E. Cunliffe, Scott B. Cohen, Torsten Kleffmann, Antony W. Braithwaite, Adele G. Woolley
Publikováno v:
Cancers, Vol 12, Iss 2, p 315 (2020)
Elevated levels of nuclear Y-box binding protein 1 (YB-1) are linked to poor prognosis in cancer. It has been proposed that entry into the nucleus requires specific proteasomal cleavage. However, evidence for cleavage is contradictory and high YB-1 l
Externí odkaz:
https://doaj.org/article/289b321ab9ba48a3bb42a86410a3e1b4
Autor:
Tara K. Bartolec, Xabier Vázquez-Campos, Alexander Norman, Clement Luong, Marcus Johnson, Richard J. Payne, Marc R. Wilkins, Joel P. Mackay, Jason K. K. Low
Publikováno v:
Proceedings of the National Academy of Sciences. 120
Significant recent advances in structural biology, particularly in the field of cryoelectron microscopy, have dramatically expanded our ability to create structural models of proteins and protein complexes. However, many proteins remain refractory to
Autor:
Tara K. Bartolec, Xabier Vázquez-Campos, Alexander Norman, Clement Luong, Richard J. Payne, Marc R. Wilkins, Joel P. Mackay, Jason K. K. Low
Significant recent advances in structural biology, particularly in the field of cryo-electron microscopy, have dramatically expanded our ability to create structural models of proteins and protein complexes. However, many proteins remain refractory t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::85725471ceaac38881f1a80a9fc0e70f
https://doi.org/10.1101/2022.11.16.516813
https://doi.org/10.1101/2022.11.16.516813
Autor:
Tara K. Bartolec, Joshua J. Hamey, Andrew Keller, Juan D. Chavez, James E. Bruce, Marc.R. Wilkins
Publikováno v:
Molecularcellular proteomics : MCP. 21(7)
The methylation of histidine is a post-translational modification whose function is poorly understood. Methyltransferase histidine protein methyltransferase 1 (Hpm1p) monomethylates H243 in the ribosomal protein Rpl3p and represents the only known hi
Autor:
Jessie Zhang, Elizabeth Hinde, Lorenzo Scipioni, Katharina Gaus, Jieqiong Lou, Enrico Gratton, Tara K. Bartolec, V. Pragathi Masamsetti, Belinda K. Wright, Anthony J. Cesare
Publikováno v:
Lou, Jieqiong; Scipioni, Lorenzo; Wright, Belinda K; Bartolec, Tara K; Zhang, Jessie; Masamsetti, V Pragathi; et al.(2019). Phasor histone FLIM-FRET microscopy quantifies spatiotemporal rearrangement of chromatin architecture during the DNA damage response.. Proceedings of the National Academy of Sciences of the United States of America, 116(15), 7323-7332. doi: 10.1073/pnas.1814965116. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/7hc8r45x
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America
Significance Chromatin dynamics play a central role in the DNA damage response (DDR). A longstanding experimental obstacle was the lack of technology capable of visualizing chromatin dynamics at double-strand break (DSB) sites. Here, we describe biop
Publikováno v:
Journal of Molecular Biology. 434:167500
Histone lysine methylation is a key epigenetic modification that regulates eukaryotic transcription. In Saccharomyces cerevisiae, it is controlled by a reduced but evolutionarily conserved suite of methyltransferase (Set1p, Set2p, Dot1p, and Set5p) a
Autor:
Torsten Kleffmann, Puja Bhatia, Cushla McKinney, Tara K. Bartolec, Maree Gould, Anthony J. Cesare, Heather E. Cunliffe, Chandra S. Verma, Kim Parker, Sunali Mehta, Antony W. Braithwaite, Rhodri Harfoot, Michael Algie, Scott B. Cohen, Alistair J. Fisher, Srinivasaraghavan Kannan, Adele G. Woolley
Publikováno v:
Cancers
Volume 12
Issue 2
Cancers, Vol 12, Iss 2, p 315 (2020)
Volume 12
Issue 2
Cancers, Vol 12, Iss 2, p 315 (2020)
Elevated levels of nuclear Y-box binding protein 1 (YB-1) are linked to poor prognosis in cancer. It has been proposed that entry into the nucleus requires specific proteasomal cleavage. However, evidence for cleavage is contradictory and high YB-1 l
Autor:
Megan Chircop, Tara K. Bartolec, Weini Ma, Antony W. Braithwaite, Rhodri Harfoot, Srinivasaraghavan Kannan, Tariq Al-Jabry, Maree Gould, Anthony J. Cesare, Scott B. Cohen, Jessie Zhang, V. Pragathi Masamsetti, Puja Bhatia, Cushla McKinney, Chandra S. Verma, Adele G. Woolley, Sunali Mehta, Luke Henderson, Kim Parker, Torsten Kleffmann, Michael Algie
Publikováno v:
Cancers
Volume 12
Issue 9
Cancers, Vol 12, Iss 2473, p 2473 (2020)
Volume 12
Issue 9
Cancers, Vol 12, Iss 2473, p 2473 (2020)
High levels of the cold shock protein Y-box-binding protein-1, YB-1, are tightly correlated with increased cell proliferation and progression. However, the precise mechanism by which YB-1 regulates proliferation is unknown. Here, we found that YB-1 d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::304e92f8ffe99c7357c00eb1efd76b7b
https://hdl.handle.net/10356/146593
https://hdl.handle.net/10356/146593
Autor:
Chi Nam Ignatius Pang, Joshua J. Hamey, Daniela-Lee Smith, You Dan Xu, Tara K. Bartolec, Marc R. Wilkins
Publikováno v:
Analytical chemistry. 92(2)
Saccharomyces cerevisiae has the most comprehensively characterized protein-protein interaction network, or interactome, of any eukaryote. This has predominantly been generated through multiple, systematic studies of protein-protein interactions by t