Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Laura Pontano-Vaites"'
Autor:
Lior Izhar, Britt Adamson, Alberto Ciccia, Jedd Lewis, Laura Pontano-Vaites, Yumei Leng, Anthony C. Liang, Thomas F. Westbrook, J. Wade Harper, Stephen J. Elledge
Publikováno v:
Cell Reports, Vol 11, Iss 9, Pp 1486-1500 (2015)
Localization to sites of DNA damage is a hallmark of DNA damage response (DDR) proteins. To identify DDR factors, we screened epitope-tagged proteins for localization to sites of chromatin damaged by UV laser microirradiation and found >120 proteins
Externí odkaz:
https://doaj.org/article/1e266c5645c54457ba46da3fda7395d2
Autor:
Premchendar Nandhikonda, Joao A. Paulo, Rosa Viner, Aaron M. Robitaille, Ian Pike, Steven P. Gygi, John C. Rogers, Chris Etienne, Laura Pontano Vaites, Jonathan G. Van Vranken, Andrew Hugin Thompson, Karsten Kuhn, Devin K. Schweppe, Jiaming Li, Edward L. Huttlin, Ryan Bomgarden
Publikováno v:
Nat Methods
Isobaric labeling empowers proteome-wide expression measurements simultaneously across multiple samples. Here an expanded set of 16 isobaric reagents based on an isobutyl-proline immonium ion reporter structure (TMTpro) is presented. These reagents h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::666c41bf415d89946ebabb2bac45a452
https://doi.org/10.1038/s41592-020-0781-4
https://doi.org/10.1038/s41592-020-0781-4
Autor:
Trey Ideker, J. Wade Harper, John J. Lee, Steven P. Gygi, Laura Pontano Vaites, Denis L. J. Lafontaine, Edward L. Huttlin, Erica Silva, Michael Chen, Jason F. Kreisberg, Casper F. Winsnes, Fan Zheng, Leah V. Schaffer, Gene W. Yeo, Tian Zhang, Wei Ouyang, Anna Bäckström, Katherine Licon, Jisoo Park, Jianzhu Ma, Emma Lundberg, Maya L. Gosztyla, Yue Qin, Steven M. Blue, Adriana Pitea, Sophie Liu, Ludivine Wacheul, Marcus R. Kelly
Publikováno v:
Nature, vol 600, iss 7889
Nature
Nature
The cell is a multi-scale structure with modular organization across at least four orders of magnitude(1). Two central approaches for mapping this structure—protein fluorescent imaging and protein biophysical association—each generate extensive d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e8d0c903c0d98dbe86f611fad1f98ee
https://escholarship.org/uc/item/9d15g18z
https://escholarship.org/uc/item/9d15g18z
Autor:
Joseph D Mancias, Laura Pontano Vaites, Sahar Nissim, Douglas E Biancur, Andrew J Kim, Xiaoxu Wang, Yu Liu, Wolfram Goessling, Alec C Kimmelman, J Wade Harper
Publikováno v:
eLife, Vol 4 (2015)
NCOA4 is a selective cargo receptor for the autophagic turnover of ferritin, a process critical for regulation of intracellular iron bioavailability. However, how ferritinophagy flux is controlled and the roles of NCOA4 in iron-dependent processes ar
Externí odkaz:
https://doaj.org/article/5af6e8d673d04762ad593f5eaec09092
Autor:
Andrea M. Dickey, William B. Redwine, J. Wade Harper, Monika Dzieciatkowska, Laura Pontano Vaites, Samara L. Reck-Peterson, Phuoc Tien Tran, Agnieszka A. Kendrick
Publikováno v:
The Journal of cell biology, vol 218, iss 9
The Journal of Cell Biology
The Journal of Cell Biology
Intracellular transport can be driven by unidirectional motors acting in opposing directions, but how bidirectional transport of cargo is regulated is unclear. Kendrick et al. show that the dynein-activating adaptor Hook3 interacts with the opposite-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2669214998474e72e833c6e863a139e2
https://doi.org/10.1083/jcb.201812170
https://doi.org/10.1083/jcb.201812170
Autor:
J. Wade Harper, Zuzana Storchova, Angelika Amon, Joao A. Paulo, Jonathan N. Wells, Stefano Santaguida, Laura Pontano Vaites, Joseph A. Marsh, Christopher M. Brennan
Publikováno v:
Brennan, C M, Vaites, L P, Wells, J N, Santaguida, S, Paulo, J A, Storchova, Z, Harper, J W, Marsh, J A & Amon, A 2019, ' Protein aggregation mediates stoichiometry of protein complexes in aneuploid cells ', Genes and Development, vol. 33, no. 15-16, pp. 1031-1047 . https://doi.org/10.1101/gad.327494.119
Aneuploidy, a condition characterized by chromosome gains and losses, causes reduced fitness and numerous cellular stresses, including increased protein aggregation. Here, we identify protein complex stoichiometry imbalances as a major cause of prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42dca479f57c0d40c4c87e4473653d02
https://doi.org/10.1101/gad.327494.119
https://doi.org/10.1101/gad.327494.119
Autor:
Steven P. Gygi, Michele Pagano, J. Wade Harper, Bearach Miwatani-Minter, Luca Lignitto, Joao A. Paulo, Laura Pontano Vaites, Colin O’Leary, Gergely Róna, Callie J Donahue, Elijah L. Mena, Beatrix Ueberheide, Avantika Dhabaria, Robert A. Davey, Jie Li, Stephen J. Elledge
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Understanding the functions of the genes encoded in the SARS-CoV-2 genome is imperative to understanding its pathogenesis. One unique feature of the SARS-CoV-2 genome is ORF10, a small putative protein that was hypothesized to promote in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d4ee40b11c4c97e115760b0e60ff890
https://doi.org/10.1073/pnas.2023157118
https://doi.org/10.1073/pnas.2023157118
Autor:
Zhenying Cai, Steven P. Gygi, Joao A. Paulo, Jiaming Li, Ning Shen, Dylan C. Mitchell, Edward L. Huttlin, Brian L. Harry, Laura Pontano Vaites
Publikováno v:
Mol Cell
Rapid protein degradation enables cells to quickly modulate protein abundance. Dysregulation of short-lived proteins plays essential roles in disease pathogenesis. A focused map of short-lived proteins remains understudied. Cycloheximide, a translati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d05e18d9d26c4657311d1de0aba2e1b
https://doi.org/10.1016/j.molcel.2021.09.015
https://doi.org/10.1016/j.molcel.2021.09.015
Autor:
Sharan Swarup, J. Wade Harper, Kejie Li, Gabriela Zarraga, Joe R. Cannon, Brian K. Erickson, John Szpyt, Robert A. Obar, Spyros Artavanis-Tsakonas, Ramin Rad, Steven P. Gygi, Laura Pontano-Vaites, Edward L. Huttlin, Lily Ting, Kurt Baltier, Joao A. Paulo, Melanie P. Gygi, Stanley Tam, Raphael J. Bruckner, Greg Colby, K. G. Guruharsha, Devin K. Schweppe, Fana Gebreab, Anne E. White, Hannah Parzen
Publikováno v:
Nature
The physiology of a cell can be viewed as the product of thousands of proteins acting in concert to shape the cellular response. Coordination is achieved in part through networks of protein-protein interactions that assemble functionally related prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b736553c07aad86555516af63f8c553
https://doi.org/10.1038/nature22366
https://doi.org/10.1038/nature22366
Autor:
Sipei Fu, Laura Pontano Vaites, Joe R. Cannon, Alexandra Panov, Ramin Rad, J. Wade Harper, Joshua Pan, Gabriela Zarraga, Sanjukta Guha Thakurta, Arvene Golbazi, Stanley Tam, Raphael J. Bruckner, Edward L. Huttlin, Hannah Parzen, John Szpyt, Keegan Stricker, David P. Nusinow, Joao A. Paulo, Devin K. Schweppe, Kurt Baltier, Melanie P. Gygi, Fana Gebreab, Eila Maenpaa, Alexandra Thornock, Steven P. Gygi, José Navarrete-Perea
SUMMARYThousands of interactions assemble proteins into modules that impart spatial and functional organization to the cellular proteome. Through affinity-purification mass spectrometry, we have created two proteome-scale, cell-line-specific interact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b92863dd46f2652ee366b11711fd786