Zobrazeno 1 - 10
of 167
pro vyhledávání: '"JOSEPH H. DAVIS"'
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-10 (2024)
Abstract AAA+ proteolytic machines unfold proteins before degrading them. Here, we present cryoEM structures of ClpXP-substrate complexes that reveal a postulated but heretofore unseen intermediate in substrate unfolding/degradation. A ClpX hexamer d
Externí odkaz:
https://doaj.org/article/30da034fd98e4f60aca290141a491821
Autor:
Alireza Ghanbarpour, Steven E. Cohen, Xue Fei, Laurel F. Kinman, Tristan A. Bell, Jia Jia Zhang, Tania A. Baker, Joseph H. Davis, Robert T. Sauer
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-10 (2023)
Abstract AAA+ proteases degrade intracellular proteins in a highly specific manner. E. coli ClpXP, for example, relies on a C-terminal ssrA tag or other terminal degron sequences to recognize proteins, which are then unfolded by ClpX and subsequently
Externí odkaz:
https://doaj.org/article/f72b46a348b247609e8481dbe950089a
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-9 (2022)
Abstract Spt-Ada-Gcn5-Acetyltransferase (SAGA) is a conserved multi-subunit complex that activates RNA polymerase II-mediated transcription by acetylating and deubiquitinating nucleosomal histones and by recruiting TATA box binding protein (TBP) to D
Externí odkaz:
https://doaj.org/article/bdaf52a87abe48e3938c902b224a46dc
Publikováno v:
IUCrJ, Vol 9, Iss 6, Pp 713-714 (2022)
Externí odkaz:
https://doaj.org/article/d42d5d5932c94100934fae1fd5add1ee
Publikováno v:
Proceedings of the National Academy of Sciences. 120
Energy-dependent protein degradation by the AAA+ ClpXP protease helps maintain protein homeostasis in bacteria and eukaryotic organelles of bacterial origin. In Escherichia coli and many other proteobacteria, the SspB adaptor assists ClpXP in degradi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c99c661cba77b1740c675dc851657765
https://doi.org/10.1073/pnas.2219044120
https://doi.org/10.1073/pnas.2219044120
Publikováno v:
Nature Protocols.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::474ab8f43c8c0c94a99e9a00ddccd43d
https://doi.org/10.1038/s41596-022-00763-x
https://doi.org/10.1038/s41596-022-00763-x
Energy-dependent protein degradation by the AAA+ClpXP protease helps maintain protein homeostasis in organisms ranging from simple bacteria to humans. InE. coliand many other proteobacteria, the SspB adaptor assists ClpXP in degrading ssrA-tagged pol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0c2cd7feb20105b424224b5838da8a6a
https://doi.org/10.1101/2022.11.06.515074
https://doi.org/10.1101/2022.11.06.515074
Autor:
Xue Fei, Joseph H. Davis, Tania Baker, Alireza Ghanbarpour, Tristan Bell, Steven Cohen, Robert Sauer
Intracellular proteases must be specific to avoid degrading the wrong proteins. Here, we present cryo-EM structures of E. coli ClpXP, a AAA+ protease, which reveal that the axial channel of ClpX is closed prior to the binding and subsequent transloca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::45eb165b98c0d662593c5f582c758d7c
https://doi.org/10.1101/2022.08.27.505532
https://doi.org/10.1101/2022.08.27.505532
Publikováno v:
The Journal of Financial Data Science. 3:9-20
Predicting long-term equity market returns is of great importance for investors to strategically allocate their assets. The authors explore machine learning (ML) methods to forecast 10-year-ahead US stock returns and compare the results with the trad
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0bd61a40bed61ccc2205e72b0ad3b059
https://doi.org/10.3905/jfds.2021.3.2.009
https://doi.org/10.3905/jfds.2021.3.2.009
Publikováno v:
Nature methods
PMC
PMC
Cryo-electron microscopy (cryo-EM) single-particle analysis has proven powerful in determining the structures of rigid macromolecules. However, many imaged protein complexes exhibit conformational and compositional heterogeneity that poses a major ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa85ac033ea2fcf332a11a77120020f7
https://doi.org/10.1038/s41592-020-01049-4
https://doi.org/10.1038/s41592-020-01049-4