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David Fushman

Showing results (111-120 of 123) with videos related to

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Bioscience Reports|July 17, 2015
Base-CP proteasome can serve as a platform for stepwise lid formationZanlin Yu, Nurit Livnat-Levanon, Oded Kleifeld, et al.
Genes & Development|November 9, 2019
Crosstalk between Lys63- and Lys11-polyubiquitin signaling at DNA damage sites is driven by CezanneXiao Wu, Shichang Liu, Cari Sagum, et al.
Science (New York, N.Y.)|October 2, 2004
Ubistatins inhibit proteasome-dependent degradation by binding the ubiquitin chainRati Verma, Noel R Peters, Mariapina D'Onofrio, et al.
Plos One|October 27, 2010
Perturbing the ubiquitin pathway reveals how mitosis is hijacked to denucleate and regulate cell proliferation and differentiation in vivoAndrea Caceres, Fu Shang, Eric Wawrousek, et al.
Elife|November 11, 2021
Branched ubiquitin chain binding and deubiquitination by UCH37 facilitate proteasome clearance of stress-induced inclusionsAixin Song, Zachary Hazlett, Dulith Abeykoon, et al.
Biorxiv : the Preprint Server for Biology|May 13, 2022
Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitinPawel M Wydorski, Jerzy Osipiuk, Benjamin T Lanham, et al.
Nature Communications|May 15, 2023
Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitinPawel M Wydorski, Jerzy Osipiuk, Benjamin T Lanham, et al.
Cell Chemical Biology|March 24, 2017
Polyubiquitin-Photoactivatable Crosslinking Reagents for Mapping Ubiquitin Interactome Identify Rpn1 as a Proteasome Ubiquitin-Associating SubunitMichal Chojnacki, Wissam Mansour, Dharjath S Hameed, et al.
Nature Chemistry|June 12, 2019
De novo macrocyclic peptides that specifically modulate Lys48-linked ubiquitin chainsMickal Nawatha, Joseph M Rogers, Steven M Bonn, et al.
Science Advances|September 24, 2021
Ubiquitin is a carbon dioxide-binding proteinVictoria L Linthwaite, Wes Pawloski, Hamish B Pegg, et al.
Pageof 13

Showing results (111-120 of 123) with videos related to

Sort By:
Pageof 13
Bioscience Reports|July 17, 2015
Base-CP proteasome can serve as a platform for stepwise lid formationZanlin Yu, Nurit Livnat-Levanon, Oded Kleifeld, et al.
Genes & Development|November 9, 2019
Crosstalk between Lys63- and Lys11-polyubiquitin signaling at DNA damage sites is driven by CezanneXiao Wu, Shichang Liu, Cari Sagum, et al.
Science (New York, N.Y.)|October 2, 2004
Ubistatins inhibit proteasome-dependent degradation by binding the ubiquitin chainRati Verma, Noel R Peters, Mariapina D'Onofrio, et al.
Plos One|October 27, 2010
Perturbing the ubiquitin pathway reveals how mitosis is hijacked to denucleate and regulate cell proliferation and differentiation in vivoAndrea Caceres, Fu Shang, Eric Wawrousek, et al.
Elife|November 11, 2021
Branched ubiquitin chain binding and deubiquitination by UCH37 facilitate proteasome clearance of stress-induced inclusionsAixin Song, Zachary Hazlett, Dulith Abeykoon, et al.
Biorxiv : the Preprint Server for Biology|May 13, 2022
Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitinPawel M Wydorski, Jerzy Osipiuk, Benjamin T Lanham, et al.
Nature Communications|May 15, 2023
Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitinPawel M Wydorski, Jerzy Osipiuk, Benjamin T Lanham, et al.
Cell Chemical Biology|March 24, 2017
Polyubiquitin-Photoactivatable Crosslinking Reagents for Mapping Ubiquitin Interactome Identify Rpn1 as a Proteasome Ubiquitin-Associating SubunitMichal Chojnacki, Wissam Mansour, Dharjath S Hameed, et al.
Nature Chemistry|June 12, 2019
De novo macrocyclic peptides that specifically modulate Lys48-linked ubiquitin chainsMickal Nawatha, Joseph M Rogers, Steven M Bonn, et al.
Science Advances|September 24, 2021
Ubiquitin is a carbon dioxide-binding proteinVictoria L Linthwaite, Wes Pawloski, Hamish B Pegg, et al.
Pageof 13