Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

Ronald T Hay

Showing results (11-20 of 130) with videos related to

Pageof 13
Sort By:
Methods in Enzymology|March 10, 2019
Methods to analyze STUbL activityEmma Branigan, Anna Plechanovová, Ronald T Hay
Nature Methods|August 1, 2012
Reanalysis of phosphoproteomics data uncovers ADP-ribosylation sitesIvan Matic, Ivan Ahel, Ronald T Hay
Biophysical Chemistry|March 27, 2004
Hydrodynamic bead modelling of the 2:1 p50-IkappaBgamma complexMichaela Smolle, Ronald T Hay, Olwyn Byron
Nature Communications|June 7, 2020
Ubiquitin transfer by a RING E3 ligase occurs from a closed E2~ubiquitin conformationEmma Branigan, J Carlos Penedo, Ronald T Hay
Biochemistry|March 19, 2003
Role of two residues proximal to the active site of Ubc9 in substrate recognition by the Ubc9.SUMO-1 thiolester complexMichael H Tatham, Yuan Chen, Ronald T Hay
Molecular Biology of the Cell|December 15, 2010
The SUMO protease SENP6 is a direct regulator of PML nuclear bodiesNeil Hattersley, Linnan Shen, Ellis G Jaffray, et al.
Science Signaling|July 9, 2015
Proteotoxic stress reprograms the chromatin landscape of SUMO modificationAnne Seifert, Pietà Schofield, Geoffrey J Barton, et al.
Seminars in Cell & Developmental Biology|June 24, 2004
SUMO and transcriptional regulationDavid W H Girdwood, Michael H Tatham, Ronald T Hay
Science Signaling|June 23, 2011
Comparative proteomic analysis identifies a role for SUMO in protein quality controlMichael H Tatham, Ivan Matic, Matthias Mann, et al.
Nature Protocols|May 1, 2010
High-stringency tandem affinity purification of proteins conjugated to ubiquitin-like moietiesFilip Golebiowski, Michael H Tatham, Akihiro Nakamura, et al.
Pageof 13

Showing results (11-20 of 130) with videos related to

Sort By:
Pageof 13
Methods in Enzymology|March 10, 2019
Methods to analyze STUbL activityEmma Branigan, Anna Plechanovová, Ronald T Hay
Nature Methods|August 1, 2012
Reanalysis of phosphoproteomics data uncovers ADP-ribosylation sitesIvan Matic, Ivan Ahel, Ronald T Hay
Biophysical Chemistry|March 27, 2004
Hydrodynamic bead modelling of the 2:1 p50-IkappaBgamma complexMichaela Smolle, Ronald T Hay, Olwyn Byron
Nature Communications|June 7, 2020
Ubiquitin transfer by a RING E3 ligase occurs from a closed E2~ubiquitin conformationEmma Branigan, J Carlos Penedo, Ronald T Hay
Biochemistry|March 19, 2003
Role of two residues proximal to the active site of Ubc9 in substrate recognition by the Ubc9.SUMO-1 thiolester complexMichael H Tatham, Yuan Chen, Ronald T Hay
Molecular Biology of the Cell|December 15, 2010
The SUMO protease SENP6 is a direct regulator of PML nuclear bodiesNeil Hattersley, Linnan Shen, Ellis G Jaffray, et al.
Science Signaling|July 9, 2015
Proteotoxic stress reprograms the chromatin landscape of SUMO modificationAnne Seifert, Pietà Schofield, Geoffrey J Barton, et al.
Seminars in Cell & Developmental Biology|June 24, 2004
SUMO and transcriptional regulationDavid W H Girdwood, Michael H Tatham, Ronald T Hay
Science Signaling|June 23, 2011
Comparative proteomic analysis identifies a role for SUMO in protein quality controlMichael H Tatham, Ivan Matic, Matthias Mann, et al.
Nature Protocols|May 1, 2010
High-stringency tandem affinity purification of proteins conjugated to ubiquitin-like moietiesFilip Golebiowski, Michael H Tatham, Akihiro Nakamura, et al.
Pageof 13