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Leah Randles

Showing results (1-10 of 9) with videos related to

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Frontiers in Bioscience (Landmark Edition)|June 2, 2012
Ubiquitin and its binding domainsLeah Randles, Kylie J Walters
The Journal of Biological Chemistry|February 25, 2016
The Proteasome Ubiquitin Receptor hRpn13 and Its Interacting Deubiquitinating Enzyme Uch37 Are Required for Proper Cell Cycle ProgressionLeah Randles, Ravi K Anchoori, Richard B S Roden, et al.
Structure (London, England : 1993)|July 12, 2016
Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the ProteasomeXiang Chen, Leah Randles, Ke Shi, et al.
Proteins|December 10, 2015
Mycobacterium tuberculosis copper-regulated protein SocB is an intrinsically disordered protein that folds upon interaction with a synthetic phospholipid bilayerUrszula Nowicka, Morgan Hoffman, Leah Randles, et al.
Nature|May 24, 2008
Proteasome subunit Rpn13 is a novel ubiquitin receptorKoraljka Husnjak, Suzanne Elsasser, Naixia Zhang, et al.
BMC Structural Biology|November 17, 2012
MTMDAT-HADDOCK: high-throughput, protein complex structure modeling based on limited proteolysis and mass spectrometryJanosch Hennig, Sjoerd J de Vries, Klaus Dm Hennig, et al.
Nature|May 24, 2008
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interactionPatrick Schreiner, Xiang Chen, Koraljka Husnjak, et al.
Molecular Cell|August 18, 2009
Structure of the s5a:k48-linked diubiquitin complex and its interactions with rpn13Naixia Zhang, Qinghua Wang, Aaron Ehlinger, et al.
Nature Communications|June 10, 2017
Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targetsXiuxiu Lu, Urszula Nowicka, Vinidhra Sridharan, et al.
Pageof 1

Showing results (1-10 of 9) with videos related to

Sort By:
Pageof 1
Frontiers in Bioscience (Landmark Edition)|June 2, 2012
Ubiquitin and its binding domainsLeah Randles, Kylie J Walters
The Journal of Biological Chemistry|February 25, 2016
The Proteasome Ubiquitin Receptor hRpn13 and Its Interacting Deubiquitinating Enzyme Uch37 Are Required for Proper Cell Cycle ProgressionLeah Randles, Ravi K Anchoori, Richard B S Roden, et al.
Structure (London, England : 1993)|July 12, 2016
Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the ProteasomeXiang Chen, Leah Randles, Ke Shi, et al.
Proteins|December 10, 2015
Mycobacterium tuberculosis copper-regulated protein SocB is an intrinsically disordered protein that folds upon interaction with a synthetic phospholipid bilayerUrszula Nowicka, Morgan Hoffman, Leah Randles, et al.
Nature|May 24, 2008
Proteasome subunit Rpn13 is a novel ubiquitin receptorKoraljka Husnjak, Suzanne Elsasser, Naixia Zhang, et al.
BMC Structural Biology|November 17, 2012
MTMDAT-HADDOCK: high-throughput, protein complex structure modeling based on limited proteolysis and mass spectrometryJanosch Hennig, Sjoerd J de Vries, Klaus Dm Hennig, et al.
Nature|May 24, 2008
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interactionPatrick Schreiner, Xiang Chen, Koraljka Husnjak, et al.
Molecular Cell|August 18, 2009
Structure of the s5a:k48-linked diubiquitin complex and its interactions with rpn13Naixia Zhang, Qinghua Wang, Aaron Ehlinger, et al.
Nature Communications|June 10, 2017
Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targetsXiuxiu Lu, Urszula Nowicka, Vinidhra Sridharan, et al.
Pageof 1