Allosteric Activation of the Ubiquitin ligase UBR 1 by Short Peptides: Molecular Mechanisms and Physiological Functions

Allosteric Activation of the Ubiquitin ligase UBR 1 by Short Peptides: Molecular Mechanisms and Physiological Functions

<p>The N-end rule relates the in vivo half life of a protein to the identity of its N-terminal residue. UBR1, the E3 of the N-end rule pathway in Sacchnromzyces cerevisiae, targets proteins that bear destabilizing N-terminal residues for Ub-dependent, processive degradation. UBR1 binds prot...

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Bibliographic Details
Main Author: Du, Fangyong
Format: Others
Published: 2002
Online Access:https://thesis.library.caltech.edu/6830/1/Du_f_2002.pdf
Du, Fangyong (2002) Allosteric Activation of the Ubiquitin ligase UBR 1 by Short Peptides: Molecular Mechanisms and Physiological Functions. Dissertation (Ph.D.), California Institute of Technology. doi:10.7907/S3VT-0641. https://resolver.caltech.edu/CaltechTHESIS:02232012-110128910 <https://resolver.caltech.edu/CaltechTHESIS:02232012-110128910>

Internet

https://thesis.library.caltech.edu/6830/1/Du_f_2002.pdf
Du, Fangyong (2002) Allosteric Activation of the Ubiquitin ligase UBR 1 by Short Peptides: Molecular Mechanisms and Physiological Functions. Dissertation (Ph.D.), California Institute of Technology. doi:10.7907/S3VT-0641. https://resolver.caltech.edu/CaltechTHESIS:02232012-110128910 <https://resolver.caltech.edu/CaltechTHESIS:02232012-110128910>

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