Unknown

Dataset Information

0

All change: protein conformation and the ubiquitination reaction cascade.


ABSTRACT: The structures of enzymes that collectively modify proteins by covalent addition of ubiquitin-like protein moieties have provided significant insights into the regulatory pathways they compose and have highlighted the importance of protein flexibility for the mechanism and regulation of the ubiquitination reaction.

SUBMITTER: Riedinger C 

PROVIDER: S-EPMC2920667 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

All change: protein conformation and the ubiquitination reaction cascade.

Riedinger Christiane C   Endicott Jane A JA  

F1000 biology reports 20090317


The structures of enzymes that collectively modify proteins by covalent addition of ubiquitin-like protein moieties have provided significant insights into the regulatory pathways they compose and have highlighted the importance of protein flexibility for the mechanism and regulation of the ubiquitination reaction. ...[more]

Similar Datasets

| S-EPMC4652583 | biostudies-literature
| S-EPMC1134202 | biostudies-other
| S-EPMC7094371 | biostudies-literature
| S-EPMC1184849 | biostudies-other
| S-EPMC2770613 | biostudies-literature
| S-EPMC5936888 | biostudies-literature
| S-EPMC1432123 | biostudies-literature
| S-EPMC3859641 | biostudies-literature
| S-EPMC2717260 | biostudies-literature
| S-EPMC5052792 | biostudies-literature