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Journal Articles (Chemistry)
Items in this Collection
- 3Macauley, Matthew S.
- 2Errington, Wesley J.
- 2Mackereth, Cameron D.
- 2Schärpf, Manuela
- 1Blaszczak, Adam G.
- 1Chin, Danielle
- 3Crystal-Structure
- 2Backbone Dynamics
- 1Alzheimers-Disease
- 1Beta-D-Glucosaminidase
- 1Binding
- 1Conjugation
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Beads-on-a-string, characterization of ETS-1 sumoylated within its flexible N-terminal sequence
Download2006
Mackereth, Cameron D., Graves, Barbara J., Macauley, Matthew S., Schärpf, Manuela, McIntosh, Lawrence P. , Blaszczak, Adam G., Errington, Wesley J.
Sumoylation regulates the activities of several members of the ETS transcription factor family. To provide a molecular framework for understanding this regulation, we have characterized the conjugation of Ets-1 with SUMO-1. Ets-1 is modified in vivo predominantly at a consensus sumoylation motif...
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O-GlcNAcase uses substrate-assisted catalysis Kinetic analysis and development of highly selective mechanism-inspired inhibitors
Download2005
Vocadlo, David J., Whitworth, Garrett E., Macauley, Matthew S., Debowski, Aleksandra W., Chin, Danielle
The post-translational modification of serine and threonine residues of nucleocytoplasmic proteins with 2-acetamido-2-deoxy-d-glucopyranose (GlcNAc) is a reversible process implicated in multiple cellular processes. The enzyme O-GlcNAcase catalyzes the cleavage of β-O-linked GlcNAc (O-GlcNAc)...
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2004
Okon, Mark, Schulman, Brenda A., Macauley, Matthew S., McIntosh, Lawrence P., Mackereth, Cameron D., Schärpf, Manuela, Errington, Wesley J.
Although sumoylation regulates a diverse and growing number of recognized biological processes, the molecular mechanisms by which the covalent attachment of the ubiquitin-like protein SUMO can alter the properties of a target protein remain to be established. To address this question, we have...