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Title
How the 26S Proteasome Degrades Ubiquitinated Proteins in the Cell
Authors
Keywords
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Journal
Biomolecules
Volume 9, Issue 9, Pages 395
Publisher
MDPI AG
Online
2019-08-23
DOI
10.3390/biom9090395
References
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Related references
Note: Only part of the references are listed.- Structural Snapshots of 26S Proteasome Reveal Tetraubiquitin-Induced Conformations
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- Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome
- (2018) Yuanchen Dong et al. NATURE
- Substrate-engaged 26S proteasome structures reveal mechanisms for ATP-hydrolysis–driven translocation
- (2018) Andres H. de la Peña et al. SCIENCE
- In Vivo Ubiquitin Linkage-type Analysis Reveals that the Cdc48-Rad23/Dsk2 Axis Contributes to K48-Linked Chain Specificity of the Proteasome
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- Proteasomes tether to two distinct sites at the nuclear pore complex
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- Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing
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- Structure of a AAA+ unfoldase in the process of unfolding substrate
- (2017) Zev A Ripstein et al. eLife
- Structural basis of protein translocation by the Vps4-Vta1 AAA ATPase
- (2017) Nicole Monroe et al. eLife
- Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase
- (2017) Célia Deville et al. Science Advances
- An assay for 26S proteasome activity based on fluorescence anisotropy measurements of dye-labeled protein substrates
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- Conserved Sequence Preferences Contribute to Substrate Recognition by the Proteasome
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- A molecular census of 26S proteasomes in intact neurons
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- Synthetic biology approach to reconstituting the ubiquitylation cascade in bacteria
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- Monoubiquitination of RPN10 Regulates Substrate Recruitment to the Proteasome
- (2010) Marta Isasa et al. MOLECULAR CELL
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