ArticleThe Journal of biological chemistry2009
ATP-dependent proteases differ substantially in their ability to unfold globular proteins.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed.
- Protein Fragments: From Biomarkers to Therapeutic Targets-A Focus on α1-Antitrypsin-Derived Peptides.Mediators of inflammation · 2026Review
- Lipid bilayer properties govern substrate engagement and extraction by the AAA+ ATPase Msp1.The Journal of biological chemistry · 2025Article
- An automated positive selection screen in yeast provides support for boron-containing compounds as inhibitors of SARS-CoV-2 main protease.Microbiology spectrum · 2024Article
- The AAA+ protein Msp1 recognizes substrates by a hydrophobic mismatch.bioRxiv : the preprint server for biology · 2024Article
- Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease.Cell reports · 2023Article
- Substrate-specific effects of natural genetic variation on proteasome activity.PLoS genetics · 2023Article
- FtsH degrades kinetically stable dimers of cyclopropane fatty acid synthase via an internal degron.Molecular microbiology · 2023Article
- Single molecule microscopy reveals diverse actions of substrate sequences that impair ClpX AAA+ ATPase function.The Journal of biological chemistry · 2022Article
- Identification of Potential Cytokinin Responsive Key Genes in Rice Treated With Trans-Zeatin Through Systems Biology Approach.Frontiers in genetics · 2021Article
- Mode of targeting to the proteasome determines GFP fate.The Journal of biological chemistry · 2020Article
- Multistep substrate binding and engagement by the AAA+ ClpXP protease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Phage-EncodedViruses · 2020Article
- The proteasome 19S cap and its ubiquitin receptors provide a versatile recognition platform for substrates.Nature communications · 2020Article
- Ubiquitin receptors are required for substrate-mediated activation of the proteasome's unfolding ability.Scientific reports · 2019Article
- Proteolysis mediated by the membrane-integrated ATP-dependent protease FtsH has a unique nonlinear dependence on ATP hydrolysis rates.Protein science : a publication of the Protein Society · 2019Article
- Regulated Proteolysis in Bacteria.Annual review of biochemistry · 2018Review
- Folding-Degradation Relationship of a Membrane Protein Mediated by the Universally Conserved ATP-Dependent Protease FtsH.Journal of the American Chemical Society · 2018Article
- The C-Terminal Region of Bacillus subtilis SwrA Is Required for Activity and Adaptor-Dependent LonA Proteolysis.Journal of bacteriology · 2018Article
- Effect of directional pulling on mechanical protein degradation by ATP-dependent proteolytic machines.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Posttranslational control of the scaffold for Fe-S cluster biogenesis as a compensatory regulatory mechanism.Current genetics · 2017Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
ATP-dependent proteases control the concentrations of hundreds of regulatory proteins and remove damaged or misfolded proteins from cells. They select their substrates primarily by recognizing sequence motifs or covalent modifications. Once a substrate is bound to the protease, it has to be unfolded and translocated into the proteolytic chamber to be degraded. Some proteases appear to be promiscuous, degrading substrates with poorly defined targeting signals, which suggests that selectivity may be controlled at additional levels. Here we compare the abilities of representatives from all classes of ATP-dependent proteases to unfold a model substrate protein and find that the unfolding abilities range over more than 2 orders of magnitude. We propose that these differences in unfolding abilities contribute to the fates of substrate proteins and may act as a further layer of selectivity during protein destruction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.