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Opposing roles of Ubp3‐dependent deubiquitination regulate replicative life span and heat resistance
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/yea.1142openalex-snapshot
A versatile toolbox for PCR‐based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes
inferredcites →https://doi.org/10.1007/978-1-61779-474-2_35openalex-snapshot
Use of CPY* and Its Derivatives to Study Protein Quality Control in Various Cell Compartments
inferredcites →https://doi.org/10.1007/s002940050354openalex-snapshot
Isolation of UBP3, encoding a de-ubiquitinating enzyme, as a multicopy suppressor of a heat-shock mutant strain of S. cerevisiae
inferredcites →https://doi.org/10.1016/0076-6879(91)94004-vopenalex-snapshot
Getting started with yeast
inferredcites →https://doi.org/10.1016/j.bbamcr.2004.10.003openalex-snapshot
Mechanism and function of deubiquitinating enzymes
inferredcites →https://doi.org/10.1016/j.cell.2004.11.027openalex-snapshot
Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation through the Central Pore of ClpB
inferredcites →https://doi.org/10.1016/j.cell.2007.10.047openalex-snapshot
Atypical AAA+ Subunit Packing Creates an Expanded Cavity for Disaggregation by the Protein-Remodeling Factor Hsp104
inferredcites →https://doi.org/10.1016/j.febslet.2008.11.015openalex-snapshot
Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1
inferredcites →https://doi.org/10.1016/j.femsyr.2004.05.008openalex-snapshot
The role of respiration, reactive oxygen species and oxidative stress in mother cell-specific ageing of yeast strains defective in the signalling pathway
inferredcites →https://doi.org/10.1016/j.jmb.2007.04.070openalex-snapshot
Processing of Proteins by the Molecular Chaperone Hsp104
inferredcites →https://doi.org/10.1016/j.molcel.2008.04.018openalex-snapshot
Reversal of RNA Polymerase II Ubiquitylation by the Ubiquitin Protease Ubp3
inferredcites →https://doi.org/10.1016/j.yexcr.2010.09.005openalex-snapshot
The Rsp5 ubiquitin ligase and the AAA-ATPase Cdc48 control the ubiquitin-mediated degradation of the COPII component Sec23
inferredcites →https://doi.org/10.1016/s0021-9258(18)50100-9openalex-snapshot
Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family
inferredcites →https://doi.org/10.1016/s0076-6879(02)50985-xopenalex-snapshot
Use of two-dimensional gels in yeast proteomics
inferredcites →https://doi.org/10.1016/s0076-6879(03)70001-9openalex-snapshot
Construction, Purification, and Characterization of Escherichia coli RNA Polymerases Tagged with Different Fluorescent Proteins
inferredcites →https://doi.org/10.1016/s0092-8674(00)80139-7openalex-snapshot
A Deubiquitinating Enzyme Interacts with SIR4 and Regulates Silencing in S. cerevisiae
inferredcites →https://doi.org/10.1016/s0092-8674(00)81223-4openalex-snapshot
Hsp104, Hsp70, and Hsp40
inferredcites →https://doi.org/10.1016/s1046-2023(05)80158-6openalex-snapshot
Overview of manual and automated DNA sequencing by the dideoxy chain termination method
inferredcites →https://doi.org/10.1016/s1097-2765(02)00638-xopenalex-snapshot
Multiple Associated Proteins Regulate Proteasome Structure and Function
inferredcites →https://doi.org/10.1038/198403a0openalex-snapshot
Radioprotection of Mice by Hypoxia and Chemical Agents
inferredcites →https://doi.org/10.1038/nature01071openalex-snapshot
A cryptic protease couples deubiquitination and degradation by the proteasome
inferredcites →https://doi.org/10.1038/nature07195openalex-snapshot
Misfolded proteins partition between two distinct quality control compartments
inferredcites →https://doi.org/10.1038/ncb1003openalex-snapshot
Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23
inferredcites →https://doi.org/10.1038/ncb1723openalex-snapshot
Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
inferredcites →https://doi.org/10.1038/nmeth.1697openalex-snapshot
Firefly luciferase mutants as sensors of proteome stress
inferredcites →https://doi.org/10.1038/sj.embor.7400164openalex-snapshot
A genomic screen identifies Dsk2p and Rad23p as essential components of ER‐associated degradation
inferredcites →https://doi.org/10.1042/bj20101152openalex-snapshot
Transcriptional activation requires protection of the TATA-binding protein Tbp1 by the ubiquitin-specific protease Ubp3
inferredcites →https://doi.org/10.1073/pnas.1205829109openalex-snapshot
Compartmentalization of superoxide dismutase 1 (SOD1G93A) aggregates determines their toxicity
inferredcites →https://doi.org/10.1073/pnas.1216778110openalex-snapshot
Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins
inferredcites →https://doi.org/10.1074/jbc.271.17.10263openalex-snapshot
Rapid Identification of Yeast Proteins on Two-dimensional Gels
inferredcites →https://doi.org/10.1074/jbc.271.42.25790openalex-snapshot
A Yeast Ubc9 Mutant Protein with Temperature-sensitive in Vivo Function Is Subject to Conditional Proteolysis by a Ubiquitin- and Proteasome-dependent Pathway
inferredcites →https://doi.org/10.1074/jbc.m110.170175openalex-snapshot
Yeast Deubiquitinase Ubp3 Interacts with the 26 S Proteasome to Facilitate Rad4 Degradation
inferredcites →https://doi.org/10.1074/jbc.m112.449751openalex-snapshot
Ras Protein/cAMP-dependent Protein Kinase Signaling Is Negatively Regulated by a Deubiquitinating Enzyme, Ubp3, in Yeast
inferredcites →https://doi.org/10.1074/jbc.m410085200openalex-snapshot
Rpn4 Is a Physiological Substrate of the Ubr2 Ubiquitin Ligase
inferredcites →https://doi.org/10.1080/10409239891204251openalex-snapshot
Deubiquitinating Enzymes: A New Class of Biological Regulators
inferredcites →https://doi.org/10.1083/jcb.143.7.1883openalex-snapshot
Aggresomes: A Cellular Response to Misfolded Proteins
inferredcites →https://doi.org/10.1083/jcb.201106037openalex-snapshot
Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1083/jcb.201201074openalex-snapshot
Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation
inferredcites →https://doi.org/10.1091/mbc.e06-04-0338openalex-snapshot
The Cytoplasmic Hsp70 Chaperone Machinery Subjects Misfolded and Endoplasmic Reticulum Import-incompetent Proteins to Degradation via the Ubiquitin–Proteasome System
inferredcites →https://doi.org/10.1091/mbc.e12-03-0194openalex-snapshot
Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates
inferredcites →https://doi.org/10.1093/genetics/162.3.1079openalex-snapshot
The Yeast Ubiquitin Protease, Ubp3p, Promotes Protein Stability
inferredcites →https://doi.org/10.1099/vir.0.012179-0openalex-snapshot
Degradation and aggresome formation of the Gn tail of the apathogenic Tula hantavirus
inferredcites →https://doi.org/10.1101/gad.13.19.2570openalex-snapshot
The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
inferredcites →https://doi.org/10.1101/gad.439307openalex-snapshot
Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p
inferredcites →https://doi.org/10.1126/science.1075898openalex-snapshot
Role of Rpn11 Metalloprotease in Deubiquitination and Degradation by the 26 S Proteasome
inferredcites →https://doi.org/10.1128/mcb.7.7.2568-2577.1987openalex-snapshot
Complex Interactions Among Members of an Essential Subfamily of hsp70 Genes in Saccharomyces Cerevisiae
inferredcites →https://doi.org/10.1371/journal.pgen.1002253openalex-snapshot
Elevated Proteasome Capacity Extends Replicative Lifespan in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1515/bc.2000.121openalex-snapshot
Analysis of the Deubiquitinating Enzymes of the Yeast Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1534/genetics.108.094524openalex-snapshot
Disruption of Rpn4-Induced Proteasome Expression in Saccharomyces cerevisiae Reduces Cell Viability Under Stressed Conditions
inferredcites →https://doi.org/10.1534/genetics.109.106229openalex-snapshot
The Mother Enrichment Program: A Genetic System for Facile Replicative Life Span Analysis in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.18632/aging.100613openalex-snapshot
Enhancing protein disaggregation restores proteasome activity in aged cells
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Role of J-Domain Proteins in Yeast Physiology and Protein Quality Control
inferred← citeshttps://doi.org/10.1002/bies.201400208openalex-snapshot
The dual role of a yeast metacaspase: What doesn't kill you makes you stronger
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UPS Activation in the Battle Against Aging and Aggregation-Related Diseases: An Extended Review
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Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease
inferred← citeshttps://doi.org/10.1007/s00294-016-0596-0openalex-snapshot
Protein aggregation as a mechanism of adaptive cellular responses
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Dysregulated proteostasis
inferred← citeshttps://doi.org/10.1016/j.arr.2014.12.003openalex-snapshot
Proteasome activation: An innovative promising approach for delaying aging and retarding age-related diseases
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2019.02.015openalex-snapshot
Nuclear proteasomal degradation of Saccharomyces cerevisiae inorganic pyrophosphatase Ipp1p, a nucleocytoplasmic protein whose stability depends on its subcellular localization
inferred← citeshttps://doi.org/10.1016/j.bbrc.2017.03.059openalex-snapshot
Molecular chaperones of the Hsp70 family assist in the assembly of 20S proteasomes
inferred← citeshttps://doi.org/10.1016/j.cell.2016.05.006openalex-snapshot
Lifespan Control by Redox-Dependent Recruitment of Chaperones to Misfolded Proteins
inferred← citeshttps://doi.org/10.1016/j.celrep.2016.06.016openalex-snapshot
Asymmetric Inheritance of Aggregated Proteins and Age Reset in Yeast Are Regulated by Vac17-Dependent Vacuolar Functions
inferred← citeshttps://doi.org/10.1016/j.celrep.2021.109328openalex-snapshot
An Hsp90 co-chaperone links protein folding and degradation and is part of a conserved protein quality control
inferred← citeshttps://doi.org/10.1016/j.celrep.2023.113372openalex-snapshot
Calmodulin regulates protease versus co-chaperone activity of a metacaspase
inferred← citeshttps://doi.org/10.1016/j.jbc.2021.100348openalex-snapshot
Deubiquitinase Ubp3 enhances the proteasomal degradation of key enzymes in sterol homeostasis
inferred← citeshttps://doi.org/10.1016/j.jbc.2022.102476openalex-snapshot
Using reporters of different misfolded proteins reveals differential strategies in processing protein aggregates
inferred← citeshttps://doi.org/10.1016/j.jbc.2022.102680openalex-snapshot
Differential contributions of the proteasome, autophagy, and chaperones to the clearance of arsenite-induced protein aggregates in yeast
inferred← citeshttps://doi.org/10.1016/j.jmb.2024.168484openalex-snapshot
Role of J-domain Proteins in Yeast Physiology and Protein Quality Control
inferred← citeshttps://doi.org/10.1016/j.tibs.2017.08.002openalex-snapshot
There Is an Inclusion for That: Material Properties of Protein Granules Provide a Platform for Building Diverse Cellular Functions
inferred← citeshttps://doi.org/10.1038/ncomms12907openalex-snapshot
Deubiquitinase activity is required for the proteasomal degradation of misfolded cytosolic proteins upon heat-stress
inferred← citeshttps://doi.org/10.1038/s41598-018-31726-6openalex-snapshot
High-Reynolds Microfluidic Sorting of Large Yeast Populations
inferred← citeshttps://doi.org/10.1038/s41598-023-41188-0openalex-snapshot
The yeast guanine nucleotide exchange factor Sec7 is a bottleneck in spatial protein quality control and detoxifies neurological disease proteins
inferred← citeshttps://doi.org/10.1039/bk9781839165986-00001openalex-snapshot
Introduction: Molecular Chaperones and Protein Quality Control
inferred← citeshttps://doi.org/10.1042/ebc20160085openalex-snapshot
How and why do toxic conformers of aberrant proteins accumulate during ageing?
inferred← citeshttps://doi.org/10.1073/pnas.1324035111openalex-snapshot
Dynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentin
inferred← citeshttps://doi.org/10.1073/pnas.1412504111openalex-snapshot
Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1
inferred← citeshttps://doi.org/10.1073/pnas.2020997118openalex-snapshot
Nuclear envelope budding is a response to cellular stress
inferred← citeshttps://doi.org/10.1091/mbc.e13-10-0591openalex-snapshot
Loss of Ubp3 increases silencing, decreases unequal recombination in rDNA, and shortens the replicative life span inSaccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1091/mbc.e15-10-0697openalex-snapshot
Cytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeast
inferred← citeshttps://doi.org/10.1091/mbc.e25-01-0027openalex-snapshot
Hsp70 chaperones, Ssa1 and Ssa2, limit poly(A) binding protein aggregation
inferred← citeshttps://doi.org/10.1091/mbc.e25-10-0479openalex-snapshot
Yeast ribosomal protein Rpl32 modulates ribosome biogenesis, ribosome stability and the cell cycle #
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The structure and function of deubiquitinases: lessons from budding yeast
inferred← citeshttps://doi.org/10.1101/gad.287474.116openalex-snapshot
The pleiotropic deubiquitinase Ubp3 confers aneuploidy tolerance
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Alternative systems for misfolded protein clearance: life beyond the proteasome
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Protein aggregation: A detrimental symptom or an adaptation mechanism?
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Life-span extension by a metacaspase in the yeast Saccharomyces cerevisiae
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iPAR: a new reporter for eukaryotic cytoplasmic protein aggregation
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Evolution of Robustness to Protein Mistranslation by Accelerated Protein Turnover
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Essential Genetic Interactors of SIR2 Required for Spatial Sequestration and Asymmetrical Inheritance of Protein Aggregates
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Differential role of cytosolic Hsp70s in longevity assurance and protein quality control
inferred← citeshttps://doi.org/10.1371/journal.pone.0232755openalex-snapshot
The degradation-promoting roles of deubiquitinases Ubp6 and Ubp3 in cytosolic and ER protein quality control
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Restricted access: spatial sequestration of damaged proteins during stress and aging
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Insights into the Role of P-Bodies and Stress Granules in Protein Quality Control
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Balanced activities of Hsp70 and the ubiquitin proteasome system underlie cellular protein homeostasis
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Studying Spatial Protein Quality Control, Proteopathies, and Aging Using Different Model Misfolding Proteins in S. cerevisiae
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Protein aggregates are associated with replicative aging without compromising protein quality control
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