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The spatial and temporal organization of ubiquitin networks
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Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/j.1460-2075.1988.tb03158.xopenalex-snapshot
Immunoelectron microscopic localization of ubiquitin in hepatoma cells.
inferredcites →https://doi.org/10.1016/j.bbadis.2010.03.007openalex-snapshot
CK2 and GSK3 phosphorylation on S29 controls wild-type ATXN3 nuclear uptake
inferredcites →https://doi.org/10.1016/j.cell.2004.11.013openalex-snapshot
A Series of Ubiquitin Binding Factors Connects CDC48/p97 to Substrate Multiubiquitylation and Proteasomal Targeting
inferredcites →https://doi.org/10.1016/j.cell.2005.11.007openalex-snapshot
A Genomic and Functional Inventory of Deubiquitinating Enzymes
inferredcites →https://doi.org/10.1016/j.cell.2006.02.025openalex-snapshot
Endocytosis Conducts the Cell Signaling Orchestra
inferredcites →https://doi.org/10.1016/j.cell.2006.05.043openalex-snapshot
Distinct Ubiquitin-Ligase Complexes Define Convergent Pathways for the Degradation of ER Proteins
inferredcites →https://doi.org/10.1016/j.cell.2006.09.051openalex-snapshot
Ubiquitin Chains Are Remodeled at the Proteasome by Opposing Ubiquitin Ligase and Deubiquitinating Activities
inferredcites →https://doi.org/10.1016/j.cell.2007.06.052openalex-snapshot
SCRAPPER-Dependent Ubiquitination of Active Zone Protein RIM1 Regulates Synaptic Vesicle Release
inferredcites →https://doi.org/10.1016/j.cell.2008.01.020openalex-snapshot
Shared Principles in NF-κB Signaling
inferredcites →https://doi.org/10.1016/j.cell.2008.09.025openalex-snapshot
Arrestin-Related Ubiquitin-Ligase Adaptors Regulate Endocytosis and Protein Turnover at the Cell Surface
inferredcites →https://doi.org/10.1016/j.cell.2009.01.041openalex-snapshot
Quantitative Proteomics Reveals the Function of Unconventional Ubiquitin Chains in Proteasomal Degradation
inferredcites →https://doi.org/10.1016/j.cell.2009.03.007openalex-snapshot
Specific Recognition of Linear Ubiquitin Chains by NEMO Is Important for NF-κB Activation
inferredcites →https://doi.org/10.1016/j.cell.2009.04.042openalex-snapshot
Defining the Human Deubiquitinating Enzyme Interaction Landscape
inferredcites →https://doi.org/10.1016/j.cell.2010.04.018openalex-snapshot
Peroxisomes Are Signaling Platforms for Antiviral Innate Immunity
inferredcites →https://doi.org/10.1016/j.cell.2010.10.026openalex-snapshot
What Determines the Specificity and Outcomes of Ubiquitin Signaling?
inferredcites →https://doi.org/10.1016/j.cell.2010.11.016openalex-snapshot
Will the Ubiquitin System Furnish as Many Drug Targets as Protein Kinases?
inferredcites →https://doi.org/10.1016/j.cub.2003.10.028openalex-snapshot
Ubiquitin-Mediated Proteasome Activity Is Required for Agonist-Induced Endocytosis of GluRs
inferredcites →https://doi.org/10.1016/j.cub.2004.11.010openalex-snapshot
The Anaphase-Promoting Complex Regulates the Abundance of GLR-1 Glutamate Receptors in the Ventral Nerve Cord of C. elegans
inferredcites →https://doi.org/10.1016/j.cub.2007.10.034openalex-snapshot
Human USP3 Is a Chromatin Modifier Required for S Phase Progression and Genome Stability
inferredcites →https://doi.org/10.1016/j.devcel.2010.06.009openalex-snapshot
Gradients of a Ubiquitin E3 Ligase Inhibitor and a Caspase Inhibitor Determine Differentiation or Death in Spermatids
inferredcites →https://doi.org/10.1016/j.jmb.2007.11.092openalex-snapshot
Molecular Basis for the Unique Deubiquitinating Activity of the NF-κB Inhibitor A20
inferredcites →https://doi.org/10.1016/j.mcpro.2022.100262openalex-snapshot
Molecular & Cellular Proteomics
inferredcites →https://doi.org/10.1016/j.molcel.2005.01.008openalex-snapshot
The Deubiquitinating Enzyme USP1 Regulates the Fanconi Anemia Pathway
inferredcites →https://doi.org/10.1016/j.molcel.2008.03.021openalex-snapshot
Mechanism and Consequences for Paralog-Specific Sumoylation of Ubiquitin-Specific Protease 25
inferredcites →https://doi.org/10.1016/j.molcel.2008.08.027openalex-snapshot
Distinct Modes of Regulation of the Uch37 Deubiquitinating Enzyme in the Proteasome and in the Ino80 Chromatin-Remodeling Complex
inferredcites →https://doi.org/10.1016/j.molcel.2009.01.012openalex-snapshot
Structural Basis for Recognition of Diubiquitins by NEMO
inferredcites →https://doi.org/10.1016/j.molcel.2009.04.026openalex-snapshot
A Role for Ubiquitin in Selective Autophagy
inferredcites →https://doi.org/10.1016/j.molcel.2009.10.013openalex-snapshot
Recruitment of the Linear Ubiquitin Chain Assembly Complex Stabilizes the TNF-R1 Signaling Complex and Is Required for TNF-Mediated Gene Induction
inferredcites →https://doi.org/10.1016/j.molcel.2009.11.029openalex-snapshot
A Tangled Web of Ubiquitin Chains: Breaking News in TNF-R1 Signaling
inferredcites →https://doi.org/10.1016/j.molcel.2010.05.003openalex-snapshot
The Diversity of Ubiquitin Recognition: Hot Spots and Varied Specificity
inferredcites →https://doi.org/10.1016/j.neuron.2004.12.058openalex-snapshot
LIN-23-Mediated Degradation of β-Catenin Regulates the Abundance of GLR-1 Glutamate Receptors in the Ventral Nerve Cord of C. elegans
inferredcites →https://doi.org/10.1016/j.tcb.2006.09.002openalex-snapshot
Endocytosis: the DUB version
inferredcites →https://doi.org/10.1016/j.tibs.2005.02.004openalex-snapshot
Multiubiquitylation by E4 enzymes: ‘one size’ doesn't fit all
inferredcites →https://doi.org/10.1016/j.tibs.2005.04.005openalex-snapshot
Regulated protein degradation
inferredcites →https://doi.org/10.1016/j.tibs.2007.09.010openalex-snapshot
ESCRTing proteins in the endocytic pathway
inferredcites →https://doi.org/10.1016/s0021-9258(19)49552-5openalex-snapshot
Subcellular localization of ubiquitin and ubiquitinated proteins in Arabidopsis thaliana.
inferredcites →https://doi.org/10.1016/s0092-8674(00)00206-3openalex-snapshot
Short-Range and Long-Range Guidance by Slit and Its Robo Receptors
inferredcites →https://doi.org/10.1016/s0092-8674(00)80574-7openalex-snapshot
A Novel Ubiquitination Factor, E4, Is Involved in Multiubiquitin Chain Assembly
inferredcites →https://doi.org/10.1016/s0092-8674(02)00901-7openalex-snapshot
Comm Sorts Robo to Control Axon Guidance at the Drosophila Midline
inferredcites →https://doi.org/10.1016/s0896-6273(00)00151-3openalex-snapshot
Short-Range and Long-Range Guidance by Slit and Its Robo Receptors
inferredcites →https://doi.org/10.1016/s0896-6273(01)00551-7openalex-snapshot
Chemotropic Responses of Retinal Growth Cones Mediated by Rapid Local Protein Synthesis and Degradation
inferredcites →https://doi.org/10.1016/s0896-6273(02)00795-xopenalex-snapshot
Drosophila Nedd4, a Ubiquitin Ligase, Is Recruited by Commissureless to Control Cell Surface Levels of the Roundabout Receptor
inferredcites →https://doi.org/10.1016/s0960-9822(03)00338-5openalex-snapshot
The Ubiquitin Proteasome System Acutely Regulates Presynaptic Protein Turnover and Synaptic Efficacy
inferredcites →https://doi.org/10.1016/s1097-2765(03)00050-9openalex-snapshot
p53 Has a Direct Apoptogenic Role at the Mitochondria
inferredcites →https://doi.org/10.1016/s1534-5807(01)00057-0openalex-snapshot
The DSmurf Ubiquitin-Protein Ligase Restricts BMP Signaling Spatially and Temporally during Drosophila Embryogenesis
inferredcites →https://doi.org/10.1021/cr800413popenalex-snapshot
Functional Roles of Ubiquitin-Like Domain (ULD) and Ubiquitin-Binding Domain (UBD) Containing Proteins
inferredcites →https://doi.org/10.1038/35056563openalex-snapshot
Themes and variations on ubiquitylation
inferredcites →https://doi.org/10.1038/387296a0openalex-snapshot
Mdm2 promotes the rapid degradation of p53
inferredcites →https://doi.org/10.1038/cdd.2009.168openalex-snapshot
Regulation of death receptor signaling by the ubiquitin system
inferredcites →https://doi.org/10.1038/cdd.2009.77openalex-snapshot
The multiple levels of regulation by p53 ubiquitination
inferredcites →https://doi.org/10.1038/cr.2008.75openalex-snapshot
GIDE is a mitochondrial E3 ubiquitin ligase that induces apoptosis and slows growth
inferredcites →https://doi.org/10.1038/cr.2010.166openalex-snapshot
Deubiquitinases in the regulation of NF-κB signaling
inferredcites →https://doi.org/10.1038/emboj.2008.5openalex-snapshot
Inflammatory cardiac valvulitis in TAX1BP1‐deficient mice through selective NF‐κB activation
inferredcites →https://doi.org/10.1038/emboj.2009.241openalex-snapshot
NEMO specifically recognizes K63‐linked poly‐ubiquitin chains through a new bipartite ubiquitin‐binding domain
inferredcites →https://doi.org/10.1038/emboj.2010.100openalex-snapshot
Balanced ubiquitylation and deubiquitylation of Frizzled regulate cellular responsiveness to Wg/Wnt
inferredcites →https://doi.org/10.1038/emboj.2010.173openalex-snapshot
Protein homeostasis and synaptic plasticity
inferredcites →https://doi.org/10.1038/emboj.2010.300openalex-snapshot
c‐IAP1 and UbcH5 promote K11‐linked polyubiquitination of RIP1 in TNF signalling
inferredcites →https://doi.org/10.1038/embor.2008.183openalex-snapshot
Function and regulation of protein neddylation
inferredcites →https://doi.org/10.1038/embor.2008.93openalex-snapshot
Atypical ubiquitin chains: new molecular signals
inferredcites →https://doi.org/10.1038/embor.2009.144openalex-snapshot
Linear polyubiquitination: a new regulator of NF‐κB activation
inferredcites →https://doi.org/10.1038/embor.2009.55openalex-snapshot
Molecular discrimination of structurally equivalent Lys 63‐linked and linear polyubiquitin chains
inferredcites →https://doi.org/10.1038/embor.2009.69openalex-snapshot
The ER‐resident ubiquitin‐specific protease 19 participates in the UPR and rescues ERAD substrates
inferredcites →https://doi.org/10.1038/nature02794openalex-snapshot
De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling
inferredcites →https://doi.org/10.1038/nature06256openalex-snapshot
Regulation of cell cycle progression and gene expression by H2A deubiquitination
inferredcites →https://doi.org/10.1038/nature06924openalex-snapshot
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
inferredcites →https://doi.org/10.1038/nature06926openalex-snapshot
Proteasome subunit Rpn13 is a novel ubiquitin receptor
inferredcites →https://doi.org/10.1038/nature07960openalex-snapshot
Targeting the ubiquitin system in cancer therapy
inferredcites →https://doi.org/10.1038/nature07961openalex-snapshot
The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
inferredcites →https://doi.org/10.1038/nature07962openalex-snapshot
The ubiquitylation machinery of the endoplasmic reticulum
inferredcites →https://doi.org/10.1038/nature07963openalex-snapshot
Principles of ubiquitin and SUMO modifications in DNA repair
inferredcites →https://doi.org/10.1038/nature08467openalex-snapshot
The DNA-damage response in human biology and disease
inferredcites →https://doi.org/10.1038/nature09297openalex-snapshot
Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1
inferredcites →https://doi.org/10.1038/nature09814openalex-snapshot
SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis
inferredcites →https://doi.org/10.1038/nature09815openalex-snapshot
SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex
inferredcites →https://doi.org/10.1038/nature09816openalex-snapshot
Linear ubiquitination prevents inflammation and regulates immune signalling
inferredcites →https://doi.org/10.1038/ncb0910-836openalex-snapshot
Selective autophagy: ubiquitin-mediated recognition and beyond
inferredcites →https://doi.org/10.1038/ncb1378openalex-snapshot
Regulation of monoubiquitinated PCNA by DUB autocleavage
inferredcites →https://doi.org/10.1038/ncb1460openalex-snapshot
Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1
inferredcites →https://doi.org/10.1038/ncb1558openalex-snapshot
Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue
inferredcites →https://doi.org/10.1038/ncb1716openalex-snapshot
RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
inferredcites →https://doi.org/10.1038/ncb1717openalex-snapshot
Arsenic degrades PML or PML–RARα through a SUMO-triggered RNF4/ubiquitin-mediated pathway
inferredcites →https://doi.org/10.1038/ncb1730openalex-snapshot
Regulation of autophagy by cytoplasmic p53
inferredcites →https://doi.org/10.1038/ncb1821openalex-snapshot
Involvement of linear polyubiquitylation of NEMO in NF-κB activation
inferredcites →https://doi.org/10.1038/ncb1865openalex-snapshot
RAD18 transmits DNA damage signalling to elicit homologous recombination repair
inferredcites →https://doi.org/10.1038/ncb2008openalex-snapshot
HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes
inferredcites →https://doi.org/10.1038/ncb2012openalex-snapshot
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
inferredcites →https://doi.org/10.1038/nn.2656openalex-snapshot
APC/CFzr/Cdh1-dependent regulation of cell adhesion controls glial migration in the Drosophila PNS
inferredcites →https://doi.org/10.1038/nn1013openalex-snapshot
Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
inferredcites →https://doi.org/10.1038/nrm2468openalex-snapshot
Diversity of degradation signals in the ubiquitin–proteasome system
inferredcites →https://doi.org/10.1038/nrm2673openalex-snapshot
Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways
inferredcites →https://doi.org/10.1038/nrm2731openalex-snapshot
Breaking the chains: structure and function of the deubiquitinases
inferredcites →https://doi.org/10.1038/nrm2767openalex-snapshot
Ubiquitin-binding domains — from structures to functions
inferredcites →https://doi.org/10.1038/nrm2780openalex-snapshot
Building ubiquitin chains: E2 enzymes at work
inferredcites →https://doi.org/10.1038/nrm2921openalex-snapshot
Ubiquitin signalling in DNA replication and repair
inferredcites →https://doi.org/10.1038/nrm2937openalex-snapshot
Membrane budding and scission by the ESCRT machinery: it's all in the neck
inferredcites →https://doi.org/10.1038/nsmb1252openalex-snapshot
FANCI is a second monoubiquitinated member of the Fanconi anemia pathway
inferredcites →https://doi.org/10.1038/sj.emboj.7600710openalex-snapshot
The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme
inferredcites →https://doi.org/10.1038/sj.emboj.7600808openalex-snapshot
Ubiquitylation and cell signaling
inferredcites →https://doi.org/10.1038/sj.emboj.7601249openalex-snapshot
A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics
inferredcites →https://doi.org/10.1038/sj.emboj.7601338openalex-snapshot
A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes
inferredcites →https://doi.org/10.1038/sj.emboj.7601490openalex-snapshot
Cytoplasmic destruction of p53 by the endoplasmic reticulum‐resident ubiquitin ligase ‘Synoviolin’
inferredcites →https://doi.org/10.1042/bj20090427openalex-snapshot
NEMO oligomerization and its ubiquitin-binding properties
inferredcites →https://doi.org/10.1042/bst0360791openalex-snapshot
Versatile role of the yeast ubiquitin ligase Rsp5p in intracellular trafficking
inferredcites →https://doi.org/10.1073/pnas.0510664103openalex-snapshot
Activation of the E3 ubiquitin ligase Itch through a phosphorylation-induced conformational change
inferredcites →https://doi.org/10.1073/pnas.0807485106openalex-snapshot
The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks
inferredcites →https://doi.org/10.1074/mcp.r110.003871openalex-snapshot
Trimming of Ubiquitin Chains by Proteasome-associated Deubiquitinating Enzymes
inferredcites →https://doi.org/10.1083/jcb.200406001openalex-snapshot
Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import
inferredcites →https://doi.org/10.1083/jcb.200511028openalex-snapshot
Requirement of dendritic Akt degradation by the ubiquitin–proteasome system for neuronal polarity
inferredcites →https://doi.org/10.1083/jcb.200811130openalex-snapshot
ESCRT ubiquitin-binding domains function cooperatively during MVB cargo sorting
inferredcites →https://doi.org/10.1083/jcb.201007013openalex-snapshot
Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
inferredcites →https://doi.org/10.1091/mbc.e05-08-0794openalex-snapshot
KEL-8 Is a Substrate Receptor for CUL3-dependent Ubiquitin Ligase That Regulates Synaptic Glutamate Receptor Turnover
inferredcites →https://doi.org/10.1091/mbc.e06-06-0557openalex-snapshot
Hse1, a Component of the Yeast Hrs-STAM Ubiquitin-sorting Complex, Associates with Ubiquitin Peptidases and a Ligase to Control Sorting Efficiency into Multivesicular Bodies
inferredcites →https://doi.org/10.1091/mbc.e07-11-1103openalex-snapshot
Regulation of Mitochondrial Morphology by USP30, a Deubiquitinating Enzyme Present in the Mitochondrial Outer Membrane
inferredcites →https://doi.org/10.1091/mbc.e08-02-0227openalex-snapshot
Ubiquitin–Proteasome-dependent Degradation of a Mitofusin, a Critical Regulator of Mitochondrial Fusion
inferredcites →https://doi.org/10.1093/emboj/18.6.1660openalex-snapshot
A leucine‐rich nuclear export signal in the p53 tetramerization domain: regulation of subcellular localization and p53 activity by NES masking
inferredcites →https://doi.org/10.1093/hmg/ddl164openalex-snapshot
Ataxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates
inferredcites →https://doi.org/10.1096/fj.06-6751comopenalex-snapshot
Aging perturbs 26S proteasome assembly in Drosophila melanogaster
inferredcites →https://doi.org/10.1101/gad.494808openalex-snapshot
Medea SUMOylation restricts the signaling range of the Dpp morphogen in the Drosophila embryo
inferredcites →https://doi.org/10.1126/science.1065874openalex-snapshot
Identification of Ubiquitin Ligases Required for Skeletal Muscle Atrophy
inferredcites →https://doi.org/10.1126/science.1091362openalex-snapshot
Mono- Versus Polyubiquitination: Differential Control of p53 Fate by Mdm2
inferredcites →https://doi.org/10.1126/science.1093712openalex-snapshot
Cdh1-APC Controls Axonal Growth and Patterning in the Mammalian Brain
inferredcites →https://doi.org/10.1126/science.1120615openalex-snapshot
Ubiquitin-Binding Domains in Y-Family Polymerases Regulate Translesion Synthesis
inferredcites →https://doi.org/10.1126/science.1127085openalex-snapshot
Proteasome-Independent Functions of Ubiquitin in Endocytosis and Signaling
inferredcites →https://doi.org/10.1126/science.1139516openalex-snapshot
RAP80 Targets BRCA1 to Specific Ubiquitin Structures at DNA Damage Sites
inferredcites →https://doi.org/10.1126/science.1177087openalex-snapshot
A Cdc20-APC Ubiquitin Signaling Pathway Regulates Presynaptic Differentiation
inferredcites →https://doi.org/10.1126/science.1182364openalex-snapshot
Inhibition of NF-κB Signaling by A20 Through Disruption of Ubiquitin Enzyme Complexes
inferredcites →https://doi.org/10.1126/science.1183147openalex-snapshot
N-Terminal Acetylation of Cellular Proteins Creates Specific Degradation Signals
inferredcites →https://doi.org/10.1126/science.278.5344.1806openalex-snapshot
Role of Cue1p in Ubiquitination and Degradation at the ER Surface
inferredcites →https://doi.org/10.1128/mcb.00818-10openalex-snapshot
UMI, a Novel RNF168 Ubiquitin Binding Domain Involved in the DNA Damage Signaling Pathway
inferredcites →https://doi.org/10.1128/mcb.21.24.8521-8532.2001openalex-snapshot
C-Terminal Ubiquitination of p53 Contributes to Nuclear Export
inferredcites →https://doi.org/10.1128/mcb.25.10.3886-3895.2005openalex-snapshot
Regulation of the Deubiquitinating Enzyme CYLD by IκB Kinase Gamma-Dependent Phosphorylation
inferredcites →https://doi.org/10.1146/annurev.biochem.67.1.425openalex-snapshot
THE UBIQUITIN SYSTEM
inferredcites →https://doi.org/10.1146/annurev.biochem.78.070907.102750openalex-snapshot
The Role of Ubiquitin in NF-κB Regulatory Pathways
inferredcites →https://doi.org/10.1146/annurev.biochem.78.081507.101607openalex-snapshot
Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome
inferredcites →https://doi.org/10.1146/annurev.biochem.78.101807.093809openalex-snapshot
RING Domain E3 Ubiquitin Ligases
inferredcites →https://doi.org/10.1186/1471-2199-10-55openalex-snapshot
RNF168, a new RING finger, MIU-containing protein that modifies chromatin by ubiquitination of histones H2A and H2AX
inferredcites →https://doi.org/10.1196/annals.1427.012openalex-snapshot
Role of the Ubiquitin Conjugation System in the Maintenance of Mitochondrial Homeostasis
inferredcites →https://doi.org/10.1240/sav_gbm_2008_m_002187openalex-snapshot
Human USP3 is a chromatin modifier required for S-phase progression and genome stability
inferredcites →https://doi.org/10.1242/dev.010900openalex-snapshot
Asymmetric localisation of Miranda and its cargo proteins during neuroblast division requires the anaphase-promoting complex/cyclosome
inferredcites →https://doi.org/10.1242/dev.02214openalex-snapshot
Shaping BMP morphogen gradients in theDrosophilaembryo and pupal wing
inferredcites →https://doi.org/10.1242/jcs.019729openalex-snapshot
NCAM is ubiquitylated, endocytosed and recycled in neurons
inferredcites →https://doi.org/10.1242/jcs.049049openalex-snapshot
Developmental-stage-specific regulation of the polyubiquitin receptors inDrosophila melanogaster
inferredcites →https://doi.org/10.1371/journal.pbio.0050251openalex-snapshot
A Ubiquitin Ligase Complex Regulates Caspase Activation During Sperm Differentiation in Drosophila
inferredcites →https://doi.org/10.1371/journal.pone.0001487openalex-snapshot
Genome-Wide and Functional Annotation of Human E3 Ubiquitin Ligases Identifies MULAN, a Mitochondrial E3 that Regulates the Organelle's Dynamics and Signaling
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4583218openalex-extracted
Ubiquitinome And Transcriptome Analyses Reveal Ubiquitinated Antioxidant Enzymes Related to Juice Sac Granulation Through H 2 O 2 Activating Lignin Biosynthesis in Pomelo
inferred← citeshttps://doi.org/10.1002/adbi.202300083openalex-snapshot
Targeted Protein Degradation: Principles, Strategies, and Applications
inferred← citeshttps://doi.org/10.1002/advs.202303207openalex-snapshot
The Deubiquitinase OTUD1 Suppresses Secretory Neutrophil Polarization And Ameliorates Immunopathology of Periodontitis
inferred← citeshttps://doi.org/10.1002/ange.201207171openalex-snapshot
Nonenzymatic Polymerization of Ubiquitin: Single‐Step Synthesis and Isolation of Discrete Ubiquitin Oligomers
inferred← citeshttps://doi.org/10.1002/anie.201207171openalex-snapshot
Nonenzymatic Polymerization of Ubiquitin: Single‐Step Synthesis and Isolation of Discrete Ubiquitin Oligomers
inferred← citeshttps://doi.org/10.1002/art.70300openalex-snapshot
FSCN1 Promotes Rheumatoid Arthritis Progression via Inhibiting TRIM38–Mediated Ubiquitination of IGF2BP1 in Fibroblast‐Like Synoviocytes
inferred← citeshttps://doi.org/10.1002/bit.25957openalex-snapshot
Proteomic differences in recombinant CHO cells producing two similar antibody fragments
inferred← citeshttps://doi.org/10.1002/bit.70081openalex-snapshot
Proteomic and Ubiquitinated Proteome Insights Into ER Stress Responses in Chinese Hamster Ovary Cells Under Mild Hypothermic Conditions
inferred← citeshttps://doi.org/10.1002/cam4.1069openalex-snapshot
Ubiquitination in melanoma pathogenesis and treatment
inferred← citeshttps://doi.org/10.1002/cbf.3704openalex-snapshot
Simultaneous proteasome and autophagy inhibition synergistically enhances cytotoxicity of doxorubicin in breast cancer cells
inferred← citeshttps://doi.org/10.1002/cbic.201402059openalex-snapshot
Chemoenzymatic Synthesis of Bifunctional Polyubiquitin Substrates for Monitoring Ubiquitin Chain Remodeling
inferred← citeshttps://doi.org/10.1002/cbic.201900146openalex-snapshot
Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy
inferred← citeshttps://doi.org/10.1002/cbic.202300670openalex-snapshot
Targeted Preparation and NMR Spectroscopic Characterization of Lys11‐Linked Ubiquitin Trimers
inferred← citeshttps://doi.org/10.1002/cbin.11186openalex-snapshot
An optical and non‐invasive method to detect the accumulation of ubiquitin chains
inferred← citeshttps://doi.org/10.1002/ctm2.770openalex-snapshot
Ubiquitylation of cyclin C by HACE1 regulates cisplatin‐associated sensitivity in gastric cancer
inferred← citeshttps://doi.org/10.1002/emmm.201100707openalex-snapshot
Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications
inferred← citeshttps://doi.org/10.1002/jcb.30516openalex-snapshot
Linc‐ROR inhibits NK cell‐killing activity by promoting RXRA ubiquitination and reducing MICB expression in gastric cancer patients
inferred← citeshttps://doi.org/10.1002/mc.70030openalex-snapshot
Targeting Posttranslational Modifications in the Tumor Stromal Microenvironment for Antitumor Therapy
inferred← citeshttps://doi.org/10.1002/pmic.201200244openalex-snapshot
Unraveling the ubiquitin‐regulated signaling networks by mass spectrometry‐based proteomics
inferred← citeshttps://doi.org/10.1002/pro.2834openalex-snapshot
Comparison of native and non-native ubiquitin oligomers reveals analogous structures and reactivities
inferred← citeshttps://doi.org/10.1002/pro.4885openalex-snapshot
Structural and functional validation of a highly specific Smurf2 inhibitor
inferred← citeshttps://doi.org/10.1007/82_2014_379openalex-snapshot
Function and Regulation of the Mono-ADP-Ribosyltransferase ARTD10
inferred← citeshttps://doi.org/10.1007/82_2016_27openalex-snapshot
New Aspects on Bacterial Effectors Targeting Rho GTPases
inferred← citeshttps://doi.org/10.1007/978-1-0716-1186-9_7openalex-snapshot
Polyubiquitin Profile in Down Syndrome and Alzheimer’s Disease Brain
inferred← citeshttps://doi.org/10.1007/978-1-4614-6528-7_12openalex-snapshot
Regulation of Endocytic Trafficking and Signalling by Deubiquitylating Enzymes
inferred← citeshttps://doi.org/10.1007/978-1-4614-6528-7_9openalex-snapshot
Efficient Enhancement of Signalling Capacity: The Ubiquitin System
inferred← citeshttps://doi.org/10.1007/978-1-4939-1130-1_14openalex-snapshot
Systems-Wide Analysis of Protein Ubiquitylation: We Finally Have the Tiger by the Tail
inferred← citeshttps://doi.org/10.1007/978-1-4939-3756-1_13openalex-snapshot
Bimolecular Fluorescence Complementation to Assay the Interactions of Ubiquitylation Enzymes in Living Yeast Cells
inferred← citeshttps://doi.org/10.1007/978-3-319-15263-9_12openalex-snapshot
Cardiac Cytoarchitecture: How to Maintain a Working Heart—Waste Disposal and Recycling in Cardiomyocytes
inferred← citeshttps://doi.org/10.1007/978-3-319-46044-4_4openalex-snapshot
Molecular Organization, Trafficking, and Degradation of the GABAB Receptor
inferred← citeshttps://doi.org/10.1007/978-3-319-77674-3_7openalex-snapshot
Defects of Innate Immunity
inferred← citeshttps://doi.org/10.1007/978-981-99-2452-3_7openalex-snapshot
Role and Application of Biomolecules for Regeneration of Cartilage Tissue
inferred← citeshttps://doi.org/10.1007/s00109-020-02015-5openalex-snapshot
Roles of E3 ubiquitin ligases in gastric cancer carcinogenesis and their effects on cisplatin resistance
inferred← citeshttps://doi.org/10.1007/s00232-011-9394-2openalex-snapshot
SMURF and NEDD4: Sharp Shooters Monitor the Gate Keepers and Ion Traffic Controllers of Lead Astray Cell
inferred← citeshttps://doi.org/10.1007/s00425-021-03647-8openalex-snapshot
Critical role of cysteine-266 of SIE3 in regulating the ubiquitination and degradation of SIP1 transcription factor in Lotus japonicus
inferred← citeshttps://doi.org/10.1007/s10571-021-01106-2openalex-snapshot
Comprehensive Analysis of Proteasomal Complexes in Mouse Brain Regions Detects ENO2 as a Potential Partner of the Proteasome in the Striatum
inferred← citeshttps://doi.org/10.1007/s10787-021-00890-zopenalex-snapshot
Deubiquitylating enzymes: potential target in autoimmune diseases
inferred← citeshttps://doi.org/10.1007/s11033-021-07057-7openalex-snapshot
F-box only protein 9 and its role in cancer
inferred← citeshttps://doi.org/10.1007/s11064-015-1681-3openalex-snapshot
Battling Alzheimer’s Disease: Targeting SUMOylation-Mediated Pathways
inferred← citeshttps://doi.org/10.1007/s11064-025-04346-6openalex-snapshot
Regulation of Synaptic NMDA Receptor Activity by Post-Translational Modifications
inferred← citeshttps://doi.org/10.1007/s12013-013-9621-9openalex-snapshot
Measuring Activity in the Ubiquitin–Proteasome System: From Large Scale Discoveries to Single Cells Analysis
inferred← citeshttps://doi.org/10.1007/s12026-023-09400-5openalex-snapshot
Ubiquitin ligase enzymes and de-ubiquitinating enzymes regulate innate immunity in the TLR, NLR, RLR, and cGAS-STING pathways
inferred← citeshttps://doi.org/10.1007/s12031-017-0969-yopenalex-snapshot
Single-Base Resolution Mapping of 5-Hydroxymethylcytosine Modifications in Hippocampus of Alzheimer’s Disease Subjects
inferred← citeshttps://doi.org/10.1007/s12035-026-05822-yopenalex-snapshot
Proteomic Analysis of Ubiquitination Modified Proteins in Brain Tissue of Rats at Different Times after Severe Traumatic Brain Injury
inferred← citeshttps://doi.org/10.1007/s43657-025-00233-wopenalex-snapshot
Protein Neddylation Beyond Tumor Cells is a Vital Modulator of Anticancer Immunity
inferred← citeshttps://doi.org/10.1016/b978-0-12-386456-7.01404-0openalex-snapshot
Cell Adaptation, Injury, and Death: Ubiquitin–Proteasome System
inferred← citeshttps://doi.org/10.1016/b978-0-12-800186-8.00003-1openalex-snapshot
Proteasomal Degradation of Soluble, Misfolded Proteins
inferred← citeshttps://doi.org/10.1016/bs.acr.2020.05.001openalex-snapshot
Epigenetic regulation of cancer stem cell and tumorigenesis
inferred← citeshttps://doi.org/10.1016/bs.apha.2014.11.002openalex-snapshot
Regulation of Cell Surface GABAB Receptors
inferred← citeshttps://doi.org/10.1016/bs.mie.2018.12.020openalex-snapshot
A genetic approach to study polyubiquitination in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1016/bs.mie.2018.12.024openalex-snapshot
Purification and functional characterization of the DUB domain of SdeA
inferred← citeshttps://doi.org/10.1016/bs.mie.2018.12.030openalex-snapshot
Detection of ubiquitinated targets in mammalian and Drosophila models
inferred← citeshttps://doi.org/10.1016/bs.pmbts.2016.02.006openalex-snapshot
Chapter Eight - Ubiquitin-Mediated Regulation of Cellular Responses to Vascular Endothelial Growth Factors
inferred← citeshttps://doi.org/10.1016/j.antiviral.2024.106027openalex-snapshot
Berberine promotes K48-linked polyubiquitination of HNF4α, leading to the inhibition of HBV replication
inferred← citeshttps://doi.org/10.1016/j.apsb.2023.08.008openalex-snapshot
Targeting autophagy and beyond: Deconvoluting the complexity of Beclin-1 from biological function to cancer therapy
inferred← citeshttps://doi.org/10.1016/j.apsb.2025.10.039openalex-snapshot
Radiation-induced nuclear translocation of NPRL2 hijacks E3 ubiquitin ligases to enhance DNA repair via the AMPK/WDR24 axis, contributing to CRC radioresistance
inferred← citeshttps://doi.org/10.1016/j.bbadis.2023.166884openalex-snapshot
Expanding the ubiquitin code in pancreatic cancer
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.07.002openalex-snapshot
The N-end rule pathway: From recognition by N-recognins, to destruction by AAA+proteases
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2013.06.027openalex-snapshot
Regulation of proteolysis by human deubiquitinating enzymes
inferred← citeshttps://doi.org/10.1016/j.bbrc.2011.11.071openalex-snapshot
mHERC6 is the essential ISG15 E3 ligase in the murine system
inferred← citeshttps://doi.org/10.1016/j.bbrc.2013.05.080openalex-snapshot
The parallel reaction monitoring method contributes to a highly sensitive polyubiquitin chain quantification
inferred← citeshttps://doi.org/10.1016/j.bbrc.2021.03.151openalex-snapshot
LAPTM4α is targeted from the Golgi to late endosomes/lysosomes in a manner dependent on the E3 ubiquitin ligase Nedd4-1 and ESCRT proteins
inferred← citeshttps://doi.org/10.1016/j.bbrep.2016.02.003openalex-snapshot
Rapid identification of ubiquitination and SUMOylation target sites by microfluidic peptide array
inferred← citeshttps://doi.org/10.1016/j.bbrep.2020.100784openalex-snapshot
HM1.24/BST-2 is constitutively poly-ubiquitinated at the N-terminal amino acid in the cytoplasmic domain
inferred← citeshttps://doi.org/10.1016/j.bcp.2011.07.001openalex-snapshot
DNA damage response: The emerging role of c-Abl as a regulatory switch?
inferred← citeshttps://doi.org/10.1016/j.biochi.2020.04.025openalex-snapshot
The beclin 1 interactome: Modification and roles in the pathology of autophagy-related disorders
inferred← citeshttps://doi.org/10.1016/j.bioorg.2023.106347openalex-snapshot
Site-directed double monoubiquitination of the repeat domain of the amyloid-forming protein tau impairs self-assembly and coacervation
inferred← citeshttps://doi.org/10.1016/j.brainres.2019.146569openalex-snapshot
The ubiquitin-editing enzyme A20 regulates synapse remodeling and efficacy
inferred← citeshttps://doi.org/10.1016/j.canlet.2025.217663openalex-snapshot
CUL4A exhibits tumor-suppressing role via regulation of HUWE1-mediated SMAD3 intracellular shuttling
inferred← citeshttps://doi.org/10.1016/j.cbpa.2015.06.001openalex-snapshot
Peeling away the layers of ubiquitin signaling complexities with synthetic ubiquitin–protein conjugates
inferred← citeshttps://doi.org/10.1016/j.cca.2019.08.020openalex-snapshot
E2 ubiquitin-conjugating enzymes in cancer: Implications for immunotherapeutic interventions
inferred← citeshttps://doi.org/10.1016/j.cclet.2022.107781openalex-snapshot
Chemical tools for E3 ubiquitin ligase study
inferred← citeshttps://doi.org/10.1016/j.ceb.2020.02.005openalex-snapshot
Recognising the signals for endosomal trafficking
inferred← citeshttps://doi.org/10.1016/j.cell.2013.03.014openalex-snapshot
Cullins Getting Undressed by the Protein Exchange Factor Cand1
inferred← citeshttps://doi.org/10.1016/j.cell.2014.04.026openalex-snapshot
Deciphering Functions of Branched Ubiquitin Chains
inferred← citeshttps://doi.org/10.1016/j.cell.2016.02.047openalex-snapshot
The Dark Side of Cell Signaling: Positive Roles for Negative Regulators
inferred← citeshttps://doi.org/10.1016/j.cell.2016.11.019openalex-snapshot
Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination
inferred← citeshttps://doi.org/10.1016/j.cellsig.2012.11.024openalex-snapshot
Ubiquitin-dependent regulation of G protein-coupled receptor trafficking and signaling
inferred← citeshttps://doi.org/10.1016/j.cellsig.2014.03.006openalex-snapshot
PMA induces SnoN proteolysis and CD61 expression through an autocrine mechanism
inferred← citeshttps://doi.org/10.1016/j.cellsig.2014.04.008openalex-snapshot
Ubiquitination-dependent CARM1 degradation facilitates Notch1-mediated podocyte apoptosis in diabetic nephropathy
inferred← citeshttps://doi.org/10.1016/j.cellsig.2017.05.012openalex-snapshot
The many faces of compartmentalized PKA signalosomes
inferred← citeshttps://doi.org/10.1016/j.cellsig.2020.109719openalex-snapshot
Drosophila Uev1a is dually required for Ben-dependent DNA-damage response and fly mobility
inferred← citeshttps://doi.org/10.1016/j.cellsig.2023.110994openalex-snapshot
The role of abnormal ubiquitination in hepatocellular carcinoma pathology
inferred← citeshttps://doi.org/10.1016/j.celrep.2012.11.011openalex-snapshot
Deubiquitinases as a Signaling Target of Oxidative Stress
inferred← citeshttps://doi.org/10.1016/j.csbj.2014.08.004openalex-snapshot
Proteomics for systems toxicology
inferred← citeshttps://doi.org/10.1016/j.csbj.2025.06.044openalex-snapshot
Structural insights into Beclin 1 interactions with it's regulators for autophagy modulation
inferred← citeshttps://doi.org/10.1016/j.cub.2014.02.002openalex-snapshot
Ubiquitin code assembly and disassembly
inferred← citeshttps://doi.org/10.1016/j.cytogfr.2013.07.002openalex-snapshot
Dynamic regulation of innate immunity by ubiquitin and ubiquitin-like proteins
inferred← citeshttps://doi.org/10.1016/j.devcel.2012.08.011openalex-snapshot
Governance of Endocytic Trafficking and Signaling by Reversible Ubiquitylation
inferred← citeshttps://doi.org/10.1016/j.ebiom.2018.03.025openalex-snapshot
Identification of Serine 119 as an Effective Inhibitor Binding Site of M. tuberculosis Ubiquitin-like Protein Ligase PafA Using Purified Proteins and M. smegmatis
inferred← citeshttps://doi.org/10.1016/j.ebiom.2018.11.047openalex-snapshot
A new gold(I) complex-Au(PPh3)PT is a deubiquitinase inhibitor and inhibits tumor growth
inferred← citeshttps://doi.org/10.1016/j.ejmcr.2026.100332openalex-snapshot
PROTACs in targeted protein degradation: Advances in development and AI-enhanced drug discovery
inferred← citeshttps://doi.org/10.1016/j.exppara.2018.11.003openalex-snapshot
Characterization of N-glycosylations in Entamoeba histolytica ubiquitin
inferred← citeshttps://doi.org/10.1016/j.febslet.2012.03.037openalex-snapshot
Regulation of TGF‐β signal transduction by mono‐ and deubiquitylation of Smads
inferred← citeshttps://doi.org/10.1016/j.febslet.2012.04.046openalex-snapshot
Ubiquitination and phosphorylation of Beclin 1 and its binding partners: Tuning class III phosphatidylinositol 3‐kinase activity and tumor suppression
inferred← citeshttps://doi.org/10.1016/j.febslet.2012.04.053openalex-snapshot
Selectivity of the ubiquitin‐binding modules
inferred← citeshttps://doi.org/10.1016/j.febslet.2012.05.051openalex-snapshot
Inhibitory effect of SPE‐39 due to tyrosine phosphorylation and ubiquitination on the function of Vps33B in the EGF‐stimulated cells
inferred← citeshttps://doi.org/10.1016/j.gendis.2024.101341openalex-snapshot
Role of ubiquitin-specific proteases in programmed cell death of breast cancer cells
inferred← citeshttps://doi.org/10.1016/j.gene.2011.12.027openalex-snapshot
Regulation of gene transcription by the oncoprotein MYC
inferred← citeshttps://doi.org/10.1016/j.genrep.2020.100677openalex-snapshot
In silico prediction of UCLH1 disease-causing SNPs and its effects on protein stability
inferred← citeshttps://doi.org/10.1016/j.hpj.2023.09.006openalex-snapshot
Interaction of MaERF11 with the E3 ubiquitin ligase MaRFA1 is involved in the regulation of banana starch degradation during postharvest ripening
inferred← citeshttps://doi.org/10.1016/j.ijpddr.2011.12.001openalex-snapshot
The proteasome of malaria parasites: A multi-stage drug target for chemotherapeutic intervention?
inferred← citeshttps://doi.org/10.1016/j.isci.2021.102146openalex-snapshot
Stress-induced NEDDylation promotes cytosolic protein aggregation through HDAC6 in a p62-dependent manner
inferred← citeshttps://doi.org/10.1016/j.isci.2023.106276openalex-snapshot
An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes
inferred← citeshttps://doi.org/10.1016/j.it.2012.09.005openalex-snapshot
Caspases and immunity in a deadly grip
inferred← citeshttps://doi.org/10.1016/j.jaci.2016.02.040openalex-snapshot
Persistent nodal histoplasmosis in nuclear factor kappa B essential modulator deficiency: Report of a case and review of infection in primary immunodeficiencies
inferred← citeshttps://doi.org/10.1016/j.jmb.2011.07.024openalex-snapshot
Intrinsic Disorder in Ubiquitination Substrates
inferred← citeshttps://doi.org/10.1016/j.jmb.2013.12.008openalex-snapshot
Core Structures of Ubiquitin Dictate Its Dynamics and Function
inferred← citeshttps://doi.org/10.1016/j.lfs.2026.124224openalex-snapshot
Reversible ubiquitination regulates HSF1 phase separation in response to proteotoxic stress
inferred← citeshttps://doi.org/10.1016/j.mcpro.2025.100920openalex-snapshot
Localized K63 Ubiquitin Signaling Is Regulated by VCP/p97 During Oxidative Stress
inferred← citeshttps://doi.org/10.1016/j.molcel.2012.06.017openalex-snapshot
Fluorescence-Based Sensors to Monitor Localization and Functions of Linear and K63-Linked Ubiquitin Chains in Cells
inferred← citeshttps://doi.org/10.1016/j.molcel.2014.03.016openalex-snapshot
Binding of OTULIN to the PUB Domain of HOIP Controls NF-κB Signaling
inferred← citeshttps://doi.org/10.1016/j.molcel.2016.04.015openalex-snapshot
Global Analysis of Host and Bacterial Ubiquitinome in Response to Salmonella Typhimurium Infection
inferred← citeshttps://doi.org/10.1016/j.mrfmmm.2018.02.003openalex-snapshot
Drosophila bendless catalyzes K63-linked polyubiquitination and is involved in the response to DNA damage
inferred← citeshttps://doi.org/10.1016/j.neuint.2017.08.013openalex-snapshot
Alterations in the E3 ligases Parkin and CHIP result in unique metabolic signaling defects and mitochondrial quality control issues
inferred← citeshttps://doi.org/10.1016/j.pharmthera.2021.107809openalex-snapshot
Exploring the “Other” subfamily of HECT E3-ligases for therapeutic intervention
inferred← citeshttps://doi.org/10.1016/j.phrs.2017.03.024openalex-snapshot
Hidden targets of ubiquitin proteasome system: To prevent diabetic nephropathy
inferred← citeshttps://doi.org/10.1016/j.pneurobio.2013.10.003openalex-snapshot
Role of the ubiquitin–proteasome system in brain ischemia: Friend or foe?
inferred← citeshttps://doi.org/10.1016/j.postharvbio.2020.111142openalex-snapshot
Ubiquitylome study highlights ubiquitination of primary metabolism related proteins in fruit response to postharvest pathogen infection
inferred← citeshttps://doi.org/10.1016/j.redox.2021.102194openalex-snapshot
Redox regulation of DUBs and its therapeutic implications in cancer
inferred← citeshttps://doi.org/10.1016/j.semcdb.2012.05.006openalex-snapshot
Quantitative phosphoproteomics to characterize signaling networks
inferred← citeshttps://doi.org/10.1016/j.steroids.2012.12.002openalex-snapshot
PGRMC2, a yet uncharacterized protein with potential as tumor suppressor, migration inhibitor, and regulator of cytochrome P450 enzyme activity
inferred← citeshttps://doi.org/10.1016/j.str.2019.01.002openalex-snapshot
Structural and Functional Characterization of Ubiquitin Variant Inhibitors of USP15
inferred← citeshttps://doi.org/10.1016/j.tcb.2015.03.002openalex-snapshot
The demographics of the ubiquitin system
inferred← citeshttps://doi.org/10.1016/j.tibs.2011.11.001openalex-snapshot
RINGs hold the key to ubiquitin transfer
inferred← citeshttps://doi.org/10.1016/j.tibs.2012.07.001openalex-snapshot
Allosteric post-translational modification codes
inferred← citeshttps://doi.org/10.1016/j.tibs.2016.09.008openalex-snapshot
Emerging Mechanisms in Initiating and Terminating Autophagy
inferred← citeshttps://doi.org/10.1016/j.tips.2022.04.004openalex-snapshot
Thapsigargin: key to new host-directed coronavirus antivirals?
inferred← citeshttps://doi.org/10.1016/j.vetmic.2019.108552openalex-snapshot
Comprehensive analysis of the ubiquitome in rabies virus-infected brain tissue of Mus musculus
inferred← citeshttps://doi.org/10.1016/j.yexcr.2020.112317openalex-snapshot
Ubiquitin-specific protease 4 predicts an unfavorable prognosis and promotes malignant behaviors in vitro in pancreatic cancer
inferred← citeshttps://doi.org/10.1021/acs.analchem.6b04804openalex-snapshot
Large-Scale Filter-Aided Sample Preparation Method for the Analysis of the Ubiquitinome
inferred← citeshttps://doi.org/10.1021/acs.analchem.9b04092openalex-snapshot
Specific and Unbiased Detection of Polyubiquitination via a Sensitive Non-Antibody Approach
inferred← citeshttps://doi.org/10.1021/acs.analchem.9b04340openalex-snapshot
Ac-LysargiNase Complements Trypsin for the Identification of Ubiquitinated Sites
inferred← citeshttps://doi.org/10.1021/acs.biochem.9b01107openalex-snapshot
The Two Deubiquitinating Enzymes from Chlamydia trachomatis Have Distinct Ubiquitin Recognition Properties
inferred← citeshttps://doi.org/10.1021/acs.chemrev.7b00122openalex-snapshot
ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease
inferred← citeshttps://doi.org/10.1021/acs.jproteome.7b00381openalex-snapshot
Ubiquitin Chain Enrichment Middle-Down Mass Spectrometry (UbiChEM-MS) Reveals Cell-Cycle Dependent Formation of Lys11/Lys48 Branched Ubiquitin Chains
inferred← citeshttps://doi.org/10.1021/acsmaterialslett.4c02671openalex-snapshot
Recent Progresses of Peptide Fluorescent Probes for Protein Analysis in Living Cells
inferred← citeshttps://doi.org/10.1021/bi5006305openalex-snapshot
Middle-Down Mass Spectrometry Enables Characterization of Branched Ubiquitin Chains
inferred← citeshttps://doi.org/10.1021/cb2004059openalex-snapshot
Unraveling the Complexity of Ubiquitin Signaling
inferred← citeshttps://doi.org/10.1021/ja300500aopenalex-snapshot
Forging Isopeptide Bonds Using Thiol–Ene Chemistry: Site-Specific Coupling of Ubiquitin Molecules for Studying the Activity of Isopeptidases
inferred← citeshttps://doi.org/10.1021/jacsau.3c00421openalex-snapshot
Cell-Permeable Stimuli-Responsive Ubiquitin Probe for Time-Resolved Monitoring of Substrate Ubiquitination in Live Cells
inferred← citeshttps://doi.org/10.1021/pr5009724openalex-snapshot
Comprehensive Profiling of the Rice Ubiquitome Reveals the Significance of Lysine Ubiquitination in Young Leaves
inferred← citeshttps://doi.org/10.1038/cdd.2013.7openalex-snapshot
The E3 ligase PIRH2 polyubiquitylates CHK2 and regulates its turnover
inferred← citeshttps://doi.org/10.1038/cr.2017.132openalex-snapshot
Excessive UBE3A dosage impairs retinoic acid signaling and synaptic plasticity in autism spectrum disorders
inferred← citeshttps://doi.org/10.1038/cr.2017.40openalex-snapshot
Ubiquitylation of p62/sequestosome1 activates its autophagy receptor function and controls selective autophagy upon ubiquitin stress
inferred← citeshttps://doi.org/10.1038/emboj.2011.237openalex-snapshot
Healthy ageing through regulated proteostasis
inferred← citeshttps://doi.org/10.1038/emboj.2012.148openalex-snapshot
Innate immunity: regulation of caspases by IAP‐dependent ubiquitylation
inferred← citeshttps://doi.org/10.1038/emboj.2012.240openalex-snapshot
A20 inhibits LUBAC‐mediated NF‐κB activation by binding linear polyubiquitin chains via its zinc finger 7
inferred← citeshttps://doi.org/10.1038/embor.2012.164openalex-snapshot
Phosphatidylinositol 4‐kinase IIα function at endosomes is regulated by the ubiquitin ligase Itch
inferred← citeshttps://doi.org/10.1038/ncomms14004openalex-snapshot
Structural basis for the recognition and degradation of host TRIM proteins by Salmonella effector SopA
inferred← citeshttps://doi.org/10.1038/nm.3739openalex-snapshot
Ubiquitination in disease pathogenesis and treatment
inferred← citeshttps://doi.org/10.1038/nprot.2013.089openalex-snapshot
Selective monitoring of ubiquitin signals with genetically encoded ubiquitin chain–specific sensors
inferred← citeshttps://doi.org/10.1038/nsmb.2117openalex-snapshot
Conformational flexibility and rotation of the RING domain in activation of cullin–RING ligases
inferred← citeshttps://doi.org/10.1038/nsmb.3142openalex-snapshot
Secondary ubiquitin-RING docking enhances Arkadia and Ark2C E3 ligase activity
inferred← citeshttps://doi.org/10.1038/onc.2017.313openalex-snapshot
Functional significance and therapeutic implication of ring-type E3 ligases in colorectal cancer
inferred← citeshttps://doi.org/10.1038/s41388-017-0092-0openalex-snapshot
The deubiquitylase USP15 regulates topoisomerase II alpha to maintain genome integrity
inferred← citeshttps://doi.org/10.1038/s41389-026-00621-5openalex-snapshot
Ubiquitin-specific protease 11 suppresses cuproptosis in colorectal cancer by regulating the ubiquitination and stability of ISCU
inferred← citeshttps://doi.org/10.1038/s41418-018-0254-9openalex-snapshot
Post-translational modifications of Beclin 1 provide multiple strategies for autophagy regulation
inferred← citeshttps://doi.org/10.1038/s41419-021-03888-1openalex-snapshot
PRDX2 promotes the proliferation of colorectal cancer cells by increasing the ubiquitinated degradation of p53
inferred← citeshttps://doi.org/10.1038/s41419-026-08582-8openalex-snapshot
K48 and K63 linkage-competed ubiquitination of BECN1 promotes circPDE4D-mediated autophagy in chronic obstructive pulmonary disease
inferred← citeshttps://doi.org/10.1038/s41420-024-02010-6openalex-snapshot
Ubiquitin specific peptidase 3: an emerging deubiquitinase that regulates physiology and diseases
inferred← citeshttps://doi.org/10.1038/s41420-024-02243-5openalex-snapshot
NEDD4L contributes to ferroptosis and cell growth inhibition in esophageal squamous cell carcinoma by facilitating xCT ubiquitination
inferred← citeshttps://doi.org/10.1038/s41467-019-09844-0openalex-snapshot
K27-linked ubiquitination of BRAF by ITCH engages cytokine response to maintain MEK-ERK signaling
inferred← citeshttps://doi.org/10.1038/s41467-020-16211-xopenalex-snapshot
Legionella effector MavC targets the Ube2N~Ub conjugate for noncanonical ubiquitination
inferred← citeshttps://doi.org/10.1038/s41467-021-26429-yopenalex-snapshot
Structural basis for protein glutamylation by the Legionella pseudokinase SidJ
inferred← citeshttps://doi.org/10.1038/s41467-022-29401-6openalex-snapshot
USP8 inhibition reshapes an inflamed tumor microenvironment that potentiates the immunotherapy
inferred← citeshttps://doi.org/10.1038/s41573-023-00749-8openalex-snapshot
The therapeutic potential of targeting regulated non-apoptotic cell death
inferred← citeshttps://doi.org/10.1038/s41577-018-0048-9openalex-snapshot
Forkhead box transcription factors as context-dependent regulators of lymphocyte homeostasis
inferred← citeshttps://doi.org/10.1038/s41594-021-00576-8openalex-snapshot
Structural basis of FANCD2 deubiquitination by USP1−UAF1
inferred← citeshttps://doi.org/10.1038/s41598-019-44595-4openalex-snapshot
CSN5 inhibition triggers inflammatory signaling and Rho/ROCK-dependent loss of endothelial integrity
inferred← citeshttps://doi.org/10.1038/s41598-019-56748-6openalex-snapshot
Inflammatory bowel disease-associated ubiquitin ligase RNF183 promotes lysosomal degradation of DR5 and TRAIL-induced caspase activation
inferred← citeshttps://doi.org/10.1038/s41598-026-49884-3openalex-snapshot
Identification of small ubiquitin-related modifier (SUMO)-related genes-based biomarkers in Alzheimer’s disease based on bioinformatics analysis
inferred← citeshttps://doi.org/10.1038/s42255-022-00572-2openalex-snapshot
β-Klotho promotes glycolysis and glucose-stimulated insulin secretion via GP130
inferred← citeshttps://doi.org/10.1038/srep16694openalex-snapshot
Osteoblast Lineage Cells Play an Essential Role in Periodontal Bone Loss Through Activation of Nuclear Factor-Kappa B
inferred← citeshttps://doi.org/10.1038/srep30955openalex-snapshot
Genome-wide identification and gene expression profiling of ubiquitin ligases for endoplasmic reticulum protein degradation
inferred← citeshttps://doi.org/10.1039/c2mb25052gopenalex-snapshot
The origins and evolution of ubiquitination sites
inferred← citeshttps://doi.org/10.1039/c5an01429hopenalex-snapshot
Identification of a p53-based portable degron based on the MDM2-p53 binding region
inferred← citeshttps://doi.org/10.1042/bcj20160082openalex-snapshot
Ubiquitin C-terminal hydrolase L1 (UCH-L1): structure, distribution and roles in brain function and dysfunction
inferred← citeshttps://doi.org/10.1042/bj20111300openalex-snapshot
A global survey of CRM1-dependent nuclear export sequences in the human deubiquitinase family
inferred← citeshttps://doi.org/10.1042/bj20111815openalex-snapshot
Ubiquitin links to cytoskeletal dynamics, cell adhesion and migration
inferred← citeshttps://doi.org/10.1042/bj20151195openalex-snapshot
Chemical ubiquitination for decrypting a cellular code
inferred← citeshttps://doi.org/10.1042/bsr20150171openalex-snapshot
The cellular response to vascular endothelial growth factors requires co-ordinated signal transduction, trafficking and proteolysis
inferred← citeshttps://doi.org/10.1042/bsr20193537openalex-snapshot
Ubiquitome analysis reveals the involvement of lysine ubiquitination in the spermatogenesis process of adult buffalo (Bubalus bubalis) testis
inferred← citeshttps://doi.org/10.1055/s-0038-1676344openalex-snapshot
Human Platelet Protein Ubiquitylation and Changes following GPVI Activation
inferred← citeshttps://doi.org/10.1073/pnas.1317185110openalex-snapshot
Breaking the limits of artificial ubiquitination
inferred← citeshttps://doi.org/10.1073/pnas.1422313112openalex-snapshot
A comprehensive method for detecting ubiquitinated substrates using TR-TUBE
inferred← citeshttps://doi.org/10.1073/pnas.1620153114openalex-snapshot
Proteasome-independent polyubiquitin linkage regulates synapse scaffolding, efficacy, and plasticity
inferred← citeshttps://doi.org/10.1073/pnas.2005539118openalex-snapshot
Downregulation of autophagy by Met30-mediated Atg9 ubiquitination
inferred← citeshttps://doi.org/10.1073/pnas.2425831122openalex-snapshot
Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain
inferred← citeshttps://doi.org/10.1074/jbc.m112.347195openalex-snapshot
Analysis of Nuclear Factor-κB (NF-κB) Essential Modulator (NEMO) Binding to Linear and Lysine-linked Ubiquitin Chains and Its Role in the Activation of NF-κB
inferred← citeshttps://doi.org/10.1074/jbc.m112.364752openalex-snapshot
Molecular Basis of Lys-63-linked Polyubiquitination Inhibition by the Interaction between Human Deubiquitinating Enzyme OTUB1 and Ubiquitin-conjugating Enzyme UBC13
inferred← citeshttps://doi.org/10.1074/jbc.m112.390294openalex-snapshot
Spg5 Protein Regulates the Proteasome in Quiescence
inferred← citeshttps://doi.org/10.1074/jbc.m112.413393openalex-snapshot
Role of RNF4 in the Ubiquitination of Rta of Epstein-Barr Virus
inferred← citeshttps://doi.org/10.1074/jbc.m113.545475openalex-snapshot
The Ubiquitin-associated Domain of Cellular Inhibitor of Apoptosis Proteins Facilitates Ubiquitylation
inferred← citeshttps://doi.org/10.1074/jbc.ra118.002896openalex-snapshot
NFAT5 up-regulates expression of the kidney-specific ubiquitin ligase gene Rnf183 under hypertonic conditions in inner-medullary collecting duct cells
inferred← citeshttps://doi.org/10.1074/mcp.m111.013284openalex-snapshot
A Proteome-wide, Quantitative Survey of In Vivo Ubiquitylation Sites Reveals Widespread Regulatory Roles
inferred← citeshttps://doi.org/10.1074/mcp.m112.017905openalex-snapshot
Proteomic Analyses Reveal Divergent Ubiquitylation Site Patterns in Murine Tissues
inferred← citeshttps://doi.org/10.1080/08941939.2020.1863527openalex-snapshot
Prognostic Value and Molecular Mechanisms of Proteasome 26S Subunit, Non-ATPase Family Genes for Pancreatic Ductal Adenocarcinoma Patients after Pancreaticoduodenectomy
inferred← citeshttps://doi.org/10.1080/13543776.2022.2003780openalex-snapshot
The intriguing role of USP30 inhibitors as deubiquitinating enzymes from the patent literature since 2013
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