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Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1001/archneur.62.1.82openalex-snapshot
Parkin Mutations and Early-Onset Parkinsonism in a Taiwanese Cohort
inferredcites →https://doi.org/10.1002/(sici)1522-2683(19991201)20:18<3551::aid-elps3551>3.0.co;2-2openalex-snapshot
Probability-based protein identification by searching sequence databases using mass spectrometry data
inferredcites →https://doi.org/10.1016/0003-2697(89)90602-7openalex-snapshot
Calculation of protein extinction coefficients from amino acid sequence data
inferredcites →https://doi.org/10.1016/j.jmb.2004.05.035openalex-snapshot
Structure of the C-terminal RING Finger from a RING-IBR-RING/TRIAD Motif Reveals a Novel Zinc-binding Domain Distinct from a RING
inferredcites →https://doi.org/10.1016/j.molcel.2007.01.033openalex-snapshot
Structure of a Herpesvirus-Encoded Cysteine Protease Reveals a Unique Class of Deubiquitinating Enzymes
inferredcites →https://doi.org/10.1016/j.molcel.2009.11.010openalex-snapshot
Insights into Ubiquitin Transfer Cascades from a Structure of a UbcH5B∼Ubiquitin-HECTNEDD4L Complex
inferredcites →https://doi.org/10.1016/j.parkreldis.2004.12.004openalex-snapshot
Early-onset Parkinson's disease in a Chinese population: 99mTc-TRODAT-1 SPECT, Parkin gene analysis and clinical study
inferredcites →https://doi.org/10.1016/j.tibs.2011.11.001openalex-snapshot
RINGs hold the key to ubiquitin transfer
inferredcites →https://doi.org/10.1016/s0092-8674(02)01199-6openalex-snapshot
Crystal Structure of a UBP-Family Deubiquitinating Enzyme in Isolation and in Complex with Ubiquitin Aldehyde
inferredcites →https://doi.org/10.1016/s0968-0004(99)01381-xopenalex-snapshot
A novel transactivation domain in parkin
inferredcites →https://doi.org/10.1016/s1097-2765(02)00774-8openalex-snapshot
Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT Domain E3 Ligase
inferredcites →https://doi.org/10.1021/cb9000348openalex-snapshot
Ubiquitin C-Terminal Electrophiles Are Activity-Based Probes for Identification and Mechanistic Study of Ubiquitin Conjugating Machinery
inferredcites →https://doi.org/10.1038/77060openalex-snapshot
Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
inferredcites →https://doi.org/10.1038/emboj.2012.217openalex-snapshot
The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING‐IBR‐RING domain and the unique LDD extension
inferredcites →https://doi.org/10.1038/embor.2012.105openalex-snapshot
LUBAC synthesizes linear ubiquitin chains via a thioester intermediate
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/nature09966openalex-snapshot
UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
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/nsmb.1511openalex-snapshot
Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
inferredcites →https://doi.org/10.1038/nsmb.1517openalex-snapshot
Structure of a Shigella effector reveals a new class of ubiquitin ligases
inferredcites →https://doi.org/10.1073/pnas.0610548104openalex-snapshot
Structure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's disease
inferredcites →https://doi.org/10.1073/pnas.0811058106openalex-snapshot
A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases
inferredcites →https://doi.org/10.1074/jbc.273.31.19509openalex-snapshot
Functional Characteristics of the Oxyanion Hole in Human Acetylcholinesterase
inferredcites →https://doi.org/10.1074/jbc.m110.209338openalex-snapshot
Parkin Mediates Proteasome-dependent Protein Degradation and Rupture of the Outer Mitochondrial Membrane
inferredcites →https://doi.org/10.1074/jbc.m111.282020openalex-snapshot
The USP19 Deubiquitinase Regulates the Stability of c-IAP1 and c-IAP2
inferredcites →https://doi.org/10.1074/jbc.m312201200openalex-snapshot
The -4 Phenylalanine Is Required for Substrate Ubiquitination Catalyzed by HECT Ubiquitin Ligases
inferredcites →https://doi.org/10.1074/jbc.m410770200openalex-snapshot
Structure of the Ubiquitin Hydrolase UCH-L3 Complexed with a Suicide Substrate
inferredcites →https://doi.org/10.1074/jbc.m510393200openalex-snapshot
Diverse Effects of Pathogenic Mutations of Parkin That Catalyze Multiple Monoubiquitylation in Vitro
inferredcites →https://doi.org/10.1074/jbc.m704398200openalex-snapshot
Structural Basis for Ubiquitin Recognition by the Otu1 Ovarian Tumor Domain Protein
inferredcites →https://doi.org/10.1074/jbc.m808700200openalex-snapshot
Identification of a Novel Zn2+-binding Domain in the Autosomal Recessive Juvenile Parkinson-related E3 Ligase Parkin
inferredcites →https://doi.org/10.1083/jcb.200809125openalex-snapshot
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
inferredcites →https://doi.org/10.1083/jcb.200910140openalex-snapshot
PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
inferredcites →https://doi.org/10.1083/jcb.201005012openalex-snapshot
Ubiquitin accumulation in autophagy-deficient mice is dependent on the Nrf2-mediated stress response pathway: a potential role for protein aggregation in autophagic substrate selection
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/10.1093/emboj/20.18.5187openalex-snapshot
A novel active site‐directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14
inferredcites →https://doi.org/10.1093/hmg/ddh089openalex-snapshot
Parkin genetics: one model for Parkinson's disease
inferredcites →https://doi.org/10.1093/hmg/ddr048openalex-snapshot
Broad activation of the ubiquitin–proteasome system by Parkin is critical for mitophagy
inferredcites →https://doi.org/10.1093/hmg/dds325openalex-snapshot
ROS-dependent regulation of Parkin and DJ-1 localization during oxidative stress in neurons
inferredcites →https://doi.org/10.1093/nar/gkq366openalex-snapshot
Dali server: conservation mapping in 3D
inferredcites →https://doi.org/10.1098/rsob.120080openalex-snapshot
PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65
inferredcites →https://doi.org/10.1107/s0907444910007493openalex-snapshot
Features and development of Coot
inferredcites →https://doi.org/10.1107/s0907444910045749openalex-snapshot
Overview of the CCP 4 suite and current developments
inferredcites →https://doi.org/10.1107/s0907444996012255openalex-snapshot
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
inferredcites →https://doi.org/10.1111/j.1365-2443.2010.01426.xopenalex-snapshot
p62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria
inferredcites →https://doi.org/10.1146/annurev.biochem.70.1.503openalex-snapshot
Mechanisms Underlying Ubiquitination
inferredcites →https://doi.org/10.1146/annurev.biochem.78.101807.093809openalex-snapshot
RING Domain E3 Ubiquitin Ligases
inferredcites →https://doi.org/10.1186/1741-7007-10-24openalex-snapshot
Following Ariadne's thread: a new perspective on RBR ubiquitin ligases
inferredcites →https://doi.org/10.1371/journal.pone.0019720openalex-snapshot
Parkin Mediates Apparent E2-Independent Monoubiquitination In Vitro and Contains an Intrinsic Activity That Catalyzes Polyubiquitination
inferredcites →https://doi.org/10.2174/1874091x01105010009openalex-snapshot
Parkin, A Top Level Manager in the Cells Sanitation Department
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Ring E3 Ubiquitin Ligase Bvrnf170 Postively Regulates Salt Tolerance in Transgenic Arabidopsis
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A Small‐Molecule Probe for Selective Profiling and Imaging of Monoamine Oxidase B Activities in Models of Parkinson’s Disease
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A Small‐Molecule Probe for Selective Profiling and Imaging of Monoamine Oxidase B Activities in Models of Parkinson’s Disease
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Chemical Tools for Probing the Ub/Ubl Conjugation Cascades
inferred← citeshttps://doi.org/10.1002/embr.201338225openalex-snapshot
Dynamic survey of mitochondria by ubiquitin
inferred← citeshttps://doi.org/10.1002/humu.22808openalex-snapshot
Structural and Functional Impact of Parkinson Disease-Associated Mutations in the E3 Ubiquitin Ligase Parkin
inferred← citeshttps://doi.org/10.1002/jcb.70000openalex-snapshot
Proteasomal Dysfunction in Cancer: Mechanistic Pathways and Targeted Therapies
inferred← citeshttps://doi.org/10.1002/mds.26357openalex-snapshot
Structural studies of parkin and sacsin: Mitochondrial dynamics in neurodegenerative diseases
inferred← citeshttps://doi.org/10.1002/mds.26524openalex-snapshot
Double homozygous mutations (R275W and M432V) in the ParkinGene associated with late‐onset Parkinson's disease
inferred← citeshttps://doi.org/10.1002/med.22041openalex-snapshot
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Characterization of RING-Between-RING E3 Ubiquitin Transfer Mechanisms
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Mutation Analysis in PARK2 Gene Uncovers Patterns of Associated Genetic Variants
inferred← citeshttps://doi.org/10.1007/978-3-319-13939-5_6openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/978-3-319-28637-2_11openalex-snapshot
Mitochondrial Degradation, Autophagy and Neurodegenerative Disease
inferred← citeshttps://doi.org/10.1007/978-3-319-42139-1_8openalex-snapshot
PARKIN/PINK1 Pathway for the Selective Isolation and Degradation of Impaired Mitochondria
inferred← citeshttps://doi.org/10.1007/s00018-019-03203-4openalex-snapshot
Mechanisms of PINK1, ubiquitin and Parkin interactions in mitochondrial quality control and beyond
inferred← citeshttps://doi.org/10.1007/s00109-013-1107-0openalex-snapshot
An emerging role of PARK2 in cancer
inferred← citeshttps://doi.org/10.1007/s00109-013-1112-3openalex-snapshot
Nilotinib-induced autophagic changes increase endogenous parkin level and ubiquitination, leading to amyloid clearance
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Leukemia and mitophagy: a novel perspective for understanding oncogenesis and resistance
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Mitochondrial quality control by the Pink1/Parkin system
inferred← citeshttps://doi.org/10.1007/s00441-024-03912-8openalex-snapshot
An in-depth review of the function of RNA-binding protein FXR1 in neurodevelopment
inferred← citeshttps://doi.org/10.1007/s10571-016-0407-7openalex-snapshot
Parkin Overexpression Ameliorates PrP106–126-Induced Neurotoxicity via Enhanced Autophagy in N2a Cells
inferred← citeshttps://doi.org/10.1007/s10571-020-00914-2openalex-snapshot
Parkin, an E3 Ubiquitin Ligase, Plays an Essential Role in Mitochondrial Quality Control in Parkinson’s Disease
inferred← citeshttps://doi.org/10.1007/s10930-016-9679-5openalex-snapshot
Proteomic Analysis of Parkin Isoforms Expression in Different Rat Brain Areas
inferred← citeshttps://doi.org/10.1007/s11064-015-1598-xopenalex-snapshot
Folic Acid Supplementation Ameliorates Oxidative Stress, Metabolic Functions and Developmental Anomalies in a Novel Fly Model of Parkinson’s Disease
inferred← citeshttps://doi.org/10.1007/s12035-021-02494-8openalex-snapshot
Mitochondrial Quality Control in Cerebral Ischemia–Reperfusion Injury
inferred← citeshttps://doi.org/10.1007/s12640-019-00060-8openalex-snapshot
Neuronal Mitophagy: Lessons from a Pathway Linked to Parkinson’s Disease
inferred← citeshttps://doi.org/10.1007/s13238-016-0307-0openalex-snapshot
The critical roles of mitophagy in cerebral ischemia
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Mitochondria: how eminent in ageing and neurodegenerative disorders?
inferred← citeshttps://doi.org/10.1016/b978-0-12-801032-7.00018-6openalex-snapshot
The Role of Parkin and PINK1 in Mitochondrial Quality Control
inferred← citeshttps://doi.org/10.1016/b978-0-12-821562-3.00037-xopenalex-snapshot
Mitochondrial biogenesis and mitophagy
inferred← citeshttps://doi.org/10.1016/b978-0-443-15260-3.00013-2openalex-snapshot
PINK1-Parkin quality control mitophagy pathway in Parkinson’s disease
inferred← citeshttps://doi.org/10.1016/bs.ircmb.2015.05.003openalex-snapshot
New Insights into the Role of Ubiquitin Networks in the Regulation of Antiapoptosis Pathways
inferred← citeshttps://doi.org/10.1016/bs.pmbts.2016.04.003openalex-snapshot
Chapter Nine - Cellular Roles of Beta-Arrestins as Substrates and Adaptors of Ubiquitination and Deubiquitination
inferred← citeshttps://doi.org/10.1016/j.arr.2022.101817openalex-snapshot
PINK1/Parkin-mediated mitophagy in neurodegenerative diseases
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Ubiquitin E3 ligases assisted technologies in protein degradation: Sharing pathways in neurodegenerative disorders and cancer
inferred← citeshttps://doi.org/10.1016/j.bbabio.2016.03.014openalex-snapshot
Central Parkin: The evolving role of Parkin in the heart
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The regulation of mitochondrial homeostasis by the ubiquitin proteasome system
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Mitochondrial and calcium perturbations in rat CNS neurons induce calpain-cleavage of Parkin: Phosphatase inhibition stabilizes pSer65Parkin reducing its calpain-cleavage
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A mechanistic review of Parkin activation
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Molecular mechanisms underlying PINK1 and Parkin catalyzed ubiquitylation of substrates on damaged mitochondria
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Cell death as a result of calcium signaling modulation: A cancer-centric prospective
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Decreased amount of vimentin N-terminal truncated proteolytic products in parkin-mutant skin fibroblasts
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E3 ubiquitin ligases and their therapeutic potential in disease Management
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Defending the mitochondria: The pathways of mitophagy and mitochondrial-derived vesicles
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Parkin and PINK1 functions in oxidative stress and neurodegeneration
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Unraveling correlative roles of dopamine transporter (DAT) and Parkin in Parkinson’s disease (PD) – A road to discovery?
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Genome-wide identification and analysis of HECT E3 ubiquitin ligase gene family in Ruditapes philippinarum and their involvement in the response to heat stress and Vibrio anguillarum infection
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PINK1/Parkin-mediated mitophagy in mammalian cells
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Single-Domain Antibodies as Crystallization Chaperones to Enable Structure-Based Inhibitor Development for RBR E3 Ubiquitin Ligases
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Self and Nonself: How Autophagy Targets Mitochondria and Bacteria
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Beyond CRBN and VHL: Parkin driven lysine-based ternary complexes for selective β3-Tubulin degradation
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PTEN-induced kinase 1 (PINK1) and Parkin: Unlocking a mitochondrial quality control pathway linked to Parkinson's disease
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Novel insights into Parkin-mediated mitochondrial dysfunction and neuroinflammation in Parkinson's disease
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Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance
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Parkin is a critical factor in grouper immune response to virus infection
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Diquat exacerbates oxidative stress and neuroinflammation by blocking the autophagic flux of microglia in the hippocampus
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The use of nanopore analysis for discovering drugs which bind to α-synuclein for treatment of Parkinson's disease
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The cysteine proteome
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Mechanisms of mitophagy: PINK1, Parkin, USP30 and beyond
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A comprehensive computational study on pathogenic mis-sense mutations spanning the RING2 and REP domains of Parkin protein
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Analysis of the structural dynamics of the mutations in the kinase domain of PINK1 protein associated with Parkinson’s disease
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Parkin, a key player in Parkinson's disease pathogenesis: A review
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PINK1/Parkin-mediated mitophagy in cardiovascular disease: From pathogenesis to novel therapy
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Hepatic ischemia-reperfusion and mitochondrial quality control: potential therapeutic targets
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Engineering a cell-based orthogonal ubiquitin transfer cascade for profiling the substrates of RBR E3 Parkin
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Structure of the second phosphoubiquitin–binding site in parkin
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Structural basis for the pathogenicity of parkin catalytic domain mutants
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When Worlds Collide—Mechanisms at the Interface between Phosphorylation and Ubiquitination
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RING-Between-RING E3 Ligases: Emerging Themes amid the Variations
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Ubiquitin and Receptor-Dependent Mitophagy Pathways and Their Implication in Neurodegeneration
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Role of Autophagy Pathway in Parkinson’s Disease and Related Genetic Neurological Disorders
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Complex Conformational Interplay for Parkin Activation is Revealed by 19F NMR Spectroscopy
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Methods to detect mitophagy in neurons during disease
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The Ku–Mar zinc finger: A segment-swapped zinc ribbon in MarR-like transcription regulators related to the Ku bridge
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PHF23 negatively regulates the autophagy of chondrocytes in osteoarthritis
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Mitochondrial transfer in the progression and treatment of cardiac disease
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Unlocking immune responses via mitophagy genes: A dual-pronged strategy against hematologic tumors
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Molecular targets and approaches to restore autophagy and lysosomal capacity in neurodegenerative disorders
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Pathologic and therapeutic implications for the cell biology of parkin
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Autophagy and lysosomal pathways in nervous system disorders
inferred← citeshttps://doi.org/10.1016/j.mito.2014.11.001openalex-snapshot
Parkin modulates heteroplasmy of truncated mtDNA in Caenorhabditis elegans
inferred← citeshttps://doi.org/10.1016/j.mito.2024.101928openalex-snapshot
Role of mitophagy in pulmonary hypertension: Targeting the mechanism and pharmacological intervention
inferred← citeshttps://doi.org/10.1016/j.molcel.2014.09.007openalex-snapshot
Quantitative Proteomics Reveal a Feedforward Mechanism for Mitochondrial PARKIN Translocation and Ubiquitin Chain Synthesis
inferred← citeshttps://doi.org/10.1016/j.molcel.2015.08.011openalex-snapshot
Parkin Regulates Mitosis and Genomic Stability through Cdc20/Cdh1
inferred← citeshttps://doi.org/10.1016/j.neubiorev.2017.07.017openalex-snapshot
The role of hypernitrosylation in the pathogenesis and pathophysiology of neuroprogressive diseases
inferred← citeshttps://doi.org/10.1016/j.neuint.2015.03.007openalex-snapshot
Linking a compound-heterozygous Parkin mutant (Q311R and A371T) to Parkinson's disease by using proteomic and molecular approaches
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.neures.2020.01.006openalex-snapshot
The PINK1–Parkin axis: An Overview
inferred← citeshttps://doi.org/10.1016/j.neures.2020.03.009openalex-snapshot
Two sides of a coin: Physiological significance and molecular mechanisms for damage-induced mitochondrial localization of PINK1 and Parkin
inferred← citeshttps://doi.org/10.1016/j.neuron.2014.12.007openalex-snapshot
The Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson’s Disease
inferred← citeshttps://doi.org/10.1016/j.neuroscience.2025.03.052openalex-snapshot
Defective PINK1-dependent mitophagy is involved in high glucose-induced neurotoxicity
inferred← citeshttps://doi.org/10.1016/j.pharmthera.2017.04.005openalex-snapshot
Mitophagy and age-related pathologies: Development of new therapeutics by targeting mitochondrial turnover
inferred← citeshttps://doi.org/10.1016/j.phrs.2015.09.020openalex-snapshot
Targeting Pink1-Parkin-mediated mitophagy for treating liver injury
inferred← citeshttps://doi.org/10.1016/j.phymed.2024.155472openalex-snapshot
Traditional Chinese medicine and mitophagy: A novel approach for cardiovascular disease management
inferred← citeshttps://doi.org/10.1016/j.redox.2020.101767openalex-snapshot
The PINK1/PARK2/optineurin pathway of mitophagy is activated for protection in septic acute kidney injury
inferred← citeshttps://doi.org/10.1016/j.semcancer.2020.03.006openalex-snapshot
NEDD4 E3 ligase: Functions and mechanism in human cancer
inferred← citeshttps://doi.org/10.1016/j.str.2017.04.013openalex-snapshot
Structural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1
inferred← citeshttps://doi.org/10.1016/j.str.2022.05.017openalex-snapshot
Cullin-independent recognition of HHARI substrates by a dynamic RBR catalytic domain
inferred← citeshttps://doi.org/10.1016/j.str.2024.09.012openalex-snapshot
Mechanism of phospho-Ubls’ specificity and conformational changes that regulate Parkin activity
inferred← citeshttps://doi.org/10.1016/j.tcb.2013.12.003openalex-snapshot
Perilous journey: a tour of the ubiquitin–proteasome system
inferred← citeshttps://doi.org/10.1016/j.tcb.2014.01.001openalex-snapshot
Parkin and mitochondrial quality control: toward assembling the puzzle
inferred← citeshttps://doi.org/10.1016/j.tibs.2016.08.003openalex-snapshot
Noncovalent Ubiquitin Interactions Regulate the Catalytic Activity of Ubiquitin Writers
inferred← citeshttps://doi.org/10.1016/j.tim.2022.03.010openalex-snapshot
Bag it, tag it: ubiquitin ligases and host resistance to Mycobacterium tuberculosis
inferred← citeshttps://doi.org/10.1016/j.xcrm.2026.103015openalex-snapshot
Lysyl oxidase inhibition disrupts mitochondrial homeostasis to create vulnerability to ferroptosis in TNBC
inferred← citeshttps://doi.org/10.1016/s0891-5849(03)00485-4openalex-snapshot
Free radical biology and medicine
inferred← citeshttps://doi.org/10.1021/acs.biochem.6c00007openalex-snapshot
Mitochondrial Ubiquitination as a Signaling Hub: Balancing Mitophagy, Inflammation, and Cell Death
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5c02124openalex-snapshot
Mechanistic Insights into Ligand-Mediated Modulation of 14-3-3η/Parkin Interaction through Molecular Dynamics and Enhanced Sampling Simulations
inferred← citeshttps://doi.org/10.1021/acschemneuro.0c00366openalex-snapshot
Piperine-Coated Gold Nanoparticles Alleviate Paraquat-Induced Neurotoxicity in Drosophila melanogaster
inferred← citeshttps://doi.org/10.1021/acschemneuro.4c00630openalex-snapshot
Computational Study of the Activation Mechanism of Wild-Type Parkin and Its Clinically Relevant Mutant
inferred← citeshttps://doi.org/10.1021/bi400780vopenalex-snapshot
Ataxin-3 Is a Multivalent Ligand for the Parkin Ubl Domain
inferred← citeshttps://doi.org/10.1038/cddis.2014.278openalex-snapshot
Inhibition of apoptotic Bax translocation to the mitochondria is a central function of parkin
inferred← citeshttps://doi.org/10.1038/cr.2014.79openalex-snapshot
Phosphorylated ubiquitin: a new shade of PINK1 in Parkin activation
inferred← citeshttps://doi.org/10.1038/emboj.2013.158openalex-snapshot
Compact Parkin only: insights into the structure of an autoinhibited ubiquitin ligase
inferred← citeshttps://doi.org/10.1038/emboj.2013.209openalex-snapshot
TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin‐RING ligase complexes
inferred← citeshttps://doi.org/10.1038/nature12638openalex-snapshot
Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP
inferred← citeshttps://doi.org/10.1038/nature13392openalex-snapshot
Ubiquitin is phosphorylated by PINK1 to activate parkin
inferred← citeshttps://doi.org/10.1038/nature14879openalex-snapshot
Mechanism of phospho-ubiquitin-induced PARKIN activation
inferred← citeshttps://doi.org/10.1038/nature16511openalex-snapshot
Structure of a HOIP/E2~ubiquitin complex reveals RBR E3 ligase mechanism and regulation
inferred← citeshttps://doi.org/10.1038/nchembio.2045openalex-snapshot
Probes of ubiquitin E3 ligases enable systematic dissection of parkin activation
inferred← citeshttps://doi.org/10.1038/ncomms14697openalex-snapshot
Structure-guided mutagenesis reveals a hierarchical mechanism of Parkin activation
inferred← citeshttps://doi.org/10.1038/ncomms4276openalex-snapshot
A sensitive two-photon probe to selectively detect monoamine oxidase B activity in Parkinson’s disease models
inferred← citeshttps://doi.org/10.1038/nrm.2016.91openalex-snapshot
Structural insights into the catalysis and regulation of E3 ubiquitin ligases
inferred← citeshttps://doi.org/10.1038/nrm.2017.129openalex-snapshot
Building and decoding ubiquitin chains for mitophagy
inferred← citeshttps://doi.org/10.1038/nrm3919openalex-snapshot
Protein neddylation: beyond cullin–RING ligases
inferred← citeshttps://doi.org/10.1038/nsmb.2780openalex-snapshot
New insights into ubiquitin E3 ligase mechanism
inferred← citeshttps://doi.org/10.1038/nsmb.3400openalex-snapshot
Parkin–phosphoubiquitin complex reveals cryptic ubiquitin-binding site required for RBR ligase activity
inferred← citeshttps://doi.org/10.1038/s41418-020-00706-7openalex-snapshot
Ubiquitin signalling in neurodegeneration: mechanisms and therapeutic opportunities
inferred← citeshttps://doi.org/10.1038/s41418-021-00922-9openalex-snapshot
The role of Ubiquitination in Apoptosis and Necroptosis
inferred← citeshttps://doi.org/10.1038/s41418-023-01251-9openalex-snapshot
Activation of Ca2+ phosphatase Calcineurin regulates Parkin translocation to mitochondria and mitophagy in flies
inferred← citeshttps://doi.org/10.1038/s41419-022-04906-6openalex-snapshot
Mitochondrial autophagy: molecular mechanisms and implications for cardiovascular disease
inferred← citeshttps://doi.org/10.1038/s41422-025-01203-7openalex-snapshot
Mitophagy in the pathogenesis and management of disease
inferred← citeshttps://doi.org/10.1038/s41467-017-00272-6openalex-snapshot
Structural insights into the mechanism and E2 specificity of the RBR E3 ubiquitin ligase HHARI
inferred← citeshttps://doi.org/10.1038/s41467-017-01947-wopenalex-snapshot
Parkin targets HIF-1α for ubiquitination and degradation to inhibit breast tumor progression
inferred← citeshttps://doi.org/10.1038/s41467-023-35871-zopenalex-snapshot
The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family
inferred← citeshttps://doi.org/10.1038/s41467-024-51889-3openalex-snapshot
Activation of parkin by a molecular glue
inferred← citeshttps://doi.org/10.1038/s41531-024-00707-0openalex-snapshot
PARKIN is not required to sustain OXPHOS function in adult mammalian tissues
inferred← citeshttps://doi.org/10.1038/s41556-018-0176-2openalex-snapshot
Mechanisms of mitophagy in cellular homeostasis, physiology and pathology
inferred← citeshttps://doi.org/10.1038/s41556-026-01886-zopenalex-snapshot
Lysine-11 ubiquitination drives type-I/III interferon induction by cGAS–STING and Toll-like receptors 3 and 4
inferred← citeshttps://doi.org/10.1038/s41573-024-01105-0openalex-snapshot
Targeting mitophagy in neurodegenerative diseases
inferred← citeshttps://doi.org/10.1038/s41586-018-0224-xopenalex-snapshot
Mechanism of parkin activation by PINK1
inferred← citeshttps://doi.org/10.1038/s41586-021-03197-9openalex-snapshot
Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assembly
inferred← citeshttps://doi.org/10.1038/s41589-021-00858-8openalex-snapshot
CUL5-ARIH2 E3-E3 ubiquitin ligase structure reveals cullin-specific NEDD8 activation
inferred← citeshttps://doi.org/10.1038/s41594-018-0063-3openalex-snapshot
RBR ligase–mediated ubiquitin transfer: a tale with many twists and turns
inferred← citeshttps://doi.org/10.1038/s41594-018-0088-7openalex-snapshot
Mechanism of parkin activation by phosphorylation
inferred← citeshttps://doi.org/10.1038/s41598-018-20860-wopenalex-snapshot
Impact of different ionization states of phosphorylated Serine-65 on ubiquitin structure and interactions
inferred← citeshttps://doi.org/10.1038/s41598-018-28656-8openalex-snapshot
Structural insights into ubiquitin phosphorylation by PINK1
inferred← citeshttps://doi.org/10.1038/s41598-020-61796-4openalex-snapshot
Mdm2 enhances ligase activity of parkin and facilitates mitophagy
inferred← citeshttps://doi.org/10.1038/s41598-022-18890-6openalex-snapshot
Characterisation of HOIP RBR E3 ligase conformational dynamics using integrative modelling
inferred← citeshttps://doi.org/10.1038/s42003-024-06656-xopenalex-snapshot
Naturally occurring hyperactive variants of human parkin
inferred← citeshttps://doi.org/10.1038/srep33019openalex-snapshot
Structural insights into Parkin substrate lysine targeting from minimal Miro substrates
inferred← citeshttps://doi.org/10.1038/srep39318openalex-snapshot
Deficiency of Mkrn2 causes abnormal spermiogenesis and spermiation, and impairs male fertility
inferred← citeshttps://doi.org/10.1038/srep43748openalex-snapshot
Determination of the pKa of the N-terminal amino group of ubiquitin by NMR
inferred← citeshttps://doi.org/10.1042/bcj20160498openalex-snapshot
Ubiquitin and Parkinson's disease through the looking glass of genetics
inferred← citeshttps://doi.org/10.1042/bcj20170476openalex-snapshot
Activation mechanisms of the E3 ubiquitin ligase parkin
inferred← citeshttps://doi.org/10.1042/bcj20210741openalex-snapshot
Distinct phosphorylation signals drive acceptor versus free ubiquitin chain targeting by parkin
inferred← citeshttps://doi.org/10.1042/bj20140006openalex-snapshot
RBR E3 ubiquitin ligases: new structures, new insights, new questions
inferred← citeshttps://doi.org/10.1042/bj20140334openalex-snapshot
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65
inferred← citeshttps://doi.org/10.1042/bj20140459openalex-snapshot
Switching on ubiquitylation by phosphorylating a ubiquitous activator
inferred← citeshttps://doi.org/10.1042/bsr20221036openalex-snapshot
Redefining the catalytic HECT domain boundaries for the HECT E3 ubiquitin ligase family
inferred← citeshttps://doi.org/10.1042/bst20140321openalex-snapshot
Activation of the E3 ubiquitin ligase Parkin
inferred← citeshttps://doi.org/10.1042/bst20150209openalex-snapshot
Specificity and disease in the ubiquitin system
inferred← citeshttps://doi.org/10.1042/bst20160400openalex-snapshot
Bio-Zombie: the rise of pseudoenzymes in biology
inferred← citeshttps://doi.org/10.1042/bst20200237openalex-snapshot
Chain reactions: molecular mechanisms of RBR ubiquitin ligases
inferred← citeshttps://doi.org/10.1042/bst20211107openalex-snapshot
Therapeutic targeting of mitophagy in Parkinson's disease
inferred← citeshttps://doi.org/10.1042/bst20253050openalex-snapshot
Canonical and alternate mechanisms that regulate ubiquitylation by the E3 ligase parkin
inferred← citeshttps://doi.org/10.1042/ebc20253048openalex-snapshot
Cis or trans: a puzzle of Parkin activation mechanism
inferred← citeshttps://doi.org/10.1073/pnas.1506593112openalex-snapshot
Defining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy
inferred← citeshttps://doi.org/10.1073/pnas.1612283113openalex-snapshot
Miro phosphorylation sites regulate Parkin recruitment and mitochondrial motility
inferred← citeshttps://doi.org/10.1073/pnas.1613040114openalex-snapshot
Structure of phosphorylated UBL domain and insights into PINK1-orchestrated parkin activation
inferred← citeshttps://doi.org/10.1073/pnas.1915534117openalex-snapshot
Proteins containing ubiquitin-like (Ubl) domains not only bind to 26S proteasomes but also induce their activation
inferred← citeshttps://doi.org/10.1073/pnas.2403114121openalex-snapshot
Capturing the catalytic intermediates of parkin ubiquitination
inferred← citeshttps://doi.org/10.1073/pnas.2524899122openalex-snapshot
E2 variants for probing E3 ubiquitin ligase activities
inferred← citeshttps://doi.org/10.1074/jbc.m113.467530openalex-snapshot
Parkin-catalyzed Ubiquitin-Ester Transfer Is Triggered by PINK1-dependent Phosphorylation
inferred← citeshttps://doi.org/10.1074/jbc.m113.495846openalex-snapshot
Target Specificity of the E3 Ligase LUBAC for Ubiquitin and NEMO Relies on Different Minimal Requirements
inferred← citeshttps://doi.org/10.1074/jbc.m114.607150openalex-snapshot
Short Mitochondrial ARF Triggers Parkin/PINK1-dependent Mitophagy
inferred← citeshttps://doi.org/10.1074/jbc.m115.649269openalex-snapshot
Itch WW Domains Inhibit Its E3 Ubiquitin Ligase Activity by Blocking E2-E3 Ligase Trans-thiolation
inferred← citeshttps://doi.org/10.1074/jbc.m115.671446openalex-snapshot
Site-specific Interaction Mapping of Phosphorylated Ubiquitin to Uncover Parkin Activation
inferred← citeshttps://doi.org/10.1074/jbc.m115.687319openalex-snapshot
Interaction between RING1 (R1) and the Ubiquitin-like (UBL) Domains Is Critical for the Regulation of Parkin Activity
inferred← citeshttps://doi.org/10.1074/jbc.m116.728600openalex-snapshot
Dual Function of Phosphoubiquitin in E3 Activation of Parkin
inferred← citeshttps://doi.org/10.1074/jbc.m116.773200openalex-snapshot
UbMES and UbFluor: Novel probes for ring-between-ring (RBR) E3 ubiquitin ligase PARKIN
inferred← citeshttps://doi.org/10.1074/jbc.r115.653675openalex-snapshot
Using Protein Motion to Read, Write, and Erase Ubiquitin Signals
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