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The membrane peroxin PEX3 induces peroxisome-ubiquitination-linked pexophagy

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1007/s00418-009-0564-6openalex-snapshot
Degradation of excess peroxisomes in mammalian liver cells by autophagy and other mechanisms
inferredcites →https://doi.org/10.1016/j.bbamcr.2006.09.030openalex-snapshot
Import of peroxisomal membrane proteins: The interplay of Pex3p- and Pex19p-mediated interactions
inferredcites →https://doi.org/10.1016/j.ceb.2011.03.003openalex-snapshot
Ubiquitination-mediated autophagy against invading bacteria
inferredcites →https://doi.org/10.1016/j.devcel.2007.12.011openalex-snapshot
PpAtg30 Tags Peroxisomes for Turnover by Selective Autophagy
inferredcites →https://doi.org/10.1016/j.molcel.2009.01.020openalex-snapshot
A Role for NBR1 in Autophagosomal Degradation of Ubiquitinated Substrates
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.yexcr.2008.09.015openalex-snapshot
The peroxin Pex14p is involved in LC3-dependent degradation of mammalian peroxisomes
inferredcites →https://doi.org/10.1016/j.ymgme.2004.08.016openalex-snapshot
Peroxisomes, lipid metabolism, and peroxisomal disorders
inferredcites →https://doi.org/10.1016/s0014-5793(00)01667-7openalex-snapshot
Peroxisome biogenesis and peroxisome biogenesis disorders
inferredcites →https://doi.org/10.1016/s0168-9525(00)02056-4openalex-snapshot
Peroxisome biogenesis disorders
inferredcites →https://doi.org/10.1038/emboj.2010.293openalex-snapshot
Structural basis for docking of peroxisomal membrane protein carrier Pex19p onto its receptor Pex3p
inferredcites →https://doi.org/10.1038/emboj.2012.151openalex-snapshot
Pex3‐anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1038/nature10744openalex-snapshot
Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
inferredcites →https://doi.org/10.1073/pnas.0810611105openalex-snapshot
Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes
inferredcites →https://doi.org/10.1073/pnas.95.14.8087openalex-snapshot
Identification of a human PTS1 receptor docking protein directly required for peroxisomal protein import
inferredcites →https://doi.org/10.1073/pnas.96.5.2116openalex-snapshot
Human PEX19 : cDNA cloning by functional complementation, mutation analysis in a patient with Zellweger syndrome, and potential role in peroxisomal membrane assembly
inferredcites →https://doi.org/10.1074/jbc.274.18.12593openalex-snapshot
The Peroxin Pex14p
inferredcites →https://doi.org/10.1074/jbc.m000720200openalex-snapshot
The Mammalian Peroxin Pex5pL, the Longer Isoform of the Mobile Peroxisome Targeting Signal (PTS) Type 1 Transporter, Translocates the Pex7p·PTS2 Protein Complex into Peroxisomes via Its Initial Docking Site, Pex14p
inferredcites →https://doi.org/10.1074/jbc.m108635200openalex-snapshot
Intracellular Localization, Function, and Dysfunction of the Peroxisome-targeting Signal Type 2 Receptor, Pex7p, in Mammalian Cells
inferredcites →https://doi.org/10.1074/jbc.m111.285197openalex-snapshot
Two Proteases, Trypsin Domain-containing 1 (Tysnd1) and Peroxisomal Lon Protease (PsLon), Cooperatively Regulate Fatty Acid β-Oxidation in Peroxisomal Matrix
inferredcites →https://doi.org/10.1074/jbc.m509819200openalex-snapshot
In Vitro Transport of Membrane Proteins to Peroxisomes by Shuttling Receptor Pex19p
inferredcites →https://doi.org/10.1074/jbc.m512283200openalex-snapshot
Excess Peroxisomes Are Degraded by Autophagic Machinery in Mammals
inferredcites →https://doi.org/10.1074/jbc.m600158200openalex-snapshot
Functional Domains and Dynamic Assembly of the Peroxin Pex14p, the Entry Site of Matrix Proteins
inferredcites →https://doi.org/10.1074/jbc.m706139200openalex-snapshot
Characterization of the Interaction between Recombinant Human Peroxin Pex3p and Pex19p
inferredcites →https://doi.org/10.1083/jcb.110.3.651openalex-snapshot
Isolation and characterization of Chinese hamster ovary cell mutants defective in assembly of peroxisomes.
inferredcites →https://doi.org/10.1083/jcb.200311131openalex-snapshot
PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins
inferredcites →https://doi.org/10.1083/jcb.200412022openalex-snapshot
Impairment of starvation-induced and constitutive autophagy in Atg7 -deficient mice
inferredcites →https://doi.org/10.1083/jcb.200507002openalex-snapshot
p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
inferredcites →https://doi.org/10.1083/jcb.200806062openalex-snapshot
The peroxisomal membrane protein import receptor Pex3p is directly transported to peroxisomes by a novel Pex19p- and Pex16p-dependent pathway
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/10.1083/jcb.201211077openalex-snapshot
Tail-anchored PEX26 targets peroxisomes via a PEX19-dependent and TRC40-independent class I pathway
inferredcites →https://doi.org/10.1086/302161openalex-snapshot
Mutation in Is Causal in the Peroxisome-Deficient Zellweger Syndrome of Complementation Group D
inferredcites →https://doi.org/10.1091/mbc.11.6.2085openalex-snapshot
The Peroxin Pex3p Initiates Membrane Assembly in Peroxisome Biogenesis
inferredcites →https://doi.org/10.1093/emboj/19.21.5720openalex-snapshot
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
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/10.1111/j.1600-0854.2012.01391.xopenalex-snapshot
Pex5p Imports Folded Tetrameric Catalase by Interaction with Pex13p
inferredcites →https://doi.org/10.1128/mcb.00878-10openalex-snapshot
Nbr1 Is a Novel Inhibitor of Ligand-Mediated Receptor Tyrosine Kinase Degradation
inferredcites →https://doi.org/10.1128/mcb.18.1.388openalex-snapshot
Peroxisome Targeting Signal Type 1 (PTS1) Receptor Is Involved in Import of Both PTS1 and PTS2: Studies with PEX5 -Defective CHO Cell Mutants
inferredcites →https://doi.org/10.1128/mcb.22.6.1639-1655.2002openalex-snapshot
Peroxisomal Targeting Signal Receptor Pex5p Interacts with Cargoes and Import Machinery Components in a Spatiotemporally Differentiated Manner: Conserved Pex5p WXXXF/Y Motifs Are Critical for Matrix Protein Import
inferredcites →https://doi.org/10.1146/annurev.bi.61.070192.001105openalex-snapshot
BIOCHEMISTRY OF PEROXISOMES
inferredcites →https://doi.org/10.1152/physrev.1966.46.2.323openalex-snapshot
Peroxisomes (microbodies and related particles).
inferredcites →https://doi.org/10.1155/2012/512721openalex-snapshot
Pexophagy: The Selective Degradation of Peroxisomes
inferredcites →https://doi.org/10.1155/2012/736905openalex-snapshot
Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy
inferredcites →https://doi.org/10.1242/jcs.01131openalex-snapshot
LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation
inferredcites →https://doi.org/10.1242/jcs.03100openalex-snapshot
Functional domain mapping of peroxin Pex19p: interaction with Pex3p is essential for function and translocation
inferredcites →https://doi.org/10.1242/jcs.114819openalex-snapshot
NBR1 acts as an autophagy receptor for peroxisomes
inferredcites →https://doi.org/10.4161/auto.5.5.8566openalex-snapshot
NBR1 co-operates with p62 in selective autophagy of ubiquitinated targets
inferredcites →https://doi.org/10.4161/auto.7.3.14487openalex-snapshot
Selective autophagy mediated by autophagic adapter proteins
inferredcites →https://doi.org/10.4161/cc.8.13.8892openalex-snapshot
NBR1 and p62 as cargo receptors for selective autophagy of ubiquitinated targets

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.4793027openalex-extracted
Intricacies of Lipid Supply in Autophagic Membrane Expansion
inferred← citeshttps://doi.org/10.1002/1873-3468.13340openalex-snapshot
The peroxisome biogenesis factors Pex3 and Pex19: multitasking proteins with disputed functions
inferred← citeshttps://doi.org/10.1002/9780470747919.ch13openalex-snapshot
Peroxisome Assembly, Degradation, and Disease
inferred← citeshttps://doi.org/10.1002/9781119436812.ch12openalex-snapshot
Peroxisome Assembly, Degradation, and Disease
inferred← citeshttps://doi.org/10.1007/978-1-0716-3048-8_34openalex-snapshot
Mouse Models to Study Peroxisomal Functions and Disorders: Overview, Caveats, and Recommendations
inferred← citeshttps://doi.org/10.1007/978-1-4939-6937-1_23openalex-snapshot
Assessing Pexophagy in Mammalian Cells
inferred← citeshttps://doi.org/10.1007/978-981-15-1169-1_3openalex-snapshot
Peroxisome Degradation and Its Molecular Machinery
inferred← citeshttps://doi.org/10.1007/s00018-020-03667-9openalex-snapshot
Selective autophagy as a therapeutic target for neurological diseases
inferred← citeshttps://doi.org/10.1007/s00018-020-03687-5openalex-snapshot
Regulation of peroxisomal trafficking and distribution
inferred← citeshttps://doi.org/10.1007/s00418-018-1724-3openalex-snapshot
Pexophagy in yeast and mammals: an update on mysteries
inferred← citeshttps://doi.org/10.1016/b978-0-12-801238-3.65924-xopenalex-snapshot
Peroxisome Biogenesis Disorders
inferred← citeshttps://doi.org/10.1016/b978-0-12-805421-5.00002-1openalex-snapshot
Molecular Mechanisms Underlying the Degradation of Peroxisomes
inferred← citeshttps://doi.org/10.1016/bs.ircmb.2025.11.006openalex-snapshot
From autophagy to mitophagy: Quality control mechanisms in skeletal muscle
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.09.024openalex-snapshot
Proliferation and fission of peroxisomes — An update
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.09.031openalex-snapshot
Towards the molecular mechanism of the integration of peroxisomal membrane proteins
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.09.032openalex-snapshot
Peroxisome homeostasis: Mechanisms of division and selective degradation of peroxisomes in mammals
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.09.034openalex-snapshot
Structural biology of the import pathways of peroxisomal matrix proteins
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.12.022openalex-snapshot
Regulation of peroxisome dynamics by phosphorylation
inferred← citeshttps://doi.org/10.1016/j.bbrc.2015.09.153openalex-snapshot
Pexophagy is induced by increasing peroxisomal reactive oxygen species in 1′10-phenanthroline-treated cells
inferred← citeshttps://doi.org/10.1016/j.bbrc.2015.12.098openalex-snapshot
2,2′-dipyridyl induces pexophagy
inferred← citeshttps://doi.org/10.1016/j.bbrc.2018.05.050openalex-snapshot
Catalase inhibition induces pexophagy through ROS accumulation
inferred← citeshttps://doi.org/10.1016/j.celrep.2017.06.077openalex-snapshot
Proteomic Analysis of the Human Tankyrase Protein Interaction Network Reveals Its Role in Pexophagy
inferred← citeshttps://doi.org/10.1016/j.celrep.2025.115783openalex-snapshot
Pexophagy-driven redox imbalance promotes virus-induced ferroptosis
inferred← citeshttps://doi.org/10.1016/j.chembiol.2020.02.005openalex-snapshot
Autophagy-Dependent Ferroptosis: Machinery and Regulation
inferred← citeshttps://doi.org/10.1016/j.cmet.2019.03.003openalex-snapshot
Watch What You (Self-) Eat: Autophagic Mechanisms that Modulate Metabolism
inferred← citeshttps://doi.org/10.1016/j.devcel.2017.02.016openalex-snapshot
Cleaning House: Selective Autophagy of Organelles
inferred← citeshttps://doi.org/10.1016/j.fbio.2023.103561openalex-snapshot
Antimicrobial mechanism of Limosilactobacillus fermentum SHY10 metabolites against pickle film-producing strain by metabolomic and transcriptomic analysis
inferred← citeshttps://doi.org/10.1016/j.fmre.2023.04.016openalex-snapshot
Peroxisome and pexophagy in neurological diseases
inferred← citeshttps://doi.org/10.1016/j.jmb.2019.05.010openalex-snapshot
History of the Selective Autophagy Research: How Did It Begin and Where Does It Stand Today?
inferred← citeshttps://doi.org/10.1016/j.jmb.2019.10.013openalex-snapshot
Selective Autophagy Receptors in Neuronal Health and Disease
inferred← citeshttps://doi.org/10.1016/j.jmb.2020.01.020openalex-snapshot
The pROS of Autophagy in Neuronal Health
inferred← citeshttps://doi.org/10.1016/j.jmb.2024.168691openalex-snapshot
Phospholipid Supply for Autophagosome Biogenesis
inferred← citeshttps://doi.org/10.1016/j.micres.2022.127236openalex-snapshot
The Pex3-mediated peroxisome biogenesis plays a critical role in metabolic biosynthesis, stress response, and pathogenicity in Alternaria alternata
inferred← citeshttps://doi.org/10.1016/j.molcel.2015.07.021openalex-snapshot
Organelle-Specific Initiation of Autophagy
inferred← citeshttps://doi.org/10.1016/j.molcel.2019.09.005openalex-snapshot
A Diversity of Selective Autophagy Receptors Determines the Specificity of the Autophagy Pathway
inferred← citeshttps://doi.org/10.1016/j.nbd.2018.07.015openalex-snapshot
Mechanisms of selective autophagy and mitophagy: Implications for neurodegenerative diseases
inferred← citeshttps://doi.org/10.1016/j.pharmr.2026.100158openalex-snapshot
Harnessing autophagy and its transcriptional regulation in tumorigenesis and neurodegeneration: Potential and existing therapeutic strategies
inferred← citeshttps://doi.org/10.1016/j.plantsci.2018.06.026openalex-snapshot
Review: Selective degradation of peroxisome by autophagy in plants: Mechanisms, functions, and perspectives
inferred← citeshttps://doi.org/10.1016/j.tibs.2020.09.006openalex-snapshot
Balancing the Opposing Principles That Govern Peroxisome Homeostasis
inferred← citeshttps://doi.org/10.1016/j.yexcr.2015.04.005openalex-snapshot
Heme oxygenase-1 enhances autophagy in podocytes as a protective mechanism against high glucose-induced apoptosis
inferred← citeshttps://doi.org/10.1016/j.yjmcc.2026.03.003openalex-snapshot
A review of peroxisome biology: Potential implications for cardiac physiology and pathology
inferred← citeshttps://doi.org/10.1016/j.ymgme.2022.07.008openalex-snapshot
Hypomorphic mutation of PEX3 with peroxisomal mosaicism reveals the oscillating nature of peroxisome biogenesis coupled with differential metabolic activities
inferred← citeshttps://doi.org/10.1038/cdd.2017.23openalex-snapshot
The making of a mammalian peroxisome, version 2.0: mitochondria get into the mix
inferred← citeshttps://doi.org/10.1038/nature21375openalex-snapshot
Newly born peroxisomes are a hybrid of mitochondrial and ER-derived pre-peroxisomes
inferred← citeshttps://doi.org/10.1038/ncb3253openalex-snapshot
A mammalian pexophagy target
inferred← citeshttps://doi.org/10.1038/s12276-020-00503-9openalex-snapshot
Peroxisome quality control and dysregulated lipid metabolism in neurodegenerative diseases
inferred← citeshttps://doi.org/10.1038/s41420-024-02066-4openalex-snapshot
EHHADH deficiency regulates pexophagy and accelerates tubulointerstitial injury in diabetic kidney disease
inferred← citeshttps://doi.org/10.1038/s41467-024-53558-xopenalex-snapshot
AAA+ ATPase chaperone p97/VCPFAF2 governs basal pexophagy
inferred← citeshttps://doi.org/10.1038/s41556-018-0037-zopenalex-snapshot
Cargo recognition and degradation by selective autophagy
inferred← citeshttps://doi.org/10.1038/s41580-022-00542-2openalex-snapshot
The mechanisms and roles of selective autophagy in mammals
inferred← citeshttps://doi.org/10.1038/s41598-025-07934-2openalex-snapshot
Pex3 promotes formation of peroxisome-peroxisome and peroxisome-lipid droplet contact sites
inferred← citeshttps://doi.org/10.1042/bst20150268openalex-snapshot
Autophagic degradation of peroxisomes in mammals
inferred← citeshttps://doi.org/10.1042/ebc20210059openalex-snapshot
Plant peroxisome proteostasis—establishing, renovating, and dismantling the peroxisomal proteome
inferred← citeshttps://doi.org/10.1042/ns20180134openalex-snapshot
Autophagy in the mammalian nervous system: a primer for neuroscientists
inferred← citeshttps://doi.org/10.1074/jbc.m114.619338openalex-snapshot
Peroxisomal Pex3 Activates Selective Autophagy of Peroxisomes via Interaction with the Pexophagy Receptor Atg30
inferred← citeshttps://doi.org/10.1080/15384101.2017.1376149openalex-snapshot
Role of PEX5 ubiquitination in maintaining peroxisome dynamics and homeostasis
inferred← citeshttps://doi.org/10.1080/15548627.2015.1061846openalex-snapshot
Export-deficient monoubiquitinated PEX5 triggers peroxisome removal in SV40 large T antigen-transformed mouse embryonic fibroblasts
inferred← citeshttps://doi.org/10.1080/15548627.2015.1091141openalex-snapshot
ER stress: Autophagy induction, inhibition and selection
inferred← citeshttps://doi.org/10.1080/15548627.2017.1291470openalex-snapshot
The peroxisomal AAA ATPase complex prevents pexophagy and development of peroxisome biogenesis disorders
inferred← citeshttps://doi.org/10.1080/15548627.2019.1569915openalex-snapshot
A facile forward-genetic screen forArabidopsisautophagy mutants reveals twenty-one loss-of-function mutations disrupting sixATGgenes
inferred← citeshttps://doi.org/10.1080/15548627.2020.1712812openalex-snapshot
Loss of HSPA9 induces peroxisomal degradation by increasing pexophagy
inferred← citeshttps://doi.org/10.1080/15548627.2020.1725377openalex-snapshot
Organelle-specific autophagy in inflammatory diseases: a potential therapeutic target underlying the quality control of multiple organelles
inferred← citeshttps://doi.org/10.1080/15548627.2020.1797280openalex-snapshot
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
inferred← citeshttps://doi.org/10.1080/15548627.2020.1831814openalex-snapshot
HIV-1 Env induces pexophagy and an oxidative stress leading to uninfected CD4 + T cell death
inferred← citeshttps://doi.org/10.1080/15548627.2022.2160566openalex-snapshot
PEX13 prevents pexophagy by regulating ubiquitinated PEX5 and peroxisomal ROS
inferred← citeshttps://doi.org/10.1080/27694127.2023.2236407openalex-snapshot
Neurodegenerative disease-associated inclusion bodies are cleared by selective autophagy in budding yeast
inferred← citeshttps://doi.org/10.1083/jcb.201511034openalex-snapshot
PEX2 is the E3 ubiquitin ligase required for pexophagy during starvation
inferred← citeshttps://doi.org/10.1083/jcb.201804172openalex-snapshot
Deubiquitinating enzyme USP30 maintains basal peroxisome abundance by regulating pexophagy
inferred← citeshttps://doi.org/10.1083/jcb.202103156openalex-snapshot
Ubiquitin ligase MARCH5 localizes to peroxisomes to regulate pexophagy
inferred← citeshttps://doi.org/10.1083/jcb.202208092openalex-snapshot
NBR1: The archetypal selective autophagy receptor
inferred← citeshttps://doi.org/10.1083/jcb.202409024openalex-snapshot
The p97 ATPase and its adaptor UBXD8 maintain peroxisome pools by preventing pexophagy
inferred← citeshttps://doi.org/10.1083/jcb.202411184openalex-snapshot
PEX14 acts as a molecular link between optineurin and the autophagic machinery to induce pexophagy
inferred← citeshttps://doi.org/10.1083/jcb.202503169openalex-snapshot
In vivo mapping of peroxisome dynamics and pexophagy using PO-TRG and CA-PO-TRG reporter mice
inferred← citeshttps://doi.org/10.1083/jcb.202505040openalex-snapshot
Protein Kinase C promotes peroxisome biogenesis and peroxisome–endoplasmic reticulum interaction
inferred← citeshttps://doi.org/10.1097/imna-d-24-00036openalex-snapshot
Selective Autophagy in Kidney Diseases: The Tip of the Iceberg
inferred← citeshttps://doi.org/10.1101/2024.05.31.596776openalex-snapshot
PEX14 functions as a molecular link between optineurin and pexophagy in human cells
inferred← citeshttps://doi.org/10.1101/2024.09.24.614749openalex-snapshot
The p97-UBXD8 complex maintains peroxisome abundance by suppressing pexophagy
inferred← citeshttps://doi.org/10.1101/2025.01.21.634043openalex-snapshot
Protein Kinase C positively regulates peroxisome biogenesis by promoting peroxisome-endoplasmic reticulum interaction
inferred← citeshttps://doi.org/10.1111/gtc.12198openalex-snapshot
Peroxin Pex14p is the key component for coordinated autophagic degradation of mammalian peroxisomes by direct binding to LC 3‐ II
inferred← citeshttps://doi.org/10.1111/jipb.13346openalex-snapshot
Protein ubiquitination in plant peroxisomes
inferred← citeshttps://doi.org/10.1111/jnc.70013openalex-snapshot
PPARβ/δ Activation Improves Corticosterone‐Induced Oxidative Stress Damage in Astrocytes by Targeting UBR5/ATM Signaling
inferred← citeshttps://doi.org/10.1111/tpj.16508openalex-snapshot
Picky eaters: selective autophagy in plant cells
inferred← citeshttps://doi.org/10.1111/tra.12376openalex-snapshot
Assembly of Peroxisomal Membrane Proteins via the Direct Pex19p‐Pex3p Pathway
inferred← citeshttps://doi.org/10.1146/annurev-cellbio-100818-125300openalex-snapshot
Diverse Cellular Roles of Autophagy
inferred← citeshttps://doi.org/10.1152/physrev.00033.2016openalex-snapshot
Redox Regulation of Homeostasis and Proteostasis in Peroxisomes
inferred← citeshttps://doi.org/10.1161/circulationaha.123.066628openalex-snapshot
Induction of DEPP1 by HIF Mediates Multiple Hallmarks of Ischemic Cardiomyopathy
inferred← citeshttps://doi.org/10.1186/s12964-024-01862-wopenalex-snapshot
Peroxisomal homeostasis in metabolic diseases and its implication in ferroptosis
inferred← citeshttps://doi.org/10.1242/jcs.259775openalex-snapshot
Mammalian pexophagy at a glance
inferred← citeshttps://doi.org/10.1248/bpb.b15-00096openalex-snapshot
Choose Delicately and Reuse Adequately: The Newly Revealed Process of Autophagy
inferred← citeshttps://doi.org/10.1371/journal.pone.0183150openalex-snapshot
New insights into the distribution, protein abundance and subcellular localisation of the endogenous peroxisomal biogenesis proteins PEX3 and PEX19 in different organs and cell types of the adult mouse
inferred← citeshttps://doi.org/10.14348/molcells.2018.2245openalex-snapshot
Pexophagy: Molecular Mechanisms and Implications for Health and Diseases.
inferred← citeshttps://doi.org/10.15252/embj.201796697openalex-snapshot
Molecular definitions of autophagy and related processes
inferred← citeshttps://doi.org/10.15252/embr.201642443openalex-snapshot
Peroxisomal protein PEX13 functions in selective autophagy
inferred← citeshttps://doi.org/10.15252/embr.201947728openalex-snapshot
Parkin‐mediated ubiquitylation redistributes MITOL/March5 from mitochondria to peroxisomes
inferred← citeshttps://doi.org/10.2183/pjab.92.463openalex-snapshot
Peroxisome biogenesis and human peroxisome-deficiency disorders
inferred← citeshttps://doi.org/10.26508/lsa.202201825openalex-snapshot
Segregation of pathways leading to pexophagy
inferred← citeshttps://doi.org/10.33612/diss.132023701openalex-snapshot
Peroxisomal membrane protein degradation in yeast
inferred← citeshttps://doi.org/10.3389/978-2-83250-838-1openalex-snapshot
Molecular Mechanisms and Physiological Significance of Organelle Interactions and Cooperation - Volume II
inferred← citeshttps://doi.org/10.3389/fcell.2015.00042openalex-snapshot
Hypoxia signaling pathways: modulators of oxygen-related organelles
inferred← citeshttps://doi.org/10.3389/fcell.2021.814047openalex-snapshot
The Peroxisome-Autophagy Redox Connection: A Double-Edged Sword?
inferred← citeshttps://doi.org/10.3389/fncel.2020.00044openalex-snapshot
Peroxisomal Dysfunction in Neurological Diseases and Brain Aging
inferred← citeshttps://doi.org/10.3389/fphys.2026.1822139openalex-snapshot
From homeostasis to pathology, organelle-specific autophagy in skeletal muscle: a PRISMA-ScR scoping review
inferred← citeshttps://doi.org/10.3389/fpls.2019.01021openalex-snapshot
Selective Autophagy of Peroxisomes in Plants: From Housekeeping to Development and Stress Responses
inferred← citeshttps://doi.org/10.3390/antiox14020126openalex-snapshot
Pexophagy and Oxidative Stress: Focus on Peroxisomal Proteins and Reactive Oxygen Species (ROS) Signaling Pathways
inferred← citeshttps://doi.org/10.3390/antiox14060649openalex-snapshot
Transcriptomic Analysis of the Liver Redox Response During Food-Anticipatory Activity Under a Time-Restricted Feeding Protocol in Rats
inferred← citeshttps://doi.org/10.3390/cells10051094openalex-snapshot
Mechanisms and Functions of Pexophagy in Mammalian Cells
inferred← citeshttps://doi.org/10.3390/cells9102219openalex-snapshot
Interplay between the Ubiquitin Proteasome System and Ubiquitin-Mediated Autophagy in Plants
inferred← citeshttps://doi.org/10.3390/cells9112349openalex-snapshot
Selective Autophagy by Close Encounters of the Ubiquitin Kind
inferred← citeshttps://doi.org/10.3390/ijms21020578openalex-snapshot
Pexophagy: A Model for Selective Autophagy
inferred← citeshttps://doi.org/10.3390/ijms21103689openalex-snapshot
Morphology Remodeling and Selective Autophagy of Intracellular Organelles during Viral Infections
inferred← citeshttps://doi.org/10.3390/ijms21238974openalex-snapshot
Autophagy and Autophagy-Related Diseases: A Review
inferred← citeshttps://doi.org/10.3390/ijms22157989openalex-snapshot
Knockdown of PEX16 Induces Autophagic Degradation of Peroxisomes
inferred← citeshttps://doi.org/10.3390/ijms241512262openalex-snapshot
Reciprocal Regulation of Peroxisome Biogenesis and Myogenic Factors Is Critical for Myogenesis
inferred← citeshttps://doi.org/10.3390/jof9111083openalex-snapshot
Regulatory Mechanism of Peroxisome Number Reduction Caused by FgPex4 and FgPex22-like Deletion in Fusarium graminearum
inferred← citeshttps://doi.org/10.3390/metabo11090588openalex-snapshot
Selective Autophagy as a Potential Therapeutic Target in Age-Associated Pathologies
inferred← citeshttps://doi.org/10.53846/goediss-6798openalex-snapshot
The interplay of SmNBR1 and SmATG8 in selective autophagy of the filamentous fungus Sordaria macrospora
inferred← citeshttps://doi.org/10.5772/63977openalex-snapshot
Choosing Lunch: The Role of Selective Autophagy Adaptor Proteins
inferred← citeshttps://doi.org/10.70675/9cf6aff1z9964z448dz9c5az05c0a6566065openalex-snapshot
L'autophagie induite par les glycoprotéines de l'enveloppe du VIH-1 dégrade les peroxysomes : rôle dans la mort des lymphocytes T CD4 non infectés
inferred← citeshttps://doi.org/10.7150/jca.25587openalex-snapshot
Development of a Novel Autophagy-related Prognostic Signature for Serous Ovarian Cancer
inferred← citeshttps://doi.org/10.7150/thno.49860openalex-snapshot
Selective autophagy of intracellular organelles: Recent research advances
inferred← citeshttps://doi.org/10.7150/thno.85390openalex-snapshot
Tat-NTS peptide protects neurons against cerebral ischemia-reperfusion injury via ANXA1 SUMOylation in microglia
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