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Atg32 Is a Mitochondrial Protein that Confers Selectivity during Mitophagy
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/(sici)1097-0061(199807)14:10<953::aid-yea293>3.0.co;2-uopenalex-snapshot
Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1002/0471143030.cb0303s04openalex-snapshot
Isolation of Mitochondria from Tissues and Cells by Differential Centrifugation
inferredcites →https://doi.org/10.1006/bbrc.1995.1636openalex-snapshot
Novel System for Monitoring Autophagy in the Yeast Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1007/s002940050145openalex-snapshot
The role of protein degradation in mitochondrial function and biogenesis
inferredcites →https://doi.org/10.1016/j.biocel.2004.04.009openalex-snapshot
Role of mitochondrial permeability transition pores in mitochondrial autophagy
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.tcb.2007.04.005openalex-snapshot
Eating the endoplasmic reticulum: quality control by autophagy
inferredcites →https://doi.org/10.1016/s0076-6879(08)03210-2openalex-snapshot
Chapter 10 Electron Microscopy in Yeast
inferredcites →https://doi.org/10.1016/s0891-5849(99)00266-xopenalex-snapshot
Oxidative stress during aging of stationary cultures of the yeast Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1016/s1534-5807(02)00373-8openalex-snapshot
Mechanism of Cargo Selection in the Cytoplasm to Vacuole Targeting Pathway
inferredcites →https://doi.org/10.1038/cr.2007.78openalex-snapshot
Physiological functions of Atg6/Beclin 1: a unique autophagy-related protein
inferredcites →https://doi.org/10.1038/nature07006openalex-snapshot
Essential role for Nix in autophagic maturation of erythroid cells
inferredcites →https://doi.org/10.1038/sj.cdd.4401697openalex-snapshot
Impairing the bioenergetic status and the biogenesis of mitochondria triggers mitophagy in yeast
inferredcites →https://doi.org/10.1038/sj.cdd.4402167openalex-snapshot
Mdm38 protein depletion causes loss of mitochondrial K+/H+ exchange activity, osmotic swelling and mitophagy
inferredcites →https://doi.org/10.1038/sj.emboj.7601963openalex-snapshot
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
inferredcites →https://doi.org/10.1073/pnas.0708818104openalex-snapshot
NIX is required for programmed mitochondrial clearance during reticulocyte maturation
inferredcites →https://doi.org/10.1074/jbc.m404399200openalex-snapshot
Cargo Proteins Facilitate the Formation of Transport Vesicles in the Cytoplasm to Vacuole Targeting Pathway
inferredcites →https://doi.org/10.1074/jbc.m406960200openalex-snapshot
Uth1p Is Involved in the Autophagic Degradation of Mitochondria
inferredcites →https://doi.org/10.1074/jbc.m605940200openalex-snapshot
Aup1p, a Yeast Mitochondrial Protein Phosphatase Homolog, Is Required for Efficient Stationary Phase Mitophagy and Cell Survival
inferredcites →https://doi.org/10.1074/jbc.m802403200openalex-snapshot
Mitophagy in Yeast Occurs through a Selective Mechanism
inferredcites →https://doi.org/10.1083/jcb.153.2.381openalex-snapshot
Cvt9/Gsa9 Functions in Sequestering Selective Cytosolic Cargo Destined for the Vacuole
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.3.3.349openalex-snapshot
CELLULAR DIFFERENTIATION IN THE KIDNEYS OF NEWBORN MICE STUDIED WITH THE ELECTRON MICROSCOPE
inferredcites →https://doi.org/10.1091/mbc.e02-07-0413openalex-snapshot
Chemical Genetic Analysis of Apg1 Reveals A Non-kinase Role in the Induction of Autophagy
inferredcites →https://doi.org/10.1091/mbc.e04-11-1035openalex-snapshot
Atg11 Links Cargo to the Vesicle-forming Machinery in the Cytoplasm to Vacuole Targeting Pathway
inferredcites →https://doi.org/10.1091/mbc.e05-07-0629openalex-snapshot
The Actin Cytoskeleton Is Required for Selective Types of Autophagy, but Not Nonspecific Autophagy, in the YeastSaccharomyces cerevisiae
inferredcites →https://doi.org/10.1091/mbc.e07-08-0826openalex-snapshot
The Atg1 Kinase Complex Is Involved in the Regulation of Protein Recruitment to Initiate Sequestering Vesicle Formation for Nonspecific Autophagy inSaccharomyces cerevisiae
inferredcites →https://doi.org/10.1091/mbc.e07-09-0892openalex-snapshot
Arp2 Links Autophagic Machinery with the Actin Cytoskeleton
inferredcites →https://doi.org/10.1091/mbc.e07-12-1292openalex-snapshot
Atg8 Controls Phagophore Expansion during Autophagosome Formation
inferredcites →https://doi.org/10.1093/genetics/144.4.1425openalex-snapshot
Genomic Libraries and a Host Strain Designed for Highly Efficient Two-Hybrid Selection in Yeast
inferredcites →https://doi.org/10.1093/genetics/147.2.435openalex-snapshot
Large Scale Identification of Genes Involved in Cell Surface Biosynthesis and Architecture in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1096/fj.01-0206fjeopenalex-snapshot
The mitochondrial permeability transition initiates autophagy in rat hepatocytes
inferredcites →https://doi.org/10.1111/j.1365-2443.2007.01050.xopenalex-snapshot
Hierarchy of Atg proteins in pre‐autophagosomal structure organization
inferredcites →https://doi.org/10.1111/j.1567-1364.2006.00160.xopenalex-snapshot
TheYCR079wgene confers a rapamycin-resistant function and encodes the sixth type 2C protein phosphatase inSaccharomyces cerevisiae
inferredcites →https://doi.org/10.1126/science.290.5497.1717openalex-snapshot
Autophagy as a Regulated Pathway of Cellular Degradation
inferredcites →https://doi.org/10.1128/mcb.8.11.4936openalex-snapshot
Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases.
inferredcites →https://doi.org/10.1146/annurev.ge.29.120195.001055openalex-snapshot
MOLECULAR GENETIC ASPECTS OF HUMAN MITOCHONDRIAL DISORDERS
inferredcites →https://doi.org/10.1146/annurev.genet.39.110304.095751openalex-snapshot
A Mitochondrial Paradigm of Metabolic and Degenerative Diseases, Aging, and Cancer: A Dawn for Evolutionary Medicine
inferredcites →https://doi.org/10.1242/jcs.01620openalex-snapshot
The molecular machinery of autophagy: unanswered questions
inferredcites →https://doi.org/10.4161/auto.1.2.1737openalex-snapshot
Pexophagy: The Selective Autophagy of Peroxisomes
inferredcites →https://doi.org/10.4161/auto.3011openalex-snapshot
Different Fates of Mitochondria: Alternative Ways for Degradation?
inferredcites →https://doi.org/10.4161/auto.4034openalex-snapshot
Selective and Non-Selective Autophagic Degradation of Mitochondria in Yeast
inferredcites →https://doi.org/10.4161/auto.4127openalex-snapshot
The Role of Autophagy in Mitochondria Maintenance: Characterization of Mitochondrial Functions in Autophagy-Deficient S. cerevisiae Strains
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/10.1002/1873-3468.14060openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/1873-3468.14509openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/1873-3468.14742openalex-snapshot
Structural view on autophagosome formation
inferred← citeshttps://doi.org/10.1002/2211-5463.13307openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/9780470015902.a0027587openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/9781119017127.ch12openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/9781119312994.apr0546openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/bies.202100271openalex-snapshot
The strange case of Drp1 in autophagy: Jekyll and Hyde?
inferred← citeshttps://doi.org/10.1002/cne.24213openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/cphy.c170005openalex-snapshot
Mitophagy as a Protective Mechanism against Myocardial Stress
inferred← citeshttps://doi.org/10.1002/embr.201438501openalex-snapshot
ULK1 translocates to mitochondria and phosphorylates FUNDC1 to regulate mitophagy
inferred← citeshttps://doi.org/10.1002/emmm.201303356openalex-snapshot
Defects in GABA metabolism affect selective autophagy pathways and are alleviated by mTOR inhibition
inferred← citeshttps://doi.org/10.1002/iub.261openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/iub.2783openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/j.2040-4603.2017.tb00786.xopenalex-snapshot
Mitophagy as a Protective Mechanism against Myocardial Stress
inferred← citeshttps://doi.org/10.1002/jcsm.12611openalex-snapshot
The effect of fasting or calorie restriction on mitophagy induction: a literature review
inferred← citeshttps://doi.org/10.1002/mds.26477openalex-snapshot
Autophagy and A lpha‐ S ynuclein: R elevance to P arkinson's D isease and R elated S ynucleopathies
inferred← citeshttps://doi.org/10.1002/mrd.23670openalex-snapshot
Deterioration of mitochondrial biogenesis and degradation in the endometrium is a cause of subfertility in cows
inferred← citeshttps://doi.org/10.1002/path.2697openalex-snapshot
Autophagy: cellular and molecular mechanisms
inferred← citeshttps://doi.org/10.1002/pmic.201800404openalex-snapshot
Mitochondrial Dysfunction in Age‐Related Metabolic Disorders
inferred← citeshttps://doi.org/10.1002/wrna.1522openalex-snapshot
On the edge of degradation: Autophagy regulation by RNA decay
inferred← citeshttps://doi.org/10.1002/yea.3705openalex-snapshot
Lipophagy pathways in yeast are controlled by their distinct modes of induction
inferred← citeshttps://doi.org/10.1007/7651_2017_11openalex-snapshot
Investigation of Yeast Mitophagy with Fluorescence Microscopy and Western Blotting
inferred← citeshttps://doi.org/10.1007/7651_2017_12openalex-snapshot
MitoPho8Δ60 Assay as a Tool to Quantitatively Measure Mitophagy Activity
inferred← citeshttps://doi.org/10.1007/7651_2017_13openalex-snapshot
Mitophagy in Yeast: A Screen of Mitophagy-Deficient Mutants
inferred← citeshttps://doi.org/10.1007/7651_2017_40openalex-snapshot
Monitoring of Iron Depletion-Induced Mitophagy in Pathogenic Yeast
inferred← citeshttps://doi.org/10.1007/978-1-0716-4067-8_1openalex-snapshot
Fluorescence Microscopy and Immunoblotting for Mitophagy in Budding Yeast
inferred← citeshttps://doi.org/10.1007/978-1-4614-4599-9_11openalex-snapshot
Cell-Death Pathways and Mitochondria
inferred← citeshttps://doi.org/10.1007/978-1-4614-6561-4_1openalex-snapshot
Historical Overview of Autophagy
inferred← citeshttps://doi.org/10.1007/978-1-4939-0799-1_11openalex-snapshot
Assays for Autophagy II: Mitochondrial Autophagy
inferred← citeshttps://doi.org/10.1007/978-1-4939-1875-1_15openalex-snapshot
Mitophagy and Mitochondrial Balance
inferred← citeshttps://doi.org/10.1007/978-1-4939-6824-4_20openalex-snapshot
Assays for Mitophagy in Yeast
inferred← citeshttps://doi.org/10.1007/978-1-4939-8873-0_42openalex-snapshot
Assays to Monitor Mitophagy in Drosophila
inferred← citeshttps://doi.org/10.1007/978-1-61779-328-8_21openalex-snapshot
Monitoring Mitophagy in Neuronal Cell Cultures
inferred← citeshttps://doi.org/10.1007/978-3-030-00683-9_1openalex-snapshot
Response Mechanisms to Oxidative Stress in Yeast and Filamentous Fungi
inferred← citeshttps://doi.org/10.1007/978-3-030-05067-2_10openalex-snapshot
Autophagy in Neurodegenerative Diseases
inferred← citeshttps://doi.org/10.1007/978-3-030-58532-7_5openalex-snapshot
Structure and Function of the Mitochondrion
inferred← citeshttps://doi.org/10.1007/978-3-030-78799-8_11openalex-snapshot
Mitochondrial Dysfunction and Mitophagy: Physiological Implications in Cardiovascular Health
inferred← citeshttps://doi.org/10.1007/978-3-031-88121-3_4openalex-snapshot
Autophagy Receptors Couple Cargo Destined to Be Degraded with the Core Autophagy Machinery
inferred← citeshttps://doi.org/10.1007/978-3-319-10635-9_7openalex-snapshot
Role of Autophagy in Plant Nutrient Deficiency
inferred← citeshttps://doi.org/10.1007/978-3-319-40007-5_64-1openalex-snapshot
Mitophagy in Starvation
inferred← citeshttps://doi.org/10.1007/978-3-642-27928-7_6openalex-snapshot
Quality control of proteins and organelles by autophagy
inferred← citeshttps://doi.org/10.1007/978-3-642-27928-7_8openalex-snapshot
Predicting fates in models of neurodegenerative disease: longitudinal measures of protein homeostasis in live neurons
inferred← citeshttps://doi.org/10.1007/978-94-007-1291-1_3openalex-snapshot
Mitochondrial Dynamics and Autophagy
inferred← citeshttps://doi.org/10.1007/978-94-007-2561-4_11openalex-snapshot
Cellular Homeostasis in Fungi: Impact on the Aging Process
inferred← citeshttps://doi.org/10.1007/978-94-007-2561-4_3openalex-snapshot
The Role of Mitochondria in the Aging Processes of Yeast
inferred← citeshttps://doi.org/10.1007/978-94-007-2561-4_8openalex-snapshot
Amino Acid Homeostasis and Chronological Longevity in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1007/978-94-007-6331-9_11openalex-snapshot
Cardiolipin-Mediated Cellular Signaling
inferred← citeshttps://doi.org/10.1007/978-981-15-0602-4_19openalex-snapshot
Autophagy in Mitochondrial Quality Control
inferred← citeshttps://doi.org/10.1007/978-981-16-2830-6_16openalex-snapshot
Screening for Genes Involved in Autophagy
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inferred← citeshttps://doi.org/10.1007/s00018-024-05556-xopenalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s00246-010-9883-6openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s00253-021-11394-9openalex-snapshot
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Nucleophagy in Aspergillus oryzae is Mediated by Autophagosome Formation and Vacuole-Mediated Degradation
inferred← citeshttps://doi.org/10.1007/s00294-017-0717-4openalex-snapshot
The influence of mitochondrial dynamics on mitochondrial genome stability
inferred← citeshttps://doi.org/10.1007/s00294-019-01035-0openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s00441-016-2472-0openalex-snapshot
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Mitochondrial function and mitochondrial DNA maintenance with advancing age
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inferred← citeshttps://doi.org/10.1007/s11046-021-00565-xopenalex-snapshot
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Alpha-synuclein and Protein Degradation Systems: a Reciprocal Relationship
inferred← citeshttps://doi.org/10.1007/s12104-017-9750-yopenalex-snapshot
Backbone and side chain resonance assignments for a structured domain within Atg32
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Identification of mitophagy-related genes impacting patient survival in glioma
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Role of plant autophagy in stress response
inferred← citeshttps://doi.org/10.1007/s13238-016-0328-8openalex-snapshot
Structural insights into the recognition of phosphorylated FUNDC1 by LC3B in mitophagy
inferred← citeshttps://doi.org/10.1007/s13340-011-0020-4openalex-snapshot
Roles of autophagy in pancreatic β-cell function and type 2 diabetes
inferred← citeshttps://doi.org/10.1007/s40139-013-0033-8openalex-snapshot
Phosphorylation Events in Selective Mitophagy: Possible Biochemical Markers?
inferred← citeshttps://doi.org/10.1007/s40263-018-0497-5openalex-snapshot
Activating Autophagy as a Therapeutic Strategy for Parkinson’s Disease
inferred← citeshttps://doi.org/10.1007/s42994-025-00218-3openalex-snapshot
SnRK1 and TOR: central regulators of autophagy in plant energy stress responses
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inferred← citeshttps://doi.org/10.1016/b978-0-12-381510-1.00030-2openalex-snapshot
Autophagy in Cardiac Physiology and Disease
inferred← citeshttps://doi.org/10.1016/b978-0-12-404599-6.00020-2openalex-snapshot
Targeted Strategies to Fight Cardiac Aging
inferred← citeshttps://doi.org/10.1016/b978-0-12-405528-5.00002-xopenalex-snapshot
Molecular Process and Physiological Significance of Mitophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-405528-5.00003-1openalex-snapshot
Principles of Mitophagy and Beyond
inferred← citeshttps://doi.org/10.1016/b978-0-12-405528-5.00004-3openalex-snapshot
Quality Control in Mitochondria
inferred← citeshttps://doi.org/10.1016/b978-0-12-405528-5.00007-9openalex-snapshot
Role of Nix in the Maturation of Erythroid Cells through Mitochondrial Autophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-405528-5.00010-9openalex-snapshot
Atg32 Confers Selective Mitochondrial Sequestration as a Cargo for Autophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-801238-3.64220-4openalex-snapshot
Cell Injury and Necrosis
inferred← citeshttps://doi.org/10.1016/b978-0-12-802936-7.00006-4openalex-snapshot
Cargo Proteins Facilitate the Formation of Transport Vesicles, but not Autophagosomes
inferred← citeshttps://doi.org/10.1016/b978-0-12-802937-4.00008-9openalex-snapshot
The Role of Autophagy and Mitophagy in Mitochondrial Diseases
inferred← citeshttps://doi.org/10.1016/b978-0-12-805420-8.00010-xopenalex-snapshot
Regulation of the DNA Damage Response by Autophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-821562-3.00037-xopenalex-snapshot
Mitochondrial biogenesis and mitophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-822416-8.00005-1openalex-snapshot
Updates on mitochondria, calorie restriction, and aging
inferred← citeshttps://doi.org/10.1016/b978-0-323-95488-4.00265-5openalex-snapshot
Cell Death Mechanisms, Associated Toxicity and Therapeutic Applications
inferred← citeshttps://doi.org/10.1016/b978-0-323-95672-7.00018-2openalex-snapshot
Autophagy and Huntington's disease
inferred← citeshttps://doi.org/10.1016/b978-0-443-15260-3.00001-6openalex-snapshot
Formation of mitophagosomes
inferred← citeshttps://doi.org/10.1016/b978-0-443-15260-3.00014-4openalex-snapshot
The antiaging role of mitophagy
inferred← citeshttps://doi.org/10.1016/b978-0-443-15260-3.00023-5openalex-snapshot
The Sodom and Gomorrah conundrum of yeast mitophagy
inferred← citeshttps://doi.org/10.1016/bs.ctdb.2015.07.012openalex-snapshot
Autophagy in Cell Life and Cell Death
inferred← citeshttps://doi.org/10.1016/bs.ircmb.2016.12.003openalex-snapshot
Molecular Biology Digest of Cell Mitophagy
inferred← citeshttps://doi.org/10.1016/bs.ircmb.2018.05.005openalex-snapshot
Novel Insights Into the Anti-aging Role of Mitophagy
inferred← citeshttps://doi.org/10.1016/bs.mcb.2019.10.006openalex-snapshot
Detection of mitophagy in mammalian cells, mice, and yeast
inferred← citeshttps://doi.org/10.1016/bs.mcb.2020.10.014openalex-snapshot
Assessing autophagic flux in yeast
inferred← citeshttps://doi.org/10.1016/bs.mie.2016.09.085openalex-snapshot
Monitoring the Formation of Autophagosomal Precursor Structures in Yeast Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1016/bs.mie.2016.10.023openalex-snapshot
Methods for Studying Interactions Between Atg8/LC3/GABARAP and LIR-Containing Proteins
inferred← citeshttps://doi.org/10.1016/j.arr.2014.12.007openalex-snapshot
Mitochondria to nucleus signaling and the role of ceramide in its integration into the suite of cell quality control processes during aging
inferred← citeshttps://doi.org/10.1016/j.bbabio.2013.11.009openalex-snapshot
Roles of autophagy in chloroplast recycling
inferred← citeshttps://doi.org/10.1016/j.bbabio.2020.148302openalex-snapshot
The regulation of mitochondrial homeostasis by the ubiquitin proteasome system
inferred← citeshttps://doi.org/10.1016/j.bbadis.2013.11.024openalex-snapshot
In vivo functions of Drp1: Lessons learned from yeast genetics and mouse knockouts
inferred← citeshttps://doi.org/10.1016/j.bbagen.2011.08.001openalex-snapshot
Mitochondria and autophagy: Critical interplay between the two homeostats
inferred← citeshttps://doi.org/10.1016/j.bbagen.2021.129858openalex-snapshot
Regulatory mechanisms of mitophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.bbagen.2021.129932openalex-snapshot
Yeast mitophagy: Unanswered questions
inferred← citeshttps://doi.org/10.1016/j.bbagen.2022.130203openalex-snapshot
An overview of the molecular mechanisms of mitophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.bbalip.2016.02.001openalex-snapshot
Lipid transfer and metabolism across the endolysosomal–mitochondrial boundary
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2010.08.007openalex-snapshot
Mitophagy and Parkinson's disease: The PINK1–parkin link
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.02.010openalex-snapshot
The retrograde response: When mitochondrial quality control is not enough
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.02.012openalex-snapshot
Mitochondrial morphology in mitophagy and macroautophagy
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.06.025openalex-snapshot
Proteolytic control of mitochondrial function and morphogenesis
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.08.007openalex-snapshot
Mitophagy is triggered by mild oxidative stress in a mitochondrial fission dependent manner
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2013.03.019openalex-snapshot
Substrate recognition in selective autophagy and the ubiquitin–proteasome system
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2014.12.039openalex-snapshot
Ceramide induced mitophagy and tumor suppression
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.01.005openalex-snapshot
Mitophagy in yeast: Molecular mechanisms and physiological role
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.02.022openalex-snapshot
Mitochondrial autophagy: Origins, significance, and role of BNIP3 and NIX
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.02.024openalex-snapshot
Mitophagy and mitochondrial dynamics in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.03.013openalex-snapshot
Selective removal of mitochondria via mitophagy: distinct pathways for different mitochondrial stresses
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.2015.12.022openalex-snapshot
Regulation of peroxisome dynamics by phosphorylation
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2017.04.012openalex-snapshot
Mitochatting – If only we could be a fly on the cell wall
inferred← citeshttps://doi.org/10.1016/j.bbrc.2010.02.106openalex-snapshot
Programmed cell clearance: Molecular regulation of the elimination of apoptotic cell corpses and its role in the resolution of inflammation
inferred← citeshttps://doi.org/10.1016/j.bbrc.2017.12.163openalex-snapshot
The Nem1-Spo7 protein phosphatase complex is required for efficient mitophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.bbrc.2018.04.114openalex-snapshot
The ER membrane insertase Get1/2 is required for efficient mitophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.bbrc.2018.05.123openalex-snapshot
The TORC1 signaling pathway regulates respiration-induced mitophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.bbrc.2022.10.052openalex-snapshot
The Dep1 protein: A new regulator of mitophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.biocel.2012.07.006openalex-snapshot
Mitophagy: A process that adapts to the cell physiology
inferred← citeshttps://doi.org/10.1016/j.biocel.2014.05.010openalex-snapshot
Mitophagy mechanisms and role in human diseases
inferred← citeshttps://doi.org/10.1016/j.biocel.2015.10.002openalex-snapshot
The Ccz1 mediates the autophagic clearance of damaged mitochondria in response to oxidative stress in Candida albicans
inferred← citeshttps://doi.org/10.1016/j.blre.2017.04.001openalex-snapshot
Autophagy: A necessary event during erythropoiesis
inferred← citeshttps://doi.org/10.1016/j.ceb.2009.12.002openalex-snapshot
Cytoprotective roles for autophagy
inferred← citeshttps://doi.org/10.1016/j.ceb.2009.12.004openalex-snapshot
The role of the Atg1/ULK1 complex in autophagy regulation
inferred← citeshttps://doi.org/10.1016/j.ceb.2011.03.003openalex-snapshot
Ubiquitination-mediated autophagy against invading bacteria
inferred← citeshttps://doi.org/10.1016/j.cellsig.2015.05.020openalex-snapshot
Pyruvate stimulates mitophagy via PINK1 stabilization
inferred← citeshttps://doi.org/10.1016/j.cellsig.2015.06.001openalex-snapshot
Ceramide signalling impinges on Sit4p and Hog1p to promote mitochondrial fission and mitophagy in Isc1p-deficient cells
inferred← citeshttps://doi.org/10.1016/j.cellsig.2018.04.002openalex-snapshot
S6 kinase 1 plays a key role in mitochondrial morphology and cellular energy flow
inferred← citeshttps://doi.org/10.1016/j.celrep.2015.01.044openalex-snapshot
Synthetic Quantitative Array Technology Identifies the Ubp3-Bre5 Deubiquitinase Complex as a Negative Regulator of Mitophagy
inferred← citeshttps://doi.org/10.1016/j.celrep.2018.05.064openalex-snapshot
The PP2A-like Protein Phosphatase Ppg1 and the Far Complex Cooperatively Counteract CK2-Mediated Phosphorylation of Atg32 to Inhibit Mitophagy
inferred← citeshttps://doi.org/10.1016/j.celrep.2018.12.050openalex-snapshot
A Mammalian Mitophagy Receptor, Bcl2-L-13, Recruits the ULK1 Complex to Induce Mitophagy
inferred← citeshttps://doi.org/10.1016/j.celrep.2020.107902openalex-snapshot
Mitochondria Associated Degradation Pathway (MAD) Function Beyond the Outer Membrane
inferred← citeshttps://doi.org/10.1016/j.celrep.2024.115001openalex-snapshot
AMPK regulates Bcl2-L-13-mediated mitophagy induction for cardioprotection
inferred← citeshttps://doi.org/10.1016/j.celrep.2025.116585openalex-snapshot
Bulk and selective autophagy cooperate to remodel a fungal proteome in response to changing nutrient availability
inferred← citeshttps://doi.org/10.1016/j.chemphyslip.2015.09.005openalex-snapshot
Cardiolipin metabolism and its causal role in the etiology of the inherited cardiomyopathy Barth syndrome
inferred← citeshttps://doi.org/10.1016/j.chemphyslip.2018.11.001openalex-snapshot
Membrane-binding domains in autophagy
inferred← citeshttps://doi.org/10.1016/j.chom.2014.03.012openalex-snapshot
Self and Nonself: How Autophagy Targets Mitochondria and Bacteria
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.conb.2011.10.016openalex-snapshot
Mitochondrial dynamics and mitophagy in Parkinson's disease: disordered cellular power plant becomes a big deal in a major movement disorder
inferred← citeshttps://doi.org/10.1016/j.cub.2018.01.004openalex-snapshot
Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance
inferred← citeshttps://doi.org/10.1016/j.cub.2022.11.002openalex-snapshot
Orchestration of selective autophagy by cargo receptors
inferred← citeshttps://doi.org/10.1016/j.devcel.2009.07.003openalex-snapshot
A Receptor for Eating Mitochondria
inferred← citeshttps://doi.org/10.1016/j.devcel.2010.07.005openalex-snapshot
The Autophagy Connection
inferred← citeshttps://doi.org/10.1016/j.devcel.2013.05.024openalex-snapshot
The Scaffold Protein Atg11 Recruits Fission Machinery to Drive Selective Mitochondria Degradation by Autophagy
inferred← citeshttps://doi.org/10.1016/j.devcel.2014.01.012openalex-snapshot
Mitochondrial ER Contacts Are Crucial for Mitophagy in Yeast
inferred← citeshttps://doi.org/10.1016/j.devcel.2014.06.006openalex-snapshot
Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria
inferred← citeshttps://doi.org/10.1016/j.devcel.2014.06.013openalex-snapshot
TRIM Proteins Regulate Autophagy and Can Target Autophagic Substrates by Direct Recognition
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.devcel.2019.06.016openalex-snapshot
Selective Autophagy of Mitochondria on a Ubiquitin-Endoplasmic-Reticulum Platform
inferred← citeshttps://doi.org/10.1016/j.drup.2024.101170openalex-snapshot
Autophagy in cancer development, immune evasion, and drug resistance
inferred← citeshttps://doi.org/10.1016/j.ecoenv.2020.110667openalex-snapshot
Methylmercury disrupts autophagic flux by inhibiting autophagosome-lysosome fusion in mouse germ cells
inferred← citeshttps://doi.org/10.1016/j.exger.2010.03.018openalex-snapshot
Impaired quality control of mitochondria: Aging from a new perspective
inferred← citeshttps://doi.org/10.1016/j.febslet.2009.12.037openalex-snapshot
Autophagy in the fission yeast Schizosaccharomyces pombe
inferred← citeshttps://doi.org/10.1016/j.febslet.2010.01.007openalex-snapshot
Autophagy in plants and phytopathogens
inferred← citeshttps://doi.org/10.1016/j.febslet.2010.01.018openalex-snapshot
Atg8‐family interacting motif crucial for selective autophagy
inferred← citeshttps://doi.org/10.1016/j.febslet.2010.01.019openalex-snapshot
Molecular mechanism and physiological role of pexophagy
inferred← citeshttps://doi.org/10.1016/j.febslet.2010.02.001openalex-snapshot
Current knowledge of the pre‐autophagosomal structure (PAS)
inferred← citeshttps://doi.org/10.1016/j.febslet.2010.02.013openalex-snapshot
The Cvt pathway as a model for selective autophagy
inferred← citeshttps://doi.org/10.1016/j.febslet.2010.02.060openalex-snapshot
Parkin‐mediated selective mitochondrial autophagy, mitophagy: Parkin purges damaged organelles from the vital mitochondrial network
inferred← citeshttps://doi.org/10.1016/j.febslet.2013.04.030openalex-snapshot
Mitochondrial degradation during starvation is selective and temporally distinct from bulk autophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.febslet.2013.06.007openalex-snapshot
Redox modification of proteins as essential mediators of CNS autophagy and mitophagy
inferred← citeshttps://doi.org/10.1016/j.febslet.2014.09.032openalex-snapshot
Hrr25 phosphorylates the autophagic receptor Atg34 to promote vacuolar transport of α‐mannosidase under nitrogen starvation conditions
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2016.03.022openalex-snapshot
A SIRT3/AMPK/autophagy network orchestrates the protective effects of trans-resveratrol in stressed peritoneal macrophages and RAW 264.7 macrophages
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2016.03.030openalex-snapshot
Mitophagy receptors sense stress signals and couple mitochondrial dynamic machinery for mitochondrial quality control
inferred← citeshttps://doi.org/10.1016/j.funbio.2015.03.001openalex-snapshot
Functional analysis of AoAtg11 in selective autophagy in the filamentous fungus Aspergillus oryzae
inferred← citeshttps://doi.org/10.1016/j.gde.2016.02.006openalex-snapshot
Mitochondrial autophagy in cardiomyopathy
inferred← citeshttps://doi.org/10.1016/j.gene.2025.149765openalex-snapshot
The anti-aging mechanisms of Catalpol by elevating mitophagy
inferred← citeshttps://doi.org/10.1016/j.heliyon.2024.e30238openalex-snapshot
RETRACTED: Guidelines for the role of autophagy in drug delivery vectors uptake pathways
inferred← citeshttps://doi.org/10.1016/j.ijfoodmicro.2026.111763openalex-snapshot
Integrated transcriptomic and metabolomic analyses reveal the mechanism of hypoxia tolerance in Aspergillus chevalieri under controlled nitrogen atmosphere
inferred← citeshttps://doi.org/10.1016/j.immuni.2010.03.002openalex-snapshot
Selective Macroautophagy for Immunity
inferred← citeshttps://doi.org/10.1016/j.jbc.2021.100891openalex-snapshot
Regulation of inorganic polyphosphate is required for proper vacuolar proteolysis in fission yeast
inferred← citeshttps://doi.org/10.1016/j.jbc.2022.102533openalex-snapshot
Eisosome protein Pil1 regulates mitochondrial morphology, mitophagy, and cell death in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1016/j.jchromb.2023.123712openalex-snapshot
Mechanisms of Xuefu Zhuyu Decoction in the treatment of coronary heart disease based on integrated metabolomics and network pharmacology approach
inferred← citeshttps://doi.org/10.1016/j.jlr.2024.100601openalex-snapshot
Cardiolipin remodeling maintains the inner mitochondrial membrane in cells with saturated lipidomes
inferred← citeshttps://doi.org/10.1016/j.jmb.2016.02.021openalex-snapshot
An overview of macroautophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.jmb.2016.02.027openalex-snapshot
Mechanisms of Selective Autophagy in Normal Physiology and Cancer
inferred← citeshttps://doi.org/10.1016/j.jmb.2017.01.003openalex-snapshot
Structural Biology of the Cvt Pathway
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.2019.06.017openalex-snapshot
Mechanistic Insights into the Role of Atg11 in Selective Autophagy
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