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Piecemeal Microautophagy of Nucleus in Saccharomyces cerevisiae

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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(19960315)12:3<259::aid-yea901>3.0.co;2-copenalex-snapshot

PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae

inferredcites →https://doi.org/10.1002/(sici)1097-0061(199808)14:11<1041::aid-yea296>3.0.co;2-4openalex-snapshot

A search in the genome ofSaccharomyces cerevisiae for genes regulated via stress response elements

inferredcites →https://doi.org/10.1002/j.1460-2075.1984.tb02264.xopenalex-snapshot

Hsp70 accelerates the recovery of nucleolar morphology after heat shock.

inferredcites →https://doi.org/10.1002/yea.320091103openalex-snapshot

Ultrastructural changes in yeast following heat shock and recovery

inferredcites →https://doi.org/10.1002/yea.320100203openalex-snapshot

Ribosome synthesis during the growth cycle of Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1006/bbrc.1995.1636openalex-snapshot

Novel System for Monitoring Autophagy in the Yeast Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1006/jsbi.1996.0013openalex-snapshot

Computer Visualization of Three-Dimensional Image Data Using IMOD

inferredcites →https://doi.org/10.1006/scdb.2000.0163openalex-snapshot

Transport of proteins to the yeast vacuole: autophagy, cytoplasm-to-vacuole targeting, and role of the vacuole in degradation

inferredcites →https://doi.org/10.1007/s004120050357openalex-snapshot

Functional compartmentalization of the nucleus in the budding yeast Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1016/0076-6879(91)94004-vopenalex-snapshot

Getting started with yeast

inferredcites →https://doi.org/10.1016/s0021-9258(18)52969-0openalex-snapshot

Phenotypic analysis of proteinase A mutants. Implications for autoactivation and the maturation pathway of the vacuolar hydrolases of Saccharomyces cerevisiae.

inferredcites →https://doi.org/10.1016/s0022-5320(76)80023-8openalex-snapshot

Nuclear pore absence from areas of close association between nucleus and vacuole in synchronous yeast cultures

inferredcites →https://doi.org/10.1016/s0092-8674(00)81520-2openalex-snapshot

The Exosome

inferredcites →https://doi.org/10.1016/s0962-8924(02)02278-xopenalex-snapshot

Yeast autophagosomes: de novo formation of a membrane structure

inferredcites →https://doi.org/10.1038/26506openalex-snapshot

A protein conjugation system essential for autophagy

inferredcites →https://doi.org/10.1038/35044114openalex-snapshot

A ubiquitin-like system mediates protein lipidation

inferredcites →https://doi.org/10.1046/j.1356-9597.2001.00499.xopenalex-snapshot

Paz2 and 13 other PAZ gene products regulate vacuolar engulfment of peroxisomes during micropexophagy

inferredcites →https://doi.org/10.1046/j.1432-1327.1999.00658.xopenalex-snapshot

Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact

inferredcites →https://doi.org/10.1073/pnas.80.2.510openalex-snapshot

Mutations in PEP4 locus of Saccharomyces cerevisiae block final step in maturation of two vacuolar hydrolases.

inferredcites →https://doi.org/10.1073/pnas.93.22.12304openalex-snapshot

Cytoplasm-to-vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole.

inferredcites →https://doi.org/10.1073/pnas.96.26.14866openalex-snapshot

Rapamycin-modulated transcription defines the subset of nutrient-sensitive signaling pathways directly controlled by the Tor proteins

inferredcites →https://doi.org/10.1074/jbc.273.51.33889openalex-snapshot

A New Protein Conjugation System in Human

inferredcites →https://doi.org/10.1074/jbc.273.7.3963openalex-snapshot

Tor, a Phosphatidylinositol Kinase Homologue, Controls Autophagy in Yeast

inferredcites →https://doi.org/10.1074/jbc.274.31.21943openalex-snapshot

Subcellular Localization, Stoichiometry, and Protein Levels of 26 S Proteasome Subunits in Yeast

inferredcites →https://doi.org/10.1074/jbc.m002813200openalex-snapshot

Apg13p and Vac8p Are Part of a Complex of Phosphoproteins That Are Required for Cytoplasm to Vacuole Targeting

inferredcites →https://doi.org/10.1074/jbc.m109134200openalex-snapshot

Convergence of Multiple Autophagy and Cytoplasm to Vacuole Targeting Components to a Perivacuolar Membrane Compartment Prior tode Novo Vesicle Formation

inferredcites →https://doi.org/10.1083/jcb.103.5.2035openalex-snapshot

Cellular and biochemical events in mammalian cells during and after recovery from physiological stress.

inferredcites →https://doi.org/10.1083/jcb.119.2.301openalex-snapshot

Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction.

inferredcites →https://doi.org/10.1083/jcb.124.6.903openalex-snapshot

Ultrastructural analysis of the autophagic process in yeast: detection of autophagosomes and their characterization

inferredcites →https://doi.org/10.1083/jcb.129.6.1601openalex-snapshot

Three-dimensional ultrastructural analysis of the Saccharomyces cerevisiae mitotic spindle.

inferredcites →https://doi.org/10.1083/jcb.138.3.517openalex-snapshot

A Multispecificity Syntaxin Homologue, Vam3p, Essential for Autophagic and Biosynthetic Protein Transport to the Vacuole

inferredcites →https://doi.org/10.1083/jcb.140.5.1063openalex-snapshot

Vac8p, a Vacuolar Protein with Armadillo Repeats, Functions in both Vacuole Inheritance and Protein Targeting from the Cytoplasm to Vacuole

inferredcites →https://doi.org/10.1083/jcb.141.3.625openalex-snapshot

Peroxisome Degradation by Microautophagy in Pichia pastoris : Identification of Specific Steps and Morphological Intermediates

inferredcites →https://doi.org/10.1083/jcb.150.6.1507openalex-snapshot

Tor-Mediated Induction of Autophagy via an Apg1 Protein Kinase Complex

inferredcites →https://doi.org/10.1083/jcb.151.3.519openalex-snapshot

Autophagic Tubes

inferredcites →https://doi.org/10.1083/jcb.151.3.529openalex-snapshot

Cell-Free Reconstitution of Microautophagic Vacuole Invagination and Vesicle Formation

inferredcites →https://doi.org/10.1083/jcb.151.5.1025openalex-snapshot

Dissection of Autophagosome Biogenesis into Distinct Nucleation and Expansion Steps

inferredcites →https://doi.org/10.1083/jcb.152.1.51openalex-snapshot

Membrane Recruitment of Aut7p in the Autophagy and Cytoplasm to Vacuole Targeting Pathways Requires Aut1p, Aut2p, and the Autophagy Conjugation Complex

inferredcites →https://doi.org/10.1091/mbc.10.4.987openalex-snapshot

Regulation of Ribosome Biogenesis by the Rapamycin-sensitive TOR-signaling Pathway inSaccharomyces cerevisiae

inferredcites →https://doi.org/10.1091/mbc.10.5.1353openalex-snapshot

Glucose-induced Autophagy of Peroxisomes inPichia pastorisRequires a Unique E1-like Protein

inferredcites →https://doi.org/10.1091/mbc.11.12.4241openalex-snapshot

Genomic Expression Programs in the Response of Yeast Cells to Environmental Changes

inferredcites →https://doi.org/10.1091/mbc.11.7.2445openalex-snapshot

Nucleus–Vacuole Junctions inSaccharomyces cerevisiaeAre Formed Through the Direct Interaction of Vac8p with Nvj1p

inferredcites →https://doi.org/10.1091/mbc.12.6.1633openalex-snapshot

Dual Targeting of Osh1p, a Yeast Homologue of Oxysterol-binding Protein, to both the Golgi and the Nucleus-Vacuole Junction

inferredcites →https://doi.org/10.1091/mbc.6.11.1515openalex-snapshot

Nucleolar accumulation of poly (A)+ RNA in heat-shocked yeast cells: implication of nucleolar involvement in mRNA transport.

inferredcites →https://doi.org/10.1091/mbc.7.1.173openalex-snapshot

Nucleolar accumulation of poly (A)+ RNA in heat-shocked yeast cells: implication of nucleolar involvement in mRNA transport.

inferredcites →https://doi.org/10.1091/mbc.7.9.1375openalex-snapshot

Multiple classes of yeast mutants are defective in vacuole partitioning yet target vacuole proteins correctly.

inferredcites →https://doi.org/10.1093/emboj/18.21.6005openalex-snapshot

Cytoplasm to vacuole trafficking of aminopeptidase I requires a t‐SNARE–Sec1p complex composed of Tlg2p and Vps45p

inferredcites →https://doi.org/10.1093/emboj/20.12.3145openalex-snapshot

Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion

inferredcites →https://doi.org/10.1093/emboj/20.21.5971openalex-snapshot

The pre‐autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation

inferredcites →https://doi.org/10.1093/genetics/102.4.665openalex-snapshot

PEP4 GENE FUNCTION IS REQUIRED FOR EXPRESSION OF SEVERAL VACUOLAR HYDROLASES IN SACCHAROMYCES CEREVISIAE

inferredcites →https://doi.org/10.1093/nar/24.13.2519openalex-snapshot

A new efficient gene disruption cassette for repeated use in budding yeast

inferredcites →https://doi.org/10.1098/rstb.1999.0501openalex-snapshot

Molecular mechanism of autophagy in yeast, Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1101/087969364.21c.363openalex-snapshot

4 Biogenesis and Function of the Yeast Vacuole

inferredcites →https://doi.org/10.1126/science.278.5338.680openalex-snapshot

Exploring the Metabolic and Genetic Control of Gene Expression on a Genomic Scale

inferredcites →https://doi.org/10.1128/mcb.18.9.5308openalex-snapshot

Vam7p, a SNAP-25-Like Molecule, and Vam3p, a Syntaxin Homolog, Function Together in Yeast Vacuolar Protein Trafficking

inferredcites →https://doi.org/10.1128/mcb.21.1.109-125.2001openalex-snapshot

Tsc13p Is Required for Fatty Acid Elongation and Localizes to a Novel Structure at the Nuclear-Vacuolar Interface in Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1146/annurev.cellbio.15.1.1openalex-snapshot

Vacuolar Import of Proteins and Organelles From The Cytoplasm

inferredcites →https://doi.org/10.1159/000350326openalex-snapshot

Antimicrobial Autophagy: A Conserved Innate Immune Response in Drosophila

inferredcites →https://doi.org/10.1242/jcs.108.1.25openalex-snapshot

Divergent modes of autophagy in the methylotrophic yeast Pichia pastoris

inferredcites →https://doi.org/10.1242/jcs.111.15.2137openalex-snapshot

YEB3/VAC8 encodes a myristylated armadillo protein of the Saccharomyces cerevisiae vacuolar membrane that functions in vacuole fusion and inheritance

inferredcites →https://doi.org/10.1242/jcs.111.20.3109openalex-snapshot

Ye1013p (Vac8p), an armadillo repeat protein related to plakoglobin and importin α, is associated with the yeast vacuole membrane

inferredcites →https://doi.org/10.1242/jcs.112.22.4079openalex-snapshot

Peroxisome degradation in Saccharomyces cerevisiae is dependent on machinery of macroautophagy and the Cvt pathway

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.3401844openalex-extracted

Membrane Dynamics of Lipid Droplet-Mediated ER Proteostasis in the Budding Yeast, Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1002/1873-3468.12750openalex-snapshot

Repair or destruction—an intimate liaison between ubiquitin ligases and molecular chaperones in proteostasis

inferred← citeshttps://doi.org/10.1002/1873-3468.14719openalex-snapshot

Autophagy as a caretaker of nuclear integrity

inferred← citeshttps://doi.org/10.1002/1873-3468.14739openalex-snapshot

Changing the guard—nuclear pore complex quality control

inferred← citeshttps://doi.org/10.1002/1873-3468.14760openalex-snapshot

ATG and ESCRT control multiple modes of microautophagy

inferred← citeshttps://doi.org/10.1002/3527600906.mcb.200300122openalex-snapshot

Biogenesis, Structure and Function of Lysosomes

inferred← citeshttps://doi.org/10.1002/9780470747919.ch12openalex-snapshot

Protein Degradation and the Lysosomal System

inferred← citeshttps://doi.org/10.1002/9781118015759.ch11openalex-snapshot

Endoplasmic Reticulum Junctions

inferred← citeshttps://doi.org/10.1002/9781118063903.ch3openalex-snapshot

Chaperone‐Mediated Autophagy and Parkinson's Disease

inferred← citeshttps://doi.org/10.1002/9781118845363.ch5openalex-snapshot

Protein Aggregation in Unicellular Eukaryotes

inferred← citeshttps://doi.org/10.1002/9781119436812.ch11openalex-snapshot

Protein Degradation and the Lysosomal System

inferred← citeshttps://doi.org/10.1002/bies.201800008openalex-snapshot

Three Distinct Types of Microautophagy Based on Membrane Dynamics and Molecular Machineries

inferred← citeshttps://doi.org/10.1002/cbin.11504openalex-snapshot

The multifaceted roles of nucleophagy in cancer development and therapy

inferred← citeshttps://doi.org/10.1002/chemv.201800061openalex-snapshot

How to Live Long and Prosper

inferred← citeshttps://doi.org/10.1002/jcb.22009openalex-snapshot

Defects in intracellular trafficking and endocytic/vacuolar acidification determine the efficiency of endocytotic DNA uptake in yeast

inferred← citeshttps://doi.org/10.1002/jcp.25355openalex-snapshot

The Malleable Nature of the Budding Yeast Nuclear Envelope: Flares, Fusion, and Fenestrations

inferred← citeshttps://doi.org/10.1002/mbo3.70278openalex-snapshot

Nuclear Microautophagy Drives Vacuolar Targeting of Yeast Iron‐Regulated Proteins During Lipid and Iron Limitation

inferred← citeshttps://doi.org/10.1002/med.21662openalex-snapshot

How autophagy can restore proteostasis defects in multiple diseases?

inferred← citeshttps://doi.org/10.1002/path.3025openalex-snapshot

Autophagy and disease: always two sides to a problem

inferred← citeshttps://doi.org/10.1002/smtd.202300447openalex-snapshot

Label‐Free Intracellular Multi‐Specificity in Yeast Cells by Phase‐Contrast Tomographic Flow Cytometry

inferred← citeshttps://doi.org/10.1002/yea.946openalex-snapshot

Current awareness on yeast

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Programmed Cell Death and Apoptosis in Fungi

inferred← citeshttps://doi.org/10.1007/978-1-59745-157-4_16openalex-snapshot

Microautophagy in the Yeast Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1007/978-3-031-14740-1_12openalex-snapshot

CHIP: A Co-chaperone for Degradation by the Proteasome and Lysosome

inferred← citeshttps://doi.org/10.1007/978-3-319-21033-9_7openalex-snapshot

Nuclear Dismantling Events: Crucial Steps During the Execution of Plant Programmed Cell Death

inferred← citeshttps://doi.org/10.1007/978-3-319-28637-2_12openalex-snapshot

The Deleterious Duo of Neurodegeneration: Lysosomes and Mitochondria

inferred← citeshttps://doi.org/10.1007/978-3-642-00302-8_14openalex-snapshot

Something Old, Something New: Plant Innate Immunity and Autophagy

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Selective autophagy in cellular quality control

inferred← citeshttps://doi.org/10.1007/978-90-481-3465-6_10openalex-snapshot

Changes in Lysosomes and Their Autophagic Function in Aging: The Comparative Biology of Lysosomal Function

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Nibbling within the nucleus: turnover of nuclear contents

inferred← citeshttps://doi.org/10.1007/s00018-011-0865-5openalex-snapshot

Microautophagy: lesser-known self-eating

inferred← citeshttps://doi.org/10.1007/s00253-013-5221-2openalex-snapshot

Self-eating to grow and kill: autophagy in filamentous ascomycetes

inferred← citeshttps://doi.org/10.1007/s00294-004-0548-yopenalex-snapshot

The yeast VPS genes affect telomere length regulation

inferred← citeshttps://doi.org/10.1007/s00294-016-0616-0openalex-snapshot

Target of rapamycin signaling mediates vacuolar fragmentation

inferred← citeshttps://doi.org/10.1007/s00294-019-00971-1openalex-snapshot

Patrolling the nucleus: inner nuclear membrane-associated degradation

inferred← citeshttps://doi.org/10.1007/s00709-022-01788-5openalex-snapshot

Investigation of the cell structure and organelles during autolytic PCD of Antirrhinum majus “Legend White” petals

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Selective Autophagy: Talking with the UPS

inferred← citeshttps://doi.org/10.1016/b978-0-12-374028-1.00031-2openalex-snapshot

Selective Autophagy in the Pathogenesis of Parkinson's Disease

inferred← citeshttps://doi.org/10.1016/b978-0-12-394447-4.30054-2openalex-snapshot

Autophagy

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Introduction to Autophagy

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Introduction to Autophagy

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Introduction to Autophagy

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Introduction to Autophagy

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Def1 mediates the degradation of excess nucleolar protein Nop1 in budding yeast

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The yeast VAPs Scs2 and Scs22 are required for NVJ integrity and micronucleophagy

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ESCRT mediates micronucleophagy and macronucleophagy in yeast

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Nuclear ESCRT is involved in intranuclear protein quality control by micronucleophagy

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The bridge-like lipid transfer protein Vps13 are required for NVJ integrity and nucleophagy

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Mechanisms of chaperone-mediated autophagy

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Lysosomal proteolysis in skeletal muscle

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Growth hormone modulates the degradative capacity of muscle nucleases but not of cathepsin D in post-weaning mice

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Turnover of organelles by autophagy in yeast

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Lipid transfer and signaling at organelle contact sites: the tip of the iceberg

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inferred← citeshttps://doi.org/10.1016/j.ceb.2016.03.009openalex-snapshot

A model for coordinating nuclear mechanics and membrane remodeling to support nuclear integrity

inferred← citeshttps://doi.org/10.1016/j.ceb.2020.01.011openalex-snapshot

CHMPions of repair: Emerging perspectives on sensing and repairing the nuclear envelope barrier

inferred← citeshttps://doi.org/10.1016/j.cellsig.2020.109884openalex-snapshot

Cdc14 protein phosphatase and topoisomerase II mediate rDNA dynamics and nucleophagic degradation of nucleolar proteins after TORC1 inactivation

inferred← citeshttps://doi.org/10.1016/j.celrep.2014.08.074openalex-snapshot

Dnase2a Deficiency Uncovers Lysosomal Clearance of Damaged Nuclear DNA via Autophagy

inferred← citeshttps://doi.org/10.1016/j.celrep.2015.06.022openalex-snapshot

Lam6 Regulates the Extent of Contacts between Organelles

inferred← citeshttps://doi.org/10.1016/j.celrep.2019.08.059openalex-snapshot

rDNA Condensation Promotes rDNA Separation from Nucleolar Proteins Degraded for Nucleophagy after TORC1 Inactivation

inferred← citeshttps://doi.org/10.1016/j.celrep.2019.08.069openalex-snapshot

Multilayered Control of Protein Turnover by TORC1 and Atg1

inferred← citeshttps://doi.org/10.1016/j.celrep.2020.108446openalex-snapshot

Nutrient Signaling, Stress Response, and Inter-organelle Communication Are Non-canonical Determinants of Cell Fate

inferred← citeshttps://doi.org/10.1016/j.coi.2006.11.009openalex-snapshot

Autophagy in MHC class II antigen processing

inferred← citeshttps://doi.org/10.1016/j.cub.2021.06.078openalex-snapshot

Post-ER degradation of misfolded GPI-anchored proteins is linked with microautophagy

inferred← citeshttps://doi.org/10.1016/j.devcel.2016.10.022openalex-snapshot

A Tether Is a Tether Is a Tether: Tethering at Membrane Contact Sites

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.2018.05.011openalex-snapshot

Vps39 Interacts with Tom40 to Establish One of Two Functionally Distinct Vacuole-Mitochondria Contact Sites

inferred← citeshttps://doi.org/10.1016/j.devcel.2019.07.009openalex-snapshot

Compartmentalized Synthesis of Triacylglycerol at the Inner Nuclear Membrane Regulates Nuclear Organization

inferred← citeshttps://doi.org/10.1016/j.devcel.2020.06.026openalex-snapshot

Tether Me, Tether Me Not—Dynamic Organelle Contact Sites in Metabolic Rewiring

inferred← citeshttps://doi.org/10.1016/j.devcel.2024.01.014openalex-snapshot

LDO proteins and Vac8 form a vacuole-lipid droplet contact site to enable starvation-induced lipophagy in yeast

inferred← citeshttps://doi.org/10.1016/j.femsyr.2004.05.001openalex-snapshot

Uth1p: a yeast mitochondrial protein at the crossroads of stress, degradation and cell death

inferred← citeshttps://doi.org/10.1016/j.femsyr.2005.07.008openalex-snapshot

Increased nuclear envelope permeability and Pep4p-dependent degradation of nucleoporins during hydrogen peroxide-induced cell death

inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2006.08.012openalex-snapshot

Lipid oxidation and autophagy in yeast

inferred← citeshttps://doi.org/10.1016/j.gene.2013.02.033openalex-snapshot

Nijmegen breakage syndrome: The clearance pathway for mutant nibrin protein is allele specific

inferred← citeshttps://doi.org/10.1016/j.ghir.2006.12.008openalex-snapshot

The modulator effect of GH on skeletal muscle lysosomal enzymes is dietary protein dependent

inferred← citeshttps://doi.org/10.1016/j.isci.2025.113314openalex-snapshot

A Spike-Accum bioconjugate protein vaccine confers potent SARS-CoV-2-specific immunity

inferred← citeshttps://doi.org/10.1016/j.jbc.2024.108045openalex-snapshot

Quiescent cells maintain active degradation-mediated protein quality control requiring proteasome, autophagy, and nucleus-vacuole junctions

inferred← citeshttps://doi.org/10.1016/j.jbiotec.2013.09.008openalex-snapshot

Sustainability of industrial yeast serial repitching practice studied by gene expression and correlation analysis

inferred← citeshttps://doi.org/10.1016/j.jgg.2021.06.011openalex-snapshot

Nucleolus-localized Def-CAPN3 protein degradation pathway and its role in cell cycle control and ribosome biogenesis

inferred← citeshttps://doi.org/10.1016/j.jmb.2016.03.030openalex-snapshot

Regulation of Autophagy By Signaling Through the Atg1/ULK1 Complex

inferred← citeshttps://doi.org/10.1016/j.mam.2012.09.001openalex-snapshot

Protein damage, repair and proteolysis

inferred← citeshttps://doi.org/10.1016/j.mib.2012.09.005openalex-snapshot

Programmed cell death in the cellular differentiation of microbial eukaryotes

inferred← citeshttps://doi.org/10.1016/j.molcel.2015.07.021openalex-snapshot

Organelle-Specific Initiation of Autophagy

inferred← citeshttps://doi.org/10.1016/j.nut.2006.04.008openalex-snapshot

Proteolytic and lipolytic responses to starvation

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.phrs.2012.10.002openalex-snapshot

Chaperones in autophagy

inferred← citeshttps://doi.org/10.1016/j.plantsci.2012.09.009openalex-snapshot

A comparison between nuclear dismantling during plant and animal programmed cell death

inferred← citeshttps://doi.org/10.1016/j.plipres.2007.06.002openalex-snapshot

Non-vesicular sterol transport in cells

inferred← citeshttps://doi.org/10.1016/j.pneurobio.2017.08.005openalex-snapshot

Progressing neurobiological strategies against proteostasis failure: Challenges in neurodegeneration

inferred← citeshttps://doi.org/10.1016/j.repbio.2019.06.006openalex-snapshot

Heat exposure affected the reproductive performance of pregnant mice: Enhancement of autophagy and alteration of subcellular structure in the corpus luteum

inferred← citeshttps://doi.org/10.1016/j.semcdb.2020.02.013openalex-snapshot

Multifarious roles of lipid droplets in autophagy – Target, product, and what else?

inferred← citeshttps://doi.org/10.1016/j.str.2017.02.010openalex-snapshot

Structure of Yeast OSBP-Related Protein Osh1 Reveals Key Determinants for Lipid Transport and Protein Targeting at the Nucleus-Vacuole Junction

inferred← citeshttps://doi.org/10.1016/j.tcb.2003.12.002openalex-snapshot

Autophagy: in sickness and in health

inferred← citeshttps://doi.org/10.1016/j.tcb.2015.08.002openalex-snapshot

Border Safety: Quality Control at the Nuclear Envelope

inferred← citeshttps://doi.org/10.1016/j.tcb.2020.02.001openalex-snapshot

ER-Phagy: Quality Control and Turnover of Endoplasmic Reticulum

inferred← citeshttps://doi.org/10.1016/j.tcb.2021.12.008openalex-snapshot

Degradation of nuclear components via different autophagy pathways

inferred← citeshttps://doi.org/10.1016/j.tcb.2023.11.005openalex-snapshot

Lysosomal microautophagy: an emerging dimension in mammalian autophagy

inferred← citeshttps://doi.org/10.1016/j.tibs.2009.12.006openalex-snapshot

A ‘garbage can’ for ribosomes: how eukaryotes degrade their ribosomes

inferred← citeshttps://doi.org/10.1016/j.tibs.2011.08.004openalex-snapshot

Staying in touch: the molecular era of organelle contact sites

inferred← citeshttps://doi.org/10.1016/j.ymeth.2014.11.023openalex-snapshot

Assays for the biochemical and ultrastructural measurement of selective and nonselective types of autophagy in the yeast Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1016/s0074-7696(03)32001-7openalex-snapshot

Dynamics of Endosomal Sorting

inferred← citeshttps://doi.org/10.1016/s0074-7696(06)53001-3openalex-snapshot

Multifunctional Arm Repeat Domains in Plants

inferred← citeshttps://doi.org/10.1016/s0076-6879(08)03207-2openalex-snapshot

Chapter 7 Monitoring Autophagy in Yeast using FM 4‐64 Fluorescence

inferred← citeshttps://doi.org/10.1016/s0076-6879(08)03209-6openalex-snapshot

Chapter 9 Monitoring Organelle Turnover in Yeast Using Fluorescent Protein Tags

inferred← citeshttps://doi.org/10.1016/s0076-6879(08)03210-2openalex-snapshot

Chapter 10 Electron Microscopy in Yeast

inferred← citeshttps://doi.org/10.1016/s0076-6879(08)03211-4openalex-snapshot

Chapter 11 Cell‐Free Reconstitution of Microautophagy in Yeast

inferred← citeshttps://doi.org/10.1016/s0091-679x(10)96010-xopenalex-snapshot

Toward Sub-second Correlative Light and Electron Microscopy of Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1016/s1359-6446(03)02636-9openalex-snapshot

Nucleus ‘hallowed ground’ no more

inferred← citeshttps://doi.org/10.1016/s1534-5807(03)00296-xopenalex-snapshot

A Unified Nomenclature for Yeast Autophagy-Related Genes

inferred← citeshttps://doi.org/10.1023/b:mcbi.0000041848.57020.57openalex-snapshot

Autophagy: Many paths to the same end

inferred← citeshttps://doi.org/10.1038/bonekey.2012.65openalex-snapshot

Non-coding RNAs and posttranscriptional regulation in cartilage and bone

inferred← citeshttps://doi.org/10.1038/cdd.2012.73openalex-snapshot

Selective autophagy in budding yeast

inferred← citeshttps://doi.org/10.1038/nature07208openalex-snapshot

Autophagy in thymic epithelium shapes the T-cell repertoire and is essential for tolerance

inferred← citeshttps://doi.org/10.1038/nature07976openalex-snapshot

Autophagy regulates lipid metabolism

inferred← citeshttps://doi.org/10.1038/nature15548openalex-snapshot

Autophagy mediates degradation of nuclear lamina

inferred← citeshttps://doi.org/10.1038/ncb1723openalex-snapshot

Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease

inferred← citeshttps://doi.org/10.1038/ncomms14354openalex-snapshot

Molecular basis for protection of ribosomal protein L4 from cellular degradation

inferred← citeshttps://doi.org/10.1038/nrm1892openalex-snapshot

Organelles on the move: insights from yeast vacuole inheritance

inferred← citeshttps://doi.org/10.1038/s41417-020-0205-8openalex-snapshot

Autophagy inhibition is the next step in the treatment of glioblastoma patients following the Stupp era

inferred← citeshttps://doi.org/10.1038/s41418-024-01442-yopenalex-snapshot

Mechanisms of regulated cell death during plant infection by the rice blast fungus Magnaporthe oryzae

inferred← citeshttps://doi.org/10.1038/s41421-020-0141-7openalex-snapshot

Lysosome biology in autophagy

inferred← citeshttps://doi.org/10.1038/s41467-019-09253-3openalex-snapshot

Coming together to define membrane contact sites

inferred← citeshttps://doi.org/10.1038/s41467-021-27420-3openalex-snapshot

Spatial control of avidity regulates initiation and progression of selective autophagy

inferred← citeshttps://doi.org/10.1038/s41467-023-36697-5openalex-snapshot

Orthodenticle homeobox 2 is transported to lysosomes by nuclear budding vesicles

inferred← citeshttps://doi.org/10.1038/s41467-024-55045-9openalex-snapshot

Macronucleophagy maintains cell viability under nitrogen starvation by modulating micronucleophagy

inferred← citeshttps://doi.org/10.1038/s41556-019-0459-2openalex-snapshot

Selective autophagy degrades nuclear pore complexes

inferred← citeshttps://doi.org/10.1038/s41556-023-01128-6openalex-snapshot

Nuclear and cytoplasmic spatial protein quality control is coordinated by nuclear–vacuolar junctions and perinuclear ESCRT

inferred← citeshttps://doi.org/10.1038/s41556-025-01612-1openalex-snapshot

A quantitative ultrastructural timeline of nuclear autophagy reveals a role for dynamin-like protein 1 at the nuclear envelope

inferred← citeshttps://doi.org/10.1038/s41556-025-01747-1openalex-snapshot

A chaperone-proteasome-based fragmentation machinery is essential for aggrephagy

inferred← citeshttps://doi.org/10.1038/s41580-018-0001-6openalex-snapshot

The coming of age of chaperone-mediated autophagy

inferred← citeshttps://doi.org/10.1038/s41580-019-0180-9openalex-snapshot

The functional universe of membrane contact sites

inferred← citeshttps://doi.org/10.1038/s41580-022-00529-zopenalex-snapshot

The emerging mechanisms and functions of microautophagy

inferred← citeshttps://doi.org/10.1038/s41598-024-64493-8openalex-snapshot

Partitioning into ER membrane microdomains impacts autophagic protein turnover during cellular aging

inferred← citeshttps://doi.org/10.1038/sj.cdd.4401697openalex-snapshot

Impairing the bioenergetic status and the biogenesis of mitochondria triggers mitophagy in yeast

inferred← citeshttps://doi.org/10.1038/sj.onc.1209884openalex-snapshot

Cell growth control: little eukaryotes make big contributions

inferred← citeshttps://doi.org/10.1042/bcj20200722openalex-snapshot

Nutrient transceptors physically interact with the yeast S6/protein kinase B homolog, Sch9, a TOR kinase target

inferred← citeshttps://doi.org/10.1042/bj20100263openalex-snapshot

Functional implications of sterol transport by the oxysterol-binding protein gene family

inferred← citeshttps://doi.org/10.1042/bst0340340openalex-snapshot

Nucleus–vacuole junctions in yeast: anatomy of a membrane contact site

inferred← citeshttps://doi.org/10.1042/bst20150277openalex-snapshot

Vacuole membrane contact sites and domains: emerging hubs to coordinate organelle function with cellular metabolism

inferred← citeshttps://doi.org/10.1042/bst20170442openalex-snapshot

Fantastic nuclear envelope herniations and where to find them

inferred← citeshttps://doi.org/10.1042/bst20250460openalex-snapshot

Small bites for big problems: stepwise aggregate degradation by autophagy

inferred← citeshttps://doi.org/10.1051/medsci/2010263259openalex-snapshot

« Attrape-moi si tu peux »

inferred← citeshttps://doi.org/10.1071/ma07067openalex-snapshot

Organelle turnover by autophagy

inferred← citeshttps://doi.org/10.1073/pnas.1409476112openalex-snapshot

Fatty acid synthase is preferentially degraded by autophagy upon nitrogen starvation in yeast

inferred← citeshttps://doi.org/10.1073/pnas.1701030114openalex-snapshot

Mechanistic insight into the nucleus–vacuole junction based on the Vac8p–Nvj1p crystal structure

inferred← citeshttps://doi.org/10.1073/pnas.2008923117openalex-snapshot

Vps13 is required for the packaging of the ER into autophagosomes during ER-phagy

inferred← citeshttps://doi.org/10.1073/pnas.2020997118openalex-snapshot

Nuclear envelope budding is a response to cellular stress

inferred← citeshttps://doi.org/10.1073/pnas.2211501120openalex-snapshot

Structures of Vac8-containing protein complexes reveal the underlying mechanism by which Vac8 regulates multiple cellular processes

inferred← citeshttps://doi.org/10.1073/pnas.2319091121openalex-snapshot

Huntingtin contains an ubiquitin-binding domain and regulates lysosomal targeting of mitochondrial and RNA-binding proteins

inferred← citeshttps://doi.org/10.1074/jbc.m109.005181openalex-snapshot

Glutathione Participates in the Regulation of Mitophagy in Yeast

inferred← citeshttps://doi.org/10.1074/jbc.m117.783761openalex-snapshot

The m6A methyltransferase Ime4 epitranscriptionally regulates triacylglycerol metabolism and vacuolar morphology in haploid yeast cells

inferred← citeshttps://doi.org/10.1074/jbc.m406960200openalex-snapshot

Uth1p Is Involved in the Autophagic Degradation of Mitochondria

inferred← citeshttps://doi.org/10.1074/jbc.m506086200openalex-snapshot

Microautophagic Vacuole Invagination Requires Calmodulin in a Ca2+-independent Function

inferred← citeshttps://doi.org/10.1074/jbc.m506916200openalex-snapshot

Specific Role for Yeast Homologs of the Diamond Blackfan Anemia-associated Rps19 Protein in Ribosome Synthesis

inferred← citeshttps://doi.org/10.1074/jbc.m708993200openalex-snapshot

Membrane Topology and Essential Amino Acid Residues of Phs1, a 3-Hydroxyacyl-CoA Dehydratase Involved in Very Long-chain Fatty Acid Elongation*

inferred← citeshttps://doi.org/10.1074/jbc.r111.338400openalex-snapshot

A Detour for Yeast Oxysterol Binding Proteins

inferred← citeshttps://doi.org/10.1074/jbc.r117.804641openalex-snapshot

Transcriptional and post-transcriptional regulation of autophagy in the yeast Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1074/jbc.r117.818237openalex-snapshot

Chaperone-mediated autophagy and endosomal microautophagy: Jointed by a chaperone

inferred← citeshttps://doi.org/10.1074/jbc.ra118.005698openalex-snapshot

Analysis of autophagy activated during changes in carbon source availability in yeast cells

inferred← citeshttps://doi.org/10.1074/mcp.m400123-mcp200openalex-snapshot

The Spatial Organization of Lipid Synthesis in the Yeast Saccharomyces cerevisiae Derived from Large Scale Green Fluorescent Protein Tagging and High Resolution Microscopy

inferred← citeshttps://doi.org/10.1074/mcp.m800372-mcp200openalex-snapshot

The Yeast Vacuolar Membrane Proteome

inferred← citeshttps://doi.org/10.1080/0886022x.2016.1274662openalex-snapshot

Advance of autophagy in chronic kidney diseases

showing the first 200 of 417

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