On the public citation graph

Atg2: A novel phospholipid transfer protein that mediates de novo autophagosome biogenesis

0 signed · 124 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

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

inferredcites →https://doi.org/10.1002/1873-3468.12901openalex-snapshot
Differential requirement for ATG2A domains for localization to autophagic membranes and lipid droplets
inferredcites →https://doi.org/10.1002/ajmg.b.31206openalex-snapshot
Novel pathogenic mutations and copy number variations in the VPS13A Gene in patients with chorea‐acanthocytosis
inferredcites →https://doi.org/10.1016/0014-5793(93)80398-eopenalex-snapshot
Isolation and characterization of autophagy‐defective mutants of Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1016/j.bbalip.2015.12.003openalex-snapshot
SMP-domain proteins at membrane contact sites: Structure and function
inferredcites →https://doi.org/10.1016/j.ceb.2015.03.002openalex-snapshot
ER–mitochondria contact sites in yeast: beyond the myths of ERMES
inferredcites →https://doi.org/10.1016/j.cell.2014.01.070openalex-snapshot
Atomistic Autophagy: The Structures of Cellular Self-Digestion
inferredcites →https://doi.org/10.1016/j.chemphyslip.2018.11.001openalex-snapshot
Membrane-binding domains in autophagy
inferredcites →https://doi.org/10.1016/j.cub.2018.01.004openalex-snapshot
Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance
inferredcites →https://doi.org/10.1016/j.devcel.2016.06.015openalex-snapshot
The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes
inferredcites →https://doi.org/10.1016/j.ejmg.2017.12.007openalex-snapshot
Current state of knowledge in Chorea-Acanthocytosis as core Neuroacanthocytosis syndrome
inferredcites →https://doi.org/10.1016/j.febslet.2010.02.001openalex-snapshot
Current knowledge of the pre‐autophagosomal structure (PAS)
inferredcites →https://doi.org/10.1016/j.jmb.2016.02.021openalex-snapshot
An overview of macroautophagy in yeast
inferredcites →https://doi.org/10.1016/j.jmb.2019.02.019openalex-snapshot
Structural Conservation of the Two Phosphoinositide-Binding Sites in WIPI Proteins
inferredcites →https://doi.org/10.1016/j.molcel.2012.05.027openalex-snapshot
Two-Site Recognition of Phosphatidylinositol 3-Phosphate by PROPPINs in Autophagy
inferredcites →https://doi.org/10.1016/j.molcel.2013.12.011openalex-snapshot
Early Steps in Autophagy Depend on Direct Phosphorylation of Atg9 by the Atg1 Kinase
inferredcites →https://doi.org/10.1016/j.sbi.2016.09.010openalex-snapshot
Structural biology of the core autophagy machinery
inferredcites →https://doi.org/10.1038/nature14506openalex-snapshot
Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus
inferredcites →https://doi.org/10.1038/ncb1991openalex-snapshot
A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation
inferredcites →https://doi.org/10.1038/ncb2979openalex-snapshot
Cargo recognition and trafficking in selective autophagy
inferredcites →https://doi.org/10.1038/nsmb.2822openalex-snapshot
Structural basis of starvation-induced assembly of the autophagy initiation complex
inferredcites →https://doi.org/10.1038/s41580-018-0071-5openalex-snapshot
Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes
inferredcites →https://doi.org/10.1038/s41594-019-0203-4openalex-snapshot
Atg2 mediates direct lipid transfer between membranes for autophagosome formation
inferredcites →https://doi.org/10.1038/s41598-017-14337-5openalex-snapshot
Structure based biophysical characterization of the PROPPIN Atg18 shows Atg18 oligomerization upon membrane binding
inferredcites →https://doi.org/10.1073/pnas.1117797109openalex-snapshot
Molecular architecture of the multisubunit homotypic fusion and vacuole protein sorting (HOPS) tethering complex
inferredcites →https://doi.org/10.1073/pnas.1205128109openalex-snapshot
Structural and functional characterization of the two phosphoinositide binding sites of PROPPINs, a β-propeller protein family
inferredcites →https://doi.org/10.1073/pnas.1715592114openalex-snapshot
Crystal structures of Mmm1 and Mdm12–Mmm1 reveal mechanistic insight into phospholipid trafficking at ER-mitochondria contact sites
inferredcites →https://doi.org/10.1073/pnas.1806727115openalex-snapshot
The Atg2-Atg18 complex tethers pre-autophagosomal membranes to the endoplasmic reticulum for autophagosome formation
inferredcites →https://doi.org/10.1073/pnas.1811874115openalex-snapshot
Insights into autophagosome biogenesis from structural and biochemical analyses of the ATG2A-WIPI4 complex
inferredcites →https://doi.org/10.1074/jbc.m102342200openalex-snapshot
Apg2 Is a Novel Protein Required for the Cytoplasm to Vacuole Targeting, Autophagy, and Pexophagy Pathways
inferredcites →https://doi.org/10.1074/jbc.m102346200openalex-snapshot
Apg2p Functions in Autophagosome Formation on the Perivacuolar Structure
inferredcites →https://doi.org/10.1074/jbc.m112.397570openalex-snapshot
Structure-based Analyses Reveal Distinct Binding Sites for Atg2 and Phosphoinositides in Atg18
inferredcites →https://doi.org/10.1074/jbc.m803180200openalex-snapshot
The Atg18-Atg2 Complex Is Recruited to Autophagic Membranes via Phosphatidylinositol 3-Phosphate and Exerts an Essential Function
inferredcites →https://doi.org/10.1074/jbc.r117.802512openalex-snapshot
The lipopolysaccharide transport (Lpt) machinery: A nonconventional transporter for lipopolysaccharide assembly at the outer membrane of Gram-negative bacteria
inferredcites →https://doi.org/10.1080/15548627.2017.1359381openalex-snapshot
Architecture of the ATG2B-WDR45 complex and an aromatic Y/HF motif crucial for complex formation
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.200711112openalex-snapshot
Quantitative analysis of autophagy-related protein stoichiometry by fluorescence microscopy
inferredcites →https://doi.org/10.1083/jcb.200912089openalex-snapshot
An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis
inferredcites →https://doi.org/10.1083/jcb.201202061openalex-snapshot
Atg9 vesicles are an important membrane source during early steps of autophagosome formation
inferredcites →https://doi.org/10.1083/jcb.201502105openalex-snapshot
ER–mitochondrial junctions can be bypassed by dominant mutations in the endosomal protein Vps13
inferredcites →https://doi.org/10.1083/jcb.201710116openalex-snapshot
Atg9 establishes Atg2-dependent contact sites between the endoplasmic reticulum and phagophores
inferredcites →https://doi.org/10.1083/jcb.201807019openalex-snapshot
VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites
inferredcites →https://doi.org/10.1083/jcb.201809032openalex-snapshot
COPII vesicles contribute to autophagosomal membranes
inferredcites →https://doi.org/10.1083/jcb.201811139openalex-snapshot
ATG2 transports lipids to promote autophagosome biogenesis
inferredcites →https://doi.org/10.1091/mbc.e11-09-0785openalex-snapshot
Mammalian Atg2 proteins are essential for autophagosome formation and important for regulation of size and distribution of lipid droplets
inferredcites →https://doi.org/10.1091/mbc.e13-07-0381openalex-snapshot
ER exit sites are physical and functional core autophagosome biogenesis components
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.1365-2443.2008.01188.xopenalex-snapshot
Transport of phosphatidylinositol 3‐phosphate into the vacuole via autophagic membranes in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1146/annurev-biophys-060414-034248openalex-snapshot
Mechanisms of Autophagy
inferredcites →https://doi.org/10.1146/annurev-cellbio-092910-154005openalex-snapshot
The Role of Atg Proteins in Autophagosome Formation
inferredcites →https://doi.org/10.1194/jlr.m046359openalex-snapshot
Lipid droplet and early autophagosomal membrane targeting of Atg2A and Atg14L in human tumor cells
inferredcites →https://doi.org/10.1242/jcs.100065openalex-snapshot
High-curvature domains of the ER are important for the organization of ER exit sites in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1242/jcs.122960openalex-snapshot
Fine mapping of autophagy-related proteins during autophagosome formation in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1242/jcs.146258openalex-snapshot
WIPI proteins: essential PtdIns3 P effectors at the nascent autophagosome
inferredcites →https://doi.org/10.1247/csf.20.465openalex-snapshot
Analysis of the Membrane Structures Involved in Autophagy in Yeast by Freeze-Replica Method.
inferredcites →https://doi.org/10.1371/journal.pone.0181047openalex-snapshot
Atg4 plays an important role in efficient expansion of autophagic isolation membranes by cleaving lipidated Atg8 in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.15252/embj.201489083openalex-snapshot
Bulk RNA degradation by nitrogen starvation‐induced autophagy in yeast
inferredcites →https://doi.org/10.15252/embr.201744559openalex-snapshot
Remodeling of ER‐exit sites initiates a membrane supply pathway for autophagosome biogenesis
inferredcites →https://doi.org/10.4161/auto.5.8.10274openalex-snapshot
3D tomography reveals connections between the phagophore and endoplasmic reticulum
inferredcites →https://doi.org/10.7554/elife.45777openalex-snapshot
The autophagic membrane tether ATG2A transfers lipids between membranes
inferredcites →https://doi.org/10.7554/elife.45777.020openalex-snapshot
Author response: The autophagic membrane tether ATG2A transfers lipids between membranes

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/10.1002/1873-3468.14726openalex-snapshot
Novel insights into autophagosome biogenesis revealed by cryo‐electron tomography
inferred← citeshttps://doi.org/10.1002/1873-3468.14742openalex-snapshot
Structural view on autophagosome formation
inferred← citeshttps://doi.org/10.1002/cbic.202500432openalex-snapshot
Artificial Peptides as Autophagy Modulators
inferred← citeshttps://doi.org/10.1002/mco2.150openalex-snapshot
Autophagy in health and disease: From molecular mechanisms to therapeutic target
inferred← citeshttps://doi.org/10.1007/s00018-020-03621-9openalex-snapshot
The crystal structure of Atg18 reveals a new binding site for Atg2 in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1007/s12374-020-09252-8openalex-snapshot
Birth, Growth, Maturation, and Demise of Plant Autophagic Vesicles
inferred← citeshttps://doi.org/10.1007/s13238-020-00793-9openalex-snapshot
Lipids and membrane-associated proteins in autophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-822003-0.00002-4openalex-snapshot
Autophagy on the road to longevity and aging
inferred← citeshttps://doi.org/10.1016/j.arr.2024.102404openalex-snapshot
Non-coding RNAs as regulators of autophagy in chondrocytes: Mechanisms and implications for osteoarthritis
inferred← citeshttps://doi.org/10.1016/j.bbalip.2020.158868openalex-snapshot
Lipid profiles of autophagic structures isolated from wild type and Atg2 mutant Drosophila
inferred← citeshttps://doi.org/10.1016/j.bbalip.2021.158956openalex-snapshot
Atg2 and Atg9: Intermembrane and interleaflet lipid transporters driving autophagy
inferred← citeshttps://doi.org/10.1016/j.bbrc.2026.153507openalex-snapshot
Muscle-specific expression of Atg2 and high-fat diet influence age-related deterioration of skeletal muscle in aged drosophila via the ATGL/Sirt1/PGC-1α pathway
inferred← citeshttps://doi.org/10.1016/j.bcp.2023.115576openalex-snapshot
A perspective on autophagy and transcription factor EB in Alcohol-Associated Alzheimer’s disease
inferred← citeshttps://doi.org/10.1016/j.ceb.2020.02.008openalex-snapshot
Inter-organelle lipid transfer: a channel model for Vps13 and chorein-N motif proteins
inferred← citeshttps://doi.org/10.1016/j.drudis.2024.104224openalex-snapshot
Highlighting roles of autophagy in human diseases: a perspective from single-cell RNA sequencing analyses
inferred← citeshttps://doi.org/10.1016/j.foodres.2025.117074openalex-snapshot
Ultrasonic regulation of β-lactoglobulin/puerarin complex: structural modification, digestive properties, and allergenicity suppression through controlled polyphenol interactions
inferred← citeshttps://doi.org/10.1016/j.fsi.2026.111593openalex-snapshot
Shrimp TM9SF4 facilitates WSSV infection probably through interacting with viral VP24 and regulating host autophagy
inferred← citeshttps://doi.org/10.1016/j.jmb.2024.168891openalex-snapshot
Phospholipid Transport Across the Bacterial Periplasm Through the Envelope-spanning Bridge YhdP
inferred← citeshttps://doi.org/10.1016/j.jmb.2025.169235openalex-snapshot
Structural Insights into Autophagy in the AlphaFold Era
inferred← citeshttps://doi.org/10.1016/j.molcel.2026.03.002openalex-snapshot
Mechanosensory channels mediate ER Ca2+ transients to trigger assembly of autophagosome initiation sites for degradation of ER subdomains
inferred← citeshttps://doi.org/10.1038/s41431-021-00872-3openalex-snapshot
Whole exome sequencing reveals putatively novel associations in retinopathies and drusen formation
inferred← citeshttps://doi.org/10.1038/s41556-024-01359-1openalex-snapshot
WIPI4 loss linked to ferroptosis
inferred← citeshttps://doi.org/10.1042/bst20200130openalex-snapshot
In vitro reconstitution of autophagic processes
inferred← citeshttps://doi.org/10.1073/pnas.2209823119openalex-snapshot
In situ structural analysis reveals membrane shape transitions during autophagosome formation
inferred← citeshttps://doi.org/10.1073/pnas.2221712120openalex-snapshot
In situ snapshots along a mammalian selective autophagy pathway
inferred← citeshttps://doi.org/10.1080/13813455.2024.2388779openalex-snapshot
Growth, fusion and degradation of lipid droplets: advances in lipid droplet regulatory protein
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/10.1080/15548627.2021.1935522openalex-snapshot
TOR and MAP kinase pathways synergistically regulate autophagy in response to nutrient depletion in fission yeast
inferred← citeshttps://doi.org/10.1080/15548627.2021.1965711openalex-snapshot
Global Proximity Interactome of the Human Macroautophagy Pathway
inferred← citeshttps://doi.org/10.1080/15548627.2023.2238578openalex-snapshot
AI-based AlphaFold2 significantly expands the structural space of the autophagy pathway
inferred← citeshttps://doi.org/10.1083/jcb.202104073openalex-snapshot
Vps13D functions in a Pink1-dependent and Parkin-independent mitophagy pathway
inferred← citeshttps://doi.org/10.1091/mbc.e24-05-0236openalex-snapshot
Proviral role of ATG2 autophagy related protein in tomato bushy stunt virus replication through bulk phospholipid transfer into the viral replication organelle
inferred← citeshttps://doi.org/10.1101/2023.10.05.561070openalex-snapshot
Phospholipid transport to the bacterial outer membrane through an envelope-spanning bridge
inferred← citeshttps://doi.org/10.1101/2023.11.06.565932openalex-snapshot
Tweek-dependent formation of ER-PM contact sites enables astrocyte phagocytic function and remodeling of neurons
inferred← citeshttps://doi.org/10.1101/2024.12.09.627529openalex-snapshot
ATG16L1 WD domain regulates lipid trafficking to maintain plasma membrane integrity to limit influenza virus infection
inferred← citeshttps://doi.org/10.1111/febs.16018openalex-snapshot
Autophagy in the retinal pigment epithelium: a new vision and future challenges
inferred← citeshttps://doi.org/10.1111/febs.16280openalex-snapshot
ATG2 and VPS13 proteins: molecular highways transporting lipids to drive membrane expansion and organelle communication
inferred← citeshttps://doi.org/10.1111/febs.17288openalex-snapshot
Atg2 controls Drosophila hematopoiesis through the PVR / TOR signaling pathways
inferred← citeshttps://doi.org/10.1111/gtc.12733openalex-snapshot
Human ATG2B possesses a lipid transfer activity which is accelerated by negatively charged lipids and WIPI4
inferred← citeshttps://doi.org/10.1128/spectrum.01301-23openalex-snapshot
The plant pathogenic bacterium Candidatus Liberibacter solanacearum induces calcium-regulated autophagy in midgut cells of its insect vector Bactericera trigonica
inferred← citeshttps://doi.org/10.1136/egastro-2023-100057openalex-snapshot
Recent insights about autophagy in pancreatitis
inferred← citeshttps://doi.org/10.1177/25152564221134328openalex-snapshot
Sequence Analysis and Structural Predictions of Lipid Transfer Bridges in the Repeating Beta Groove (RBG) Superfamily Reveal Past and Present Domain Variations Affecting Form, Function and Interactions of VPS13, ATG2, SHIP164, Hobbit and Tweek
inferred← citeshttps://doi.org/10.1177/25152564231183898openalex-snapshot
The Organization and Function of the Phagophore-ER Membrane Contact Sites
inferred← citeshttps://doi.org/10.1186/s12915-021-01183-1openalex-snapshot
Functional analyses of phosphatidylserine/PI(4)P exchangers with diverse lipid species and membrane contexts reveal unanticipated rules on lipid transfer
inferred← citeshttps://doi.org/10.1186/s12935-025-03957-xopenalex-snapshot
Crosstalk between noncoding RNAs and autophagy in renal cell carcinoma: Deciphering molecular pathways and therapeutic prospects
inferred← citeshttps://doi.org/10.1186/s13578-020-00467-3openalex-snapshot
Autophagy and its role in regeneration and remodeling within invertebrate
inferred← citeshttps://doi.org/10.1387/ijdb.190186leopenalex-snapshot
Dictyostelium discoideum and autophagy – a perfect pair
inferred← citeshttps://doi.org/10.2183/pjab.101.005openalex-snapshot
Mechanisms of autophagosome formation
inferred← citeshttps://doi.org/10.3389/fcell.2021.784367openalex-snapshot
Mechanisms of Non-Vesicular Exchange of Lipids at Membrane Contact Sites: Of Shuttles, Tunnels and, Funnels
inferred← citeshttps://doi.org/10.3389/fcell.2025.1551003openalex-snapshot
Ferritinophagy: multifaceted roles and potential therapeutic strategies in liver diseases
inferred← citeshttps://doi.org/10.3389/fcell.2026.1776289openalex-snapshot
Autophagy: mechanisms, roles in human diseases, and therapeutic perspectives
inferred← citeshttps://doi.org/10.3389/fpls.2020.00477openalex-snapshot
Membrane Contact Sites and Organelles Interaction in Plant Autophagy
inferred← citeshttps://doi.org/10.3390/antiox14060662openalex-snapshot
MAPK Signaling in the Interplay Between Oxidative Stress and Autophagy
inferred← citeshttps://doi.org/10.3390/cells11050871openalex-snapshot
The Interplay between Autophagy and Virus Pathogenesis—The Significance of Autophagy in Viral Hepatitis and Viral Hemorrhagic Fevers
inferred← citeshttps://doi.org/10.3390/cells12081132openalex-snapshot
Membrane Curvature: The Inseparable Companion of Autophagy
inferred← citeshttps://doi.org/10.3390/ijms21218196openalex-snapshot
Pathogenic Single Nucleotide Polymorphisms on Autophagy-Related Genes
inferred← citeshttps://doi.org/10.3390/ijms21238974openalex-snapshot
Autophagy and Autophagy-Related Diseases: A Review
inferred← citeshttps://doi.org/10.3390/ijms232314997openalex-snapshot
Neuroinflammation and Autophagy in Parkinson’s Disease—Novel Perspectives
inferred← citeshttps://doi.org/10.3390/jof11050391openalex-snapshot
Autophagy-Related Proteins (ATGs) Are Differentially Required for Development and Virulence of Sclerotinia sclerotiorum
inferred← citeshttps://doi.org/10.4062/biomolther.2024.094openalex-snapshot
Regulatory Mechanisms Governing the Autophagy-Initiating VPS34 Complex and Its inhibitors
inferred← citeshttps://doi.org/10.53846/goediss-9145openalex-snapshot
HORMA domain proteins in Autophagy initiation
inferred← citeshttps://doi.org/10.5772/intechopen.89683openalex-snapshot
Intracellular Lipid Homeostasis and Trafficking in Autophagy
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.