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Architecture of Lipid Droplets in Endoplasmic Reticulum Is Determined by Phospholipid Intrinsic Curvature
49/49 checkable references clean · checked 2026-07-23
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
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The 49 checked references that resolve
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Lipid droplet–organelle interactions: emerging roles in lipid metabolism
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Biogenesis of the multifunctional lipid droplet: Lipids, proteins, and sites
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ER Membrane Phospholipids and Surface Tension Control Cellular Lipid Droplet Formation
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The yeast lipin orthologue Pah1p is important for biogenesis of lipid droplets
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Diacylglycerol Enrichment of Endoplasmic Reticulum or Lipid Droplets Recruits Perilipin 3/TIP47 during Lipid Storage and Mobilization
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Acyl-CoA synthetase 3 promotes lipid droplet biogenesis in ER microdomains
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A conserved family of proteins facilitates nascent lipid droplet budding from the ER
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Form Follows Function: The Importance of Endoplasmic Reticulum Shape
resolves10.1515/znc-1973-11-1209
Elastic Properties of Lipid Bilayers: Theory and Possible Experiments
resolves10.1242/jcs.076836
Lipid droplets are functionally connected to the endoplasmic reticulum in <i>Saccharomyces cerevisiae</i>
resolves10.1194/jlr.R024117
The proteomics of lipid droplets: structure, dynamics, and functions of the organelle conserved from bacteria to humans
resolves10.1073/pnas.1110817108
Direct binding of triglyceride to fat storage-inducing transmembrane proteins 1 and 2 is important for lipid droplet formation
resolves10.1038/sj.emboj.7600672
The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth
resolves10.1016/j.bbalip.2011.07.015
Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: Lipidome meets Proteome
resolves10.1074/jbc.M802903200
An Unconventional Diacylglycerol Kinase That Regulates Phospholipid Synthesis and Nuclear Membrane Growth
resolves10.1111/j.1432-1033.1989.tb15109.x
Characterization of the methyltransferases in the yeast phosphatidylethanolamine methylation pathway by selective gene disruption
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Role of Diacylglycerol in PKD Recruitment to the TGN and Protein Transport to the Plasma Membrane
resolves10.1016/j.devcel.2011.09.005
A Highly Dynamic ER-Derived Phosphatidylinositol-Synthesizing Organelle Supplies Phosphoinositides to Cellular Membranes
resolves10.1093/emboj/20.21.5982
Recruitment of protein kinase D to the trans‐Golgi network via the first cysteine‐rich domain
resolves10.15698/mic2018.02.614
Fat storage-inducing transmembrane (FIT or FITM) proteins are related to lipid phosphatase/phosphotransferase enzymes
resolves10.1016/S0076-6879(85)11020-7
[18] Yeast sterols: Yeast mutants as tools for the study of sterol metabolism
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Global analysis of the yeast lipidome by quantitative shotgun mass spectrometry
resolves10.1016/j.devcel.2013.01.013
Triacylglycerol Synthesis Enzymes Mediate Lipid Droplet Growth by Relocalizing from the ER to Lipid Droplets
resolves10.1242/jcs.137737
Size control of lipid droplets in budding yeast requires a collaboration of Fld1 and Ldb16
resolves10.1371/journal.pone.0012811
Triglyceride Blisters in Lipid Bilayers: Implications for Lipid Droplet Biogenesis and the Mobile Lipid Signal in Cancer Cell Membranes
resolves10.1111/j.1600-0854.2012.01339.x
Lipid Droplet <i>De Novo</i> Formation and Fission Are Linked to the Cell Cycle in Fission Yeast
resolves10.1016/S0006-3495(94)81008-2
Structural dimensions and their changes in a reentrant hexagonal-lamellar transition of phospholipids
resolves10.1083/jcb.148.5.883
In Vitro Formation of the Endoplasmic Reticulum Occurs Independently of Microtubules by a Controlled Fusion Reaction
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Mechanisms Shaping the Membranes of Cellular Organelles
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Microtubules and the endoplasmic reticulum are highly interdependent structures.
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High-resolution mapping reveals topologically distinct cellular pools of phosphatidylserine
resolves10.7554/eLife.01607
Arf1/COPI machinery acts directly on lipid droplets and enables their connection to the ER for protein targeting
The 2 references without a DOI — listed, not checked
no DOI — not checked10.1016/j.cub.2018.02.020_bib37
no DOI — not checked10.1016/j.cub.2018.02.020_bib38
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