Evidence map›Paper›PMID 37150040›Full record

ReviewCurrent opinion in structural biology2023

Structure and function of lipid droplet assembly complexes.

Tobias C Walther, Siyoung Kim, Henning Arlt, Gregory A Voth, Robert V Farese

Open access · hybridAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
9.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
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  9. Review
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  15. Article
  16. Review
  17. Lipid droplets and cellular lipid flux.Nature cell biology · 2024
    Review
  18. Review
  19. Article
  20. The Vacuole Lipid Droplet Contact Site vCLIP.Contact (Thousand Oaks (Ventura County, Calif.))
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 1 country.

Tobias C WaltherCell Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, 10065, USA; Howard Hughes Medical Institute, New York, NY 10065, USA. Electronic address: twalther@mskcc.org.
Siyoung KimPritzker School of Molecular Engineering, University of Chicago, Chicago, IL, 60637, USA.
Henning ArltHoward Hughes Medical Institute, New York, NY 10065, USA.
Gregory A VothDepartment of Chemistry, Chicago Center for Theoretical Chemistry, James Franck Institute, and Institute for Biophysical Dynamics, University of Chicago, Chicago, IL, 60637, USA.
Robert V FareseCell Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, 10065, USA.
Memorial Sloan Kettering Cancer Center · USChicago Institute for Psychoanalysis · USHoward Hughes Medical Institute · USUniversity of Chicago · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
New Method for Biomembrane SimulationsR01GM063796 · NIGMS · UNIVERSITY OF UTAH · PI VOTH, GREGORY A. · 2001 to 2025
$6.3M
Mechanisms of Lipid Droplet FormationR01GM124348 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI FARESE, ROBERT V · 2017 to 2024
$2.9M
NCI NIH HHS P30 CA008748NIGMS NIH HHS R01 GM063796NIGMS NIH HHS R01 GM124348
6 · The paper itself

Abstract

Cells store lipids as a reservoir of metabolic energy and membrane component precursors in organelles called lipid droplets (LDs). LD formation occurs in the endoplasmic reticulum (ER) at LD assembly complexes (LDAC), consisting of an oligomeric core of seipin and accessory proteins. LDACs determine the sites of LD formation and are required for this process to occur normally. Seipin oligomers form a cage-like structure in the membrane that may serve to facilitate the phase transition of neutral lipids in the membrane to form an oil droplet within the LDAC. Modeling suggests that, as the LD grows, seipin anchors it to the ER bilayer and conformational shifts of seipin transmembrane segments open the LDAC dome toward the cytoplasm, enabling the emerging LD to egress from the ER.

Indexed as

Lipid DropletsProteinsEndoplasmic ReticulumLipid MetabolismLipidsLipidsProteinsEndoplasmic reticulumLipid dropletPhase separationPhospholipidsSeipinSterol estersSurface tensionTriacylglycerol

Identifiers

PMID37150040
PMCPMC10853036
OpenAlexW4372211501

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.