Evidence map›Paper›PMID 26311849›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

In situ structural analysis of Golgi intracisternal protein arrays.

Benjamin D Engel, Miroslava Schaffer, Sahradha Albert, Shoh Asano, Jürgen M Plitzko, Wolfgang Baumeister

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

45 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
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  4. Structural glycobiology - from enzymes to organelles.Biochemical Society transactions · 2025
    Review
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  10. PreparingFrontiers in plant science · 2023
    Article
  11. Article
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  13. Review
  14. Imaging Cytoskeleton Components by Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  15. Intracellular nanoscale architecture as a master regulator of calcium carbonate crystallization in marine microalgae.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Review
  17. Article
  18. Article
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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

6 authors at 1 institution in 1 country.

Benjamin D EngelDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany baumeist@biochem.mpg.de engelben@biochem.mpg.de.
Miroslava SchafferDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
Sahradha AlbertDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
Shoh AsanoDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
Jürgen M PlitzkoDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
Wolfgang BaumeisterDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany baumeist@biochem.mpg.de engelben@biochem.mpg.de.
Max Planck Institute of Biochemistry · DE

Funding

European Research Council 318987
6 · The paper itself

Abstract

We acquired molecular-resolution structures of the Golgi within its native cellular environment. Vitreous Chlamydomonas cells were thinned by cryo-focused ion beam milling and then visualized by cryo-electron tomography. These tomograms revealed structures within the Golgi cisternae that have not been seen before. Narrow trans-Golgi lumina were spanned by asymmetric membrane-associated protein arrays that had ∼6-nm lateral periodicity. Subtomogram averaging showed that the arrays may determine the narrow central spacing of the trans-Golgi cisternae through zipper-like interactions, thereby forcing cargo to the trans-Golgi periphery. Additionally, we observed dense granular aggregates within cisternae and intracisternal filament bundles associated with trans-Golgi buds. These native in situ structures provide new molecular insights into Golgi architecture and function.

Indexed as

Algal ProteinsChlamydomonas reinhardtiiCryoelectron MicroscopyElectron Microscope TomographyGolgi ApparatusMembrane ProteinsModels, AnatomicModels, BiologicalProtein Transporttrans-Golgi NetworkAlgal ProteinsMembrane ProteinsChlamydomonascryo-electron tomographyfocused ion beamglycosyltransferaseGolgi

Identifiers

PMID26311849
PMCPMC4568700
OpenAlexW1855243629

What OpenQuestion holds

Textmetadata
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.