Evidence map›Paper›PMID 15774580›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography.

Friedrich Förster, Ohad Medalia, Nathan Zauberman, Wolfgang Baumeister, Deborah Fass

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 163 papers.

0numbers the graph read from it
0cells of the map it votes in
163citing papers in PubMed
7.4field-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

163 citing papers in PubMed, 317 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Structure and organization of full-length epidermal growth factor receptor in extracellular vesicles by cryo-electron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  15. Interdigitated immunoglobulin arrays form the hyperstable surface layer of the extremophilic bacteriumProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Computational methods forFrontiers in cellular and infection microbiology · 2023
    Review
  17. Review
  18. Article
  19. Article
  20. Article

103 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Friedrich FörsterAbteilung für Molekulare Strukturbiologie, Max-Planck-Institut für Biochemie, Am Klopferspitz 18, D-82152 Martinsried, Germany. foerster@biochem.mpg.de
Ohad Medalia
Nathan Zauberman
Wolfgang Baumeister
Deborah Fass
Weizmann Institute of Science · ILMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We used cryo-electron tomography in conjunction with single-particle averaging techniques to study the structures of frozen-hydrated envelope glycoprotein (Env) complexes on intact Moloney murine leukemia retrovirus particles. Cryo-electron tomography allows 3D imaging of viruses in toto at a resolution sufficient to locate individual macromolecules, and local averaging of abundant complexes substantially improves the resolution. The averaging of repetitive features in electron tomograms is hampered by a low signal-to-noise ratio and anisotropic resolution, which results from the "missing-wedge" effect. We developed an iterative 3D averaging algorithm that compensates for this effect and used it to determine the trimeric structure of Env to a resolution of 2.7 nm, at which individual domains can be resolved. Strikingly, the 3D reconstruction is shaped like a tripod in which the trimer penetrates the membrane at three distinct locations approximately 4.5 nm apart from one another. The Env reconstruction allows tentative docking of the x-ray crystal structure of the receptor-binding domain. This study thus provides 3D structural information regarding the prefusion conformation of an intact unstained retrovirus surface protein.

Indexed as

AlgorithmsCryoelectron MicroscopyImage Processing, Computer-AssistedMoloney murine leukemia virusProtein ConformationTomographyViral Envelope ProteinsViral Envelope Proteins

Identifiers

PMID15774580
PMCPMC555690
OpenAlexW2046542456

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.