Evidence map›Paper›PMID 20479883›Full record

ArticlePloS one2010

RETRACTED: Molecular structure and dimeric organization of the Notch extracellular domain as revealed by electron microscopy.

Deborah F Kelly, Robert J Lake, Teije C Middelkoop, Hua-Ying Fan, Spyros Artavanis-Tsakonas, Thomas Walz

RetractedOpen access · goldAbstract readRetracted Publication
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

27 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
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  9. Notch-Jagged signaling complex defined by an interaction mosaic.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  11. Review
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  18. Review
  19. The Mechanism of Regulated Release of Lasso/Teneurin-2.Frontiers in molecular neuroscience · 2016
    Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Deborah F KellyDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, United States of America.
Robert J Lake
Teije C Middelkoop
Hua-Ying Fan
Spyros Artavanis-Tsakonas
Thomas Walz
Harvard University · USFox Chase Cancer Center · US

Funding

Single particle reconstructionP01GM062580 · NIGMS · HARVARD MEDICAL SCHOOL · PI HARRISON, STEPHEN COPLAN · 2001 to 2016
$23.7M
Cell Interactions Controlling Neural DifferentiationR37NS026084 · NINDS · MASSACHUSETTS GENERAL HOSPITAL · PI ARTAVANIS-TSAKONAS, SPYRIDON · 2004 to 2010
$4.2M
Notch Signaling in Mammary Development and TumorigenesisR01CA098402 · NCI · MASSACHUSETTS GENERAL HOSPITAL · PI ARTAVANIS-TSAKONAS, SPYRIDON · 2003 to 2013
$3.6M
Basis for Distinct Functions of ATP-Dependent Chromatin Remodeling ComplexesR01GM084983 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI FAN, HUA-YING · 2008 to 2012
$1.6M
CELL INTERACTIONS CONTROLLING NEURAL DIFFERENTIATIONR01NS026084 · NINDS · YALE UNIVERSITY · PI ARTAVANIS-TSAKONAS, SPYRIDON · 1988 to 2003
$839k
Howard Hughes Medical InstituteNCI NIH HHS CA098402NCI NIH HHS R01 CA098402NIGMS NIH HHS GM062580NIGMS NIH HHS P01 GM062580NIGMS NIH HHS R01 GM084983NINDS NIH HHS NS26084NINDS NIH HHS R01 NS026084NINDS NIH HHS R37 NS026084
6 · The paper itself

Abstract

backgroundThe Notch receptor links cell fate decisions of one cell to that of the immediate cellular neighbor. In humans, malfunction of Notch signaling results in diseases and congenital disorders. Structural information is essential for gaining insight into the mechanism of the receptor as well as for potentially interfering with its function for therapeutic purposes. METHODOLOGY/PRINCIPAL

findingsWe used the Affinity Grid approach to prepare specimens of the Notch extracellular domain (NECD) of the Drosophila Notch and human Notch1 receptors suitable for analysis by electron microscopy and three-dimensional (3D) image reconstruction. The resulting 3D density maps reveal that the NECD structure is conserved across species. We show that the NECD forms a dimer and adopts different yet defined conformations, and we identify the membrane-proximal region of the receptor and its ligand-binding site. CONCLUSIONS/SIGNIFICANCE: Our results provide direct and unambiguous evidence that the NECD forms a dimer. Our studies further show that the NECD adopts at least three distinct conformations that are likely related to different functional states of the receptor. These findings open the way to now correlate mutations in the NECD with its oligomeric state and conformation.

Indexed as

Protein MultimerizationAnimalsDrosophila melanogasterExtracellular SpaceHumansMicroscopy, ElectronProtein Structure, TertiaryReceptors, NotchReceptors, Notch

Identifiers

PMID20479883
PMCPMC2866536
OpenAlexW1991443973

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.