Evidence map›Paper›PMID 33641207›Full record

ArticleProtein science : a publication of the Protein Society2021

Structural characterization of the self-association domain of swallow.

Nikolaus M Loening, Elisar Barbar

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 52% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Exploration of the interaction between dynein intermediate chain and dynactin p150Protein science : a publication of the Protein Society · 2025
    Article
  2. Structural characterization of the self-association domain of swallow.Protein science : a publication of the Protein Society · 2021
    Article
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

2 authors at 2 institutions in 1 country.

Nikolaus M LoeningDepartment of Chemistry, Lewis & Clark College, Portland, Oregon, USA.ORCID 0000-0002-5074-6906
Elisar BarbarDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon, USA.ORCID 0000-0003-4892-5259
Lewis & Clark College · USOregon State University · US

Funding

Acquisition of a 700 MHz NMR SpectrometerS10OD018518 · OD · OREGON STATE UNIVERSITY · PI BARBAR, ELISAR J · 2015 to 2015
$1.3M
NIH HHS S10 OD018518
6 · The paper itself

Abstract

Swallow, a 62 kDa multidomain protein, is required for the proper localization of several mRNAs involved in the development of Drosophila oocytes. The dimerization of Swallow depends on a 71-residue self-association domain in the center of the protein sequence, and is significantly stabilized by a binding interaction with dynein light chain (LC8). Here, we detail the use of solution-state nuclear magnetic resonance spectroscopy to characterize the structure of this self-association domain, thereby establishing that this domain forms a parallel coiled-coil and providing insight into how the stability of the dimerization interaction is regulated.

Indexed as

Protein MultimerizationAnimalsDrosophila melanogasterDrosophila ProteinsProtein DomainsRNA-Binding ProteinsDrosophila ProteinsRNA-Binding Proteinsswa protein, Drosophilacoiled-coildimerprotein structureself-association domainsolution-state NMR spectroscopy

Identifiers

PMID33641207
PMCPMC8040862
OpenAlexW3135021463

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.