Evidence map›Paper›PMID 27920276›Full record

ArticleBioscience reports2017

Studies of recombinant TWA1 reveal constitutive dimerization.

Ore Francis, Genevieve E Baker, Paul R Race, Josephine C Adams

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.0field-weighted citation impact, top 21% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Gid10 as an alternative N-recognin of the Pro/N-degron pathway.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  2. Review
  3. 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

4 authors at 1 institution in 1 country.

Ore FrancisSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, U.K.
Genevieve E BakerSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, U.K.
Paul R RaceSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, U.K.
Josephine C AdamsSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, U.K. jo.adams@bristol.ac.uk.
University of Bristol · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J014400/1Biotechnology and Biological Sciences Research Council BB/L01386X/1
6 · The paper itself

Abstract

The mammalian muskelin/RanBP9/C-terminal to LisH (CTLH) complex and the Saccharomyces cerevisiae glucose-induced degradation (GID) complex are large, multi-protein complexes that each contain a RING E3 ubiquitin ligase. The yeast GID complex acts to degrade a key enzyme of gluconeogenesis, fructose 1,6-bisphosphatase, under conditions of abundant fermentable carbon sources. However, the assembly and functions of the mammalian complex remain poorly understood. A striking feature of these complexes is the presence of multiple proteins that contain contiguous lissencephaly-1 homology (LisH), CTLH and C-terminal CT11-RanBP9 (CRA) domains. TWA1/Gid8, the smallest constituent protein of these complexes, consists only of LisH, CTLH and CRA domains and is highly conserved in eukaryotes. Towards better knowledge of the role of TWA1 in these multi-protein complexes, we established a method for bacterial expression and purification of mouse TWA1 that yields tag-free, recombinant TWA1 in quantities suitable for biophysical and biochemical studies. CD spectroscopy of recombinant TWA1 indicated a predominantly α-helical protein. Gel filtration chromatography, size-exclusion chromatography (SEC) with multi-angle light scattering (SEC-MALS) and native PAGE demonstrated a propensity of untagged TWA1 to form stable dimers and, to a lesser extent, higher order oligomers. TWA1 has a single cysteine residue, Cys

Indexed as

Protein MultimerizationAnimalsCircular DichroismCloning, MolecularEscherichia coliMiceProtein Conformation, alpha-HelicalProtein DomainsProteinsRecombinant ProteinsProteinsRecombinant ProteinsTwa1 protein, mouseCTLHLisHprotein purificationTWA1Ubiquitin

Identifiers

PMID27920276
PMCPMC5234100
OpenAlexW2560820847

What OpenQuestion holds

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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.