Evidence map›Paper›PMID 30791644›Full record

ArticleInternational journal of molecular sciences2019

Covalently Linking Oligomerization-Impaired GlpF Protomers Does Not Completely Re-establish Wild-Type Channel Activity.

Noreen Klein, Margareta Trefz, Dirk Schneider

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. 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
0.3field-weighted citation impact, top 42% 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. Article
  2. Review
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

3 authors at 1 institution in 1 country.

Noreen KleinJohannes Gutenberg-University Mainz, Institute of Pharmacy and Biochemistry, Johann-Joachim-Becher-Weg 30, 55128 Mainz, Germany. noreen-klein@freenet.de.
Margareta TrefzJohannes Gutenberg-University Mainz, Institute of Pharmacy and Biochemistry, Johann-Joachim-Becher-Weg 30, 55128 Mainz, Germany. martrefz@uni-mainz.de.
Dirk SchneiderJohannes Gutenberg-University Mainz, Institute of Pharmacy and Biochemistry, Johann-Joachim-Becher-Weg 30, 55128 Mainz, Germany. dirk.schneider@uni-mainz.de.ORCID 0000-0003-4517-6387
Johannes Gutenberg University Mainz · DE

Funding

German Chemical Industry fund N/AResearch Center for Complex Materials (COMATT) N/AStiftung Rheinland-Pfalz für Innovation N/A
6 · The paper itself

Abstract

Integral membrane proteins of the aquaporin family facilitate rapid water flux across cellular membranes in all domains of life. Although the water-conducting pore is clearly defined in an aquaporin monomer, all aquaporins assemble into stable tetramers. In order to investigate the role of protomer⁻protomer interactions, we analyzed the activity of heterotetramers containing increasing fractions of mutated monomers, which have an impaired oligomerization propensity and activity. In order to enforce interaction between the protomers, we designed and analyzed a genetically fused homotetramer of GlpF, the aquaglyceroporin of the bacterium

Indexed as

Protein MultimerizationAquaporinsBacterial Outer Membrane ProteinsBiological TransportCloning, MolecularEscherichia coli ProteinsGene ExpressionMutationRecombinant Fusion ProteinsStructure-Activity RelationshipAquaporinsBacterial Outer Membrane ProteinsEscherichia coli ProteinsGlpF protein, E coliRecombinant Fusion Proteinsaquaglyceroporincovalent linkageGlpFhomooligomerinteractionmembrane proteinprotein foldingtetramer

Identifiers

PMID30791644
PMCPMC6412381
OpenAlexW2915743405

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.