Evidence map›Paper›PMID 36775935›Full record

ArticleProtein science : a publication of the Protein Society2023

FkpA enhances membrane protein folding using an extensive interaction surface.

Taylor Devlin, Dagan C Marx, Michaela A Roskopf, Quenton R Bubb, Ashlee M Plummer, Karen G Fleming

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.2field-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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. FkpA enhances membrane protein folding using an extensive interaction surface.Protein science : a publication of the Protein Society · 2023
    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

6 authors at 1 institution in 1 country.

Taylor DevlinT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland, USA.
Dagan C MarxT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland, USA.
Michaela A RoskopfT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland, USA.
Quenton R BubbT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland, USA.
Ashlee M PlummerT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland, USA.
Karen G FlemingT.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland, USA.ORCID 0000-0001-5417-8830
Johns Hopkins University · US

Funding

PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
NIGMS NIH HHS T32 GM008403NIGMS NIH HHS T32-GM008403
6 · The paper itself

Abstract

Outer membrane protein (OMP) biogenesis in gram-negative bacteria is managed by a network of periplasmic chaperones that includes SurA, Skp, and FkpA. These chaperones bind unfolded OMPs (uOMPs) in dynamic conformational ensembles to suppress aggregation, facilitate diffusion across the periplasm, and enhance folding. FkpA primarily responds to heat-shock stress, but its mechanism is comparatively understudied. To determine FkpA chaperone function in the context of OMP folding, we monitored the folding of three OMPs and found that FkpA, unlike other periplasmic chaperones, increases the folded yield but decreases the folding rate of OMPs. The results indicate that FkpA behaves as a chaperone and not as a folding catalyst to influence the OMP folding trajectory. Consistent with the folding assay results, FkpA binds all three uOMPs as determined by sedimentation velocity (SV) and photo-crosslinking experiments. We determine the binding affinity between FkpA and uOmpA

Indexed as

Carrier ProteinsEscherichia coli ProteinsBacterial Outer Membrane ProteinsEscherichia coliHumansMolecular ChaperonesPeptidylprolyl IsomerasePeriplasmProtein FoldingBacterial Outer Membrane ProteinsCarrier ProteinsEscherichia coli ProteinsMolecular ChaperonesPeptidylprolyl IsomeraseFkpAmembrane protein foldingouter membrane proteinouter membrane protein biogenesisperiplasmic chaperonephoto-crosslinkingsedimentation velocity

Identifiers

PMID36775935
PMCPMC10031210
OpenAlexW4320490313

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.