Evidence map›Paper›PMID 23925141›Full record

ReviewToxins2013

pH-triggered conformational switching along the membrane insertion pathway of the diphtheria toxin T-domain.

Alexey S Ladokhin

Open access · goldAbstract readReview
In one paragraph

Review in Toxins, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

41 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Review
  3. Membrane Pore Formation by Peptides Studied by Fluorescence Techniques.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
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  7. Review
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  16. Review
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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

1 author at 1 institution in 1 country.

Alexey S LadokhinDepartment of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, KS 66160, USA. aladokhin@kumc.edu
University of Kansas Medical Center · US

Funding

pH-Triggered Membrane Insertion of ProteinsR01GM069783 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI COCCO, MELANIE J, KURNIKOVA, MARIA G · 2004 to 2014
$2.5M
NIGMS NIH HHS GM069783NIGMS NIH HHS R01 GM069783
6 · The paper itself

Abstract

The translocation (T)-domain plays a key role in the action of diphtheria toxin and is responsible for transferring the catalytic domain across the endosomal membrane into the cytosol in response to acidification. Deciphering the molecular mechanism of pH-dependent refolding and membrane insertion of the T-domain, which is considered to be a paradigm for cell entry of other bacterial toxins, reveals general physicochemical principles underlying membrane protein assembly and signaling on membrane interfaces. Structure-function studies along the T-domain insertion pathway have been affected by the presence of multiple conformations at the same time, which hinders the application of high-resolution structural techniques. Here, we review recent progress in structural, functional and thermodynamic studies of the T-domain archived using a combination of site-selective fluorescence labeling with an array of spectroscopic techniques and computer simulations. We also discuss the principles of conformational switching along the insertion pathway revealed by studies of a series of T-domain mutants with substitutions of histidine residues.

Indexed as

Catalytic DomainChemical PhenomenaCytosolDiphtheria ToxinHistidineHumansHydrogen-Ion ConcentrationMembrane ProteinsProtein TransportDiphtheria ToxinHistidineMembrane Proteins

Identifiers

PMID23925141
PMCPMC3760040
OpenAlexW2004071573

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.