Evidence map›Paper›PMID 32614588›Full record

ArticleJournal of the American Chemical Society2020

Transmembrane Epitope Delivery by Passive Protein Threading through the Pores of the OmpF Porin Trimer.

Sejeong Lee, Nicholas G Housden, Sandra A Ionescu, Matthew H Zimmer, Renata Kaminska, Colin Kleanthous, Hagan Bayley

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
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

8 citing papers in PubMed.

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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

7 authors.

Sejeong LeeChemistry Research Laboratory, University of Oxford, Oxford OX1 3TA, U.K.ORCID 0000-0001-8617-3436
Nicholas G HousdenDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, U.K.ORCID 0000-0002-4706-8278
Sandra A IonescuChemistry Research Laboratory, University of Oxford, Oxford OX1 3TA, U.K.
Matthew H ZimmerChemistry Research Laboratory, University of Oxford, Oxford OX1 3TA, U.K.
Renata KaminskaDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, U.K.
Colin KleanthousDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, U.K.
Hagan BayleyChemistry Research Laboratory, University of Oxford, Oxford OX1 3TA, U.K.ORCID 0000-0003-2499-6116

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trimeric porins in the outer membrane (OM) of Gram-negative bacteria are the conduits by which nutrients and antibiotics diffuse passively into cells. The narrow gateways that porins form in the OM are also exploited by bacteriocins to translocate into cells by a poorly understood process. Here, using single-channel electrical recording in planar lipid bilayers in conjunction with protein engineering, we explicate the mechanism by which the intrinsically unstructured N-terminal translocation domain (IUTD) of the endonuclease bacteriocin ColE9 is imported passively across the

Indexed as

EpitopesPorinsEpitopesOmpF proteinPorins

Identifiers

PMID32614588
PMCPMC7366379

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.