Genetically encoded photochemical covalent crosslinking within the Hcp-1 self-assembling bacterial secretion machinery.

Alicja K Antonczak, Kedric Milholland, Eric M Tippmann

Erratum issuedAbstract read

In one paragraph

Article in Amino acids, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

Erratum issued
Correction to: Genetically encoded photochemical covalent crosslinking within the Hcp-1 self-assembling bacterial secretion machinery.2019

5 · Who and what money

Authors and funding

3 authors.

Alicja K AntonczakDepartment of Chemistry, Indiana-Purdue University, Fort Wayne, IN, 46805, USA.

Kedric MilhollandDepartment of Chemistry, Indiana-Purdue University, Fort Wayne, IN, 46805, USA.

Eric M TippmannDepartment of Chemistry, Indiana-Purdue University, Fort Wayne, IN, 46805, USA. tippmane@ipfw.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The target protein, Hcp1, was first described as part of the bacterial Type VI secretion system from Pseudomonas aeruginosa. The protein first self-assembles into a hexamer and then the hexamers further stack into a nanotubular structure. Hcp1 monomers were targeted for mutagenesis with two widely used photoactivatable amino acids: para-benzoyl phenylalanine or para-azidophenylalanine. The ability of these amino acids to form covalent adducts within the Hcp1 self-assembled system was investigated. Multiple residues, putatively of equal distance between the monomer-monomer interface were targeted. The efficiency of each amino acid to covalently link self-assembled hexamers was determined. The results demonstrate the choice and role of genetically encoded tools applied to complicated biological processes such as self-assembly and also suggested some structural dynamics of the Hcp-1 protein not obvious from crystallographic structures.

Indexed as

LightPhotochemical ProcessesBacterial ProteinsCross-Linking ReagentsPseudomonas aeruginosaType IV Secretion SystemsBacterial ProteinsCross-Linking ReagentsType IV Secretion SystemsNoncanonical amino acidsPhotochemistrySelf-assembly

Identifiers

PMID29307074

DOI10.1038/nature17182

What OpenQuestion holds

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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.