Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers.

Jayneil R Patel, Yingqi Xu, Claudia Capitini, Fabrizio Chiti, Alfonso De Simone

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Article in Biomolecular NMR assignments, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

0.1field-weighted citation impact, top 49% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

5 authors at 2 institutions in 2 countries.

Jayneil R PatelDepartment of Life Sciences, Imperial College London, South Kensington, London, SW72AZ, UK.

Yingqi XuDepartment of Life Sciences, Imperial College London, South Kensington, London, SW72AZ, UK.

Claudia CapitiniSection of Biochemistry, Department of Experimental and Clinical Biomedical Sciences, University of Florence, Viale Morgagni 50, 50134, Firenze, Italy.

Fabrizio ChitiSection of Biochemistry, Department of Experimental and Clinical Biomedical Sciences, University of Florence, Viale Morgagni 50, 50134, Firenze, Italy.

Alfonso De SimoneDepartment of Life Sciences, Imperial College London, South Kensington, London, SW72AZ, UK. adesimon@imperial.ac.uk.

Imperial College London · GBUniversity of Florence · IT

Funding

Biotechnology and Biological Sciences Research Council BB/M023923/1Wellcome TrustWellcome Trust 104933/Z/14/Z

6 · The paper itself

Abstract

The HypF protein is involved in the maturation and regulation of hydrogenases. The N-terminal domain of HypF (HypF-N) has served as a key model system to study the pathways of protein amyloid formation and the nature of the toxicity of pre-fibrilar protein oligomers. This domain can aggregate into two forms of oligomers having significantly different toxic effects when added to neuronal cultures. Here, NMR assignments of HypF-N backbone resonances are presented in its native state and under the conditions favouring the formation of toxic and non-toxic oligomers. The analyses of chemical shifts provide insights into the protein conformational state and the possible pathways leading to the formation of different types of oligomers.

Indexed as

Nuclear Magnetic Resonance, BiomolecularProtein MultimerizationBacterial ProteinsProtein DomainsProtein Structure, QuaternaryBacterial ProteinsHypF protein, BacteriaAmyloidsBiomolecular NMRHypF-NProtein assignmentProtein oligomers

Identifiers

PMID29786756

DOI10.1007/s12104-018-9822-7

PMCPMC6132818

OpenAlexW2805003316

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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.