Identification of Acetylated Proteins in Borrelia burgdorferi.

Youyun Yang, Alan Wolfe, X Frank Yang

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

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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

1 citing paper in PubMed.

Global Profiling of Lysine Acetylation inFrontiers in microbiology · 2018
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

3 authors.

Youyun YangDepartment of Microbiology and Immunology, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, IN, 46202, USA.

Alan WolfeDepartment of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, Maywood, IL, USA.

X Frank YangDepartment of Microbiology and Immunology, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, IN, 46202, USA. xfyang@iupui.edu.

Funding

Regulatory Network of the Lyme Disease PathogenR01AI083640 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI X. Frank Yang · 2009 to 2026

$5.9M

NIAID NIH HHS R01 AI083640

6 · The paper itself

Abstract

Posttranslational modification (PTM) of proteins has emerged as a major regulatory mechanism in all three domains of life. One emerging PTM is Nε-lysine acetylation-the acetylation of the epsilon amino group of lysine residues. Nε-lysine acetylation is known to regulate multiple cellular processes. In eukaryotes, it regulates chromatin structure, transcription, metabolism, signal transduction, and the cytoskeleton. Recently, multiple groups have detected Nε-lysine acetylation in diverse bacterial phyla, but no work on protein acetylation in Borrelia burgdorferi has been reported. Here, we describe a step-by-step protocol to identify Nε-lysine acetylated proteins in B. burgdorferi.

Indexed as

Protein Processing, Post-TranslationalAcetylationAnimalsBacterial ProteinsBlotting, WesternBorrelia burgdorferiElectrophoresis, Polyacrylamide GelHumansImmunoprecipitationLyme DiseaseLysineBacterial ProteinsLysineAcetylated lysine proteinBorrelia burgdorferiImmunoprecipitationPosttranslational modificationProtein acetylation

Identifiers

PMID29032545

DOI10.1007/978-1-4939-7383-5_14

PMCPMC5864457

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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.