Using NMR Titration Experiments to Study E. coli FAS-II- and AcpP-Mediated Protein-Protein Interactions.

Desirae A Mellor, Javier O Sanlley, Michael Burkart

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

–field-weighted citation impact, top 86% 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.

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Desirae A MellorDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.

Javier O SanlleyDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.

Michael BurkartDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA. mburkart@ucsd.edu.

University of California San Diego · US

Funding

Targeting protein-protein interactions as drug targetsR21AI156484 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BURKART, MICHAEL D. · 2021 to 2022

$434k

NIAID NIH HHS R21 AI156484

6 · The paper itself

Abstract

Acyl carrier proteins (ACPs) are central to many primary and secondary metabolic pathways. In E. coli fatty acid biosynthesis (FAB), the central ACP, AcpP, transports intermediates to a suite of partner proteins (PP) for iterative modification and elongation. The regulatory protein-protein interactions that occur between AcpP and the PP in FAB are poorly understood due to the dynamic and transient nature of these interactions. Solution-state NMR spectroscopy can reveal information at the atomic level through experiments such as the 2D heteronuclear single quantum coherence (HSQC). The following protocol describes NMR HSQC titration experiments that can elucidate biomolecular recognition events.

Indexed as

Escherichia coliEscherichia coli ProteinsMagnetic Resonance ImagingMagnetic Resonance SpectroscopyEscherichia coli ProteinsAcpPCarrier proteinsFAS-IIFatty acid biosynthesisHSQCNMR spectroscopyTitration experiments

Identifiers

PMID37184699

DOI10.1007/978-1-0716-3214-7_3

PMCPMC12064005

OpenAlexW4376623200

What OpenQuestion holds

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LicenceTDM

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Registered trials

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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.