Evidence map›Paper›PMID 21279668›Full record

ArticleJournal of biomolecular NMR2011

Suppression of phospholipid biosynthesis by cerulenin in the condensed Single-Protein-Production (cSPP) system.

Lili Mao, Koichi Inoue, Yisong Tao, Gaetano T Montelione, Ann E McDermott, Masayori Inouye

Open access · greenAbstract read
In one paragraph

Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

10 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Solid-state NMR of membrane proteins in situ.Current opinion in structural biology · 2025
    Review
  3. In situ NMR reveals a pH sensor motif in an outer membrane protein that drives bacterial vesicle production.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Membrane proteins, magic-angle spinning, and in-cell NMR.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  9. Structure determination of a membrane protein in proteoliposomes.Journal of the American Chemical Society · 2012
    Article
  10. 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

6 authors at 2 institutions in 1 country.

Lili MaoDepartment of Biochemistry, Center for Advanced Biotechnology and Medicine, Robert Wood Johnson Medical School, 679 Hoes Lane, Piscataway, NJ 08854, USA.
Koichi Inoue
Yisong Tao
Gaetano T Montelione
Ann E McDermott
Masayori Inouye
Rutgers, The State University of New Jersey · USColumbia University · US

Funding

Sub 9 at AECMU54GM075026 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI HUNT, JOHN FRANCIS · 2005 to 2009
$16.8M
Structural and Functional Studies of Potassium Channels by Solid State NMRR01GM088724 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI ANN E MCDERMOTT · 2009 to 2026
$5.6M
The Method for Determination of Membrane Protein Structures without Purification R01GM085449 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI INOUYE, MASAYORI · 2008 to 2011
$1.2M
NIGMS NIH HHS 1R01GM085449NIGMS NIH HHS R01 GM085449NIGMS NIH HHS R01 GM088724NIGMS NIH HHS U54 GM075026NIGMS NIH HHS U54GM75026
6 · The paper itself

Abstract

Using the single-protein-production (SPP) system, a protein of interest can be exclusively produced in high yield from its ACA-less gene in Escherichia coli expressing MazF, an ACA-specific mRNA interferase. It is thus feasible to study a membrane protein by solid-state NMR (SSNMR) directly in natural membrane fractions. In developing isotope-enrichment methods, we observed that (13)C was also incorporated into phospholipids, generating spurious signals in SSNMR spectra. Notable, with the SPP system a protein can be produced in total absence of cell growth caused by antibiotics. Here, we demonstrate that cerulenin, an inhibitor of phospholipid biosynthesis, can suppress isotope incorporation in the lipids without affecting membrane protein yield in the SPP system. SSNMR analysis of ATP synthase subunit c, an E. coli inner membrane protein, produced by the SPP method using cerulenin revealed that (13)C resonance signals from phospholipid were markedly reduced, while signals for the isotope-enriched protein were clearly present.

Indexed as

CeruleninMembrane ProteinsNuclear Magnetic Resonance, BiomolecularPhospholipidsCeruleninMembrane ProteinsPhospholipids

Identifiers

PMID21279668
PMCPMC3164850
OpenAlexW1988663796

What OpenQuestion holds

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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.