Evidence map›Paper›PMID 19856129›Full record

ArticleJournal of structural and functional genomics2009

Production of membrane proteins for NMR studies using the condensed single protein (cSPP) production system.

Lili Mao, Yuefeng Tang, S Thangminlal Vaiphei, Tsutomu Shimazu, Sung-Gun Kim, Rajeswari Mani, Elias Fakhoury, Eileen White, Gaetano T Montelione, Masayori Inouye

Open access · greenAbstract read
In one paragraph

Article in Journal of structural and functional genomics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

13 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. Membrane proteins, magic-angle spinning, and in-cell NMR.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. A microscale protein NMR sample screening pipeline.Journal of biomolecular NMR · 2010
    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

10 authors at 3 institutions in 1 country.

Lili MaoNew York Center on Membrane Protein Structure, Rutgers, The State University of New Jersey, Piscataway, NJ, 08854, USA.
Yuefeng Tang
S Thangminlal Vaiphei
Tsutomu Shimazu
Sung-Gun Kim
Rajeswari Mani
Elias Fakhoury
Eileen White
Gaetano T Montelione
Masayori Inouye
Rutgers, The State University of New Jersey · USJohnson University · USRutgers Cancer Institute of New Jersey

Funding

Sub-project 9U54GM074958 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI GERSTEIN, MARK BENDER · 2005 to 2009
$56.6M
Sub 9 at AECMU54GM075026 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI HENDRICKSON, WAYNE A. · 2005 to 2009
$16.8M
Function of the Adenovirus E1B OncogeneR37CA053370 · NCI · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI WHITE, EILEEN P. · 2001 to 2009
$3.1M
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
FUNCTION OF THE ADENOVIRUS E1B ONCOGENER01CA053370 · NCI · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI WHITE, EILEEN · 1991 to 2000
$195k
NCI NIH HHS R37 CA053370NCI NIH HHS R37 CA53370NIGMS NIH HHS 1R01 GM085449NIGMS NIH HHS R01 GM085449NIGMS NIH HHS U54 GM074958NIGMS NIH HHS U54 GM075026NIGMS NIH HHS U54 GM75026
6 · The paper itself

Abstract

In the Single Protein Production (SPP) method, all E. coli cellular mRNAs are eliminated by the induction of MazF, an ACA-specific mRNA interferase. When an mRNA for a membrane protein, engineered to have no ACA sequences without altering its amino acid sequence, is induced in the MazF-induced cells, E. coli is converted into a bioreactor producing only the targeted membrane protein. Here we demonstrate that three prokaryotic inner membrane proteins, two prokaryotic outer membrane proteins, and one human virus membrane protein can be produced at very high levels, and assembled in appropriate membrane fractions. The condensed SPP (cSPP) system was used to selectively produce isotope-enriched membrane proteins for NMR studies in up to 150-fold condensed culture without affecting protein yields, providing more than 99% cost saving for isotopes. As a novel application of the cSPP system for studies of membrane proteins prior to purification we also demonstrate, for the first time, fast detergent screening by microcoil NMR and well-resolved NMR spectra of several targeted integral membrane proteins obtained without purification.

Indexed as

Escherichia coliNuclear Magnetic Resonance, BiomolecularDNA-Binding ProteinsEndoribonucleasesEscherichia coli ProteinsHumansRecombinant ProteinsViral Matrix ProteinsDNA-Binding ProteinsEndoribonucleasesEscherichia coli ProteinsMazF protein, E coliRecombinant ProteinsViral Matrix Proteins

Identifiers

PMID19856129
PMCPMC2923930
OpenAlexW2154512008

What OpenQuestion holds

Textmetadata
LicenceTDM
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.