Evidence map›Paper›PMID 23401533›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Coupling mutagenesis and parallel deep sequencing to probe essential residues in a genome or gene.

William P Robins, Shah M Faruque, John J Mekalanos

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

34 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  11. The bacterial tyrosine kinase system CpsBCD governs the length of capsule polymers.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Review
  13. Article
  14. Recent Advances in Carbon and Nitrogen Metabolism in C3 Plants.International journal of molecular sciences · 2020
    Review
  15. Article
  16. Review
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  18. Article
  19. Article
  20. Structure and mutagenic analysis of the lipid II flippase MurJ fromProceedings of the National Academy of Sciences of the United States of America · 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 at 2 institutions in 2 countries.

William P RobinsDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA.
Shah M Faruque
John J Mekalanos
Harvard University · USInternational Centre for Diarrhoeal Disease Research · BD

Funding

INFECTIOUS DISEASE AND BASIC MICROBIOLOGICAL MECHANISMST32AI007061 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI Marcia B Goldberg · 1985 to 2026
$12.1M
Phages and Genomic Variation in Vibrio Cholerae EvolutionR01GM068851 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI MEKALANOS, JOHN JOSEPH · 2003 to 2015
$3.9M
NIAID NIH HHS T32 AI007061NIGMS NIH HHS 2R01GM068851-09NIGMS NIH HHS R01 GM068851
6 · The paper itself

Abstract

The sequence of a protein determines its function by influencing its folding, structure, and activity. Similarly, the most conserved residues of orthologous and paralogous proteins likely define those most important. The detection of important or essential residues is not always apparent via sequence alignments because these are limited by the depth of any given gene's phylogeny, as well as specificities that relate to each protein's unique biological origin. Thus, there is a need for robust and comprehensive ways of evaluating the importance of specific amino acid residues of proteins of known or unknown function. Here we describe an approach called Mut-seq, which allows the identification of virtually all of the essential residues present in a whole genome through the application of limited chemical mutagenesis, selection for function, and deep parallel genomic sequencing. Here we have applied this method to T7 bacteriophage and T7-like virus JSF7 of Vibrio cholerae.

Indexed as

Amino Acid MotifsAmino AcidsAmino Acid SequenceAmino Acid SubstitutionBacteriophage T7Base PairingCodon, NonsenseCodon, TerminatorConserved SequenceDNA-Directed DNA PolymeraseDNA-Directed RNA PolymerasesGenes, ViralHigh-Throughput Nucleotide SequencingMolecular Sequence DataMutagenesisMutation, MissenseAmino AcidsCodon, NonsenseCodon, TerminatorDNA-Directed DNA PolymeraseDNA-Directed RNA PolymerasesViral Proteins

Identifiers

PMID23401533
PMCPMC3587248
OpenAlexW2099535366

What OpenQuestion holds

Textmetadata
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.