Evidence map›Paper›PMID 27563054›Full record

ArticleMolecular biology and evolution2016

Molecular Determinants of Mutant Phenotypes, Inferred from Saturation Mutagenesis Data.

Arti Tripathi, Kritika Gupta, Shruti Khare, Pankaj C Jain, Siddharth Patel, Prasanth Kumar, Ajai J Pulianmackal, Nilesh Aghera, Raghavan Varadarajan

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology and evolution, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 51 citations in OpenAlex.

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  12. Structural and functional determinants inferred from deep mutational scans.Protein science : a publication of the Protein Society · 2022
    Article
  13. Article
  14. Article
  15. PON-Sol2: Prediction of Effects of Variants on Protein Solubility.International journal of molecular sciences · 2021
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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

9 authors at 1 institution in 1 country.

Arti TripathiMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Kritika GuptaMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Shruti KhareMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Pankaj C JainMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Siddharth PatelMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Prasanth KumarMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Ajai J PulianmackalMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Nilesh AgheraMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Raghavan VaradarajanMolecular Biophysics Unit, Indian Institute of Science, Bangalore, India Jawaharlal Nehru Center for Advanced Scientific Research, Bangalore, India varadar@mbu.iisc.ernet.in.
Indian Institute of Science Bangalore · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Understanding how mutations affect protein activity and organismal fitness is a major challenge. We used saturation mutagenesis combined with deep sequencing to determine mutational sensitivity scores for 1,664 single-site mutants of the 101 residue Escherichia coli cytotoxin, CcdB at seven different expression levels. Active-site residues could be distinguished from buried ones, based on their differential tolerance to aliphatic and charged amino acid substitutions. At nonactive-site positions, the average mutational tolerance correlated better with depth from the protein surface than with accessibility. Remarkably, similar results were observed for two other small proteins, PDZ domain (PSD95

Indexed as

MutagenesisMutationAmino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionCatalytic DomainEscherichia coliHigh-Throughput Nucleotide SequencingMolecular Sequence DataMutagenesis, Site-DirectedPhenotypeProtein ConformationProteinsProtein StabilitySequence Analysis, ProteinStructure-Activity RelationshipProteinsdeep sequencingfitness effect predictionmutagenesisprotein folding

Identifiers

PMID27563054
PMCPMC5062330
OpenAlexW2508518100

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.