Evidence map›Paper›PMID 26075618›Full record

ArticlePloS one2015

Computational Design of the β-Sheet Surface of a Red Fluorescent Protein Allows Control of Protein Oligomerization.

Timothy M Wannier, Matthew M Moore, Yun Mou, Stephen L Mayo

Abstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. High-Throughput Cellular Thermal Shift Assays in Research and Drug Discovery.SLAS discovery : advancing life sciences R & D · 2020
    Article
  3. Monomerization of far-red fluorescent proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  4. 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

4 authors.

Timothy M WannierDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, California, United States of America.
Matthew M MooreDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California, United States of America.
Yun MouDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California, United States of America.
Stephen L MayoDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, California, United States of America; Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California, United States of America.

Funding

Rational Design of Brighter, Monomeric Far-Red Fluorescent ProteinsR21EB018579 · NIBIB · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI MAYO, STEPHEN L. · 2014 to 2015
$458k
NIBIB NIH HHS 1R21EB018579-01NIBIB NIH HHS R21 EB018579
6 · The paper itself

Abstract

Computational design has been used with mixed success for the design of protein surfaces, with directed evolution heretofore providing better practical solutions than explicit design. Directed evolution, however, requires a tractable high-throughput screen because the random nature of mutation does not enrich for desired traits. Here we demonstrate the successful design of the β-sheet surface of a red fluorescent protein (RFP), enabling control over its oligomerization. To isolate the problem of surface design, we created a hybrid RFP from DsRed and mCherry with a stabilized protein core that allows for monomerization without loss of fluorescence. We designed an explicit library for which 93 of 96 (97%) of the protein variants are soluble, stably fluorescent, and monomeric. RFPs are heavily used in biology, but are natively tetrameric, and creating RFP monomers has proven extremely difficult. We show that surface design and core engineering are separate problems in RFP development and that the next generation of RFP markers will depend on improved methods for core design.

Indexed as

Computational BiologyFluorescenceFluorescent DyesGene LibraryLuminescent ProteinsPlasmidsProtein ConformationProtein EngineeringProtein MultimerizationRed Fluorescent ProteinFluorescent DyesLuminescent ProteinsRed Fluorescent Protein

Identifiers

PMID26075618
PMCPMC4468108

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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.