Evidence map›Paper›PMID 31670785›Full record

ArticleMolecular biology and evolution2020

Protein Structural Information and Evolutionary Landscape by In Vitro Evolution.

Marco Fantini, Simonetta Lisi, Paolo De Los Rios, Antonino Cattaneo, Annalisa Pastore

Abstract readEvaluation Study
In one paragraph

Article in Molecular biology and evolution, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Emergent time scales of epistasis in protein evolution.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. In vivo functional phenotypes from a computational epistatic model of evolution.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Editorial: Molecular evolution: You learn from your mistakes.Frontiers in molecular biosciences · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Not Enough Natural Data? Sequence and Ye Shall Find.Frontiers in molecular biosciences · 2020
    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

5 authors.

Marco FantiniBioSNS Laboratory of Biology, Scuola Normale Superiore (SNS), Pisa, Italy.
Simonetta LisiBioSNS Laboratory of Biology, Scuola Normale Superiore (SNS), Pisa, Italy.
Paolo De Los RiosInstitute of Physics, School of Basic Sciences, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.
Antonino CattaneoBioSNS Laboratory of Biology, Scuola Normale Superiore (SNS), Pisa, Italy.
Annalisa PastoreDepartment of Clinical and Basic Neuroscience, Maurice Wohl Institute, King's College London, London, United Kingdom.

Funding

Medical Research Council MC_PC_13054
6 · The paper itself

Abstract

Protein structure is tightly intertwined with function according to the laws of evolution. Understanding how structure determines function has been the aim of structural biology for decades. Here, we have wondered instead whether it is possible to exploit the function for which a protein was evolutionary selected to gain information on protein structure and on the landscape explored during the early stages of molecular and natural evolution. To answer to this question, we developed a new methodology, which we named CAMELS (Coupling Analysis by Molecular Evolution Library Sequencing), that is able to obtain the in vitro evolution of a protein from an artificial selection based on function. We were able to observe with CAMELS many features of the TEM-1 beta-lactamase local fold exclusively by generating and sequencing large libraries of mutational variants. We demonstrated that we can, whenever a functional phenotypic selection of a protein is available, sketch the structural and evolutionary landscape of a protein without utilizing purified proteins, collecting physical measurements, or relying on the pool of natural protein variants.

Indexed as

Structure-Activity Relationshipbeta-LactamasesDirected Molecular EvolutionProtein FoldingSequence Analysis, DNAbeta-LactamasesAmpRbeta-lactamaseDCAdirect coupling analysiserror-prone PCRevolutionary couplingsmolecular evolutionmutagenesisPacBioSequelSMRT sequencingthird-generation sequencingβ-lactamase

Identifiers

PMID31670785
PMCPMC7086169

What OpenQuestion holds

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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.