Evidence map›Paper›PMID 35762715›Full record

ReviewProtein science : a publication of the Protein Society2022

Mechanisms of protein evolution.

Vijay Jayaraman, Saacnicteh Toledo-Patiño, Lianet Noda-García, Paola Laurino

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

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  4. Reengineering a thermostable keratinase past the boiling point.Applied and environmental microbiology · 2026
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  17. Engineering Protein-Polyelectrolyte Interactions for Cellular Applications.Annual review of chemical and biomolecular engineering · 2025
    Review
  18. Article
  19. Review
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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

4 authors.

Vijay JayaramanDepartment of Molecular Cell Biology, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0001-6288-1841
Saacnicteh Toledo-PatiñoProtein Engineering and Evolution Unit, Okinawa Institute of Science and Technology Graduate University, Okinawa, Japan.ORCID 0000-0003-0632-0075
Lianet Noda-GarcíaDepartment of Plant Pathology and Microbiology, Institute of Environmental Sciences, Robert H. Smith Faculty of Agriculture, Food and Environment, Hebrew University of Jerusalem, Rehovot, Israel.ORCID 0000-0002-0449-0700
Paola LaurinoProtein Engineering and Evolution Unit, Okinawa Institute of Science and Technology Graduate University, Okinawa, Japan.ORCID 0000-0002-3725-2645

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

How do proteins evolve? How do changes in sequence mediate changes in protein structure, and in turn in function? This question has multiple angles, ranging from biochemistry and biophysics to evolutionary biology. This review provides a brief integrated view of some key mechanistic aspects of protein evolution. First, we explain how protein evolution is primarily driven by randomly acquired genetic mutations and selection for function, and how these mutations can even give rise to completely new folds. Then, we also comment on how phenotypic protein variability, including promiscuity, transcriptional and translational errors, may also accelerate this process, possibly via "plasticity-first" mechanisms. Finally, we highlight open questions in the field of protein evolution, with respect to the emergence of more sophisticated protein systems such as protein complexes, pathways, and the emergence of pre-LUCA enzymes.

Indexed as

ProteinsHumansMutationProteins

Identifiers

PMID35762715
PMCPMC9214755

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.