Evidence map›Paper›PMID 30264233›Full record

ReviewMolecular biotechnology2018

Tailoring Proteins to Re-Evolve Nature: A Short Review.

Angelica Jimenez-Rosales, Miriam V Flores-Merino

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

7 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. A novel salt- and organic solvent-tolerant phosphite dehydrogenase fromFrontiers in bioengineering and biotechnology · 2023
    Article
  5. Review
  6. Article
  7. Review
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

2 authors at 1 institution in 1 country.

Angelica Jimenez-RosalesCenter for Research in Medical Sciences (CICMED), Autonomous University of the State of Mexico, 205 Venustiano Carranza, Universidad C.P. 50130, Toluca, Mexico. ajimenez.qfb@gmail.com.ORCID http://orcid.org/0000-0003-2822-0681
Miriam V Flores-MerinoCenter for Research in Medical Sciences (CICMED), Autonomous University of the State of Mexico, 205 Venustiano Carranza, Universidad C.P. 50130, Toluca, Mexico.
Universidad Autónoma del Estado de México · MX

Funding

Consejo Nacional de Ciencia y Tecnología 310271Secretaría de Educación Pública award 511-6/17-9932 funding 993201
6 · The paper itself

Abstract

Proteins are key biomolecules for most biological processes, their function is related to their conformation that is also dictated by their sequence of amino acids. Through evolution, nature has produced an immense variety of enzymatic tools of high efficiency and selectivity, and thanks to the understanding of the molecular basis of life and the technological advances, scientists have learned to introduce mutations and select mutant enzymes, to optimize and control their molecular fitness characteristics mainly for industrial, medical and environmental applications. The relationship between protein structure and enzymatic functionality is essential, and there are various experimental and instrumental techniques for unravelling the molecular changes, activities and specificities. Protein engineering applies computational tools, in hand with experimental tools for mutations, like directed evolution and rational design, along with screening methods to obtain protein variations with the desired properties under a short time frame. With innovations in technology, it is possible to fine tune properties in proteins and reach new frontiers in their applications. The present review will briefly discuss these points and methods, with a glimpse on their strengths and pitfalls, while giving an overview of the versatility of synthetic proteins and their huge potential for biotechnological and biomedical fields.

Indexed as

Directed Molecular EvolutionProtein EngineeringRecombinant ProteinsMutagenesisRecombinant ProteinsBiocatalysisDirected evolutionEnzyme modificationProtein engineeringRandom mutagenesisSite-directed mutagenesis

Identifiers

PMID30264233
OpenAlexW2892833978

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.