Evidence map›Paper›PMID 29090506›Full record

ArticleProtein science : a publication of the Protein Society2018

%MinMax: A versatile tool for calculating and comparing synonymous codon usage and its impact on protein folding.

Anabel Rodriguez, Gabriel Wright, Scott Emrich, Patricia L Clark

Abstract read
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Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

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41citing papers in PubMed
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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

41 citing papers in PubMed.

  1. Article
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  5. Molecular biology of the cell · 2025
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  14. Modifications of the 5' region of the CASPONMicrobial cell factories · 2024
    Article
  15. Codon-optimization in gene therapy: promises, prospects and challenges.Frontiers in bioengineering and biotechnology · 2024
    Review
  16. Article
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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Anabel RodriguezDepartment of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556.
Gabriel WrightDepartment of Computer Science & Engineering, University of Notre Dame, Notre Dame, Indiana, 46556.
Scott EmrichDepartment of Computer Science & Engineering, University of Notre Dame, Notre Dame, Indiana, 46556.
Patricia L ClarkDepartment of Chemistry & Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556.ORCID 0000-0001-5462-8248

Funding

Integrative computational framework for pattern mining in big -omics data: linking synonymous codon usage to protein biogenesisR01GM120733 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CLARK, PATRICIA LOUISE, EMRICH, SCOTT · 2016 to 2019
$1.1M
NIGMS NIH HHS R01 GM120733
6 · The paper itself

Abstract

Most amino acids can be encoded by more than one synonymous codon, but these are rarely used with equal frequency. In many coding sequences the usage patterns of rare versus common synonymous codons is nonrandom and under selection. Moreover, synonymous substitutions that alter these patterns can have a substantial impact on the folding efficiency of the encoded protein. This has ignited broad interest in exploring synonymous codon usage patterns. For many protein chemists, biophysicists and structural biologists, the primary motivation for codon analysis is identifying and preserving usage patterns most likely to impact high-yield production of functional proteins. Here we describe the core functions and new features of %MinMax, a codon usage calculator freely available as a web-based portal and downloadable script (http://www.codons.org). %MinMax evaluates the relative usage frequencies of the synonymous codons used to encode a protein sequence of interest and compares these results to a rigorous null model. Crucially, for analyzing codon usage in common host organisms %MinMax requires only the coding sequence as input; with a user-input codon frequency table, %MinMax can be used to evaluate synonymous codon usage patterns for any coding sequence from any fully sequenced genome. %MinMax makes no assumptions regarding the impact of transfer ribonucleic acid concentrations or other molecular-level interactions on translation rates, yet its output is sufficient to predict the effects of synonymous codon substitutions on cotranslational folding mechanisms. A simple calculation included within %MinMax can be used to harmonize codon usage frequencies for heterologous gene expression.

Indexed as

Protein FoldingSoftwareCodonSequence Analysis, DNACodonbiotechnologycodon harmonizationcodon optimizationcotranslational protein foldingheterologous gene expressionprotein aggregationribosome

Identifiers

PMID29090506
PMCPMC5734269

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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.