ArticleMethods in molecular biology (Clifton, N.J.)2020
An Easy Protocol for Evolutionary Analysis of Intrinsically Disordered Proteins.
Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Protein language model identifies disordered, conserved motifs implicated in phase separation.eLife · 2025Article
- Intrinsic Disorder and Other Malleable Arsenals of Evolved Protein Multifunctionality.Journal of molecular evolution · 2024Review
- Pathogenic Variants inInternational journal of molecular sciences · 2023Article
- The difficulty of aligning intrinsically disordered protein sequences as assessed by conservation and phylogeny.PloS one · 2023Article
- Dynamic, but Not Necessarily Disordered, Human-Virus Interactions Mediated through SLiMs in Viral Proteins.Viruses · 2021Review
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Authors and funding
2 authors.
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Abstract
We present an easy protocol for evolutionary analysis of proteins, with an emphasis on studying the evolutionary dynamics of disordered regions. Using the p53 protein family as an example, we provide a guide for finding homologous sequences in a database and refining a dataset before constructing the evolutionary context by building a phylogenetic tree. We show how a multiple sequence alignment and phylogeny for a protein family can be further partitioned into smaller datasets in order to investigate the changes in disorder content across the phylogeny. Based on the evolutionary context, we also investigate site-specific conservation of disorder. Last, we address how to evaluate the evolutionary dynamics of disorder-to-order transitions.
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