ArticleIntrinsically disordered proteins
Distribution and cluster analysis of predicted intrinsically disordered protein Pfam domains.
Article in Intrinsically disordered proteins. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 14 citations in OpenAlex.
- Intrinsic Disorder in the Human Tear Proteome.Investigative ophthalmology & visual science · 2023Article
- Digging into the 3D Structure Predictions of AlphaFold2 with Low Confidence: Disorder and Beyond.Biomolecules · 2022Article
- Structural and Functional Characterization of the ABA-Water Deficit Stress Domain from Wheat and Barley: An Intrinsically Disordered Domain behind the Versatile Functions of the Plant Abscissic Acid, Stress and Ripening Protein Family.International journal of molecular sciences · 2021Article
- Intrinsically disordered domains: Sequence ➔ disorder ➔ function relationships.Protein science : a publication of the Protein Society · 2019Article
- Polymorphism Analysis Reveals Reduced Negative Selection and Elevated Rate of Insertions and Deletions in Intrinsically Disordered Protein Regions.Genome biology and evolution · 2015Article
- Prediction of protein structural features from sequence data based on Shannon entropy and Kolmogorov complexity.PloS one · 2015Article
- Identifying novel cell cycle proteins in Apicomplexa parasites through co-expression decision analysis.PloS one · 2014Article
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Authors and funding
4 authors at 4 institutions in 3 countries.
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No grant is acknowledged in the PubMed record.
Abstract
The Pfam database groups regions of proteins by how well hidden Markov models (HMMs) can be trained to recognize similarities among them. Conservation pressure is probably in play here. The Pfam seed training set includes sequence and structure information, being drawn largely from the PDB. A long standing hypothesis among intrinsically disordered protein (IDP) investigators has held that conservation pressures are also at play in the evolution of different kinds of intrinsic disorder, but we find that predicted intrinsic disorder (PID) is not always conserved across Pfam domains. Here we analyze distributions and clusters of PID regions in 193024 members of the version 23.0 Pfam seed database. To include the maximum information available for proteins that remain unfolded in solution, we employ the 10 linearly independent Kidera factors
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