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Page 1
Evolutionary Study of Disorder in Protein Sequences.
Biomolecules. 2020 Oct 6;10(10):1413. doi: 10.3390/biom10101413.
Biomolecules. 2020.
PMID: 33036302
Free PMC article.
Low Complexity Induces Structure in Protein Regions Predicted as Intrinsically Disordered.
Gonçalves-Kulik M, Mier P, Kastano K, Cortés J, Bernadó P, Schmid F, Andrade-Navarro MA.
Gonçalves-Kulik M, et al. Among authors: kastano k.
Biomolecules. 2022 Aug 10;12(8):1098. doi: 10.3390/biom12081098.
Biomolecules. 2022.
PMID: 36008992
Free PMC article.
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Functional Tuning of Intrinsically Disordered Regions in Human Proteins by Composition Bias.
Kastano K, Mier P, Dosztányi Z, Promponas VJ, Andrade-Navarro MA.
Kastano K, et al.
Biomolecules. 2022 Oct 15;12(10):1486. doi: 10.3390/biom12101486.
Biomolecules. 2022.
PMID: 36291695
Free PMC article.
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REP2: A Web Server to Detect Common Tandem Repeats in Protein Sequences.
Kamel M, Kastano K, Mier P, Andrade-Navarro MA.
Kamel M, et al. Among authors: kastano k.
J Mol Biol. 2021 May 28;433(11):166895. doi: 10.1016/j.jmb.2021.166895. Epub 2021 Feb 24.
J Mol Biol. 2021.
PMID: 33972020
Free article.
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The Role of Low Complexity Regions in Protein Interaction Modes: An Illustration in Huntingtin.
Kastano K, Mier P, Andrade-Navarro MA.
Kastano K, et al.
Int J Mol Sci. 2021 Feb 9;22(4):1727. doi: 10.3390/ijms22041727.
Int J Mol Sci. 2021.
PMID: 33572172
Free PMC article.
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