ArticleBiomolecules2019
Functional Segments on Intrinsically Disordered Regions in Disease-Related Proteins.
Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Molecular driving force of a small molecule-induced protein disorder-order transition.Communications chemistry · 2026Article
- Longer internal exons tend to have more tandem repeats and more frequently experience insertions and deletions.Life science alliance · 2025Article
- Electromagnetic Field Stimulation Effects on Intrinsically Disordered Proteins and Their Role in Aging and Neurodegeneration.Journal of biomedical science and engineering · 2025Article
- Spatially resolved transcriptomic profiling of placental development in dairy cow.Zoological research · 2024Article
- Myofilament-associated proteins with intrinsic disorder (MAPIDs) and their resolution by computational modeling.Quarterly reviews of biophysics · 2023Review
- Enrichment patterns of intrinsic disorder in proteins.Biophysical reviews · 2022Review
- Improving Protein Subcellular Location Classification by Incorporating Three-Dimensional Structure Information.Biomolecules · 2021Article
- Cdk8 Kinase Module: A Mediator of Life and Death Decisions in Times of Stress.Microorganisms · 2021Review
- Budding yeast Rad51: a paradigm for how phosphorylation and intrinsic structural disorder regulate homologous recombination and protein homeostasis.Current genetics · 2021Review
- A Tale of Loops and Tails: The Role of Intrinsically Disordered Protein Regions in R-Loop Recognition and Phase Separation.Frontiers in molecular biosciences · 2021Article
- Short Disordered Epitope of CRTAM Ig-Like V Domain as a Potential Target for Blocking Antibodies.International journal of molecular sciences · 2020Article
- Protein-Protein Interactions Mediated by Intrinsically Disordered Protein Regions Are Enriched in Missense Mutations.Biomolecules · 2020Article
- NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences.Biophysics and physicobiology · 2020Article
- Intrinsically Disordered Proteins in Chronic Diseases.Biomolecules · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
One of the unique characteristics of intrinsically disordered proteins (IPDs) is the existence of functional segments in intrinsically disordered regions (IDRs). A typical function of these segments is binding to partner molecules, such as proteins and DNAs. These segments play important roles in signaling pathways and transcriptional regulation. We conducted bioinformatics analysis to search these functional segments based on IDR predictions and database annotations. We found more than a thousand potential functional IDR segments in disease-related proteins. Large fractions of proteins related to cancers, congenital disorders, digestive system diseases, and reproductive system diseases have these functional IDRs. Some proteins in nervous system diseases have long functional segments in IDRs. The detailed analysis of some of these regions showed that the functional segments are located on experimentally verified IDRs. The proteins with functional IDR segments generally tend to come and go between the cytoplasm and the nucleus. Proteins involved in multiple diseases tend to have more protein-protein interactors, suggesting that hub proteins in the protein-protein interaction networks can have multiple impacts on human diseases.
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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.