ArticleBiopolymers2013
Under-folded proteins: Conformational ensembles and their roles in protein folding, function, and pathogenesis.
Article in Biopolymers, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Molecular Serum Albumin Unmask Nanobio Properties of Molecular Graphenes in Shungite Carbon Nanoparticles.International journal of molecular sciences · 2024Article
- The protein disorder cycle.Biophysical reviews · 2021Review
- Life in Phases: Intra- and Inter- Molecular Phase Transitions in Protein Solutions.Biomolecules · 2019Review
- The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins.The Journal of membrane biology · 2019Review
- Article
- Are Charge-State Distributions a Reliable Tool Describing Molecular Ensembles of Intrinsically Disordered Proteins by Native MS?Journal of the American Society for Mass Spectrometry · 2017Review
- Unfoldome variation upon plant-pathogen interactions: strawberry infection by Colletotrichum acutatum.Plant molecular biology · 2015Article
- Standardization and quality control in quantifying non-enzymatic oxidative protein modifications in relation to ageing and disease: Why is it important and why is it hard?Redox biology · 2015Review
- Identification of inhibitors of biological interactions involving intrinsically disordered proteins.International journal of molecular sciences · 2015Review
- Electrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomics.Chemical reviews · 2015Review
- Digested disorder, Quarterly intrinsic disorder digest (October-November-December, 2013).Intrinsically disordered proteins · 2015Article
- Hbr1 Activates and Represses Hyphal Growth in Candida albicans and Regulates Fungal Morphogenesis under Embedded Conditions.PloS one · 2015Article
- Anatomy of protein disorder, flexibility and disease-related mutations.Frontiers in molecular biosciences · 2015Article
- Chaperoned amyloid proteins for immune manipulation: α-Synuclein/Hsp70 shifts immunity toward a modulatory phenotype.Immunity, inflammation and disease · 2014Article
- Article
- The quaternary structure of the recombinant bovine odorant-binding protein is modulated by chemical denaturants.PloS one · 2014Article
- Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology.PloS one · 2013Article
- Digested disorder: Quarterly intrinsic disorder digest (April-May-June, 2013).Intrinsically disordered proteinsReview
- Disorder in the lifetime of a protein.Intrinsically disordered proteinsArticle
- Molecular signaling involving intrinsically disordered proteins in prostate cancer.Asian journal of andrologyReview
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For decades, protein function was intimately linked to the presence of a unique, aperiodic crystal-like structure in a functional protein. The two only places for conformational ensembles of under-folded (or partially folded) protein forms in this picture were either the end points of the protein denaturation processes or transiently populated folding intermediates. Recent years witnessed dramatic change in this perception and conformational ensembles, which the under-folded proteins are, have moved from the shadow. Accumulated to date data suggest that a protein can exist in at least three global forms-functional and folded, functional and intrinsically disordered (nonfolded), and nonfunctional and misfolded/aggregated. Under-folded protein states are crucial for each of these forms, serving as important folding intermediates of ordered proteins, or as functional states of intrinsically disordered proteins (IDPs) and IDP regions (IDPRs), or as pathology triggers of misfolded proteins. Based on these observations, conformational ensembles of under-folded proteins can be classified as transient (folding and misfolding intermediates) and permanent (IDPs and stable misfolded proteins). Permanently under-folded proteins can further be split into intentionally designed (IDPs and IDPRs) and unintentionally designed (misfolded proteins). Although intrinsic flexibility, dynamics, and pliability are crucial for all under-folded proteins, the different categories of under-foldedness are differently encoded in protein amino acid sequences.
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