ReviewThe Journal of biological chemistry2016
Expanding the Range of Protein Function at the Far End of the Order-Structure Continuum.
Review in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed.
- Prevalence and Functional Roles of Intrinsic Disorder in the [F-actin]-monooxygenase MICAL Family Members and their Interactors.Cell biochemistry and biophysics · 2026Article
- Identification and characterization of calcium binding protein, spermatid-associated 1 (CABS1)# in selected human tissues and fluids.PloS one · 2024Article
- Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma.Biophysics reviews · 2022Review
- How C-Reactive Protein Structural Isoforms With Distinctive Bioactivities Affect Disease Progression.Frontiers in immunology · 2020Review
- Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding.Protein science : a publication of the Protein Society · 2019Review
- Intrinsically disordered proteins in synaptic vesicle trafficking and release.The Journal of biological chemistry · 2019Review
- Epichromatin and chromomeres: a 'fuzzy' perspective.Open biology · 2018Review
- Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness.Cellular and molecular life sciences : CMLS · 2017Review
- Quantifying Allosteric Communication via Both Concerted Structural Changes and Conformational Disorder with CARDS.Journal of chemical theory and computation · 2017Article
- The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease.Biochemical Society transactions · 2016Review
- Introduction to the Thematic Minireview Series on Intrinsically Disordered Proteins.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The traditional view of the structure-function paradigm is that a protein's function is inextricably linked to a well defined, three-dimensional structure, which is determined by the protein's primary amino acid sequence. However, it is now accepted that a number of proteins do not adopt a unique tertiary structure in solution and that some degree of disorder is required for many proteins to perform their prescribed functions. In this review, we highlight how a number of protein functions are facilitated by intrinsic disorder and introduce a new protein structure taxonomy that is based on quantifiable metrics of a protein's disorder.
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Registered trials
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.