ArticleQuarterly reviews of biophysics2011
Expanding the proteome: disordered and alternatively folded proteins.
Article in Quarterly reviews of biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
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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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Who cites it
90 citing papers in PubMed, 169 citations in OpenAlex.
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- Comparison of Methodologies for Absolute Binding Free Energy Calculations of Ligands to Intrinsically Disordered Proteins.Journal of chemical theory and computation · 2024Article
- Review and Comparative Analysis of Methods and Advancements in Predicting Protein Complex Structure.Interdisciplinary sciences, computational life sciences · 2024Review
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- Protein conformational ensembles in function: roles and mechanisms.RSC chemical biology · 2023Review
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- DOPAnization of tyrosine in α-synuclein by tyrosine hydroxylase leads to the formation of oligomers.Nature communications · 2022Article
- Emerging Implications of Phase Separation in Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Review
- Finite element modeling of α-helices and tropocollagen molecules referring to spike of SARS-CoV-2.Biophysical journal · 2022Article
- Review
- Mass Spectrometry for Neurobiomarker Discovery: The Relevance of Post-Translational Modifications.Cells · 2022Review
- Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma.Biophysics reviews · 2022Review
- Circulating extracellular vesicles and rheumatoid arthritis: a proteomic analysis.Cellular and molecular life sciences : CMLS · 2021Review
- The protein disorder cycle.Biophysical reviews · 2021Review
- Tau Post-Translational Modifications: Potentiators of Selective Vulnerability in Sporadic Alzheimer's Disease.Biology · 2021Review
- Intrinsically Disordered Proteins as Regulators of Transient Biological Processes and as Untapped Drug Targets.Molecules (Basel, Switzerland) · 2021Review
- Intrinsic Disorder in Tetratricopeptide Repeat Proteins.International journal of molecular sciences · 2020Article
- Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation.Frontiers in neurology · 2020Review
30 more citing papers are in PubMed but not listed here.
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1 author at 1 institution in 1 country.
Funding
Abstract
Proteins provide much of the scaffolding for life, as well as undertaking a variety of essential catalytic reactions. These characteristic functions have led us to presuppose that proteins are in general functional only when well structured and correctly folded. As we begin to explore the repertoire of possible protein sequences inherent in the human and other genomes, two stark facts that belie this supposition become clear: firstly, the number of apparent open reading frames in the human genome is significantly smaller than appears to be necessary to code for all of the diverse proteins in higher organisms, and secondly that a significant proportion of the protein sequences that would be coded by the genome would not be expected to form stable three-dimensional (3D) structures. Clearly the genome must include coding for a multitude of alternative forms of proteins, some of which may be partly or fully disordered or incompletely structured in their functional states. At the same time as this likelihood was recognized, experimental studies also began to uncover examples of important protein molecules and domains that were incompletely structured or completely disordered in solution, yet remained perfectly functional. In the ensuing years, we have seen an explosion of experimental and genome-annotation studies that have mapped the extent of the intrinsic disorder phenomenon and explored the possible biological rationales for its widespread occurrence. Answers to the question 'why would a particular domain need to be unstructured?' are as varied as the systems where such domains are found. This review provides a survey of recent new directions in this field, and includes an evaluation of the role not only of intrinsically disordered proteins but also of partially structured and highly dynamic members of the disorder-order continuum.
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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.