ArticleF1000 biology reports2013
The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure.
Article in F1000 biology reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 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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Who cites it
44 citing papers in PubMed, 101 citations in OpenAlex.
- On the Roles of Protein Intrinsic Disorder in the Origin of Life and Evolution.Life (Basel, Switzerland) · 2024Review
- Moonlighting enzymes: when cellular context defines specificity.Cellular and molecular life sciences : CMLS · 2023Review
- Electronic Polarization at the Interface between the p53 Transactivation Domain and Two Binding Partners.The journal of physical chemistry. B · 2022Article
- The mitotic spindle protein CKAP2 potently increases formation and stability of microtubules.eLife · 2022Article
- Kinetic coherence underlies the dynamics of disordered proteins.RSC advances · 2021Article
- SCO-spondin, a giant matricellular protein that regulates cerebrospinal fluid activity.Fluids and barriers of the CNS · 2021Review
- RELT stains prominently in B-cell lymphomas and binds the hematopoietic transcription factor MDFIC.Biochemistry and biophysics reports · 2020Article
- Multivalent and Bidirectional Binding of Transcriptional Transactivation Domains to the MED25 Coactivator.Biomolecules · 2020Article
- Article
- Disorder and cysteines in proteins: A design for orchestration of conformational see-saw and modulatory functions.Progress in molecular biology and translational science · 2020Review
- Analyzing IDPs in Interactomes.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Multi-functionality of proteins involved in GPCR and G protein signaling: making sense of structure-function continuum with intrinsic disorder-based proteoforms.Cellular and molecular life sciences : CMLS · 2019Review
- Intrinsic Disorder of the BAF Complex: Roles in Chromatin Remodeling and Disease Development.International journal of molecular sciences · 2019Article
- The Balancing Act of Intrinsically Disordered Proteins: Enabling Functional Diversity while Minimizing Promiscuity.Journal of molecular biology · 2019Article
- On the Regularities of the Polar Profiles of Proteins Related to Ebola Virus Infection and their Functional Domains.Cell biochemistry and biophysics · 2018Article
- Targeting Intramembrane Protein-Protein Interactions: Novel Therapeutic Strategy of Millions Years Old.Advances in protein chemistry and structural biology · 2018Review
- Intrinsic Disorder and Posttranslational Modifications: The Darker Side of the Biological Dark Matter.Frontiers in genetics · 2018Review
- Predictions of Backbone Dynamics in Intrinsically Disordered Proteins Using De Novo Fragment-Based Protein Structure Predictions.Scientific reports · 2017Article
- Flexibility of the "rigid" classics or rugged bottom of the folding funnels of myoglobin, lysozyme, RNase A, chymotrypsin, cytochromeIntrinsically disordered proteins · 2017Article
- p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure-Function Continuum Concept.International journal of molecular sciences · 2016Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The classical 'lock-and-key' and 'induced-fit' mechanisms for binding both originated in attempts to explain features of enzyme catalysis. For both of these mechanisms and for their recent refinements, enzyme catalysis requires exquisite spatial and electronic complementarity between the substrate and the catalyst. Thus, binding models derived from models originally based on catalysis will be highly biased towards mechanisms that utilize structural complementarity. If mere binding without catalysis is the endpoint, then the structural requirements for the interaction become much more relaxed. Recent observations on specific examples suggest that this relaxation can reach an extreme lack of specific 3D structure, leading to molecular recognition with biological consequences that depend not only upon structural and electrostatic complementarity between the binding partners but also upon kinetic, entropic, and generalized electrostatic effects. In addition to this discussion of binding without fixed structure, examples in which unstructured regions carry out important biological functions not involving molecular recognition will also be discussed. Finally, we discuss whether 'intrinsically disordered protein' (IDP) represents a useful new concept.
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What OpenQuestion holds
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.