ReviewMolecular and cellular biochemistry2009
Disorder-to-order conformational transitions in protein structure and its relationship to disease.
Review in Molecular and cellular biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 52 citations in OpenAlex.
- GeoPep: A Geometry-Aware Masked Language Model for Protein-Peptide Binding Site Prediction.Journal of chemical information and modeling · 2026Article
- Molecular driving force of a small molecule-induced protein disorder-order transition.Communications chemistry · 2026Article
- Neutralization of the Pandemic Influenza A/H1N1 Virus withAntibodies (Basel, Switzerland) · 2025Article
- Time-Dependent Material Properties of Aging Biomolecular Condensates from Different Viscoelasticity Measurements in Molecular Dynamics Simulations.The journal of physical chemistry. B · 2023Article
- Omicron (BA.1) and sub-variants (BA.1.1, BA.2, and BA.3) of SARS-CoV-2 spike infectivity and pathogenicity: A comparative sequence and structural-based computational assessment.Journal of medical virology · 2022Article
- Protein structural transitions critically transform the network connectivity and viscoelasticity of RNA-binding protein condensates but RNA can prevent it.Nature communications · 2022Article
- Kinetic interplay between droplet maturation and coalescence modulates shape of aged protein condensates.Scientific reports · 2022Article
- Structure-based peptide design targeting intrinsically disordered proteins: Novel histone H4 and H2A peptidic inhibitors.Computational and structural biotechnology journal · 2021Article
- Lipid Modulation in the Formation of β-Sheet Structures. Implications for De Novo Design of Human Islet Amyloid Polypeptide and the Impact on β-Cell Homeostasis.Biomolecules · 2020Article
- EGFP insertional mutagenesis reveals multiple FXR2P fibrillar states with differing ribosome association in neurons.Biology open · 2019Article
- Uncoupling the Folding and Binding of an Intrinsically Disordered Protein.Journal of molecular biology · 2018Article
- Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins.Methods in enzymology · 2018Article
- Modulation of Amyloidogenesis Controlled by the C-Terminal Domain of Islet Amyloid Polypeptide Shows New Functions on Hepatocyte Cholesterol Metabolism.Frontiers in endocrinology · 2018Article
- Protein Folding and Mechanisms of Proteostasis.International journal of molecular sciences · 2015Review
- Binding cavities and druggability of intrinsically disordered proteins.Protein science : a publication of the Protein Society · 2015Article
- Microenvironmentally controlled secondary structure motifs of apolipoprotein A-I derived peptides.Molecular and cellular biochemistry · 2014Article
- The kinesin-14 Klp2 is negatively regulated by the SIN for proper spindle elongation and telophase nuclear positioning.Molecular biology of the cell · 2012Article
- Amyloidogenic properties of a D/N mutated 12 amino acid fragment of the C-terminal domain of the Cholesteryl-Ester Transfer Protein (CETP).International journal of molecular sciences · 2011Article
- Basic mechanisms of neurodegeneration: a critical update.Journal of cellular and molecular medicine · 2010Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Function in proteins largely depends on the acquisition of specific structures through folding at physiological time scales. Under both equilibrium and non-equilibrium states, proteins develop partially structured molecules that being intermediates in the process, usually resemble the structure of the fully folded protein. These intermediates, known as molten globules, present the faculty of adopting a large variety of conformations mainly supported by changes in their side chains. Taking into account that the mechanism to obtain a fully packed structure is considered more difficult energetically than forming partially "disordered" folding intermediates, evolution might have conferred upon an important number of proteins the capability to first partially fold and-depending on the presence of specific partner ligands-switch on disorder-to-order transitions to adopt a highly ordered well-folded state and reach the lowest energy conformation possible. Disorder in this context can represent segments of proteins or complete proteins that might exist in the native state. Moreover, because this type of disorder-to-order transition in proteins has been found to be reversible, it has been frequently associated with important signaling events in the cell. Due to the central role of this phenomenon in cell biology, protein misfolding and aberrant disorder-to-order transitions have been at present associated with an important number of 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.