ArticleBiophysical journal2011
Chain collapse of an amyloidogenic intrinsically disordered protein.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed.
- In Search of Shape in the Unshaped: Constructing Ensembles of Intrinsically Disordered Proteins.Biophysics reviews · 2026Article
- Label-free optical observation of disordered-to-ordered transitions in single intrinsically disordered proteins.Npj biosensing · 2026Article
- Review
- Multisite phosphorylation and binding alter conformational dynamics of the 4E-BP2 protein.Biophysical journal · 2022Article
- A quantitative calcium phosphate nanocluster model of the casein micelle: the average size, size distribution and surface properties.European biophysics journal : EBJ · 2021Article
- Fluorescence-based techniques for the detection of the oligomeric status of proteins: implication in amyloidogenic diseases.European biophysics journal : EBJ · 2021Review
- Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein.Molecules (Basel, Switzerland) · 2021Article
- Ratiometric Single-Molecule FRET Measurements to Probe Conformational Subpopulations of Intrinsically Disordered Proteins.Current protocols in chemical biology · 2020Article
- Residue-Specific Dynamics and Local Environmental Changes in Aβ40 Oligomer and Fibril Formation.Angewandte Chemie (International ed. in English) · 2018Article
- Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions.Annual review of biophysics · 2018Article
- Sensing Tryptophan Microenvironment of Amyloid Protein Utilizing Wavelength-Selective Fluorescence Approach.Journal of fluorescence · 2017Article
- Stepwise unfolding of human βEuropean biophysics journal : EBJ · 2017Article
- Direct Observation of the Intrinsic Backbone Torsional Mobility of Disordered Proteins.Biophysical journal · 2016Article
- Relating sequence encoded information to form and function of intrinsically disordered proteins.Current opinion in structural biology · 2015Review
- Stable, metastable, and kinetically trapped amyloid aggregate phases.Biomacromolecules · 2015Article
- Misfolding of amyloidogenic proteins and their interactions with membranes.Biomolecules · 2013Review
- Dynamics and dimension of an amyloidogenic disordered state of human β(2)-microglobulin.European biophysics journal : EBJ · 2013Article
- A quantitative measure for protein conformational heterogeneity.The Journal of chemical physics · 2013Article
- Article
- The N-terminal actin-binding tandem calponin-homology (CH) domain of dystrophin is in a closed conformation in solution and when bound to F-actin.Biophysical journal · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Natively unfolded or intrinsically disordered proteins (IDPs) are under intense scrutiny due to their involvement in both normal biological functions and abnormal protein misfolding disorders. Polypeptide chain collapse of amyloidogenic IDPs is believed to play a key role in protein misfolding, oligomerization, and aggregation leading to amyloid fibril formation, which is implicated in a number of human diseases. In this work, we used bovine κ-casein, which serves as an archetypal model protein for amyloidogenic IDPs. Using a variety of biophysical tools involving both prediction and spectroscopic techniques, we first established that monomeric κ-casein adopts a collapsed premolten-globule-like conformational ensemble under physiological conditions. Our time-resolved fluorescence and light-scattering data indicate a change in the mean hydrodynamic radius from ∼4.6 nm to ∼1.9 nm upon chain collapse. We then took the advantage of two cysteines separated by 77 amino-acid residues and covalently labeled them using thiol-reactive pyrene maleimide. This dual-labeled protein demonstrated a strong excimer formation upon renaturation from urea- and acid-denatured states under both equilibrium and kinetic conditions, providing compelling evidence of polypeptide chain collapse under physiological conditions. The implication of the IDP chain collapse in protein aggregation and amyloid formation is also discussed.
Indexed as
Identifiers
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.