ArticleBiophysical journal2006
Folding, misfolding, and amyloid protofibril formation of WW domain FBP28.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed.
- Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Protein science : a publication of the Protein Society · 2026Article
- New Insights into Folding, Misfolding, and Nonfolding Dynamics of a WW Domain.The journal of physical chemistry. B · 2020Article
- A quantitative connection of experimental and simulated folding landscapes by vibrational spectroscopy.Chemical science · 2018Article
- LinkingeLife · 2018Article
- Parallel folding pathways of Fip35 WW domain explained by infrared spectra and their computer simulation.FEBS letters · 2017Article
- Probing Medin Monomer Structure and its Amyloid Nucleation UsingScientific reports · 2017Article
- The Role of Electrostatic Interactions in Folding of β-Proteins.Journal of the American Chemical Society · 2016Article
- Preventing fibril formation of a protein by selective mutation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Folding kinetics of WW domains with the united residue force field for bridging microscopic motions and experimental measurements.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A study of the influence of charged residues on β-hairpin formation by nuclear magnetic resonance and molecular dynamics.The protein journal · 2014Article
- WW domain folding complexity revealed by infrared spectroscopy.Biochemistry · 2014Article
- Association between foldability and aggregation propensity in small disulfide-rich proteins.Antioxidants & redox signaling · 2014Article
- Dynamics of an ultrafast folding subdomain in the context of a larger protein fold.Journal of the American Chemical Society · 2013Article
- Local vs global motions in protein folding.Journal of chemical theory and computation · 2013Article
- Effects of mutation, truncation, and temperature on the folding kinetics of a WW domain.Journal of molecular biology · 2012Article
- Effect of atom- and group-based truncations on biomolecules simulated with reaction-field electrostatics.Journal of molecular modeling · 2011Article
- The ensemble folding kinetics of the FBP28 WW domain revealed by an all-atom Monte Carlo simulation in a knowledge-based potential.Proteins · 2011Article
- Intrinsic determinants of Aβ(12-24) pH-dependent self-assembly revealed by combined computational and experimental studies.PloS one · 2011Article
- (Un)Folding mechanisms of the FBP28 WW domain in explicit solvent revealed by multiple rare event simulation methods.Biophysical journal · 2010Article
- Relation between free energy landscapes of proteins and dynamics.Journal of chemical theory and computation · 2010Article
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
We study the folding mechanism of a triple beta-strand WW domain from the Formin binding protein 28 (FBP28) at atomic resolution with explicit water model using replica exchange molecular dynamics computer simulations. Extended sampling over a wide range of temperatures to obtain the free energy, enthalpy, and entropy surfaces as a function of structural coordinates has been performed. Simulations were started from different configurations covering the folded and unfolded states. In the free energy landscape a transition state is identified and its structures and -values are compared with experimental data from a homologous protein, the prolyl-isomerase Pin1 WW domain. A stable intermediate state is found to accumulate during the simulation characterized by the carboxyl-terminal beta-strand 3 having misregistered hydrogen bonds and where the structural heterogeneity is due to nonnative turn II formation. Furthermore, the aggregation behavior of the FBP28 WW domain may be related to one such misfolded structure, which has a much lower free energy of dimer formation than that of the native dimer. Based on the misfolded dimer, aggregation to form protofibril structure is 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.