ArticleNature structural & molecular biology2010
Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain.
Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed, 56 citations in OpenAlex.
- Dissecting the Structural Features of Folding Asymmetry and Transient Misfolding in a Multidomain PDZ Scaffold.Small science · 2026Article
- Adjacent domains drive the emergence of misfolded intermediates in the folding pathway of the PDZ4 from MAGI1.BBA advances · 2026Article
- Structure and Dynamics of the Misfolding Intermediate in the Pathogenic T183A Prion Protein Mutant.Journal of chemical theory and computation · 2025Article
- Exploring the "misfolding problem" by systematic discovery and analysis of functional-but-degraded proteins.Molecular biology of the cell · 2023Article
- From Kuru to Alzheimer: A personal outlook.Protein science : a publication of the Protein Society · 2021Review
- Hidden kinetic traps in multidomain folding highlight the presence of a misfolded but functionally competent intermediate.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Conformational Plasticity Vista of PDZ Domains.Life (Basel, Switzerland) · 2020Review
- The Effect of ProlineInternational journal of molecular sciences · 2019Article
- The structural basis of nanobody unfolding reversibility and thermoresistance.Scientific reports · 2018Article
- Identification and Structural Characterization of an Intermediate in the Folding of the Measles Virus X Domain.The Journal of biological chemistry · 2016Article
- Decoding Structural Properties of a Partially Unfolded Protein Substrate: En Route to Chaperone Binding.PLoS computational biology · 2015Article
- Solution dependence of the collisional activation of ubiquitin [M + 7H](7+) ions.Journal of the American Society for Mass Spectrometry · 2014Article
- Understanding the frustration arising from the competition between function, misfolding, and aggregation in a globular protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Direct single-molecule observation of calcium-dependent misfolding in human neuronal calcium sensor-1.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations.Biophysical journal · 2014Article
- The role of backbone hydrogen bonds in the transition state for protein folding of a PDZ domain.PloS one · 2014Article
- Structure of the transition state for the binding of c-Myb and KIX highlights an unexpected order for a disordered system.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Allosteric activation of the Par-6 PDZ via a partial unfolding transition.Journal of the American Chemical Society · 2013Article
- Folding pathways of proteins with increasing degree of sequence identities but different structure and function.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Plasticity of PDZ domains in ligand recognition and signaling.FEBS letters · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
Abstract
Incorrectly folded states transiently populated during the protein folding process are potentially prone to aggregation and have been implicated in a range of misfolding disorders that include Alzheimer's and Parkinson's diseases. Despite their importance, however, the structures of these states and the mechanism of their formation have largely escaped detailed characterization because of their short-lived nature. Here we present the structures of all the major states involved in the folding process of a PDZ domain, which include an off-pathway misfolded intermediate. By using a combination of kinetic, protein engineering, biophysical and computational techniques, we show that the misfolded intermediate is characterized by an alternative packing of the N-terminal β-hairpin onto an otherwise native-like scaffold. Our results suggest a mechanism of formation of incorrectly folded transient compact states by which misfolded structural elements are assembled together with more extended native-like regions.
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.