ArticleProceedings of the National Academy of Sciences of the United States of America2008
Cooperativity, connectivity, and folding pathways of multidomain proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. 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.
- Adjacent domains drive the emergence of misfolded intermediates in the folding pathway of the PDZ4 from MAGI1.BBA advances · 2026Article
- Accurate prediction of protein folding mechanisms by simple structure-based statistical mechanical models.Nature communications · 2023Article
- The Wako-Saitô-Muñoz-Eaton Model for Predicting Protein Folding and Dynamics.Molecules (Basel, Switzerland) · 2022Review
- Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding.International journal of molecular sciences · 2022Review
- Investigating the trade-off between folding and function in a multidomain Y-family DNA polymerase.eLife · 2020Article
- Directed evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition.The Journal of biological chemistry · 2019Article
- Gō model revisited.Biophysics and physicobiology · 2019Review
- Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins.Biophysical reviews · 2018Review
- Fast H-DROP: A thirty times accelerated version of H-DROP for interactive SVM-based prediction of helical domain linkers.Journal of computer-aided molecular design · 2017Article
- Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human γD-Crystallin Protein.The Journal of biological chemistry · 2016Article
- Cooperativity and modularity in protein folding.Biophysics and physicobiology · 2016Review
- Nonspecific yet decisive: Ubiquitination can affect the native-state dynamics of the modified protein.Protein science : a publication of the Protein Society · 2015Article
- Folding pathway of a multidomain protein depends on its topology of domain connectivity.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- In the multi-domain protein adenylate kinase, domain insertion facilitates cooperative folding while accommodating function at domain interfaces.PLoS computational biology · 2014Article
- Conserved prosegment residues stabilize a late-stage folding transition state of pepsin independently of ground states.PloS one · 2014Article
- Modulation of a protein free-energy landscape by circular permutation.The journal of physical chemistry. B · 2013Article
- Identification of cancer fusion drivers using network fusion centrality.Bioinformatics (Oxford, England) · 2013Article
- Contributions of aromatic pairs to the folding and stability of long-lived human γD-crystallin.Protein science : a publication of the Protein Society · 2011Article
- Entropic mechanism of large fluctuation in allosteric transition.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Ubiquitin not only serves as a tag but also assists degradation by inducing protein unfolding.Proceedings of the National Academy of Sciences of the United States of America · 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
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multidomain proteins are ubiquitous in both prokaryotic and eukaryotic proteomes. Study on protein folding, however, has concentrated more on the isolated single domains of proteins, and there have been relatively few systematic studies on the effects of domain-domain interactions on folding. We here discuss this issue by examining human gammaD-crystallin, spore coat protein S, and a tandem array of the R16 and R17 domains of spectrin as example proteins by using a structure-based model of folding. The calculated results consistently explain the experimental data on folding pathways and effects of mutational perturbations, supporting the view that the connectivity of two domains and the distribution of domain-domain interactions in the native conformation are factors to determine kinetic and equilibrium properties of cooperative folding.
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.