ReviewProtein science : a publication of the Protein Society2007
Protein reconstitution and three-dimensional domain swapping: benefits and constraints of covalency.
Review in Protein science : a publication of the Protein Society, 2007. 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
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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
25 citing papers in PubMed.
- Article
- A 33-residue peptide tag increases solubility and stability of Escherichia coli produced single-chain antibody fragments.Nature communications · 2022Article
- Affinity, Specificity, and Cooperativity of DNA Binding by Bacterial Gene Regulatory Proteins.International journal of molecular sciences · 2022Review
- Crystal structures of Val58Ile tryptophan repressor in a domain-swapped array in the presence and absence of L-tryptophan.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Benefits and constrains of covalency: the role of loop length in protein stability and ligand binding.Scientific reports · 2020Article
- Human Cellular Retinol Binding Protein II Forms a Domain-Swapped Trimer Representing a Novel Fold and a New Template for Protein Engineering.Chembiochem : a European journal of chemical biology · 2020Article
- Conformational Ensembles of Calmodulin Revealed by Nonperturbing Site-Specific Vibrational Probe Groups.The journal of physical chemistry. A · 2018Article
- Exploring the Roles of Proline in Three-Dimensional Domain Swapping from Structure Analysis and Molecular Dynamics Simulations.The protein journal · 2018Article
- Small Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly.Scientific reports · 2017Article
- Domain-Swapped Dimers of Intracellular Lipid-Binding Proteins: Evidence for Ordered Folding Intermediates.Structure (London, England : 1993) · 2016Article
- Artificial domain duplication replicates evolutionary history of ketol-acid reductoisomerases.Protein science : a publication of the Protein Society · 2016Article
- Role of benzyl alcohol in the unfolding and aggregation of interferon α-2a.Journal of pharmaceutical sciences · 2015Article
- Article
- Beta-barrel scaffold of fluorescent proteins: folding, stability and role in chromophore formation.International review of cell and molecular biology · 2013Review
- 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
- Article
- Environment-dependent long-range structural distortion in a temperature-sensitive point mutant.Protein science : a publication of the Protein Society · 2012Article
- Thermodynamics, kinetics, and photochemistry of β-strand association and dissociation in a split-GFP system.Journal of the American Chemical Society · 2011Article
- In vivo protein stabilization based on fragment complementation and a split GFP system.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Non-3D domain swapped crystal structure of truncated zebrafish alphaA crystallin.Protein science : a publication of the Protein Society · 2010Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The phenomena of protein reconstitution and three-dimensional domain swapping reveal that highly similar structures can be obtained whether a protein is comprised of one or more polypeptide chains. In this review, we use protein reconstitution as a lens through which to examine the range of protein tolerance to chain interruptions and the roles of the primary structure in related features of protein structure and folding, including circular permutation, natively unfolded proteins, allostery, and amyloid fibril formation. The results imply that noncovalent interactions in a protein are sufficient to specify its structure under the constraints imposed by the covalent backbone.
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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.