ArticleJournal of the American Chemical Society2006
A localized specific interaction alters the unfolding pathways of structural homologues.
Article in Journal of the American Chemical Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
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.
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Who cites it
6 citing papers in PubMed, 23 citations in OpenAlex.
- Mechanism of the bell-shaped profile of ribonuclease a activity: molecular dynamic approach.The protein journal · 2012Article
- Further evidence for the likely completeness of the library of solved single domain protein structures.The journal of physical chemistry. B · 2012Article
- Why not consider a spherical protein? Implications of backbone hydrogen bonding for protein structure and function.Physical chemistry chemical physics : PCCP · 2011Article
- Ribonucleases as potential modalities in anticancer therapy.European journal of pharmacology · 2009Review
- Effects of tyrosine mutations on the conformational and oxidative folding of ribonuclease a: a comparative study.Biochemistry · 2009Article
- Onconase and amphinase, the antitumor ribonucleases from Rana pipiens oocytes.Current pharmaceutical biotechnology · 2008Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Reductive unfolding studies of proteins are designed to provide information about intramolecular interactions that govern the formation (and stabilization) of the native state and about folding/unfolding pathways. By mutating Tyr92 to G, A, or L in the model protein, bovine pancreatic ribonuclease A, and through analysis of temperature factors and molecular dynamics simulations of the crystal structures of these mutants, it is demonstrated that the markedly different reductive unfolding rates and pathways of ribonuclease A and its structural homologue onconase can be attributed to a single, localized, ring-stacking interaction between Tyr92 and Pro93 in the bovine variant. The fortuitous location of this specific stabilizing interaction in a disulfide-bond-containing loop region of ribonuclease A results in the localized modulation of protein dynamics that, in turn, enhances the susceptibility of the disulfide bond to reduction leading to an alteration in the reductive unfolding behavior of the homologues. These results have important implications for folding studies involving topological determinants to obtain folding/unfolding rates and pathways, for protein structure-function prediction through fold recognition, and for predicting proteolytic cleavage sites.
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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.