ArticleThe Journal of biological chemistry2011
The plasticity of the β-trefoil fold constitutes an evolutionary platform for protease inhibition.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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
10 citing papers in PubMed, 29 citations in OpenAlex.
- Mechanisms of neutralization of toxSAS from toxin-antitoxin modules.Nature chemical biology · 2025Article
- Tracing the function expansion for a primordial protein fold in the era of fold-based function prediction: β-trefoil.PloS one · 2025Article
- Canonical or noncanonical? Structural plasticity of serine protease-binding loops in Kunitz-STI protease inhibitors.Protein science : a publication of the Protein Society · 2023Article
- Polypeptide N-acetylgalactosamine transferase 3: a post-translational writer on human health.Journal of molecular medicine (Berlin, Germany) · 2022Review
- Evolutionary Aspects of the Structural Convergence and Functional Diversification of Kunitz-Domain Inhibitors.Journal of molecular evolution · 2020Review
- New homologues of Brassicaceae water-soluble chlorophyll proteins shed light on chlorophyll binding, spectral tuning, and molecular evolution.The FEBS journal · 2020Article
- Physico-Chemical and Antifungal Properties of a Trypsin Inhibitor from the Roots ofMolecules (Basel, Switzerland) · 2018Article
- Extrinsic Functions of Lectin Domains in O-N-Acetylgalactosamine Glycan Biosynthesis.The Journal of biological chemistry · 2016Article
- Article
- Crystallization and X-ray diffraction analysis of an antifungal laticifer protein.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteases carry out a number of crucial functions inside and outside the cell. To protect the cells against the potentially lethal activities of these enzymes, specific inhibitors are produced to tightly regulate the protease activity. Independent reports suggest that the Kunitz-soybean trypsin inhibitor (STI) family has the potential to inhibit proteases with different specificities. In this study, we use a combination of biophysical methods to define the structural basis of the interaction of papaya protease inhibitor (PPI) with serine proteases. We show that PPI is a multiple-headed inhibitor; a single PPI molecule can bind two trypsin units at the same time. Based on sequence and structural analysis, we hypothesize that the inherent plasticity of the β-trefoil fold is paramount in the functional evolution of this family toward multiple protease inhibition.
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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.