ArticleInternational journal of molecular sciences2017
Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation.
Article in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Structural and dynamic similarities of nanofibrils and microparticles of engineered spider silk proteins probed by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2026Article
- Structural Conformation and Activity of Spider-Derived Inhibitory Cystine Knot Peptide Pn3a Are Modulated by pH.ACS omega · 2023Article
- Article
- Structures of HIV-1 Neutralizing Antibody 10E8 Delineate the Mechanistic Basis of Its Multi-Peak Behavior on Size-Exclusion Chromatography.Antibodies (Basel, Switzerland) · 2021Article
- Frontotemporal dementia-linked P112H mutation of TDP-43 induces protein structural change and impairs its RNA binding function.Protein science : a publication of the Protein Society · 2021Article
- Protein synthesis with conformationally constrained cyclic dipeptides.Bioorganic & medicinal chemistry · 2020Article
- Ameliorating amyloid aggregation through osmolytes as a probable therapeutic molecule against Alzheimer's disease and type 2 diabetes.RSC advances · 2020Article
- Studies of the oligomerisation mechanism of a cystatin-based engineered protein scaffold.Scientific reports · 2019Article
- Prolines Affect the Nucleation Phase of Amyloid Fibrillation Reaction; Mutational Analysis of Human Stefin B.ACS chemical neuroscience · 2019Article
- Inhibition of Protein Aggregation by Several Antioxidants.Oxidative medicine and cellular longevity · 2018Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Here we discuss studies of the structure, folding, oligomerization and amyloid fibril formation of several proline mutants of human stefin B, which is a protein inhibitor of lysosomal cysteine cathepsins and a member of the cystatin family. The structurally important prolines in stefin B are responsible for the slow folding phases and facilitate domain swapping (Pro 74) and loop swapping (Pro 79). Moreover, our findings are compared to β₂-microglobulin, a protein involved in dialysis-related amyloidosis. The assessment of the contribution of proline residues to the process of amyloid fibril formation may shed new light on the critical molecular events involved in conformational disorders.
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