Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Rapid reportHuman stefin B readily forms amyloid fibrils in vitro
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Cited by (72)
Structural and functional analysis of cystatin E reveals enzymologically relevant dimer and amyloid fibril states
2018, Journal of Biological ChemistryLimited Proteolysis Reveals That Amyloids from the 3D Domain-Swapping Cystatin B Have a Non-Native β-Sheet Topology
2015, Journal of Molecular BiologyCitation Excerpt :Human cystatin C cerebral amyloid angiopathy is a hereditary disease caused by the L68Q mutation in the protein [17]. This mutant protein is difficult to purify and manipulate [18]; therefore, wild-type cystatin B has often been used as a model for amyloid formation in the cystatin family [19]. Perhaps more importantly, as a small folded protein, cystatin proves to be an ideal system to improve our understanding of how folded proteins form amyloid.
Gain in toxic function of stefin B EPM1 mutants aggregates: Correlation between cell death, aggregate number/size and oxidative stress
2014, Biochimica et Biophysica Acta - Molecular Cell ResearchCitation Excerpt :Additionally to the loss of function that occurs, gain in toxic function of some EPM1 stefin B missense mutant aggregates may play a role, as proposed by us before [41]. Stefin B in its wild type (wt) form is an amyloidogenic protein and it has served as an appropriate model for studies of amyloid formation [42,43]. Protein misfolding and aggregation are at the core of the so called conformational disorders [44,45].
On Possible Function and Toxicity of Multiple Oligomeric/Conformational States of a Globular Protein - Human Stefin B
2013, Bio-nanoimaging: Protein Misfolding and AggregationInsights in progressive myoclonus epilepsy: HSP70 promotes cystatin B polymerization
2013, Biochimica et Biophysica Acta - Proteins and ProteomicsThe cross-road between the mechanisms of protein folding and aggregation; study of human stefin B and its H75W mutant
2011, Biochemical and Biophysical Research CommunicationsCitation Excerpt :For the H75W mutant the folding to the same native-like intermediate took place at pH 7 (in 3 phases) while at pH 4.8 and 5.8 the mutant ended in another intermediate state, molten globule-like, which did not fold any further. The H75W mutant was prone to aggregate to amorphous aggregate at this pH and did not form mature fibrils (TEM data not shown), in accordance to intermediate of the molten globule type formed by the stefin B at pH 3 [24,25]. For the case of stefins, we have shown that different folding intermediates build fibrils of different morphology [25] and some may be off-pathway [23].