ArticleProceedings of the National Academy of Sciences of the United States of America2001
Destabilization of Ca2+-free gelsolin may not be responsible for proteolysis in Familial Amyloidosis of Finnish Type.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Serum gelsolin as a biomarker for differentiating familial Mediterranean fever from juvenile idiopathic arthritis in children.Biomolecules & biomedicine · 2026Article
- A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026Review
- Plant Hormone Cytokinin as Aggregation Modulator of Gelsolin Amyloidosis.Journal of peptide science : an official publication of the European Peptide Society · 2025Article
- Rational Design of a Peptidomimetic Inhibitor of Gelsolin Amyloid Aggregation.International journal of molecular sciences · 2022Article
- A novel hotspot of gelsolin instability triggers an alternative mechanism of amyloid aggregation.Computational and structural biotechnology journal · 2021Article
- The structure of N184K amyloidogenic variant of gelsolin highlights the role of the H-bond network for protein stability and aggregation properties.European biophysics journal : EBJ · 2020Article
- Clinical, histopathological, and in silico pathogenicity analyses in a pedigree with familial amyloidosis of the Finnish type (Meretoja syndrome) caused by a novel gelsolin mutation.Molecular vision · 2020Article
- Gelsolin pathogenic Gly167Arg mutation promotes domain-swap dimerization of the protein.Human molecular genetics · 2018Article
- Exome sequencing establishes a gelsolin mutation as the cause of inherited bulbar-onset neuropathy.Muscle & nerve · 2017Article
- Molecular basis of a novel renal amyloidosis due to N184K gelsolin variant.Scientific reports · 2016Article
- Regulatory role of the second gelsolin-like domain of Caenorhabditis elegans gelsolin-like protein 1 (GSNL-1) in its calcium-dependent conformation and actin-regulatory activities.Cytoskeleton (Hoboken, N.J.) · 2013Article
- Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca(2+) stabilization.The EMBO journal · 2001Article
- The disintegration of a molecule: the role of gelsolin in FAF, familial amyloidosis (Finnish type).Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Gelsolin amyloidosis: genetics, biochemistry, pathology and possible strategies for therapeutic intervention.Critical reviews in biochemistry and molecular biologyReview
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5 authors at 2 institutions in 1 country.
Funding
Abstract
Mutations at position 187 in secreted gelsolin enable aberrant proteolysis at the 172-173 and 243-244 amide bonds, affording the 71-residue amyloidogenic peptide deposited in Familial Amyloidosis of Finnish Type (FAF). Thermodynamic comparisons of two different domain 2 constructs were carried out to study possible effects of the mutations on proteolytic susceptibility. In the construct we consider to be most representative of domain 2 in the context of the full-length protein (134-266), the D187N FAF variant is slightly destabilized relative to wild type (WT) under the conditions of urea denaturation, but exhibits a T(m) identical to WT. The D187Y variant is less stable to intermediate urea concentrations and exhibits a T(m) that is estimated to be approximately 5 degrees C lower than WT (pH 7.4, Ca(2+)-free). Although the thermodynamic data indicate that the FAF mutations may slightly destabilize domain 2, these changes are probably not sufficient to shift the native to denatured state equilibrium enough to enable the proteolysis leading to FAF. Biophysical data indicate that these two FAF variants may have different native state structures and possibly different pathways of amyloidosis.
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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.