Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro.
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Summary
Near-UV CD analysis in combination with glutaraldehyde cross-linking studies suggests that a pH-mediated tetramer to monomer transition is operative in the pH range where fibril formation occurs, consistent with denaturation to a monomeric TTR intermediate which has lost its native tertiary structure and capability to form fibrils.
- Type
- article
- Published
- 1992-09-15
- Cited by
- 561
- References
- 41
- OpenAlex
- https://openalex.org/W2011606718
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:36643546
Keywords
Transthyretin, Citation, Altmetrics, Icon, Computer science
References
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Cited by
- Structural studies of FocB and Transthyretin
- Tetracycline inhibits W7FW14F apomyoglobin fibril extension and keeps the amyloid protein in a prefibrillar, highly cytotoxic state
- Experimental inhibition of fibrillogenesis and neurotoxicity by amyloid-beta (Aβ) and other disease-related peptides/proteins by plant extracts and herbal compounds.
- Unfolding and aggregation of transthyretin by the truncation of 50 N‐terminal amino acids
- Targeting Protein Aggregation for the Treatment of Degenerative Diseases
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- Targeting Amyloid Aggregation: An Overview of Strategies and Mechanisms
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- Amyloids here, amyloids there…What’s wrong with them?
- Protein aggregation from inclusion bodies to amyloid and biomaterials.
- Analysis of amyloid deposition in a transgenic mouse model of homozygous familial amyloidotic polyneuropathy.
- Molecular chaperones in biology, medicine and protein biotechnology
- Transthyretin from a structural perspective
- The Stress response in transthyretin amyloidosis
- Toxicological and therapeutic implications of interactions between polychlorinated biphenyl sulfates and human transthyretin
- Fibrinogen chaperone activity in transthyretin amyloidosis: the effect of protein glycation
- Comparison of amyloid deposition in two lines of transgenic mouse that model familial amyloidotic polyneuropathy, type I
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- Mechanisms involved in amyloid induced cytotoxicity
- Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease
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