Amyloidogenic and non-amyloidogenic transthyretin variants interact differently with human cardiomyocytes: insights into early events of non-fibrillar tissue damage. (Q34951860)

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English	Amyloidogenic and non-amyloidogenic transthyretin variants interact differently with human cardiomyocytes: insights into early events of non-fibrillar tissue damage.	scientific article

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22 February 2020

Amyloidogenic and non-amyloidogenic transthyretin variants interact differently with human cardiomyocytes: insights into early events of non-fibrillar tissue damage (English)

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22 February 2020

Natalia Reixach

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22 February 2020

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Pallavi Manral

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14 January 2015

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22 February 2020

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22 February 2020

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22 February 2020

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22 February 2020

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25 July 2019

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Quantification of quaternary structure stability in aggregation-prone proteins under physiological conditions: the transthyretin case.

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AG10 inhibits amyloidogenesis and cellular toxicity of the familial amyloid cardiomyopathy-associated V122I transthyretin

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Age-related oxidative modifications of transthyretin modulate its amyloidogenicity

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Why are some amyloidoses systemic? Does hepatic "chaperoning at a distance" prevent cardiac deposition in a transgenic model of human senile systemic (transthyretin) amyloidosis?

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8 July 2018

Potent Kinetic Stabilizers That Prevent Transthyretin-Mediated Cardiomyocyte Proteotoxicity

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Mechanisms of transthyretin cardiomyocyte toxicity inhibition by resveratrol analogs

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Transthyretin: the servant of many masters.

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Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture

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Human-murine transthyretin heterotetramers are kinetically stable and non-amyloidogenic. A lesson in the generation of transgenic models of diseases involving oligomeric proteins

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pH nanoenvironment at the surface of single melanoma cells

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Transthyretin oligomers induce calcium influx via voltage-gated calcium channels.

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Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses.

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Binding of amyloidogenic transthyretin to the plasma membrane alters membrane fluidity and induces neurotoxicity

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Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture

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Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis

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Cholesterol Modulates Amyloid Beta-peptide’s Membrane Interactions

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Only amyloidogenic intermediates of transthyretin induce apoptosis

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The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis

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Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates

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Internalization of transthyretin. Evidence of a novel yet unidentified receptor-associated protein (RAP)-sensitive receptor

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Receptor-mediated uptake and internalization of transthyretin

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Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro

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Cholesterol and anionic phospholipids increase the binding of amyloidogenic transthyretin to lipid membranes

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Formation of amyloid fibers triggered by phosphatidylserine-containing membranes

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Amyloid and nonfibrillar deposits in mice transgenic for wild-type human transthyretin: a possible model for senile systemic amyloidosis

1 reference

https://pubmed.ncbi.nlm.nih.gov/25395306

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Transthyretin V122I in African Americans with congestive heart failure

1 reference

https://pubmed.ncbi.nlm.nih.gov/25395306

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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10.1042/BSR20140155

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22 February 2020

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Europe PubMed Central

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22 February 2020

PubMed publication ID

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Europe PubMed Central

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22 February 2020

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