Results 11 to 20 of about 45,139 (271)

Bifunctional crosslinking ligands for transthyretin [PDF]

Open Biology, 2015
Wild-type and variant forms of transthyretin (TTR), a normal plasma protein, are amyloidogenic and can be deposited in the tissues as amyloid fibrils causing acquired and hereditary systemic TTR amyloidosis, a debilitating and usually fatal disease ...
P. Patrizia Mangione, Stéphanie Deroo, Stephan Ellmerich, Vittorio Bellotti, Simon Kolstoe, Stephen P. Wood, Carol V. Robinson, Martin D. Smith, Glenys A. Tennent, Robert J. Broadbridge, Claire E. Council, Joanne R. Thurston, Victoria A. Steadman, Antonio K. Vong, Christopher J. Swain, Mark B. Pepys, Graham W. Taylor   +16 more
doaj   +9 more sources

Structure of human transthyretin complexed with bromophenols: a new mode of binding [PDF]

, 2000
The binding of two organohalogen substances, pentabromophenol (PBP) and 2,4,6-tribromophenol (TBP), to human transthyretin (TTR), a thyroid hormone transport protein, has been studied by in vitro competitive binding assays and by X-ray crystallography ...
Minakshi Ghosh, Ilonka A.T.M. Meerts, Atlanta G. Cook, Åke Bergman, Abraham Brouwer, L.N. Johnson   +5 more
openalex   +4 more sources

Evolution of Transthyretin in Marsupials [PDF]

European Journal of Biochemistry, 1995
The evolution of the expression and the structure of the gene for transthyretin, a thyroxine‐binding plasma protein formerly called prealbumin, was studied in three marsupial species: the South American polyprotodont Monodelphis domestica, the Australian polyprotodont Sminthopsis macroura and the Australian diprotodont Petaurus breviceps.
Wei Duan, Samantha J. Richardson, Jeffrey J. Babon, Rebecca J. Heyes, Bridget R. Southwell, Paul J. Harms, Richard E.H. Wettenhall, Katarzyna M. Dzięgielewska, Lynne Selwood, A. J. Bradley, Charlotte Brack, Gerhard Schreiber   +11 more
openalex   +6 more sources

Transthyretin cardiac amyloidosis

Cardiovascular Research, 2022
AbstractTransthyretin cardiac amyloidosis (ATTR-CA) is an increasingly recognized cause of heart failure (HF) and mortality worldwide. Advances in non-invasive diagnosis, coupled with the development of effective treatments, have shifted ATTR-CA from a rare and untreatable disease to a relatively prevalent condition that clinicians should consider on a
Aldostefano Porcari, Marianna Fontana, Julian D Gillmore   +2 more
openaire   +4 more sources

EGCG-Mediated Protection of Transthyretin Amyloidosis by Stabilizing Transthyretin Tetramers and Disrupting Transthyretin Aggregates

International Journal of Molecular Sciences, 2023
Transthyretin amyloidosis (ATTR) is a progressive and systemic disease caused by the misfolding and amyloid aggregation of transthyretin (TTR). Stabilizing the TTR tetramers and disrupting the formed TTR aggregation are treated as a promising strategy for the treatment of ATTR.
Huizhen Zou, Shuangyan Zhou
openaire   +2 more sources

Health-related quality of life in hereditary transthyretin amyloidosis polyneuropathy: a prospective, observational study [PDF]

, 2020
Background Hereditary Transthyretin Amyloidosis Polyneuropathy is a rare life-threatening neurologic disease that imposes considerable mortality and it is associated with progressive related disabilities.
Coelho, Teresa, Conceição, Isabel, Costa, João, de Carvalho, Mamede, Ferreira, Lara, Inês, Mónica   +5 more
core   +2 more sources

Comparative Stability and Clearance of [Met30]Transthyretin and [Met119]Transthyretin [PDF]

European Journal of Biochemistry, 1997
[Met119]Transthyretin has been described as a non‐amyloidogenic transthyretin variant. In Portugal, it has also been found in compound heterozygotic individual carriers of [Met30]transthyretin, the most prevalent variant associated with familial amyloidotic polyneuropathy.
Isabel Alves, Maria João Saraiva, Marguerite T. Hays   +2 more
openaire   +3 more sources

Transthyretin Amyloidosis and the Kidney [PDF]

Clinical Journal of the American Society of Nephrology, 2012
Summary The amyloidoses are protein-misfolding disorders associated with progressive organ dysfunction. Immunoglobulin light chain is the most common, amyloid A the longest recognized, and transthyretin-associated amyloidosis (ATTR) the most frequent inherited systemic form.
Luísa Lobato, Ana Rocha
openaire   +2 more sources

Uncovering the Mechanism of Aggregation of Human Transthyretin. [PDF]

, 2015
The tetrameric thyroxine transport protein transthyretin (TTR) forms amyloid fibrils upon dissociation and monomer unfolding. The aggregation of transthyretin has been reported as the cause of the life-threatening transthyretin amyloidosis.
Cascio, Duilio, Eisenberg, David S, Jiang, Lin, Johnson, Lisa M, Liang, Wilson Y, Riek, Roland, Ruchala, Piotr, Saelices, Lorena, Sawaya, Michael R, Whitelegge, Julian   +9 more
core   +2 more sources

The prevalence and distribution of the amyloidogenic transthyretin (TTR) V122I allele in Africa [PDF]

, 2016
Transthyretin (TTR) pV142I (rs76992529-A) is one of the 113 variants in the human TTR gene associated with systemic amyloidosis. It results from a G to A transition at a CG dinucleotide in the codon for amino acid 122 of the mature protein (TTR V122I ...
Alexander, Alice A, Buxbaum, Joel N., Garvey, W. T, Jacobson, Daniel R, Kalidi, Issa, Modiano, David, Sirima, Sodiomon B, Tagoe, Clement, Tishkoff, Sara, Toure, Amadou, Williams, Scott M   +10 more
core   +1 more source