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Peter E Wright

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Articles 176
Citations 13509
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Recent Articles
1.
Ritsch I, Dyson H, Wright P
Proc Natl Acad Sci U S A . 2025 Mar; 122(11):e2425230122. PMID: 40067885
The transthyretin (TTR) tetramer, assembled as a dimer of dimers, transports thyroxine and retinol binding protein in blood plasma and cerebrospinal fluid. Aggregation of wild type (WT) or pathogenic variant...
2.
Ritsch I, Dyson H, Wright P
bioRxiv . 2024 Nov; PMID: 39605681
The transthyretin (TTR) tetramer, assembled as a dimer of dimers, transports thyroxine and retinol binding protein in blood plasma and cerebrospinal fluid. Aggregation of wild type or pathogenic variant TTR...
3.
Dyson H, Wright P
Trends Biochem Sci . 2024 Nov; 50(1):9-17. PMID: 39578215
Defects in the tumor suppressor protein p53 are found in the majority of cancers. The p53 protein (393 amino acids long) contains the folded DNA-binding domain (DBD) and tetramerization domain...
4.
Sun X, Ferguson J, Yang K, Stanfield R, Dyson H, Wright P
Protein Sci . 2024 Aug; 33(9):e5101. PMID: 39149996
Aberrant formation and deposition of human transthyretin (TTR) aggregates causes transthyretin amyloidosis. To initialize aggregation, transthyretin tetramers must first dissociate into monomers that partially unfold to promote entry into the...
5.
Leach B, Ferguson J, Morgan G, Sun X, Kroon G, Oyen D, et al.
J Mol Biol . 2024 Jun; 436(16):168673. PMID: 38909653
The aggregation pathway of transthyretin (TTR) proceeds through rate-limiting dissociation of the tetramer (a dimer of dimers) and partial misfolding of the resulting monomer, which assembles into amyloid structures through...
6.
Lemke E, Babu M, Kriwacki R, Mittag T, Pappu R, Wright P, et al.
Mol Cell . 2024 Apr; 84(7):1188-1190. PMID: 38579677
In his commentary in this issue of Molecular Cell, Struhl reasons that the term "intrinsically disordered regions" represents a vague and confusing concept for protein function. However, the term "intrinsically...
7.
Sun X, Ferguson J, Yang K, Stanfield R, Dyson H, Wright P
bioRxiv . 2024 Mar; PMID: 38464206
Aberrant formation and deposition of human transthyretin (TTR) aggregates causes transthyretin amyloidosis. To initialize aggregation, transthyretin tetramers must first dissociate into monomers that partially unfold to promote entry into the...
8.
Dyson H, Wright P
Isr J Chem . 2024 Mar; 63(10-11). PMID: 38454968
It is hard to evaluate the role of individual mentors in the genesis of important ideas. In the case of our realization that proteins do not have to be stably...
9.
Dyson H, Wright P
Curr Opin Struct Biol . 2024 Feb; 86:102791. PMID: 38417184
No abstract available.
10.
Sun X, Ferguson J, Leach B, Stanfield R, Dyson H, Wright P
J Am Chem Soc . 2023 Dec; 146(1):532-542. PMID: 38134439
Aggregation of transthyretin (TTR) is associated with devastating amyloid diseases. Amyloidosis begins with the dissociation of the native homotetramer (a dimer of dimers) to form a monomeric intermediate that assembles...