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Brandon H Toyama

Explore the profile of Brandon H Toyama including associated specialties, affiliations and a list of published articles. Areas
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Recent Articles
1.
Lev-Ram V, Lemieux S, Deerinck T, Bushong E, Perez A, Pritchard D, et al.
Cells . 2024 Oct; 13(19. PMID: 39404392
Perineuronal nets (PNNs), a specialized form of extra cellular matrix (ECM), surround numerous neurons in the CNS and allow synaptic connectivity through holes in its structure. We hypothesize that PNNs...
2.
Lev-Ram V, Lemieux S, Deerinck T, Bushong E, Toyama B, Perez A, et al.
bioRxiv . 2023 Apr; PMID: 37066274
Significance: In this multidisciplinary work, we challenge the hypothesis that the pattern of holes in the perineuronal nets (PNN) hold the code for very-long-term memories. The scope of this work...
3.
Toyama B, Arrojo E Drigo R, Lev-Ram V, Ramachandra R, Deerinck T, Lechene C, et al.
J Cell Biol . 2018 Dec; 218(2):433-444. PMID: 30552100
Many adult tissues contain postmitotic cells as old as the host organism. The only organelle that does not turn over in these cells is the nucleus, and its maintenance represents...
4.
Ori A, Toyama B, Harris M, Bock T, Iskar M, Bork P, et al.
Cell Syst . 2016 May; 1(3):224-37. PMID: 27135913
Aging is associated with the decline of protein, cell, and organ function. Here, we use an integrated approach to characterize gene expression, bulk translation, and cell biology in the brains...
5.
Toyama B, Savas J, Park S, Harris M, Ingolia N, Yates 3rd J, et al.
Cell . 2013 Sep; 154(5):971-982. PMID: 23993091
Intracellular proteins with long lifespans have recently been linked to age-dependent defects, ranging from decreased fertility to the functional decline of neurons. Why long-lived proteins exist in metabolically active cellular...
6.
Toyama B, Hetzer M
Nat Rev Mol Cell Biol . 2012 Dec; 14(1):55-61. PMID: 23258296
Protein turnover is an effective way of maintaining a functional proteome, as old and potentially damaged polypeptides are destroyed and replaced by newly synthesized copies. An increasing number of intracellular...
7.
Savas J, Toyama B, Xu T, Yates 3rd J, Hetzer M
Science . 2012 Feb; 335(6071):942. PMID: 22300851
To combat the functional decline of the proteome, cells use the process of protein turnover to replace potentially impaired polypeptides with new functional copies. We found that extremely long-lived proteins...
8.
Toyama B, Weissman J
Annu Rev Biochem . 2011 Apr; 80:557-85. PMID: 21456964
Many, perhaps most, proteins, are capable of forming self-propagating, β-sheet (amyloid) aggregates. Amyloid-like aggregates are found in a wide range of diseases and underlie prion-based inheritance. Despite intense interest in...
9.
Verges K, Smith M, Toyama B, Weissman J
Nat Struct Mol Biol . 2011 Mar; 18(4):493-9. PMID: 21423194
Prion proteins can adopt multiple infectious strain conformations. Here we investigate how the sequence of a prion protein affects its capacity to propagate specific conformations by exploiting our ability to...
10.
Ohhashi Y, Ito K, Toyama B, Weissman J, Tanaka M
Nat Chem Biol . 2010 Jan; 6(3):225-230. PMID: 20081853
Aggregation-prone proteins often misfold into multiple distinct amyloid conformations that dictate different physiological impacts. Although amyloid formation is triggered by a transient nucleus, the mechanism by which an initial nucleus...