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Tomoaki Shigeta

Explore the profile of Tomoaki Shigeta including associated specialties, affiliations and a list of published articles. Areas
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Articles 13
Citations 123
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Recent Articles
1.
Shigeta T, Sasamoto K, Yamamoto T
Biochem Biophys Rep . 2021 Mar; 26:100963. PMID: 33748437
Reducing sugars and reactive aldehydes, such as glyceraldehyde, non-enzymatically react with amino or guanidino groups of proteins to form advanced glycation end-products (AGEs) by the Maillard reaction that involves Schiff...
2.
Shigeta T, Sasamoto K, Yamamoto T
Heliyon . 2020 Nov; 6(11):e05337. PMID: 33204871
Glycation of amino or guanidino groups of proteins with glucose and glucose-derived reactive aldehydes, such as α-hydroxyaldehydes, leads to accumulation of advanced glycation end-products (AGEs) in the body, resulting in...
3.
Oguro A, Shigeta T, Machida K, Suzuki T, Iwamoto T, Matsufuji S, et al.
J Biochem . 2020 Mar; 168(2):139-149. PMID: 32181810
Antizyme (AZ) interacts with ornithine decarboxylase, which catalyzes the first step of polyamine biosynthesis and recruits it to the proteasome for degradation. Synthesizing the functional AZ protein requires transition of...
4.
Yokoyama T, Machida K, Iwasaki W, Shigeta T, Nishimoto M, Takahashi M, et al.
Mol Cell . 2019 May; 74(6):1205-1214.e8. PMID: 31080011
Translation initiation of hepatitis C virus (HCV) genomic RNA is induced by an internal ribosome entry site (IRES). Our cryoelectron microscopy (cryo-EM) analysis revealed that the HCV IRES binds to...
5.
Machida K, Shigeta T, Yamamoto Y, Ito T, Svitkin Y, Sonenberg N, et al.
Sci Rep . 2018 Nov; 8(1):17435. PMID: 30487538
Eukaryotic mRNA has a cap structure and a poly(A) tail at the 5' and 3' ends, respectively. The cap structure is recognized by eIF (eukaryotic translation initiation factor) 4 F,...
6.
Machida K, Kanzawa K, Shigeta T, Yamamoto Y, Tsumoto K, Imataka H
ACS Synth Biol . 2017 Dec; 7(2):377-383. PMID: 29232946
One of the aims of synthetic biology is bottom-up construction of reconstituted human cells for medical uses. To that end, we generated giant unilamellar vesicles (GUVs) that contained a HeLa...
7.
Machida K, Shigeta T, Kobayashi A, Masumoto A, Hidaka Y, Imataka H
J Biotechnol . 2016 Oct; 239:1-8. PMID: 27702574
Protein misfolding and aggregation is one of the major causes of neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease and Huntington's disease. So far protein aggregation related to these diseases...
8.
Kashiwagi K, Shigeta T, Imataka H, Ito T, Yokoyama S
J Struct Funct Genomics . 2016 Mar; 17(1):33-8. PMID: 27023709
Tight control of protein synthesis is necessary for cells to respond and adapt to environmental changes rapidly. Eukaryotic translation initiation factor (eIF) 2B, the guanine nucleotide exchange factor for eIF2,...
9.
Shigeta T, Zaizen Y, Sugimoto Y, Nakamura Y, Matsuo T, Okamoto S
J Plant Physiol . 2015 Mar; 178:69-73. PMID: 25778412
Brassinosteroids (BRs), a class of phytohormones, control various physiological and developmental processes in plants. Two highly homologous transcription factors, brassinosteroid insensitive 1-EMS-SUPRESSOR 1 (BES1) and brassinazole resistant 1 (BZR1), act...
10.
Shigeta T, Zaizen Y, Asami T, Yoshida S, Nakamura Y, Okamoto S, et al.
Plant Cell Rep . 2013 Dec; 33(3):499-510. PMID: 24374469
Key Message: A closer association of HSP90s with brassinosteroid signaling is suggested by the brassinosteroid-triggered formation of an HSP90-containing macromolecular complex and the direct interaction between HSP90.3 and BES1. Abstract:...