Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Mayu S. Terakawa"'
Autor:
Rachel T. Wragg, Daniel A. Parisotto, Zhenlong Li, Mayu S. Terakawa, David Snead, Ishani Basu, Harel Weinstein, David Eliezer, Jeremy S. Dittman
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 10 (2017)
Complexin is a critical presynaptic protein that regulates both spontaneous and calcium-triggered neurotransmitter release in all synapses. Although the SNARE-binding central helix of complexin is highly conserved and required for all known complexin
Externí odkaz:
https://doaj.org/article/174876fb8cbf45609c725d3f6df9d11d
Autor:
Emily M. Grasso, Mayu S. Terakawa, Alex L. Lai, Ying Xue Xie, Trudy F. Ramlall, Jack H. Freed, David Eliezer
Publikováno v:
Journal of Molecular Biology. 435:167710
Complexins play a critical role in regulating SNARE-mediated exocytosis of synaptic vesicles. Evolutionary divergences in complexin function have complicated our understanding of the role these proteins play in inhibiting the spontaneous fusion of ve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c1c99ae51acc03b2adf04fe28ba03e4
https://doi.org/10.1016/j.jmb.2022.167710
https://doi.org/10.1016/j.jmb.2022.167710
Autor:
Yuxi Lin, Naoya Fukui, Mayu S. Terakawa, Toshihiko Sugiki, Yuji Goto, Young-Ho Lee, Yasushi Kawata, Misaki Kinoshita, Tatsuya Ikenoue
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1860:757-766
Amyloid fibrillation causes serious neurodegenerative diseases and amyloidosis; however, the detailed mechanisms by which the structural states of precursor proteins in a lipid membrane-associated environment contribute to amyloidogenesis still remai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25b82ab9d1e4831fbd3df7d695987e9d
https://doi.org/10.1016/j.bbamem.2017.12.011
https://doi.org/10.1016/j.bbamem.2017.12.011
Autor:
Yuxi Lin, Misaki Kinoshita, Mayu S. Terakawa, Yuji Goto, Erina Kakimoto, Ayyalusamy Ramamoorthy, Tatsuya Ikenoue, Masatomo So, Young-Ho Lee, Toshihiko Sugiki
Publikováno v:
Physical Chemistry Chemical Physics. 19:16257-16266
We herein report the mechanism of amyloid formation of amyloid-β (Aβ) peptides on small (SUV) and large unilamellar vesicles (LUVs), which consist of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) lipids. Although Aβ1–42 formed fibrils
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9da9b63deda86149c9bad8891a7d0aa5
https://doi.org/10.1039/c6cp07774a
https://doi.org/10.1039/c6cp07774a
Autor:
Ayyalusamy Ramamoorthy, Dai Itoh, Toshihiko Sugiki, Masaki Okumura, Yuxi Lin, Shingo Kanemura, Misaki Kinoshita, Young-Ho Lee, Mayu S. Terakawa
The misfolding, amyloid aggregation, and fibril formation of intrinsically disordered proteins/peptides (or amyloid proteins) have been shown to cause a number of disorders. The underlying mechanisms of amyloid fibrillation and structural properties
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::853241c1306170c8a9aee25e0d3cc508
https://europepmc.org/articles/PMC6205921/
https://europepmc.org/articles/PMC6205921/
Publikováno v:
The Journal of biological chemistry. 290(2)
This research was originally published in the Journal of Biological Chemistry. Mayu S. Terakawa, Hisashi Yagi, Masayuki Adachi, Young-Ho Lee and Yuji Goto. Small Liposomes Accelerate the Fibrillation of Amyloid β (1–40). J. Biol. Chem. 2015; 290,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17fcf9f839c3216ec45ba2d4a1679dee
https://pubmed.ncbi.nlm.nih.gov/25406316
https://pubmed.ncbi.nlm.nih.gov/25406316
Autor:
Mayu S. Terakawa
Publikováno v:
Biophysical Journal. 108:65a
The deposition of amyloid β (Aβ) peptides is a pathological hallmark of Alzheimer's disease. Aβ peptides were previously considered to interact specifically with ganglioside-containing membranes. However, several studies have suggested that Aβ pe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ec3396420b1b230cb2311ac7f909374
https://doi.org/10.1016/j.bpj.2014.11.388
https://doi.org/10.1016/j.bpj.2014.11.388