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of 10
pro vyhledávání: '"Naoto Iwakawa"'
Autor:
Naoto Iwakawa, Daichi Morimoto, Erik Walinda, Yasushi Kawata, Masahiro Shirakawa, Kenji Sugase
Publikováno v:
International Journal of Molecular Sciences, Vol 18, Iss 11, p 2271 (2017)
Amyloid fibril formation is associated with numerous neurodegenerative diseases. To elucidate the mechanism of fibril formation, the thioflavin T (ThT) fluorescence assay is widely used. ThT is a fluorescent dye that selectively binds to amyloid fibr
Externí odkaz:
https://doaj.org/article/5cb908077f604a74929e4132aea5a073
Autor:
Kenji Sugase, Masahiro Shirakawa, Daichi Morimoto, Erik Walinda, Sarah Leeb, Jens Danielsson, Naoto Iwakawa
Publikováno v:
The Journal of Physical Chemistry B. 125:2521-2532
Aggregate formation of superoxide dismutase 1 (SOD1) inside motor neurons is known as a major factor in onset of amyotrophic lateral sclerosis. The thermodynamic stability of the SOD1 β-barrel has been shown to decrease in crowded environments such
Publikováno v:
Journal of the American Chemical Society. 143(28)
Formation of protein aggregates or fibrils entails the conversion of soluble native protein monomers via multiple molecular states. No spectroscopic techniques have succeeded in capturing the transient molecular-scale events of fibrillation in situ.
Autor:
Nicola J. Baxter, Rodrigo A.V. Morales, Naoto Iwakawa, Kenji Sugase, Michael P. Williamson, Dorothy C.C. Wai, Nicholas J. Fowler, Raymond S. Norton
Publikováno v:
Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-8 (2019)
Scientific Reports, Vol 9, Iss 1, Pp 1-8 (2019)
ShK is a 35-residue disulfide-linked polypeptide produced by the sea anemone Stichodactyla helianthus, which blocks the potassium channels Kv1.1 and Kv1.3 with pM affinity. An analogue of ShK has been developed that blocks Kv1.3 > 100 times more pote
Autor:
Kenji Sugase, Ulrich Scheler, Daichi Morimoto, Masahiro Shirakawa, Akihiko Yamamoto, Yasushi Kawata, Erik Walinda, Mayu Nishizawa, Naoto Iwakawa
Publikováno v:
Analytical Chemistry. 89:7286-7290
Shear stress can induce structural deformation of proteins, which might result in aggregate formation. Rheo-NMR spectroscopy has the potential to monitor structural changes in proteins under shear stress at the atomic level; however, existing Rheo-NM
Publikováno v:
Biomolecular NMR Assignments. 11:81-84
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease that leads to movement disorders. In motor neurons of ALS patients, intracellular aggregates of superoxide dismutase 1 (SOD1) have often been observed. To elucidate the aggregat
Autor:
Kenji Sugase, Naoki Ishii, Masahiro Shirakawa, Kazuhiro Iwai, Naoto Iwakawa, Erik Walinda, Daichi Morimoto
Publikováno v:
Biomolecular NMR assignments. 13(1)
Nuclear factor-κB (NF-κB) activation plays a central role in immunity and inflammation. In the canonical NF-κB activation pathway, linear polyubiquitin chains conjugated by the linear ubiquitin chain assembly complex (LUBAC) are specifically recog
Autor:
Arina Ono, Kenji Sugase, Naoto Iwakawa, Izuru Ohki, Masahiro Shirakawa, Daichi Morimoto, Yutaka Mahana, Erik Walinda
Publikováno v:
Biomolecular NMR assignments. 13(1)
Epigenetic regulation is essential to various biological phenomena such as cell differentiation and cancer. DNA methylation is one of the most important epigenetic signals, as it is directly involved in gene silencing of transposable elements, genomi
Autor:
Kenji Sugase, Naoto Iwakawa, Erik Walinda, Masahiro Shirakawa, Daichi Morimoto, Yasushi Kawata
Publikováno v:
International Journal of Molecular Sciences; Volume 18; Issue 11; Pages: 2271
International Journal of Molecular Sciences, Vol 18, Iss 11, p 2271 (2017)
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 18, Iss 11, p 2271 (2017)
International Journal of Molecular Sciences
Amyloid fibril formation is associated with numerous neurodegenerative diseases. To elucidate the mechanism of fibril formation, the thioflavin T (ThT) fluorescence assay is widely used. ThT is a fluorescent dye that selectively binds to amyloid fibr
Autor:
Daichi Morimoto, Walinda, Erik, Naoto Iwakawa, Mayu Nishizawa, Yasushi Kawata, Akihiko Yamamoto, Masahiro Shirakawa, Scheler, Ulrich, Sugase, Kenji
Publikováno v:
Analytical Chemistry; 7/18/2017, Vol. 89 Issue 14, p7286-7290, 5p