Zobrazeno 1 - 10
of 195
pro vyhledávání: '"Kunihiko, Gekko"'
Autor:
Kunihiko Gekko
Publikováno v:
Biophysics and Physicobiology, Vol 16 (2019)
Circular dichroism spectroscopy is widely used for analyzing the structures of chiral molecules, including biomolecules. Vacuum-ultraviolet circular dichroism (VUVCD) spectroscopy using synchrotron radiation can extend the short-wavelength limit into
Externí odkaz:
https://doaj.org/article/e926cca232bd4cc6b5894214d17c861f
Publikováno v:
Chirality. 32:594-604
α1-Acid glycoprotein (AGP) interacts with lipid membranes as a peripheral membrane protein so as to decrease the drug-binding capacity accompanying the β→α conformational change that is considered a protein-mediated uptake mechanism for releasin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbc3d04cce8de6b015798aeae5d8ebb1
https://doi.org/10.1002/chir.23208
https://doi.org/10.1002/chir.23208
Autor:
Mária Pukáncsik, Ágnes Orbán, Kinga Nagy, Koichi Matsuo, Kunihiko Gekko, Damien Maurin, Darren Hart, István Kézsmárki, Beata G Vertessy
Publikováno v:
PLoS ONE, Vol 11, Iss 6, p e0156238 (2016)
A novel uracil-DNA degrading protein factor (termed UDE) was identified in Drosophila melanogaster with no significant structural and functional homology to other uracil-DNA binding or processing factors. Determination of the 3D structure of UDE is e
Externí odkaz:
https://doaj.org/article/d4469a43c8ff4c39bc0ef5351046aefa
Publikováno v:
International Journal of Alzheimer's Disease, Vol 2011 (2011)
Clusters of GM1 gangliosides act as platforms for conformational transition of monomeric, unstructured amyloid β (Aβ) to its toxic β-structured aggregates. We have previously shown that Aβ(1–40) accommodated on the hydrophobic/hydrophilic inter
Externí odkaz:
https://doaj.org/article/0f2e7529eb5f40b28c05c9c7923f7398
Autor:
Koichi Matsuo, Kunihiko Gekko
Publikováno v:
The journal of physical chemistry. A. 124(4)
Vacuum ultraviolet (VUV) electronic circular dichroism (ECD) spectra of d-glucose, α-d-glucopyranose, and β-d-glucopyranose were measured in aqueous solution down to 163 nm using a synchrotron radiation VUV-ECD spectrophotometer and theoretically a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::954597ecf1d8ebf010d18e9b163c9397
https://pubmed.ncbi.nlm.nih.gov/31906622
https://pubmed.ncbi.nlm.nih.gov/31906622
Publikováno v:
ChiralityREFERENCES. 32(5)
α
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::315f10ca6cf2c2acacddfc6ff80ffe95
https://pubmed.ncbi.nlm.nih.gov/32125028
https://pubmed.ncbi.nlm.nih.gov/32125028
Autor:
Motonori Matsusaki, Akiho Hirose, Keiichi Kono, Reiko Urade, Kunihiko Gekko, Koichi Matsuo, Aya Okuda, Taro Masuda, Yuichiro Tsuchi, Yurika Naruo
Publikováno v:
J Biol Chem
In the endoplasmic reticulum (ER), ER oxidoreductin 1 (ERO1) catalyzes intramolecular disulfide-bond formation within its substrates in coordination with protein-disulfide isomerase (PDI) and related enzymes. However, the molecular mechanisms that re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd588efd05942626fc3604e4bf6c98ea
https://europepmc.org/articles/PMC6901294/
https://europepmc.org/articles/PMC6901294/
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 84:349-359
Knowledge of the conformations of a water-soluble protein bound to a membrane is important for understanding the membrane-interaction mechanisms and the membrane-mediated functions of the protein. In this study we applied vacuum-ultraviolet circular-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0f5a0a15ba966bef0f118318021c2fec
https://doi.org/10.1002/prot.24981
https://doi.org/10.1002/prot.24981
Autor:
Kunihiko Gekko, Koichi Matsuo
Publikováno v:
Methods in Molecular Biology ISBN: 9781493995110
Methods in Molecular Biology ISBN: 9781627032742
Methods in Molecular Biology ISBN: 9781627032742
Circular-dichroism (CD) spectroscopy is a powerful tool for the secondary-structure analysis of proteins. The structural information obtained by CD does not have atomic-level resolution (unlike X-ray crystallography and NMR spectroscopy), but it has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::992f0408ce88f1f746e44e59f103e863
https://doi.org/10.1007/978-1-4939-9512-7_12
https://doi.org/10.1007/978-1-4939-9512-7_12
Autor:
Koichi, Matsuo, Kunihiko, Gekko
Publikováno v:
Advances in experimental medicine and biology. 1104
Circular-dichroism (CD) spectroscopy is a powerful tool for analyzing the structures of chiral molecules and biomolecules. The development of CD instruments using synchrotron radiation has greatly expanded the utility of this method by extending the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::42a6a3e3203abae519d7ca898d7755f2
https://pubmed.ncbi.nlm.nih.gov/30484246
https://pubmed.ncbi.nlm.nih.gov/30484246