Zobrazeno 1 - 10
of 72
pro vyhledávání: '"Shigeyoshi NAKAMURA"'
Autor:
Shigeyoshi NAKAMURA, Siti Aisyah MOKHTAR, Misuzu OKADA, Hideaki ABURATANI, Shinya SENBA, Makoto ICHITSUBO
Publikováno v:
Journal of JSEE. 71:3_71-3_77
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f90f5e4c13285281a2b0d39ed4b958b5
https://doi.org/10.4307/jsee.71.3_71
https://doi.org/10.4307/jsee.71.3_71
Publikováno v:
Biochemistry. 59(39)
Protein amorphous aggregation has become the focus of great attention, as it can impair the ability of cells to function properly. Here, we evaluated the effects of three peptide tags, consisting of one, three, and five consecutive isoleucines attach
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9811aad9cfb0d7cbfea6ebda45b300a
https://pubmed.ncbi.nlm.nih.gov/32924442
https://pubmed.ncbi.nlm.nih.gov/32924442
Autor:
Shigeyoshi Nakamura, Akiko Nakazawa, Masao Fukuda, Yutaka Kuroda, Tomonori Saotome, Shun-ichi Kidokoro
Publikováno v:
Biochemistry. 56:2372-2378
In this study, we performed differential scanning calorimetry (DSC) and pressure perturbation calorimetry (PPC) analysis of the thermal transition of cytochrome c from an acidic molten globule (MG) state with the protein concentrations of 0.5–18.2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6d57d5ff28e2ad4b5e82b970c1a2ee4
https://doi.org/10.1021/acs.biochem.6b01225
https://doi.org/10.1021/acs.biochem.6b01225
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1964
The recent development of high-precision calorimeters allows us to monitor the structural transition of biomolecules by calorimetry and thereby characterize the thermodynamic property changes accompanying three-dimensional structure changes. We devel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8b5378225d41c6bab151a3c3aeb0aeea
https://pubmed.ncbi.nlm.nih.gov/30929232
https://pubmed.ncbi.nlm.nih.gov/30929232
Publikováno v:
Methods in Molecular Biology ISBN: 9781493991785
The recent development of high-precision calorimeters allows us to monitor the structural transition of biomolecules by calorimetry and thereby characterize the thermodynamic property changes accompanying three-dimensional structure changes. We devel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3cef4c7eee67100141abaabd4444dffd
https://doi.org/10.1007/978-1-4939-9179-2_2
https://doi.org/10.1007/978-1-4939-9179-2_2
Autor:
Shigeyoshi NAKAMURA, Siti Aisyah MOKHTAR, Misuzu OKADA, Kei MIURA, Yoshihiko MUTO, Makoto ICHITSUBO
Publikováno v:
Journal of JSEE. 69:6_122-6_127
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::13d04805f0751a72811dd2ae6f7541fb
https://doi.org/10.4307/jsee.69.6_122
https://doi.org/10.4307/jsee.69.6_122
Autor:
Hideki Wakui, Mika Yonezawa, Tatsufumi Goto, Mizuki Nakagawa, Kotomi Sugawara, Wataru Nunomura, Shigeyoshi Nakamura, Shun-ichi Kidokoro
Publikováno v:
Journal of Biochemistry. 160:299-308
It is widely believed that enzymatic activities in ectothermic organisms adapt to environmental temperatures. However, to date, no study has thoroughly compared multiple thermodynamic enzymatic characteristics across species living in dramatically di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51b3f48580665b5da1348e94823d7be2
https://doi.org/10.1093/jb/mvw039
https://doi.org/10.1093/jb/mvw039
Autor:
Mika Yonezawa, Wataru Nunomura, Shun-ichi Kidokoro, Hideki Wakui, Kotomi Sugawara, Mizuki Nakagawa, Shigeyoshi Nakamura
Publikováno v:
Fisheries Science. 82:519-527
Vertebrates have three genes (LDHA, LDHB, and LDHC) encoding skeletal muscle-, heart muscle- and testis-specific lactate dehydrogenase (LDH, E.C. 1.1.1.27), respectively. The muscle and heart LDHs are tetramers formed by polypeptides encoded by LDHA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ac82f2dde2bbafe9a1a31c19d121c04f
https://doi.org/10.1007/s12562-016-0972-1
https://doi.org/10.1007/s12562-016-0972-1
Autor:
Kuakarun Krusong, Yui Takahashi, Jarunee Kaulpiboon, Shun-ichi Kidokoro, Shigeyoshi Nakamura, Piriya Kaewpathomsri, Shuichiro Murakami, Piamsook Pongsawasdi
Publikováno v:
Process Biochemistry. 50:1814-1824
Amylomaltase catalyzes the α-1,4 glycosyl transfer between oligosaccharides. The amylomaltase gene from Thermus filiformis JCM11600 (TfAM) was cloned, expressed in Escherichia coli and purified to homogeneity. TfAM, a member of glycoside hydrolase f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4a781e471aa6c2019a7e44b7c06a22d7
https://doi.org/10.1016/j.procbio.2015.08.006
https://doi.org/10.1016/j.procbio.2015.08.006
Autor:
Shigeyoshi Nakamura, Keiichi Noguchi, Shun-ichi Kidokoro, Yutaka Kuroda, Masafumi Yohda, Mohammad Monirul Islam
Publikováno v:
Crystal Growth & Design. 15:2703-2711
Short peptide tags attached to recombinant proteins are emerging as an important tool for biochemical research. Here, we report the effects of 10 Solubilization Controlling Peptide (SCP) tags on crystallization behavior of a bovine pancreatic trypsin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ded6b8aa93589b0a0dc857f93bd65e36
https://doi.org/10.1021/acs.cgd.5b00010
https://doi.org/10.1021/acs.cgd.5b00010