Zobrazeno 1 - 10
of 81
pro vyhledávání: '"Hatsuho Uedaira"'
Autor:
Hidetoshi Kono, M. Michael Gromiha, Ponraj Prabakaran, Akinori Sarai, Hatsuho Uedaira, Samuel Selvaraj, Jianghong An
Publikováno v:
Bioinformatics. 17:1027-1034
Motivation: Protein–nucleic acid interactions are fundamental to the regulation of gene expression. In order to elucidate the molecular mechanism of protein–nucleic acid recognition and analyze the gene regulation network, not only structural dat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::344be5c4856a273f0e39a6483ab491bb
https://doi.org/10.1093/bioinformatics/17.11.1027
https://doi.org/10.1093/bioinformatics/17.11.1027
Publikováno v:
Bulletin of the Chemical Society of Japan. 74:1857-1861
The spin-lattice relaxation times, T1, of H217O have been measured for aqueous solutions of glucose and galactose derivatives, which are substituents of the 2-OH or 6-OH of these sugars, as a function of the concentration at 25 °C. The values of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6b4fe30f946f363abff012b38fe3e161
https://doi.org/10.1246/bcsj.74.1857
https://doi.org/10.1246/bcsj.74.1857
Autor:
Samuel Selvaraj, Hidetoshi Kono, Motohisa Oobatake, Akinori Sarai, Hatsuho Uedaira, Jianghong An, Ponraj Prabakaran, M. Michael Gromiha
Publikováno v:
Biopolymers. 61:121-126
Thermodynamic data regarding proteins and their interactions are important for understanding the mechanisms of protein folding, protein stability, and molecular recognition. Although there are several structural databases available for proteins and t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3cbbc8e34c3688a8e3f38ddb2ea70c63
https://doi.org/10.1002/1097-0282(2002)61:2<121::aid-bip10077>3.0.co
https://doi.org/10.1002/1097-0282(2002)61:2<121::aid-bip10077>3.0.co
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 18:281-295
For understanding the factors influencing protein stability, we have analyzed the relationship between changes in protein stability caused by partially buried mutations and changes in 48 physico-chemical, energetic and conformational properties of am
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab7f723c2c0ccfcd9f793a820f908f66
https://doi.org/10.1080/07391102.2000.10506666
https://doi.org/10.1080/07391102.2000.10506666
Autor:
Akinori Sarai, Hisayuki Morii, Kazuhiro Ogata, Hidetoshi Kono, Tahir H. Tahirov, Hatsuho Uedaira, Minoru Saito
Publikováno v:
Scopus-Elsevier
The stabilization of proteins due to cavity-filling mutations are thought to be attributable to removal of hydrophobic residues from solvent exposure in denatured (D) state and formation of close packing in native (N) state. However, it is still uncl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d1e634bce27369927e84fb02fed3eb3
https://doi.org/10.1021/jp991717f
https://doi.org/10.1021/jp991717f
Publikováno v:
Journal of Molecular Biology. 293:719-732
Thermodynamic investigations of flagellin from Salmonella typhimurium and its proteolytic fragments were conducted by differential scanning calorimetry (DSC) and circular dichroism (CD) melting measurements. A new method of analysis for a multi-state
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6fdd2dd68fe46cd18b4d527a3fac24e4
https://doi.org/10.1006/jmbi.1999.3175
https://doi.org/10.1006/jmbi.1999.3175
Publikováno v:
Journal of Molecular Biology. 292:909-920
The shape and the energetics of a functional cavity in the R2 subdomain (90-141) of the c-Myb DNA-binding domain were investigated by spectroscopy and thermodynamic analysis. We focused on the valine 103 residue located in front of the cavity. Nine m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c014df29cd44e7bcc909da1d3a86ea4b
https://doi.org/10.1006/jmbi.1999.3099
https://doi.org/10.1006/jmbi.1999.3099
Autor:
Hatsuho Uedaira, Hisayuki Morii, Keiichi Namba, Hisaaki Taniguchi, Miyuki Ishimura, Ferenc Vonderviszt
Publikováno v:
FEBS Letters. 445:126-130
Hook forms a universal joint, which mediates the torque of the flagellar motor to the outer helical filaments. Domain organization of hook protein from Salmonella typhimurium was investigated by exploring thermal denaturation properties of its proteo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff64bfdc41361306e0bb88c326225f6f
https://doi.org/10.1016/s0014-5793(99)00110-6
https://doi.org/10.1016/s0014-5793(99)00110-6
Autor:
Yukio Furukawa, Katsumi Imada, Hatsuho Uedaira, Ferenc Vonderviszt, Keiichi Namba, Hisaaki Taniguchi
Publikováno v:
Journal of Molecular Biology. 284:1399-1416
HAP2 forms a capping structure, which binds very tightly to the distal end of flagellar filaments and still allows insertion of flagellin subunits below the cap by an unknown mechanism. Terminal regions of HAP2 from Salmonella typhimurium were found
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::934754171249088b3f2c11b15317e439
https://doi.org/10.1006/jmbi.1998.2274
https://doi.org/10.1006/jmbi.1998.2274
Publikováno v:
Pure and Applied Chemistry. 70:671-676
The DNA binding domain of c-Myb protein, a regulator of the transcription, consists of three homologous tandem repeats (Rl, R2 and R3) with 51-52 amino acid residues. Previously, we found that the thermal transition of the binding domain (RlR2R3) is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b157cd2390c88ccdbfc1f947daad0dee
https://doi.org/10.1351/pac199870030671
https://doi.org/10.1351/pac199870030671