Výsledky vyhledávání - "Tomonori Mishima"

Reduction in contact resistance and structural evaluation of Al/Ti electrodes on Si-implanted GaN

Autor: Tohru Nakamura, Tomoaki Nishimura, Tomonori Mishima, Kazuo Kuriyama, Takeshi Kasai

Publikováno v: Nuclear Instruments and Methods in Physics Research Section B: Beam Interactions with Materials and Atoms. 450:244-247

We investigated the conditions of sample preparation for obtaining low contact resistance to Al/Ti electrode on n-GaN fabricated by Si implantation and analyzed its interface structure. In conditions of sample preparation showing the lowest resistanc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a74ccec8d15fe13e9b957850b9acd738
https://doi.org/10.1016/j.nimb.2018.09.001

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124 EFFECTIVENESS OF PREOPERATIVE TOTAL COLONOSCOPY AND COMPUTED TOMOGRAPHIC COLONOGRAPHY AFTER PLACEMENT OF A SELF-EXPANDABLE METALLIC STENT AS A BRIDGE TO SURGERY

Autor: Yorinobu Sumida, Eikichi Ihara, Tomonori Mishima, Naohiko Harada, Masafumi Wada, Makoto Nakamuta, Yoichiro Iboshi, Takashi Osoegawa, Hirotaka Turu

Publikováno v: Gastrointestinal Endoscopy. 87:AB56-AB57

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::95ed576f90b19b15767bd61694b63f86
https://doi.org/10.1016/j.gie.2018.04.036

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Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein

Autor: Masahiro Abe, Shigenobu Kanba, Yoshito Abe, Akira Monji, Tomonori Mishima, Tadashi Ueda, Takatoshi Ohkuri

Publikováno v: Protein Science. 22:467-474

Sugars, which function as osmolytes within cells, retard the amyloid fibril formation of the amyloidosis peptides and proteins. To examine the mechanism of this retardation in detail, we analyzed the effect of sugars (trehalose, sucrose, and glucose)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::593fc8c9061a36b55ec882464492835b
https://doi.org/10.1002/pro.2228

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Effects of His mutations on the fibrillation of amyloidogenic Vλ6 protein Wil under acidic and physiological conditions

Autor: Takaaki Kanemaru, Tadashi Ueda, Akira Monji, Yoshito Abe, Tomonori Mishima, Takatoshi Ohkuri

Publikováno v: Biochemical and Biophysical Research Communications. 391:615-620

Recently, we showed that the recombinant (r) Vlambda6 protein Wil exhibits a more disrupted residual structure and a longer lag time for fibril formation than the rVlambda6 protein Jto under highly unfolding conditions at pH 2. Here, we focused on th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e9e79e89efeccbbc78656fface56e65
https://doi.org/10.1016/j.bbrc.2009.11.108

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Analyses of Native Disulfide Bond Formations in the Early Stage of the Folding Process in Mutant Lysozymes Where the Long-Range Interactions in the Denatured State Were Modulated

Autor: Taiji Imoto, Tadashi Ueda, Tomonori Mishima, Takatoshi Ohkuri

Publikováno v: Bioscience, Biotechnology, and Biochemistry. 71:2072-2074

In order to clarify whether modulation of long-range interactions in the denatured state affect native disulfide bond (SS bond) formations of hen egg white lysozyme (HEL) containing a pair of cysteine residues, we examined the extent of SS bond forma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4074aa689bf7db1712b7093d128dde5c
https://doi.org/10.1271/bbb.70155

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Domain separation and characterization of PriC, a replication restart primosome factor in Escherichia coli

Autor: Takahiko Aramaki, Tsutomu Katayama, Shoji Yamashita, Tadashi Ueda, Tomonori Mishima, Yoshito Abe, Takatoshi Ohkuri

Publikováno v: Genes to cells : devoted to molecularcellular mechanisms. 18(9)

In Escherichia coli the oriC-independent primosome plays an essential role in replication restart after dissociation of the replication DNA–protein complex by DNA damage. Primosome is thought to form via two pathways: one PriA dependent and the oth

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc67e0c85d82e447f9e3711b49ff0097
https://pubmed.ncbi.nlm.nih.gov/23819889

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Residual structures in the acid-unfolded states of Vlambda6 proteins affect amyloid fibrillation

Autor: Takaaki Kanemaru, Akira Monji, Yoshito Abe, Takatoshi Ohkuri, Tadashi Ueda, Tomonori Mishima

Publikováno v: Journal of molecular biology. 392(4)

Many proteins form amyloid-like fibrils in vitro under partially or highly unfolding conditions. Recently, we showed that the residual structure in highly unfolded state is closely related to amyloid fibril formation in hen lysozyme. Thus, to better

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbe863f2f0c6233d5e0dc4de50af570a
https://pubmed.ncbi.nlm.nih.gov/19647748

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A particular hydrophobic cluster in the residual structure of reduced lysozyme drastically affects the amyloid fibrils formation

Autor: Taiji Imoto, Tomonori Mishima, Akira Monji, Tadashi Ueda, Takatoshi Ohkuri

Publikováno v: Biochemical and biophysical research communications. 356(3)

Six hydrophobic clusters involved in long-range interaction have been identified in the residual structure of reduced lysozyme at pH 2. Recently, it was found that modulation in the residual structure affected amyloid formation. In this paper, we exa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32b0c81e7379f5a0f005fdb626ba2e4f
https://pubmed.ncbi.nlm.nih.gov/17382294

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