Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Yasuyuki Shitomi"'
Autor:
Kumi Hidaka, Tomoko Emura, Saisei Honna, Hiroshi Sugiyama, Yasuyuki Shitomi, Yihong Feng, Takeshi Tohgasaki, Masayuki Endo
Publikováno v:
Bioconjugate Chemistry. 30:1860-1863
We report a nanosized DNA capsule with a photoinducible mechanical unlocking system for creation of a carrier for delivery system to the cells. A photocage system was introduced into the nanocapsule (NC) for control of opening of the NC with photoirr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87f41591f383630de2f5724889755c23
https://doi.org/10.1021/acs.bioconjchem.9b00040
https://doi.org/10.1021/acs.bioconjchem.9b00040
Publikováno v:
Methods in enzymology. 641
It is important to create new, specifically designed and controlled nanomaterials that can be used as molecular delivery systems for cells. Here, we describe a method for creating a nanosized DNA capsule (NC) using a photocaged unlocking system as a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d04976835d391dbfc7ebdaf1d5c47eaf
https://pubmed.ncbi.nlm.nih.gov/32713528
https://pubmed.ncbi.nlm.nih.gov/32713528
Publikováno v:
Methods in Enzymology ISBN: 9780128211564
It is important to create new, specifically designed and controlled nanomaterials that can be used as molecular delivery systems for cells. Here, we describe a method for creating a nanosized DNA capsule (NC) using a photocaged unlocking system as a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9bdd3c6936814d9b59bb237c93eaa0b8
https://doi.org/10.1016/bs.mie.2020.04.045
https://doi.org/10.1016/bs.mie.2020.04.045
Autor:
Yasuyuki Shitomi, Anna M. Woskowicz, Brit Wolters, Kazuyo Kaneko, Motoharu Seiki, Noriko Ito, Sarah A. Weaver, Yoshifumi Itoh
Publikováno v:
Journal of Cell Science
The membrane-anchored collagenase membrane type 1 matrix metalloprotease (MT1-MMP) has been shown to play an essential role during epithelial tubulogenesis in 3D collagen matrices; however, its regulation during tubulogenesis is not understood. Here,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e7ec04f44decee1d6f84d017348da937
http://europepmc.org/articles/PMC4117704
http://europepmc.org/articles/PMC4117704
Localization of membrane type I matrix metalloproteinase (MT1-MMP) to the leading edge is thought to be a crucial step during cancer cell invasion. However, its mechanisms and functional impact on cellular invasion have not been clearly defined. In t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34b18dd79c0f3a5685a82bb5fb4c6ae2
https://doi.org/10.1074/jbc.m113.496067
https://doi.org/10.1074/jbc.m113.496067
Autor:
Kazuhiro, Yamamoto, Hiroshi, Okano, Wakako, Miyagawa, Robert, Visse, Yasuyuki, Shitomi, Salvatore, Santamaria, Jayesh, Dudhia, Linda, Troeberg, Dudley K, Strickland, Satoshi, Hirohata, Hideaki, Nagase
Publikováno v:
Matrix Biology
Matrix metalloproteinase 13 (MMP-13) degrades collagenous extracellular matrix and its aberrant activity associates with diseases such as arthritis, cancer, atherosclerosis and fibrosis. The wide range of MMP-13 proteolytic capacity suggests that it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::22869ae97fca0c0580b028f999ea31ea
https://pubmed.ncbi.nlm.nih.gov/27084377
https://pubmed.ncbi.nlm.nih.gov/27084377
Autor:
Anna Tochowicz, Klaus Richter, Hideaki Nagase, Wolfram Bode, Robert Visse, Klaus Maskos, Richard Evans, Peter Goettig, Noriko Ito, Yoshifumi Itoh, Daniel Franke, Ralf Palmisano, Yasuyuki Shitomi, Dmitri I. Svergun
Publikováno v:
The journal of biological chemistry 286, 7587-7600 (2011). doi:10.1074/jbc.M110.178434
The Journal of Biological Chemistry
The Journal of Biological Chemistry
Homodimerization is an essential step for membrane type 1 matrix metalloproteinase (MT1-MMP) to activate proMMP-2 and to degrade collagen on the cell surface. To uncover the molecular basis of the hemopexin (Hpx) domain-driven dimerization of MT1-MMP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::326609ab62d10c9d41e7d089cdcb19c8
https://doi.org/10.1074/jbc.m110.178434
https://doi.org/10.1074/jbc.m110.178434
Autor:
Yasuyuki Shitomi, Ganesh N. Pandian, Kohsuke Haginoya, Masaaki Azuma, Hidetaka Hori, Chanan Angsuthanasombat, Vaijayanthi Thangavel, Kazuya Tomimoto
Publikováno v:
Applied Entomology and Zoology. 45:477-488
Liposome was prepared using phosphatidylcholine (PC), and calcein, a fluorescent chemical, was simultaneously enclosed within the liposome (PC-Lipo). The stability of PC-Lipo in its ability to retain calcein was evaluated under various conditions. PC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f061aaca3d89fa1ebeb5fc6565d078a4
https://doi.org/10.1303/aez.2010.477
https://doi.org/10.1303/aez.2010.477
Autor:
Hidetaka Hori, Ryoichi Sato, Delwar Hossain, Kimiko Itoh, Yasuyuki Shitomi, Toshiaki Mitsui, Tohru Hayakawa
Publikováno v:
Pesticide Biochemistry and Physiology. 87:30-38
We analyzed the binding of the Bacillus thuringiensis insecticidal toxins, CrylAa, CrylAb and CrylAc, to midgut tissue of the silkworm, Bombyx mori with ligand blot analysis and histochemical observations. CrylAa, CrylAb and CrylAc bound to unique se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::30ee285cfe2652abca66301a57064807
https://doi.org/10.1016/j.pestbp.2006.01.011
https://doi.org/10.1016/j.pestbp.2006.01.011
Autor:
Tohru Hayakawa, Kazuhisa Miyamoto, Masahiro Higuchi, Ryoichi Sato, Yasuyuki Shitomi, Kazuko Nakanishi, Delwar Hossain, Hidetaka Hori
Publikováno v:
The Journal of Biochemistry. 139:223-233
Proteins in the brush border membrane (BBM) of the midgut binding to the insecticidal Cry1Ac toxin from Bacillus thuringiensis were investigated to examine the lower sensitivity of Bombyx mori to Cry1Ac, and new aminopeptidase N that bound to Cry1Ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e034e43fb3b7535ed8e8f6f08d4aac7a
https://doi.org/10.1093/jb/mvj024
https://doi.org/10.1093/jb/mvj024