Výsledky vyhledávání - "Takaki, Koide"

Spatiotemporal regulation of PEDF signaling by type I collagen remodeling

Autor: Takahiro Maruno, Yuji Kobayashi, Kazuki Kawahara, Takuya Yoshida, Hiroya Oki, Takaki Koide, Tadayasu Ohkubo

Publikováno v: Proc Natl Acad Sci U S A

Dynamic remodeling of the extracellular matrix affects many cellular processes, either directly or indirectly, through the regulation of soluble ligands; however, the mechanistic details of this process remain largely unknown. Here we propose that ty

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b09501c328d83abf0acc751b9756126
https://doi.org/10.1073/pnas.2004034117

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Synthetic Collagen-like Polymer That Undergoes a Sol–Gel Transition Triggered by O–N Acyl Migration at Physiological pH

Autor: Shinichiro F. Ichise, Takaki Koide

Publikováno v: International Journal of Molecular Sciences, Vol 23, Iss 1584, p 1584 (2022)
International Journal of Molecular Sciences; Volume 23; Issue 3; Pages: 1584

We previously reported an artificial collagen gel that can be used as a cell-culture substrate by end-to-end cross-linking of collagen-like triple-helical peptides via disulfide bonds. However, the gel had to be formed a priori by polymerizing the pe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::358cd26ee7a3f75b1976275081435895
https://www.mdpi.com/1422-0067/23/3/1584

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Synthetic Collagen-like Polymer That Undergoes a Sol-Gel Transition Triggered by

Autor: Shinichiro F, Ichise, Takaki, Koide

Publikováno v: International journal of molecular sciences. 23(3)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4cad6ffb4accc1a52636207b9ef64828
https://pubmed.ncbi.nlm.nih.gov/35163505

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A Strategy for Discovering Heterochiral Bioactive Peptides by Using the OB2 n P Library and SPOTs Method

Autor: Takato H. Yoneda, Hinako Udagawa, Ryo Masuda, Takaki Koide

Publikováno v: ChemBioChem. 20:2070-2073

d-Amino acid containing peptides are promising as drug lead compounds because of their expected higher stability in vivo. A heterochiral random peptide library called the one-bead-2n -peptide (OB2n P) library, which can display 2n peptide diastereome

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1a21e3281ed5576a3cea6bcbcd0f3581
https://doi.org/10.1002/cbic.201900237

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Peptide precursors that acquire denatured collagen-hybridizing ability by O-to-N acyl migration at physiological pH

Autor: Ryo Masuda, Sayaka Kanai, Takaki Koide, Koshi Machida

Publikováno v: Organicbiomolecular chemistry. 18(15)

Here, we report peptide probes with either single or cyclic double stranded collagen-like sequences that spontaneously acquire collagen-hybridizing ability at physiological pH. These peptides have ester bonds derived from O-acyl isopeptide units that

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62d4b88492785bb460204c2eee376e72
https://pubmed.ncbi.nlm.nih.gov/32232252

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The Thermal Stability of the Collagen Triple Helix Is Tuned According to the Environmental Temperature

Autor: Kazunori K. Fujii, Yuki Taga, Yusuke K. Takagi, Ryo Masuda, Shunji Hattori, Takaki Koide

Publikováno v: International Journal of Molecular Sciences; Volume 23; Issue 4; Pages: 2040

Triple helix formation of procollagen occurs in the endoplasmic reticulum (ER) where the single-stranded α-chains of procollagen undergo extensive post-translational modifications. The modifications include prolyl 4- and 3-hydroxylations, lysyl hydr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::143eae3f77494359d8813a8c36aede19
https://doi.org/10.3390/ijms23042040

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Akademický článek

NMR and mutational identification of the collagen-binding site of the chaperone Hsp47.

Autor: Maho Yagi-Utsumi, Sumi Yoshikawa, Yoshiki Yamaguchi, Yohei Nishi, Eiji Kurimoto, Yoshihito Ishida, Takayuki Homma, Jun Hoseki, Yoshimi Nishikawa, Takaki Koide, Kazuhiro Nagata, Koichi Kato

Publikováno v: PLoS ONE, Vol 7, Iss 9, p e45930 (2012)

Heat shock protein 47 (Hsp47) acts as a client-specific chaperone for collagen and plays a vital role in collagen maturation and the consequent embryonic development. In addition, this protein can be a potential target for the treatment of fibrosis.

Externí odkaz: https://doaj.org/article/5dae327d8d044f7b90243b47228b1f84

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Cyclic Peptides for Efficient Detection of Collagen

Autor: Kazunori K. Fujii, Koh K. Takita, Ryo Masuda, Tetsuya Kadonosono, Takaki Koide

Publikováno v: ChemBioChem. 19:1613-1617

We report here a new class of collagen-binding peptides, cyclic collagen-mimetic peptides (cCMPs), that efficiently hybridize with the triple-helix-forming portions of collagen. cCMPs are composed of two parallel collagen-like (Xaa-Yaa-Gly)n strands

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3c19ef5322d4a7109e50945f3f81684
https://doi.org/10.1002/cbic.201800166

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Development of a carboplatin derivative conjugated with a collagen-like triple-helical peptide

Autor: Risa Hayashi, Hiroshi Nose, Takaki Koide, Ryo Masuda, Akihiro Taguchi, Yoshio Hayashi, Hiroyuki Yasui

Publikováno v: Future Medicinal Chemistry. 10:619-629

Aim: The development of a platinum anticancer agent that has improved efficacy by efficient delivery to a tumor and that suppresses side effects has been investigated. Arginine-rich triple-helical peptides are promising drug carriers because of their

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9efb559fcd7c29df4b9f6c893144998b
https://doi.org/10.4155/fmc-2017-0183

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