Výsledky vyhledávání - "Yoshifumi Takahara"

Specific Recognition of the Collagen Triple Helix by Chaperone HSP47

Autor: Yoshimi Nishikawa, Chisato M. Yamazaki, Takaki Koide, Daisuke L. Homma, Nobutaka Wakamiya, Yoshifumi Takahara, Kazuhiro Nagata, Shinichi Asada, Katsuki Ohtani, Akira Otaka, Kouki Kitagawa

Publikováno v: Journal of Biological Chemistry. 281:11177-11185

The endoplasmic reticulum-resident chaperone heat-shock protein 47 (HSP47) plays an essential role in procollagen biosynthesis. The function of HSP47 relies on its specific interaction with correctly folded triple-helical regions comprised of Gly-Xaa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::73ab16393cd67095b5f8006afa15c6b0
https://doi.org/10.1074/jbc.m601369200

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Specific Recognition of the Collagen Triple Helix by Chaperone HSP47

Autor: Takaki Koide, Yoshifumi Takahara, Shinichi Asada, Kazuhiro Nagata, Yoshimi Nishikawa, Kouki Kitagawa

Publikováno v: Journal of Biological Chemistry. 281:3432-3438

The unique folding of procollagens in the endoplasmic reticulum is achieved with the assistance of procollagen-specific molecular chaperones. Heat-shock protein 47 (HSP47) is an endoplasmic reticulum-resident chaperone that plays an essential role in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0859bf34155a892f46a465cd103b1849
https://doi.org/10.1074/jbc.m509707200

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Xaa-Arg-Gly Triplets in the Collagen Triple Helix Are Dominant Binding Sites for the Molecular Chaperone HSP47

Autor: Yoshifumi Takahara, Shinichi Asada, Kazuhiro Nagata, Takaki Koide

Publikováno v: Journal of Biological Chemistry. 277:6178-6182

HSP47 is an essential procollagen-specific molecular chaperone that resides in the endoplasmic reticulum of procollagen-producing cells. Recent advances have revealed that HSP47 recognizes the (Pro-Pro-Gly)(n) sequence but not (Pro-Hyp-Gly)(n) and th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cc96e0e6efce196e121294461464f80
https://doi.org/10.1074/jbc.m106497200

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Specific recognition of the collagen triple helix by chaperone HSP47. II. The HSP47-binding structural motif in collagens and related proteins

Autor: Takaki, Koide, Yoshimi, Nishikawa, Shinichi, Asada, Chisato M, Yamazaki, Yoshifumi, Takahara, Daisuke L, Homma, Akira, Otaka, Katsuki, Ohtani, Nobutaka, Wakamiya, Kazuhiro, Nagata, Kouki, Kitagawa

Publikováno v: The Journal of biological chemistry. 281(16)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6541e5dfc8e196dd5fd6c011b784460d
https://pubmed.ncbi.nlm.nih.gov/16484215

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Specific recognition of the collagen triple helix by chaperone HSP47: minimal structural requirement and spatial molecular orientation

Autor: Takaki, Koide, Shinichi, Asada, Yoshifumi, Takahara, Yoshimi, Nishikawa, Kazuhiro, Nagata, Kouki, Kitagawa

Publikováno v: The Journal of biological chemistry. 281(6)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::93e3a67777a50e6ad191c621a4a79aa0
https://pubmed.ncbi.nlm.nih.gov/16326708

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Synthesis of heterotrimeric collagen models containing Arg residues in Y-positions and analysis of their conformational stability

Autor: Yoshifumi Takahara, Yoshimi Nishikawa, Takaki Koide

Publikováno v: Bioorganicmedicinal chemistry letters. 14(1)

An Arg residue incorporated into the Y-position of collagenous host–guest peptide Ac-(Gly-Pro-Hyp) 3 -Gly-Pro-Y-(Gly-Pro-Hyp) 4 -Gly-Gly-NH 2 is reported to stabilize the triple helical structure as well as a 4( R )-hydroxyproline (Hyp) residue. He

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0da5fcb14bbdc2ebc795ce6881f4b151
https://pubmed.ncbi.nlm.nih.gov/14684312

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