Zobrazeno 1 - 10
of 119
pro vyhledávání: '"Hidenari, Takahara"'
Autor:
Mizuki Sawata, Hiroki Shima, Kazutaka Murayama, Toshitaka Matsui, Kazuhiko Igarashi, Kazumasa Funabashi, Kenji Ite, Kenji Kizawa, Hidenari Takahara, Masaki Unno
Publikováno v:
ACS Omega. 7:28378-28387
Autor:
Méchin, Marie-Claire1 marie-claire.mechin@inserm.fr, Hidenari Takahara2 hidenari86ta@msn.com, Simon, Michel1 michel.simon@inserm.fr
Publikováno v:
International Journal of Molecular Sciences. 1/15/2020, Vol. 21 Issue 2, p1-15. 15p. 4 Diagrams, 2 Charts.
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, MDPI, 2020, 21 (2), pp.566. ⟨10.3390/ijms21020566⟩
International Journal of Molecular Sciences, Vol 21, Iss 2, p 566 (2020)
International Journal of Molecular Sciences, 2020, 21 (2), pp.566. ⟨10.3390/ijms21020566⟩
International Journal of Molecular Sciences, MDPI, 2020, 21 (2), pp.566. ⟨10.3390/ijms21020566⟩
International Journal of Molecular Sciences, Vol 21, Iss 2, p 566 (2020)
International Journal of Molecular Sciences, 2020, 21 (2), pp.566. ⟨10.3390/ijms21020566⟩
International audience; Deimination, also known as citrullination, corresponds to the conversion of the amino acid arginine, within a peptide sequence, into the non-standard amino acid citrulline. This post-translational modification is catalyzed by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d426e953ccb2bd8b6e2833328c6dbfd
https://hal-univ-tlse3.archives-ouvertes.fr/hal-03153570
https://hal-univ-tlse3.archives-ouvertes.fr/hal-03153570
Autor:
Stéphane Chavanas, Véronique Adoue, Marie-Claire Méchin, Shibo Ying, Sijun Dong, Hélène Duplan, Marie Charveron, Hidenari Takahara, Guy Serre, Michel Simon
Publikováno v:
PLoS ONE, Vol 3, Iss 10, p e3408 (2008)
Transcription control at a distance is a critical mechanism, particularly for contiguous genes. The peptidylarginine deiminases (PADs) catalyse the conversion of protein-bound arginine into citrulline (deimination), a critical reaction in the pathoph
Externí odkaz:
https://doaj.org/article/09991c18c5b3478fab826f14e0cc398c
Autor:
Masaki Unno, Kenji Ite, Anna Nagai, Megumi Akimoto, Paul R. Thompson, Kenichi Kitanishi, Kazumasa Funabashi, Mizuki Sawata, Ryutaro Mashimo, Kenji Kizawa, Hidenari Takahara
Publikováno v:
Archives of Biochemistry and Biophysics. 708:108911
Peptidylarginine deiminase type III (PAD3) is an isozyme belonging to the PAD enzyme family that converts arginine to citrulline residue(s) within proteins. PAD3 is expressed in most differentiated keratinocytes of the epidermis and hair follicles, w
Autor:
Anna Nagai, Nobutaka Shimizu, Toshiki Yabe-Wada, Saya Kinjo, Ryutaro Mashimo, Kenji Kizawa, Hidenari Takahara, Masaki Unno, Shinya Saijo, Megumi Akimoto
Publikováno v:
Proceedings of the 3rd International Symposium of Quantum Beam Science at Ibaraki University "Quantum Beam Science in Biology and Soft Materials (ISQBSS2018)".
Publikováno v:
Journal of Investigative Dermatology
Journal of Investigative Dermatology, 2019, 139 (9), pp.1889-1897.e4. ⟨10.1016/j.jid.2019.02.026⟩
Journal of Investigative Dermatology, Nature Publishing Group, 2019, 139 (9), pp.1889-1897.e4. ⟨10.1016/j.jid.2019.02.026⟩
J Invest Dermatol
Journal of Investigative Dermatology, 2019, 139 (9), pp.1889-1897.e4. ⟨10.1016/j.jid.2019.02.026⟩
Journal of Investigative Dermatology, Nature Publishing Group, 2019, 139 (9), pp.1889-1897.e4. ⟨10.1016/j.jid.2019.02.026⟩
J Invest Dermatol
International audience; Deimination, a post-translational modification catalyzed by a family of enzymes called peptidylarginine deiminases (PADs), is the conversion of arginine into citrulline residues in a protein. Deimination has been associated wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93f9749a5b19b13328a286eb478c2584
https://ut3-toulouseinp.hal.science/hal-03156447/document
https://ut3-toulouseinp.hal.science/hal-03156447/document
Autor:
Emeline Lhuillier, Hidenari Takahara, Paul R. Thompson, Guy Serre, Valérie Pendaries, Michel Simon, Marie-Claire Méchin, Laura Cau
Publikováno v:
Journal of Dermatological Science
Journal of Dermatological Science, 2017, 86 (2), pp.106-113. ⟨10.1016/j.jdermsci.2017.02.280⟩
Journal of Dermatological Science, Elsevier, 2017, 86 (2), pp.106-113. ⟨10.1016/j.jdermsci.2017.02.280⟩
Journal of Dermatological Science, 2017, 86 (2), pp.106-113. ⟨10.1016/j.jdermsci.2017.02.280⟩
Journal of Dermatological Science, Elsevier, 2017, 86 (2), pp.106-113. ⟨10.1016/j.jdermsci.2017.02.280⟩
International audience; Background: Deimination (also known as citrullination), the conversion of arginine in a protein to citrulline, is catalyzed by a family of enzymes called peptidylarginine deiminases (PADs). Three PADs are expressed in the epid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3329a089f3a3ec98ecd7c2067a086df
https://ut3-toulouseinp.hal.science/hal-03156353
https://ut3-toulouseinp.hal.science/hal-03156353
Autor:
Hidenari Takahara
Publikováno v:
Protein Deimination in Human Health and Disease ISBN: 9783319582436
The research on protein deimination and the enzymes responsible for catalyzing this posttranslational modification started from investigations of the hair follicle and myelin in central nerve system. About 60 years ago, in 1958, the presence of prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d81252c98b04b1121e782738bae6e364
https://doi.org/10.1007/978-3-319-58244-3_1
https://doi.org/10.1007/978-3-319-58244-3_1
Publikováno v:
Protein Deimination in Human Health and Disease ISBN: 9783319582436
Molecular structures of peptidylarginine deiminase (PAD) isozymes are strongly associated with their functions. This chapter summarizes the X-ray structures of PAD1, PAD2, and PAD4 as well as that of the PAD from the periodontal pathogen Porphyromona
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3018bd0f3af6f6b4822255b7fc9505d3
https://doi.org/10.1007/978-3-319-58244-3_3
https://doi.org/10.1007/978-3-319-58244-3_3