Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Gen-ichiro Uechi"'
Publikováno v:
Nucleic Acids Research
The tRNA modification m1G37, introduced by the tRNA methyltransferase TrmD, is thought to be essential for growth in bacteria because it suppresses translational frameshift errors at proline codons. However, because bacteria can tolerate high levels
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84a10e3bee2201123728cfc349e9c9aa
https://doi.org/10.1093/nar/gkab1067
https://doi.org/10.1093/nar/gkab1067
Publikováno v:
Proceedings of the National Academy of Sciences. 119
Nucleobase-containing coenzymes are considered the relics of an early RNA-based world that preceded the emergence of protein domains. Despite the importance of coenzyme-protein synergisms, their emergence and evolution remain poorly understood. An ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6ffa7757fd592c3415d2cd0a00dcbd2
https://doi.org/10.1073/pnas.2207965119
https://doi.org/10.1073/pnas.2207965119
The tRNA modification m1G37, which is introduced by the tRNA methyltransferase TrmD, is thought to be essential for growth in bacteria due to its role in suppressing translational frameshift errors at proline codons. However, because bacteria can tol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c300e60215ef64e83c1daf19f6a7598a
https://doi.org/10.1101/2021.07.14.452415
https://doi.org/10.1101/2021.07.14.452415
Autor:
Giorgio Giardina, Davide Chiasserini, Mirco Dindo, Stefano Pascarelli, Silvia Grottelli, Paola Laurino, Gen-Ichiro Uechi, Claudio Costantini, Barbara Cellini
Genetic variations expand the conformational landscape of proteins and may underlie cryptic functions able to influence protein adaptability under unfavorable conditions. Cryptic functions usually associate with regions of increased frustration or ev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b51eebaea674d285452c8166a1c71ca6
https://doi.org/10.1101/2021.05.24.445519
https://doi.org/10.1101/2021.05.24.445519
Autor:
Mirco Dindo, Stefano Pascarelli, Davide Chiasserini, Silvia Grottelli, Claudio Costantini, Gen‐Ichiro Uechi, Giorgio Giardina, Paola Laurino, Barbara Cellini
Publikováno v:
Protein Science. 31(5):e4303
The conformational landscape of a protein is constantly expanded by genetic variations that have a minimal impact on the function(s) while causing subtle effects on protein structure. The wider the conformational space sampled by these variants, the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::196591061ae0f17a238ced10a31e8fbc
http://id.nii.ac.jp/1394/00002381/
http://id.nii.ac.jp/1394/00002381/
Publikováno v:
The Journal of Biological Chemistry
The epidermal growth factor receptor (EGFR) is a membrane-anchored tyrosine kinase that is able to selectively respond to multiple extracellular stimuli. Previous studies have indicated that the modularity of this system may be caused by ligand-induc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::190996a7c2ff7509097b7342c43d5e13
http://id.nii.ac.jp/1394/00001986/
http://id.nii.ac.jp/1394/00001986/
The Epidermal Growth Factor Receptor (EGFR) is a membrane-anchored tyrosine kinase that is able to selectively respond to multiple extra-cellular stimuli. Previous studies have indicated that the modularity of this system is affected by ligand-induce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e9b822fa12b5708a04c058590abecbaf
https://doi.org/10.1101/677393
https://doi.org/10.1101/677393
Autor:
Le Quynh Mai, Kinuyo Ozaki, Etsuro Ono, Toshiyo Yabuta, Hiroki Takakuwa, Gen Ichiro Uechi, Toshihiro Ito, Yoshikazu Fujimoto, Masami Morimatsu, Haruka Suyama, Yukiko Tomioka, Koichi Otsuki, Tetsu Yamashiro, Sayo Yamamoto
Publikováno v:
The Journal of general virology. 97(9)
The nucleoprotein (NP) possesses regions that are highly conserved among influenza A viruses, and has therefore been one of the target viral proteins for development of a universal influenza vaccine. It has been expected that human or humanized antib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd669915b187ffa7f36b592c369652d2
https://pubmed.ncbi.nlm.nih.gov/27260213
https://pubmed.ncbi.nlm.nih.gov/27260213
Publikováno v:
The Protein Journal. 30(6):422-428
The sea anemone Actineria villosa expresses a lethal protein toxin. We isolated a novel 120-kDa protein, Avt120, from partially purified toxin and found it to possess extremely strong lethal activity. The 3,453-bp Avt120 gene translates to a 995-amin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1ef8afcc6ca8be3fadda7e9ae85f676
http://hdl.handle.net/10069/25469
http://hdl.handle.net/10069/25469
Publikováno v:
Toxicon : official journal of the International Society on Toxinology. 56(8):1470-1476
We recently identified the existence of new isoforms of Avt-I (from sea anemone Actineria villosa) and Pstx20 (from sea anemone Phyllodiscus semoni) hemolytic toxins, and named them Avt-II and Pst-I. Avt-II and Pst-I differ in length by 14 and 7bp, r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::329f277c62bceba609802512b6b9a077
http://hdl.handle.net/10069/24835
http://hdl.handle.net/10069/24835