Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Apinya Buranaprapuk"'
Publikováno v:
Journal of Photochemistry and Photobiology A: Chemistry. 436:114424
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d4b3f56407cbe9da3eb929a61f988d4c
https://doi.org/10.1016/j.jphotochem.2022.114424
https://doi.org/10.1016/j.jphotochem.2022.114424
Autor:
Siritron Samosorn, Challa V. Kumar, Apinya Buranaprapuk, Mayuso Kuno, Teerayuth Liwporncharoenvong, Sudarat Yenjai
Publikováno v:
Journal of Photochemistry and Photobiology B: Biology. 186:23-30
Rational design of photoreagents with systematic modifications of their structures can provide valuable information for a better understanding of the protein photocleavage mechanism by these reagents. Variation of the length of the linker connecting
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f1e457558f20a9c3d39c04c779c91bc
https://doi.org/10.1016/j.jphotobiol.2018.07.001
https://doi.org/10.1016/j.jphotobiol.2018.07.001
Autor:
Apinya Buranaprapuk, Teerayuth Liwporncharoenvong, Sudarat Yenjai, Mayuso Kuno, Siritron Samosorn
Publikováno v:
Journal of Photochemistry and Photobiology B: Biology. 173:35-42
A new photochemical reagent, succinic acid-1(1-pyrene)methylamide (PMA-SUC), was developed to recognize the specific binding sites on model proteins, egg-white lysozyme and avidin. The interaction of the photochemical reagent with the proteins was st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f556ab6b67516d1883e9cc51368be3a4
https://doi.org/10.1016/j.jphotobiol.2017.05.029
https://doi.org/10.1016/j.jphotobiol.2017.05.029
Autor:
Dhanya T. Jayaram, Bobbi S. Stromer, Sudarat Yenjai, Melissa R. Limbacher, Apinya Buranaprapuk, Ruma Chowdhury, Challa V. Kumar, Danaboyina Ramaiah
Publikováno v:
Journal of Photochemistry and Photobiology A: Chemistry. 340:181-200
A powerful strategy to photocleave the protein backbone at a single site, developed over nearly two decades, is described here. The remarkable ability to target one or even a couple of sites on a large protein with a small molecule, under photochemic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::09d51681550a36b6d9801149cf4ac8d3
https://doi.org/10.1016/j.jphotochem.2017.01.027
https://doi.org/10.1016/j.jphotochem.2017.01.027
Autor:
Challa Kumar, Apinya Buranaprapuk
The remarkable ability to target one or even a couple of sites on a large protein with a small molecule, under photochemical control, is a considerable challenge and this challenge has been addressed in some depth in this book. Systematic modificatio
Publikováno v:
Inorganic Chemistry Communications. 55:129-131
Three molybdenum(VI) peroxo α-amino acid complexes, MoO(O2)2(α-aa) (H2O) (aa = leucine, glutamine and glycine), were prepared and used as artificial proteases for site-specific cleavage of porcine pepsin. The reaction was activated by incubation of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1ad984e0aa48eb7ea30e24df9787e436
https://doi.org/10.1016/j.inoche.2015.03.037
https://doi.org/10.1016/j.inoche.2015.03.037
Publikováno v:
Journal of Photochemistry and Photobiology B: Biology. 126:55-59
In this study, a molybdenum(VI) peroxo a-amino acid complex, MoO(O2)2(a-leucine) (H2O), was prepared and used as an artificial protease for site-specific cleavage of porcine pepsin, a model protein. Cleavage of pepsin by MoO(O2)2(a-leucine) (H2O) was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9eee1e40e4bb5d4e6332f12db7734d53
https://doi.org/10.1016/j.jphotobiol.2013.07.004
https://doi.org/10.1016/j.jphotobiol.2013.07.004
Publikováno v:
Biochemical and Biophysical Research Communications. 419:126-129
Graphical abstract: Molybdenum metallopeptidase: the Mo(VI) cluster with six molybdenum cations has the ability to cleave protein under mild conditions (37 Degree-Sign C, pH 7) without reducing agents. The reaction required only low concentration of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cad6e2faec6fb724e1969d101f5562a0
https://doi.org/10.1016/j.bbrc.2012.01.147
https://doi.org/10.1016/j.bbrc.2012.01.147
Publikováno v:
The Journal of Physical Chemistry B. 112:9258-9265
Strong chiral discrimination and site-selective photocleavage of two model proteins, lysozyme and bovine serum albumin (BSA), by new pyrenyl probes are reported here. The enantiomeric pyrenyl probes D-phenylalanine-1(1-pyrene)methylamide (PMA- D-Phe)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c25bbf1efa7e48198d5e13675293ce4
https://doi.org/10.1021/jp802791c
https://doi.org/10.1021/jp802791c