Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Yapei Tong"'
Publikováno v:
BBA Advances, Vol 4, Iss , Pp 100097- (2023)
In recent years, studies have shown that a large number of bacteria secrete multi-flavinylated proteins. The exact roles and properties, of these extracellular flavoproteins that contain multiple covalently anchored FMN cofactors, are still largely u
Externí odkaz:
https://doaj.org/article/47bacea9a7bd4e00836afb0201bd2f67
Autor:
Yapei Tong
Site-specific protein labeling plays a core role in investigating protein function at molecular level. A multitude of protein labelling techniques has been developed which are based on chemical and/or enzymatic methods. Enzyme-based labeling of prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df7a56be62085be1476368e176ad825d
https://research.rug.nl/en/publications/c6b8f56e-35a4-42ec-8a8a-21ba5205eb5a
https://research.rug.nl/en/publications/c6b8f56e-35a4-42ec-8a8a-21ba5205eb5a
Publikováno v:
BIOCONJUGATE CHEMISTRY, 32(8), 1559-1563. AMER CHEMICAL SOC
Site-specific protein labeling methods are highly valuable tools for research and applications. We present a new protein labeling method that allows covalent attachment of a chromo-and fluorogenic flavin (FMN) to any targeted protein using a short fl
Publikováno v:
ChemBioChem, 23(11):e202200144. WILEY-V C H VERLAG GMBH
Methods for facile site-selective modifications of proteins are in high demand. We have recently shown that a flavin transferase can be used for site-specific covalent attachment of a chromo- and fluorogenic flavin (FMN) to any targeted protein. Alth
Publikováno v:
The Journal of Biological Chemistry, 295(47), 16013-16022. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
J Biol Chem
Journal of Biological Chemistry 295 (2020) 47
Journal of Biological Chemistry, 295(47), 16013-16022
J Biol Chem
Journal of Biological Chemistry 295 (2020) 47
Journal of Biological Chemistry, 295(47), 16013-16022
Fungal bioluminescence was recently shown to depend on a unique oxygen-dependent system of several enzymes. However, the identities of the enzymes did not reveal the full biochemical details of this process, as the enzymes do not bear resemblance to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b42915ad2c9ff76579956aeb7c8fa84e
https://research.rug.nl/en/publications/741c2e3d-0420-468b-b3a4-eb4d15024d8a
https://research.rug.nl/en/publications/741c2e3d-0420-468b-b3a4-eb4d15024d8a
Autor:
Yapei Tong1, Trajkovic, Milos1, Savino, Simone1, van Berkel, Willem J. H.2, Fraaije, Marco W.1 m.w.fraaije@rug.nl
Publikováno v:
Journal of Biological Chemistry. 11/20/2020, Vol. 295 Issue 47, p16013-16022. 10p.