Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Thilini Abeywansha"'
Autor:
Xin Lan, Wei Huang, Su Bin Kim, Dechen Fu, Thilini Abeywansha, Jiemin Lou, Udayakumaran Balamurugan, Yong Tae Kwon, Chang Hoon Ji, Derek J. Taylor, Yi Zhang
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract The arginyl-transferase ATE1 is a tRNA-dependent enzyme that covalently attaches an arginine molecule to a protein substrate. Conserved from yeast to humans, ATE1 deficiency in mice correlates with defects in cardiovascular development and a
Externí odkaz:
https://doaj.org/article/21fd2c37adcb4c90b6c019346c342c39
Autor:
Thilini Abeywansha, Wei Huang, Xuan Ye, Allison Nawrocki, Xin Lan, Eckhard Jankowsky, Derek J. Taylor, Yi Zhang
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-12 (2023)
Abstract Arginyl-tRNA-protein transferase 1 (ATE1) is a master regulator of protein homeostasis, stress response, cytoskeleton maintenance, and cell migration. The diverse functions of ATE1 arise from its unique enzymatic activity to covalently attac
Externí odkaz:
https://doaj.org/article/bd567ad855694ce5bcdeca9731c3b665
Publikováno v:
Antibiotics, Vol 10, Iss 7, p 830 (2021)
The RND family efflux pump AcrAB-TolC in E. coli and its homologs in other Gram-negative bacteria are major players in conferring multidrug resistance to the cells. While the structure of the pump complex has been elucidated with ever-increasing reso
Externí odkaz:
https://doaj.org/article/b054900998f74d2399989046764be77c
Publikováno v:
Antibiotics
Volume 10
Issue 7
Antibiotics, Vol 10, Iss 830, p 830 (2021)
Volume 10
Issue 7
Antibiotics, Vol 10, Iss 830, p 830 (2021)
The RND family efflux pump AcrAB-TolC in E. coli and its homologs in other Gram-negative bacteria are major players in conferring multidrug resistance to the cells. While the structure of the pump complex has been elucidated with ever-increasing reso
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27e786f5e8ec35a15914fbc18e56b038
https://doi.org/10.3390/antibiotics10070830
https://doi.org/10.3390/antibiotics10070830
Publikováno v:
Biochemistry. 57(38)
The AAA+ protease ClpXP has long been established as the cellular rescue system that degrades ssrA-tagged proteins resulting from stalled ribosomes. Until recently, in all of these studies soluble proteins were used as model substrates, since the Clp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::081e8927d4225eac23e286b28f073cbf
https://pubmed.ncbi.nlm.nih.gov/30169015
https://pubmed.ncbi.nlm.nih.gov/30169015
Autor:
Lan, Xin, Huang, Wei, Kim, Su Bin, Fu, Dechen, Abeywansha, Thilini, Lou, Jiemin, Balamurugan, Udayakumaran, Kwon, Yong Tae, Ji, Chang Hoon, Taylor, Derek J., Zhang, Yi
Publikováno v:
Nature Communications; 7/28/2024, Vol. 15 Issue 1, p1-14, 14p
Autor:
Abeywansha, Thilini, Huang, Wei, Ye, Xuan, Nawrocki, Allison, Lan, Xin, Jankowsky, Eckhard, Taylor, Derek J., Zhang, Yi
Publikováno v:
Nature Communications; 4/19/2023, Vol. 14 Issue 1, p1-12, 12p
Autor:
Rajapaksha, Prasangi, Ojo, Isoiza, Yang, Ling, Pandeya, Ankit, Abeywansha, Thilini, Wei, Yinan
Publikováno v:
Antibiotics (2079-6382); Jul2021, Vol. 10 Issue 7, p830, 1p
Autor:
Abeywansha, Thilini
ClpXP is an Escherichia coli protease that carries out energy-dependent intracellular proteolysis. In recent years, this system has been widely studied due to its importance as protein regulatory machinery and a virulence factor. Protein substrates o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a35a410aaae5bbd0af13100b4b97531
