Zobrazeno 1 - 10
of 60
pro vyhledávání: '"Scott, Cherry"'
Publikováno v:
Current Research in Structural Biology, Vol 5, Iss , Pp 100095- (2023)
Dihydroneopterin aldolase (DHNA) is essential for folate biosynthesis in microorganisms. Without a counterpart in mammals, DHNA is an attractive target for antimicrobial agents. Helicobacter pylori infection occurs in human stomach of over 50% of the
Externí odkaz:
https://doaj.org/article/60527449d7c541a6b156266368e98bd5
Autor:
Istvan Botos, George T. Lountos, Weimin Wu, Scott Cherry, Rodolfo Ghirlando, Arsen M. Kudzhaev, Tatyana V. Rotanova, Natalia de Val, Joseph E. Tropea, Alla Gustchina, Alexander Wlodawer
Publikováno v:
Current Research in Structural Biology, Vol 1, Iss , Pp 13-20 (2019)
Energy-dependent Lon proteases play a key role in cellular regulation by degrading short-lived regulatory proteins and misfolded proteins in the cell. The structure of the catalytically inactive S679A mutant of Escherichia coli LonA protease (EcLon)
Externí odkaz:
https://doaj.org/article/3a4bafe2973a426e8039983c811a2c88
Autor:
Lesley-Ann Giddings, George T Lountos, Kang Woo Kim, Matthew Brockley, Danielle Needle, Scott Cherry, Joseph E Tropea, David S Waugh
Publikováno v:
PLoS ONE, Vol 16, Iss 3, p e0248385 (2021)
N-hydroxylating flavin-dependent monooxygenases (FMOs) are involved in the biosynthesis of hydroxamate siderophores, playing a key role in microbial virulence. Herein, we report the first structural and kinetic characterization of a novel alkyl diami
Externí odkaz:
https://doaj.org/article/37885d7357e34f33bcf53c3a5a1c0417
Autor:
Alla, Gustchina, Mi, Li, Anna G, Andrianova, Arsen M, Kudzhaev, George T, Lountos, Bartosz, Sekula, Scott, Cherry, Joseph E, Tropea, Ivan V, Smirnov, Alexander, Wlodawer, Tatyana V, Rotanova
Publikováno v:
International journal of molecular sciences. 23(19)
ATP-dependent Lon proteases are key participants in the quality control system that supports the homeostasis of the cellular proteome. Based on their unique structural and biochemical properties, Lon proteases have been assigned in the MEROPS databas
Publikováno v:
Journal of structural biology. 214(4)
C/EBPβ is a key regulator of numerous cellular processes, but it can also contribute to tumorigenesis and viral diseases. It binds to specific DNA sequences (C/EBP sites) and interacts with other transcription factors to control expression of multip
Autor:
Bryan M Zhao, Sarah L Keasey, Joseph E Tropea, George T Lountos, Beverly K Dyas, Scott Cherry, Sreejith Raran-Kurussi, David S Waugh, Robert G Ulrich
Publikováno v:
PLoS ONE, Vol 10, Iss 8, p e0134984 (2015)
Protein tyrosine phosphatases dephosphorylate tyrosine residues of proteins, whereas, dual specificity phosphatases (DUSPs) are a subgroup of protein tyrosine phosphatases that dephosphorylate not only Tyr(P) residue, but also the Ser(P) and Thr(P) r
Externí odkaz:
https://doaj.org/article/f687ef066e5f4c6595a050a153f0b35c
Publikováno v:
BJPsych Bulletin
Autor:
A. M. Kudzhaev, Alexander Wlodawer, Weimin Wu, Rodolfo Ghirlando, Alla Gustchina, T. V. Rotanova, Joseph E. Tropea, George T. Lountos, Scott Cherry, Istvan Botos, Natalia de Val
Publikováno v:
Current Research in Structural Biology
Current Research in Structural Biology, Vol 1, Iss, Pp 13-20 (2019)
Current Research in Structural Biology, Vol 1, Iss, Pp 13-20 (2019)
Energy-dependent Lon proteases play a key role in cellular regulation by degrading short-lived regulatory proteins and misfolded proteins in the cell. The structure of the catalytically inactive S679A mutant of Escherichia coli LonA protease (EcLon)
Autor:
Scott Cherry
Publikováno v:
Forum: Qualitative Social Research, Vol 9, Iss 2 (2008)
Various domains of inquiry have engaged a shift to the concept of performativity as an organising principle for how forms of life are performatively brought into being. What appears surprising is that this move towards a performatively emergent world
Externí odkaz:
https://doaj.org/article/50e5676b5c574e9b9e1be6447478e746
Autor:
Joseph E. Tropea, Rajesh Gumpena, George T. Lountos, Scott Cherry, Sreejith Raran-Kurussi, David S. Waugh
Publikováno v:
Protein Science. 27:561-567
The dual specificity phosphatase DUSP1 was the first mitogen activated protein kinase phosphatase (MKP) to be identified. It dephosphorylates conserved tyrosine and threonine residues in the activation loops of mitogen activated protein kinases ERK2,