Zobrazeno 1 - 10
of 158
pro vyhledávání: '"David S, Waugh"'
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:
Evgeny Kiselev, Yves Pommier, Xue Zhi Zhao, John S. Schneekloth, Terrence R. Burke, Wenjie Wang, David S. Waugh, D. Needle, Thomas A. Hilimire, Joseph E. Tropea, George T. Lountos
Publikováno v:
Chemical Science
Tyrosyl-DNA phosphodiesterase 1 (TDP1) is a member of the phospholipase D family of enzymes, which catalyzes the removal of both 3′- and 5′-DNA phosphodiester adducts. Importantly, it is capable of reducing the anticancer effects of type I topois
Autor:
Gyula Hoffka, George T. Lountos, Danielle Needle, Alexander Wlodawer, David S. Waugh, József Tőzsér, János András Mótyán
Publikováno v:
Journal of Molecular Biology. 435:168012
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:
Acta Crystallogr F Struct Biol Commun
Yersinia pestis, the causative agent of bubonic plague, is one of the most lethal pathogens in recorded human history. Today, the concern is the possible misuse ofY. pestisas an agent in bioweapons and bioterrorism. Current therapies for the treatmen
Autor:
Sreejith Raran-Kurussi, David S Waugh
Publikováno v:
PLoS ONE, Vol 7, Iss 11, p e49589 (2012)
Escherichia coli maltose binding protein (MBP) is commonly used to promote the solubility of its fusion partners. To investigate the mechanism of solubility enhancement by MBP, we compared the properties of MBP fusion proteins refolded in vitro with
Externí odkaz:
https://doaj.org/article/fc92b6c4c25644c19d01833f8fb1955d
Autor:
Teri L Kissner, Gordon Ruthel, Shahabuddin Alam, Enrique Mann, Dariush Ajami, Mitra Rebek, Eileen Larkin, Stefan Fernandez, Robert G Ulrich, Sun Ping, David S Waugh, Julius Rebek, Kamal U Saikh
Publikováno v:
PLoS ONE, Vol 7, Iss 7, p e40773 (2012)
Staphylococcal enterotoxin B (SEB) exposure triggers an exaggerated pro-inflammatory cytokine response that often leads to toxic shock syndrome (TSS) associated with organ failure and death. MyD88 mediates pro-inflammatory cytokine signaling induced
Externí odkaz:
https://doaj.org/article/50b5c0b07b3e4f4ea5ee96de78fc9670
Autor:
David S. Waugh, Sreejith Raran-Kurussi, Bryan M. Zhao, Robert G. Ulrich, Beverly Dyas, Terrence R. Burke, George T. Lountos
Publikováno v:
Acta Crystallographica Section D Structural Biology. 74:1015-1026
Here, new crystal structures are presented of the isolated membrane-proximal D1 and distal D2 domains of protein tyrosine phosphatase epsilon (PTP∊), a protein tyrosine phosphatase that has been shown to play a positive role in the survival of huma
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 74:549-557
The production of high-quality crystals is the main bottleneck in determining the structures of proteins using X-ray crystallography. In addition to being recognized as a very effective solubility-enhancing fusion partner,Escherichia colimaltose-bind
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,