ofstaphylococcus aureus
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2019 ◽  
Vol 16 (5) ◽  
pp. 317-324 ◽  
Author(s):  
Qiuxia Fan ◽  
Chunhong Yan ◽  
Chao Shi ◽  
Yunfeng Xu ◽  
Yan Ma ◽  
...  


2019 ◽  
Vol 366 (4) ◽  
Author(s):  
Jialin Yi ◽  
Yuelin Zhang ◽  
Wenshu Lin ◽  
Bing Niu ◽  
Qin Chen


2019 ◽  
Vol 28 (2) ◽  
pp. 161-168 ◽  
Author(s):  
Carine Mainzer ◽  
Thomas Packard ◽  
Sylvie Bordes ◽  
Brigitte Closs ◽  
Warner C. Greene ◽  
...  


2019 ◽  
Vol 21 (3) ◽  
pp. e12997 ◽  
Author(s):  
Adriana Moldovan ◽  
Martin J. Fraunholz


2019 ◽  
Vol 11 (29) ◽  
pp. 3665-3670 ◽  
Author(s):  
Yun Zhang ◽  
Wenqing Tan ◽  
Lin Zhang ◽  
Shuyou Shi ◽  
Yuna Niu ◽  
...  

Utilization of chicken anti-protein A IgY as an antibody pair for sensitive and selective detection ofS. aureus.



The Analyst ◽  
2019 ◽  
Vol 144 (13) ◽  
pp. 3999-4005 ◽  
Author(s):  
Chandan Hunsur Ravikumar ◽  
Manjunath Ira Gowda ◽  
R. Geetha Balakrishna

mAb-Strep-QDs-GO probe in an OFF state due to energy transfer from QDs to GO turns into an ON state when the energy transfer is inhibited by MNase, thus allowing the sensing of MNase (Micrococcal Nuclease, an extracellular endonuclease ofStaphylococcus Aureus).



2018 ◽  
Vol 61 (23) ◽  
pp. 10651-10664 ◽  
Author(s):  
Trent Kunkle ◽  
Sanofar Abdeen ◽  
Nilshad Salim ◽  
Anne-Marie Ray ◽  
Mckayla Stevens ◽  
...  


2018 ◽  
Author(s):  
Ian R. Monk ◽  
Nausad Shaikh ◽  
Stephanie L. Begg ◽  
Mike Gajdiss ◽  
Jean Y. H. Lee ◽  
...  

ABSTRACTWalKR (YycFG) is the only essential two-component regulator in the human pathogenStaphylococcus aureus.WalKR regulates peptidoglycan synthesis, but this function alone appears not to explain its essentiality. To understand WalKR function we investigated a suppressor mutant that arose when WalKR activity was impaired; a single histidine to tryptophan substitution (H271Y) in the cytoplasmic Per-Arnt-Sim (PASCYT) domain of the histidine kinase WalK. Introduction of the WalKH271Ymutation into wild-typeS.aureusactivated the WalKR regulon. Structural analyses of the WalK PASCYTdomain revealed a hitherto unknown metal binding site, in which a zinc ion (Zn2+) was tetrahedrally-coordinated by four amino acid residues including H271. The WallkH271Ymutation abrogated metal binding, increasing WalK kinase activity and WalR phosphorylation. Thus, Zn2+-binding negatively regulates WalKR activity. Identification of a metal ligand sensed by the WalKR system substantially expands our understanding of this criticalS.aureusregulon.



2018 ◽  
Vol 94 (4) ◽  
pp. 735-746 ◽  
Author(s):  
Felix Wolter ◽  
Jeannette Klemm ◽  
Holger Puchta


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