Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Xiaozhen TENG"'
Publikováno v:
Meitan xuebao, Vol 49, Iss 1, Pp 601-615 (2024)
During the coal mining process, the change in the floor stress state of coal seam will produce deformation and failure. The seam floor failure in different coal mining processes has a certain law. At present, the water disaster monitoring of coal sea
Externí odkaz:
https://doaj.org/article/01e02723a0944a9e81c2d0004401c18b
Publikováno v:
Sustainability (2071-1050); Dec2022, Vol. 14 Issue 24, p17011, 12p
Autor:
Yueyang Xu, Qionglin Zhang, Tingting Li, Xiaorui Lou, Xiaozhen Teng, Shanshan Li, Mark Bartlam
Publikováno v:
Biochemical and Biophysical Research Communications. 506:997-1003
Bacterial cyclic-di-GMP (c-di-GMP) is an important messenger molecule that influences diverse cellular processes including motility, virulence and cytotoxicity systems, polysaccharide synthesis and biofilm formation. The YfiBNR tripartite signalling
Publikováno v:
Biochemical and Biophysical Research Communications. 500:804-809
The C5 pathway in bacteria is responsible for the synthesis of 5-aminolevulinic acid, which forms the core skeleton of cofactors required for metabolism. One of the key actors in this pathway is a pyridoxamine-5'-phosphate (PMP)/pyridoxal-5'-phosphat
Autor:
Shanshan Li, Xiaorui Lou, Yueyang Xu, Xiaozhen Teng, Ruihua Liu, Qionglin Zhang, Weihui Wu, Yingying Wang, Mark Bartlam
Publikováno v:
The FEBS journalReferences. 286(24)
Alginate production in Pseudomonas aeruginosa is regulated by the alternate σ factor AlgU, which in turn is regulated by the MucABCD system. The anti-σ factor MucA binds AlgU in the cytoplasm and prevents AlgU from binding to the RNA polymerase for
Autor:
Mark Bartlam, Li Su, Yingying Wang, Qionglin Zhang, Tingting Li, Riuhua Liu, Yueyang Xu, Shanshan Li, Xiaozhen Teng, Guannan Mao
Publikováno v:
FEBS letters. 591(12)
To investigate the function of the pa4079 gene from the opportunistic pathogen Pseudomonas aeruginosa PAO1, we determined its crystal structure and confirmed it to be a NAD(P)-dependent short-chain dehydrogenase/reductase. Structural similarity and a