Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Hosam E. Ewis"'
Nonclassical Protein Secretion by Bacillus subtilis in the Stationary Phase Is Not Due to Cell Lysis
Autor:
Xiao-Zhou Zhang, Hae-Jin Hu, Hosam E. Ewis, Ahmed T. Abdelal, Chung-Dar Lu, Yi Pan, Chun-Kai Yang, Phang C. Tai
Publikováno v:
Journal of Bacteriology. 193:5607-5615
The carboxylesterase Est55 has been cloned and expressed in Bacillus subtilis strains. Est55, which lacks a classical, cleavable N-terminal signal sequence, was found to be secreted during the stationary phase of growth such that there is more Est55
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63:1003-1007
The sodA gene of Bacillus subtilis was expressed in Escherichia coli, purified and crystallized. The crystal structure of MnSOD was solved by molecular replacement with four dimers per asymmetric unit and refined to an R factor of 21.1% at 1.8 A reso
Autor:
Hosam E. Ewis, Chung-Dar Lu
Publikováno v:
FEMS Microbiology Letters. 253:295-301
When over-expressed in the cytoplasm of Escherichia coli, carboxylesterase Est55 of Geobacillus stearothermophilus was found to be released from cells upon osmotic shock. Comparing two osmotic shock protocols showed that release of Est55 was abolishe
Several mammalian carboxylesterases were shown to activate the prodrug irinotecan (CPT-11) to produce 7-ethyl-10-hydroxycamptothecin (SN-38), a topoisomerase inhibitor used in cancer therapy. However, the potential use of bacterial carboxylesterases,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4adac4806731fb941e44efa23983236
https://europepmc.org/articles/PMC1950602/
https://europepmc.org/articles/PMC1950602/
Autor:
Irene T. Weber, Yuan-Fang Wang, Robert W. Harrison, Chung-Dar Lu, Ping Liu, Ahmed T. Abdelal, Hosam E. Ewis
Publikováno v:
Journal of molecular biology. 342(2)
Est30 is a thermophilic carboxylesterase cloned from Geobacillus stearothermophilus that showed optimal hydrolysis of esters with short acyl chains at 70 degrees C. Est30 is a member of a new family of carboxylesterases with representatives in other
Publikováno v:
Gene. 329
Screening of the genomic libraries of Geobacillus stearothermophilus ATCC12980 and ATCC7954 for esterase/lipase activity led to the isolation of two positive clones. The results of subclonings and sequence analyses identified two genes, est30 and est
A genomic library from a strain of Salmonella enterica serovar Paratyphi B that exhibits multiple drug resistance (MDR) was constructed in Escherichia coli . Two of the recombinant plasmids, pNOR5 and pNOR5, conferred resistance only to fluoroquinolo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::102fa670e65aa29712816aecf6d5c4d9
https://europepmc.org/articles/PMC127067/
https://europepmc.org/articles/PMC127067/
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 59:1472-1473
Crystals have been grown of the carboxylesterase Est30 from Bacillus stearothermophilus by hanging-drop vapor diffusion using ammonium sulfate as precipitant. The crystals diffracted to better than 2.0 A resolution. X-ray diffraction data were reduce