Results 11 to 20 of about 752,160 (359)

Recombinant protein expression in Escherichia coli: advances and challenges

open access: yesFrontiers in Microbiology, 2014
Escherichia coli is the organism of choice for the production of recombinant proteins. Its use as a cell factory is well-established and it has become the most popular expression platform.
Germán Leandro Rosano   +3 more
doaj   +3 more sources

Mutant MotB proteins in Escherichia coli [PDF]

open access: yesJournal of Bacteriology, 1991
The MotB protein of Escherichia coli is an essential component in each of eight torque generators in the flagellar rotary motor. Based on its membrane topology, it has been suggested that MotB might be a linker that fastens the torque-generating machinery to the cell wall.
D F, Blair, D Y, Kim, H C, Berg
openaire   +2 more sources

Producing GST-Cbx7 Fusion Proteins from Escherichia coli

open access: yesBio-Protocol, 2017
This protocol describes the production of GST-Cbx7 fusion proteins from E. coli, originally developed in the recent publication (Zhen et al., 2016). The pGEX-6P-1-GST plasmids encoding the Cbx7 variants were transformed into BL21 competent cells.
Thao Huynh, Xiaojun Ren
doaj   +1 more source

The Outer Membrane Proteins and Their Synergy Triggered the Protective Effects against Pathogenic Escherichia coli

open access: yesMicroorganisms, 2022
Colibacillosis caused by pathogenic Escherichia coli (E. coli) is one of the most serious infectious diseases, causing an extensive burden on animal husbandry and the human healthcare system. Vaccination is one of the ideal ways to prevent E.
Guihong Pen   +5 more
doaj   +1 more source

Mechanisms of Intestinal Epithelial Barrier Dysfunction by Adherent-Invasive Escherichia coli. [PDF]

open access: yes, 2016
Pathobiont expansion, such as that of adherent-invasive Escherichia coli (AIEC), is an emerging factor associated with inflammatory bowel disease. The intestinal epithelial barrier is the first line of defense against these pathogens.
McCole, Declan F, Shawki, Ali
core   +1 more source

Recombinant protein production data after expression in the bacterium Escherichia coli

open access: yesData in Brief, 2016
Fusion proteins have become essential for the expression and purification of recombinant proteins in Escherichia coli. The metal-binding protein CusF has shown several features that make it an attractive fusion protein and affinity tag: ''Expression and ...
J. Enrique Cantu-Bustos   +5 more
doaj   +1 more source

Isolation, Characterization, and Genomic Analysis of Three Novel E. coli Bacteriophages That Effectively Infect E. coli O18

open access: yesMicroorganisms, 2022
Escherichia coli (E. coli) is one of the most common pathogenic bacteria worldwide. Avian pathogenic E. coli (APEC) causes severe systemic disease in poultry (Colibacillosis), and accordingly, has an extreme risk to the poultry industry and public health
Fatma Abdelrahman   +6 more
doaj   +1 more source

Bioinformatic and Molecular Analysis of Inverse Autotransporters from Escherichia coli

open access: yesmSphere, 2019
Proteins secreted by the type V secretion system possess multiple functions, including the capacity to mediate adhesion, aggregation, and biolfilm formation.
Kelvin G. K. Goh   +4 more
doaj   +1 more source

Comparative proteomics of uropathogenic Escherichia coli during growth in human urine identify UCA-like (UCL) fimbriae as an adherence factor involved in biofilm formation and binding to uroepithelial cells [PDF]

open access: yes, 2015
Uropathogenic Escherichia coli (UPEC) are the primary cause of urinary tract infection (UTI) in humans. For the successful colonisation of the human urinary tract, UPEC employ a diverse collection of secreted or surface-exposed virulence factors ...
Allsopp, LP   +5 more
core   +1 more source

Acid shock proteins of Escherichia coli [PDF]

open access: yesFEMS Microbiology Letters, 1990
Synthesis of total cellular proteins of Escherichia coli was studied after transfer of cultures from pH 6.9 to pH 4.3. Proteins induced by such an external pH shift down were identified by mono- and bi-dimensional electrophoresis. 30 to 45 min after an acid shift, a group of at least sixteen polypeptides was markedly induced. Four of these polypeptides
M, Heyde, R, Portalier
openaire   +2 more sources

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