Results 261 to 270 of about 492,895 (317)

Genomic Map of Escherichia coli and Single Nucleotide Polymorphism Markers in Colorectal Cancer. [PDF]

Microb Biotechnol
Xi Y, Liping Z, Yating X, Yang X, Jian C, Caiyun C, Shuwen L, Zian Z, Xiaojian Y, Shuwen H, Wei W.   +10 more
europepmc   +1 more source

Crystal Structure and Activity Analysis of <i>Chlamydophila pneumoniae</i> AP Endonuclease IV. [PDF]

Biomolecules
Jin J, Zhang Y, Guo S, Yang L, Liu H, Liu L, Gao W.   +6 more
europepmc   +1 more source

Different strategies to enhance the solubility of acylsucrose transferase PaxASAT1 expression in <i>Escherichia coli</i>. [PDF]

Biochem Biophys Rep
Han L, Yu X, Ning Y, Wang C, Lu C, Dong Z, Liu C, Ni X, Chen Z.   +8 more
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Visualizing the interplay of Cas1-Cas2 with DNA replication-repair that creates CRISPR-Cas immunity. [PDF]

Nucleic Acids Res
Hashemloo MA, Killelea T, Mamić T, Ireland TH, Lou-Hing A, Kemm F, Dimude JU, Žagar M, Ivančić-Baće I, Rudolph CJ, Bolt EL.   +10 more
europepmc   +1 more source

Genomic analysis of jumbo coliphage fEgEco12. [PDF]

Arch Virol
Badawy S, Skurnik M.
europepmc   +1 more source

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Protein export in Escherichia coli

Current Opinion in Biotechnology, 1992
The export of protein from Escherichia coli has been studied by genetic, biochemical and biophysical techniques. These studies have defined a number of steps in the export pathway and have identified the cellular components required for the translocation process. New information is presented on the function of some of these components.
K, Johnson, C K, Murphy, J, Beckwith
openaire   +2 more sources

Protein export in Escherichia coli

Annales de l'Institut Pasteur / Microbiologie, 1985
Hyperproduction of phosphate-binding protein (PhoS) resulted in saturation of export sites, and pre-PhoS was accumulated both in the inner membrane and in the cytoplasm. The cytoplasmic pre-PhoS could not be exported post-translationally; only the membrane-associated precursor could be matured and exported.
Pages, J.M., Anba, J., Lazdunski, C.
openaire   +4 more sources

The Escherichia coli SeqA protein

Plasmid, 2009
The Escherichia coli SeqA protein contributes to regulation of chromosome replication by preventing re-initiation at newly replicated origins. SeqA protein binds to new DNA which is hemimethylated at the adenine of GATC sequences. Most of the cellular SeqA is found complexed with the new DNA at the replication forks.
Torsten, Waldminghaus, Kirsten, Skarstad
openaire   +2 more sources