Results 211 to 220 of about 729,912 (260)

Dynamics and Interactions of OmpF Porin in an Asymmetric Bacterial Outer Membrane including LPS, ECA, and CPS. [PDF]

Biomacromolecules
Gao Y, Widmalm G, Im W.
europepmc   +1 more source

Some of the next articles are maybe not open access.

Related searches:

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   +5 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

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.
Jon Beckwith, Christopher K. Murphy, Kit Johnson   +2 more
openaire   +4 more sources

Ribosomal protein pools in Escherichia coli

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1969
xxx
Marchis-Mouren, G., Cozzone, A., Marvaldi, J.   +2 more
openaire   +4 more sources

Phosphorylation of an Escherichia coli protein at tyrosine

Journal of Molecular Biology, 1986
The analysis of protein phosphorylation in the bacterium Escherichia coli showed that, while most phosphoproteins are modified at serine and/or threonine residues, one of them is modified exclusively at tyrosine. This particular protein which has a molecular weight of 54,500 and a pHi value of 5.6 is found associated with the membrane/ribosome fraction
Cortay, Jc, Duclos, B., Cozzone, Aj
openaire   +4 more sources

Protein secretion pathways in Escherichia coli

Current Opinion in Biotechnology, 1994
The export of proteins to the Escherichia coli periplasm is a well established system for heterologous protein production. With a better understanding of the protein export (SecA, Y-dependent) process and a greater awareness of the conditions necessary for correct folding of proteins in the periplasm, serious efforts are now being made to manipulate ...
Mark A. Blight, Christian Chervaux, I. Barry Holland   +2 more
openaire   +3 more sources