Results 51 to 60 of about 1,964,169 (255)

Transport and catabolism of murein tripeptide in Escherichia coli K-12 [PDF]

open access: yes, 2011
In bacteria, extracellular peptides are not only a source of nutrients but also play important roles in cell-cell communication. The primary mode of uptake of these peptides in bacteria is via ATP Binding Cassette (ABC) transporters.
Maqbool, Abbas
core   +6 more sources

Active Protein Aggregates Produced in Escherichia coli [PDF]

open access: yesInternational Journal of Molecular Sciences, 2011
Since recombinant proteins are widely used in industry and in research, the need for their low-cost production is increasing. Escherichia coli is one of the best known and most often used host organisms for economical protein production. However, upon over-expression, protein aggregates called inclusion bodies (IBs) are often formed. Until recently IBs
Peternel, Špela, Komel, Radovan
openaire   +3 more sources

Chromosomal macrodomains and associated proteins : implications for DNA organization and replication in gram negative bacteria [PDF]

open access: yes, 2011
The Escherichia coli chromosome is organized into four macrodomains, the function and organisation of which are poorly understood. In this review we focus on the MatP, SeqA, and SlmA proteins that have recently been identified as the first examples of ...
Kalmykowa, Olga J.   +14 more
core   +1 more source

dnaX36 mutator of Escherichia coli: effects of the tau subunit of the DNA polymerase III holoenzyme on chromosomal DNA replication fidelity. [PDF]

open access: yes, 2011
The Escherichia coli dnaX36 mutant displays a mutator effect, reflecting a fidelity function of the dnaX-encoded τ subunit of the DNA polymerase III (Pol III) holoenzyme.
Jonczyk, Piotr   +7 more
core   +2 more sources

Repetitive N-WASP–binding elements of the Enterohemorrhagic Escherichia coli Effector EspFU Synergistically Activate Actin Assembly [PDF]

open access: yes, 2008
Enterohemorrhagic Escherichia coli (EHEC) generate F-actin–rich adhesion pedestals by delivering effector proteins into mammalian cells. These effectors include the translocated receptor Tir, along with EspFU, a protein that associates indirectly with ...
McGhie, E.J.   +49 more
core   +1 more source

SYNTHESIS OF NASCENT PROTEIN BY RIBOSOMES IN ESCHERICHIA COLI [PDF]

open access: yesProceedings of the National Academy of Sciences, 1959
Cells and tissues of all kinds of living organisms have been found to contain ribonucleic acid (RNA) and protein both as separate constituents and as complexes in the form of ribonucleoprotein particles. From a variety of experimental data it has been inferred that these particles are probably intimately involved in the processes of protein synthesis.
McQuillen, Kenneth   +2 more
openaire   +3 more sources

Microarray analysis of the ler regulon in enteropathogenic and enterohaemorrhagic escherichia coli strains [PDF]

open access: yes, 2014
The type III protein secretion system is an important pathogenicity factor of enteropathogenic and enterohaemorrhagic Escherichia coli pathotypes. The genes encoding this apparatus are located on a pathogenicity island (the locus of enterocyte effacement)
Islam, Md. Shahidul   +42 more
core   +1 more source

Chromatographic Analysis of Recombinant Lysostaphin Expressed in Escherichia coli [PDF]

open access: yes, 2011
Lysostaphin (EC.3.4.24.75) is an extracellular glycylglycine endopeptidase produced exclusively by Staphylococcus simulans biovar staphylolyticus (ATCC 1362, NRRL B-2628).
Jennings, Claire
core  

Studien zur Proteintranslokation in Escherichia coli : Untersuchung der Membranproteine SecYEG und YidC unter Verwendung biochemischer und kristallographischer Methoden [PDF]

open access: yes, 2008
Transport of proteins into or across cellular membranes is mediated by the conserved and ubiquitous Sec-machinery. The Sec-homologue in the inner membrane of Escherichia coli is SecYEG.
Lotz, Mirko
core  

Crystal Structure of the Escherichia coli Fic Toxin-Like Protein in Complex with Its Cognate Antitoxin [PDF]

open access: yes, 2016
FIC domain proteins mediate post-translational modifications of target proteins, which typically results in their inactivation. Depending on the conservation of crucial active site residues, the FIC fold serves as structural scaffold for various ...
Stanger, Frédéric V.   +11 more
core   +2 more sources

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