Results 91 to 100 of about 762,581 (360)

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   +1 more source

CadC-mediated activation of the cadBA promoter in Escherichia coli [PDF]

open access: yes, 2005
The transcriptional activator CadC in Escherichia coli, a member of the ToxR-like proteins, activates transcription of the cadBA operon encoding the lysine decarboxylase CadA and the lysine-cadaverine antiporter CadB. cadBA is induced under conditions of
Jung, K., Kuper, C.
core   +1 more source

SmallTalk: a novel small‐sized fusion tag for peptide expression and purification

open access: yesFEBS Open Bio, EarlyView.
The SmallTalk fusion tag allows for the efficient expression and purification of soluble recombinant proteins or peptides in Escherichia coli. Testing with SmallTalk‐GFP confirmed that the proteins were soluble and folded correctly, while SmallTalk‐Bin1b maintained its antimicrobial activity against various bacterial isolates. This streamlined workflow
Atika Tariq   +3 more
wiley   +1 more source

PhoU homologs from Staphylococcus aureus dimerization and protein interactions

open access: yesMicrobiology Spectrum
PhoU proteins are negative regulators of the phosphate response, regulate virulence, and contribute to antibiotic resistance. Staphylococcus aureus has multiple genes encoding PhoU homologs that regulate persister formation and potentially virulence, but
Clayton T. Matthews   +2 more
doaj   +1 more source

Expression and Purification of Mini G Proteins from Escherichia coli

open access: yesBio-Protocol, 2017
Heterotrimeric G proteins modulate intracellular signalling by transducing information from cell surface G protein-coupled receptors (GPCRs) to cytoplasmic effector proteins.
Byron Carpenter, Christopher Tate
doaj   +1 more source

Universal Stress Proteins inEscherichia coli [PDF]

open access: yesJournal of Bacteriology, 2005
Multiple members of the UspA family of proteins are found in the genomes of bacteria, archaea, fungi, protozoa, and plants, but the biological and biochemical functions of these proteins are not known. In this issue of Journal of Bacteriology, Nachin et al.
openaire   +2 more sources

Modeling reaction-diffusion of molecules on surface and in volume spaces with the E-Cell System [PDF]

open access: yes, 2009
The-Cell System is an advanced open-source simulation platform to model and analyze biochemical reaction networks. The present algorithm modules of the system assume that the reacting molecules are all homogeneously distributed in the reaction ...
Masaru Tomita, Satya N. V. Arjunan
core   +1 more source

A P-type ATPase importer that discriminates between essential and toxic transition metals [PDF]

open access: yes, 2009
Transition metals, although being essential cofactors in many physiological processes, are toxic at elevated concentrations. Among the membrane-embedded transport proteins that maintain appropriate intracellular levels of transition metals are ATP-driven
A. T. Lee   +25 more
core   +2 more sources

dUTPase is essential in zebrafish development and possesses several single‐nucleotide variants with pronounced structural and functional consequences

open access: yesFEBS Open Bio, EarlyView.
dUTPases are involved in balancing the appropriate nucleotide pools. We showed that dUTPase is essential for normal development in zebrafish. The different zebrafish genomes contain several single‐nucleotide variations (SNPs) of the dut gene. One of the dUTPase variants displayed drastically lower protein stability and catalytic efficiency as compared ...
Viktória Perey‐Simon   +6 more
wiley   +1 more source

Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space [PDF]

open access: yes, 2017
Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways.
Cardenas-Rodriguez, Mauricio   +1 more
core   +1 more source

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