Results 51 to 60 of about 268,169 (218)

Structure and function of bacterial dynamin-like proteins [PDF]

open access: yes, 2012
Membrane dynamics are essential for numerous cellular processes in eukaryotic and prokaryotic cells. In eukaryotic cells, membrane fusion and fission are often catalyzed by large GTPases of the dynamin protein family. These proteins couple GTP hydrolysis
Bramkamp, Marc
core   +1 more source

Acquisition of ionic copper by a bacterial outer membrane protein [PDF]

open access: yes, 2020
AbstractCopper, while toxic in excess, is an essential micronutrient in all kingdoms of life due to its essential role in the structure and function of many proteins. Proteins mediating ionic copper import have been characterised in detail for eukaryotes, but much less so for prokaryotes. In particular, it is still unclear whether and how Gram-negative
van den Berg B   +6 more
openaire   +2 more sources

Construction of a bacterial surface display system based on outer membrane protein F

open access: yesMicrobial Cell Factories, 2019
Background Bacterial surface display systems were developed to surface expose heterologous proteins or peptides for different applications, such as peptide libraries screening and live bacterial vaccine design.
Tingting Chen   +12 more
doaj   +1 more source

In vitro and in vivo screening for novel essential cell-envelope proteins in Pseudomonas aeruginosa [PDF]

open access: yes, 2015
The Gram-negative bacterium Pseudomonas aeruginosa represents a prototype of multi-drug resistant opportunistic pathogens for which novel therapeutic options are urgently required.
Bragonzi, Alessandra   +5 more
core   +1 more source

Small and mighty: adaptation of superphylum Patescibacteria to groundwater environment drives their genome simplicity. [PDF]

open access: yes, 2020
BackgroundThe newly defined superphylum Patescibacteria such as Parcubacteria (OD1) and Microgenomates (OP11) has been found to be prevalent in groundwater, sediment, lake, and other aquifer environments.
Adams, Benjamin G   +21 more
core   +2 more sources

The Landscape of Pseudomonas aeruginosa Membrane-Associated Proteins

open access: yesCells, 2020
Background: Pseudomonas aeruginosa cell envelope-associated proteins play a relevant role in infection mechanisms. They can contribute to the antibiotic resistance of the bacterial cells and be involved in the interaction with host cells.
Sara Motta   +7 more
doaj   +1 more source

Biogenesis of mitochondrial c-type cytochromes [PDF]

open access: yes, 1990
Cytochromesc andc 1 are essential components of the mitochondrial respiratory chain. In both cytochromes the heme group is covalently linked to the polypeptide chain via thioether bridges. The location of the two cytochromes is in the intermembrane space;
Gonzales, Daniel H., Neupert, Walter
core   +2 more sources

Living on the edge: Simulations of bacterial outer-membrane proteins

open access: yesBiochimica et Biophysica Acta (BBA) - Biomembranes, 2016
Gram-negative bacteria are distinguished in part by a second, outer membrane surrounding them. This membrane is distinct from others, possessing an outer leaflet composed not of typical phospholipids but rather large, highly charged molecules known as lipopolysaccharides.
Karl Lundquist   +4 more
openaire   +3 more sources

Inflammasome Activation by Bacterial Outer Membrane Vesicles Requires Guanylate Binding Proteins

open access: yesmBio, 2017
The Gram-negative bacterial cell wall component lipopolysaccharide (LPS) is recognized by the noncanonical inflammasome protein caspase-11 in the cytosol of infected host cells and thereby prompts an inflammatory immune response linked to sepsis.
Ryan Finethy   +8 more
doaj   +1 more source

Mucin adsorbed by E. coli can affect neutrophil activation in vitro

open access: yesFEBS Open Bio, 2020
Bacteria colonizing human intestine adhere to the gut mucosa and avoid the innate immune system. We previously demonstrated that Escherichia coli isolates can adsorb mucin from a diluted solution in vitro.
Elena Mikhalchik   +11 more
doaj   +1 more source

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