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High-Resolution Patterned Delivery of Chemical Signals From 3D-Printed Picoliter Droplet Networks. [PDF]

Adv Mater
Riexinger J, Caganek T, Wang X, Yin Y, Chung K, Zhou L, Bayley H, Krishna Kumar R.   +7 more
europepmc   +1 more source

Whole-Genome Sequencing of Invasive Neonatal Escherichia coli From Uppsala County, Sweden. [PDF]

J Infect Dis
Heydecke A, Myrelid Å, Normann E, Gullsby K, Tano E, Sütterlin S.   +5 more
europepmc   +1 more source

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Gating Movements of Colicin A and Colicin Ia Are Different

Journal of Membrane Biology, 2004
Both colicin A and colicin Ia belong to a subfamily of the bacterial colicins that act by forming a voltage-dependent channel in the inner membrane of target bacteria. Both colicin A and Ia open at positive and close at negative potential, but only colicin A exhibits distinctly biphasic turnoff kinetics, implying the existence of two open states ...
Stephen L Slatin, Daniel Baty, Denis Duché   +2 more
exaly   +3 more sources

Colicins : A minireview

Toxicon, 1982
Colicin are toxins that kill specifically E. coli bacteria. These cells have both an outer and a cytoplasmic membrane. Thus, three steps can be distinguished in colicin action: a) the interaction with specific receptors located at the cell surface, b) the uptake through the outer and eventually through the inner membrane, c) the action of the cell ...
C, Lazdunski, D, Cavard
openaire   +2 more sources

Colicin crystal structures: pathways and mechanisms for colicin insertion into membranes

Biochimica Et Biophysica Acta - Biomembranes, 2002
The X-ray structures of the channel-forming colicins Ia and N, and endoribonucleolytic colicin E3, as well as of the channel domains of colicins A and E1, and spectroscopic and calorimetric data for intact colicin E1, are discussed in the context of the mechanisms and pathways by which colicins are imported into cells. The extensive helical coiled-coil
William A Cramer
exaly   +3 more sources

Identification of a New Type of Colicine (Colicine L)

Nature, 1962
THE strain Escherichia coli 398 of the collection in this Institute produces a colicine, which cannot be identified as one of the known types1–3. This new type is related to the colicines of the group E, and was at first considered to be a complex colicine, containing colicines E and I.
P, HAUDUROY, J, PAPAVASSILIOU
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Colicin S8 export: extracellular and cytoplasmic colicin are different

International Microbiology, 2003
The properties of colicin S8 are different for the cytoplasmic, periplasmic and extracellular protein. Interactions with its specific receptors reflect this. Active cell extracts separate into a non-anionic along with an anionic fraction by DEAE-Sephacell chromatography.
Maria-Elena, Garcia Diaz, Juan Luis, Concepción Curbelo   +1 more
openaire   +2 more sources

Colicin E3 is an Endonuclease

The Journal of Biochemistry, 1978
It was confirmed by polyacrylamide gel electrophoresis that isolated 16S rRNA was cleaved by the active component (protein A) or the active fragment (T2A) of colicin E3. However, the degradation was random, in contrast with the specific cleavage observed in the interaction of colicin E3 with ribosomes.
S, Ohno, K, Imahori
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Functional domains of colicin A

Molecular Microbiology, 1988
SummaryA large number of mutations which introduce deletions in colicin A have been constructed. The partially deleted colicin A proteins were purified and their activity in vivo (on sensitive cells) and in vitro (in planar lipid bilayers) was assayed. The receptor‐binding properties of each protein were also analysed.
D, Baty, M, Frenette, R, Lloubès, V, Geli, S P, Howard, F, Pattus, C, Lazdunski   +6 more
openaire   +2 more sources