Results 41 to 50 of about 2,051,564 (362)

Structure and genetics of Escherichia coli O antigens

open access: yesFEMS Microbiology Reviews, 2019
Escherichia coli includes clonal groups of both commensal and pathogenic strains, with some of the latter causing serious infectious diseases. O antigen variation is current standard in defining strains for taxonomy and epidemiology, providing the basis ...
B. Liu   +9 more
semanticscholar   +1 more source

Transient drift of Escherichia coli under diffusing Step nutrient profile [PDF]

open access: yesPhys. Rev. E 98, 052413 (2018), 2018
Bacteria such as Escherichia coli (E. coli) exhibit biased motion if kept in a spatially non-uniform chemical environment. Here, we bring out unique time-dependent characteristics of bacterial chemotaxis, in response to a diffusing spatial step ligand profile.
arxiv   +1 more source

Kontaminasi Bakteri Escherichia Coli pada Botol Susu dengan Kejadian Diare pada Bayi [PDF]

open access: yes, 2014
Penderita diare di Kota Makassar setiap tahunnya masih diatas 29.000 kasus dalam kurun waktu tiga tahun terakhir. Bayi dan Balita menjadi kelompok yang rentan terkena diare.
Arsin, A. A. (Andi)   +1 more
core  

Chemotaxis in Escherichia coli

open access: yesCold Spring Harbor Symposia on Quantitative Biology, 1965
Motile bacteria are attracted to a variety of chemicals — a phenomenon called chemotaxis (for a review, see Weibull, 1960). Although chemotaxis by bacteria has been recognized since the end of the nineteenth century, thanks to the pioneering work of Engelmann, Pfeffer, and other biologists, the mechanisms involved are still almost entirely unknown. How
openaire   +3 more sources

A histidine‐rich extension of the mitochondrial F0 subunit ATP6 from the ice worm Mesenchytraeus solifugus increases ATP synthase activity in bacteria

open access: yesFEBS Letters, EarlyView.
The glacier ice worm Mesenchytraeus solifugus survives year‐round at 0 °C. Its ATP6 subunit, which forms a regulatory component of the proton pore in mitochondrial ATP synthase, has a carboxy‐terminal extension not found in any other organism examined to date. Here, we show that fusion of this extension to the homologous AtpB protein in E. coli results
Truman Dunkley   +2 more
wiley   +1 more source

Novel Plasmid-Mediated Colistin Resistance Gene mcr-3 in Escherichia coli

open access: yesmBio, 2017
The mobile colistin resistance gene mcr-1 has attracted global attention, as it heralds the breach of polymyxins, one of the last-resort antibiotics for the treatment of severe clinical infections caused by multidrug-resistant Gram-negative bacteria.
Wenjuan Yin   +9 more
semanticscholar   +1 more source

A Gapless, Unambiguous Genome Sequence of the Enterohemorrhagic Escherichia coli O157:H7 Strain EDL933. [PDF]

open access: yes, 2014
Escherichia coli EDL933 is the prototypic strain for enterohemorrhagic E. coli serotype O157:H7, associated with deadly food-borne outbreaks. Because the publicly available sequence of the EDL933 genome has gaps and >6,000 ambiguous base calls, we ...
Aziz, Ramy K   +4 more
core   +2 more sources

Elucidation of interface interactions between a dehydratase domain and an acyl carrier protein in cremimycin polyketide synthase

open access: yesFEBS Letters, EarlyView.
In modular polyketide synthases, the dehydratase (DH) domain catalyzes the dehydration reaction of the β‐hydroxyacyl unit attached to the cognate acyl carrier protein (ACP) domain. However, it is unclear how DH interacts with ACP during the reaction. In this study, we identified DH–ACP interface residues, providing the first detailed insights into DH ...
Kaede Kotagiri   +8 more
wiley   +1 more source

Environmental Escherichia coli: ecology and public health implications—a review

open access: yesJournal of Applied Microbiology, 2017
Escherichia coli is classified as a rod‐shaped, Gram‐negative bacterium in the family Enterobacteriaceae. The bacterium mainly inhabits the lower intestinal tract of warm‐blooded animals, including humans, and is often discharged into the environment ...
Jeonghwan Jang   +5 more
semanticscholar   +1 more source

Structure of protease-cleaved escherichia coliα-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment [PDF]

open access: yes, 2015
Bacterial -2-macroglobulins have been suggested to function in defence as broad-spectrum inhibitors of host proteases that breach the outer membrane.
Burchmore, R.J.S.   +9 more
core   +2 more sources

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