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UnknownE-SegNet: E-Shaped Structure Networks for Accurate 2D and 3D Medical Image Segmentation.
Not available
S-EPMC12408157 | biostudies-literature
Proteomics2D-LC/MS/MS analysis of Escherichia coli under optimal growth condition
2D-LC/MS/MS analysis was used to examine the proteome of E. coli O157:H7 strain Sakai during exponential growth under optimal condition (i.e., from 35°C aw 0.993). MS/MS data obtained from each protein sample were processed by the Computational Proteomics Analysis System (CPAS), a web-based system ...
ORGANISM(S): Escherichia coli 
2019-12-04 | PXD000583 | Pride
Optimal growth condition Physiology 2d-lc/ms/ms E. coli 
TranscriptomicsHuSE2,2Dvs3D
HCV proliferation is closely related to three-dimentional cellular condition. In case of blood-borne (bb) HCV culture in HuS-E2 cells, bbHCV was reproduced only from 3D-cultured cells in hollow fibers. Thus, in order to identify novel factors which support HCV proliferation under three-dimentional c...
ORGANISM(S): Homo sapiens 
2013-12-10 | E-MTAB-1491 | biostudies-arrayexpress
ProteomicsRevisiting Ehrlichia ruminantium Replication Cycle Using Proteomics : The Host and the Bacterium Perspectives
The Rickettsiales Ehrlichia ruminantium (ER), the causal agent of the fatal tick-borne disease Heartwater, induces severe damage to the vascular endothelium in ruminants. Nevertheless, E. ruminantium-induced pathobiology remains largely unknown. Our work paves the way for understanding this phenomen...
ORGANISM(S): Bos taurus (Bovine) Ehrlichia ruminantium str. Gardel 
2021-07-14 | PXD026092 | Pride
Ehrlichia ruminantium  endothelial cells  host response  immunomodulation  bacterial life cycle  differential protein expression  infection biomarkers  virulence factors 
ProteomicsMucin-binding proteins of E. coli membrane
Proteins from E. coli outer membrane were extracted with carbonate method, separated in 2D-PAGE and transferred onto nitrocellulose membrane. After incubation with flourescent-labelled mucin, mucin-binding protein spots were cut out, subjected to trypsinolysis and identified by protein analysis wit...
ORGANISM(S): Escherichia coli 
2019-12-16 | PXD010472 | Pride
Escherichia coli Hplc-ms-ms Mucin binding Membrane 
Proteomics2D-LC/MS/MS analysis of Escherichia coli during exposure to abrupt downshifts in temperature and water activity
2D-LC/MS/MS analysis was used to examine time-dependent changes in proteome of E. coli O157:H7 strain Sakai upon abrupt downshifts from 35°C aw 0.993 to 14°C aw 0.967. Bacterial cells were harvested before abrupt downshifts in both temperature and aw (i.e. control), or at 0 (i.e. immediately after t...
ORGANISM(S): Escherichia coli 
2016-09-29 | PXD004803 | Pride
Cold temperature 2d-lc/ms/ms Water activity stress E. coli 
UnknownTopology engineering of COFs <i>via</i> localized 1D-2D unit interconnection to facilitate interfacial electron transfer for efficient gold recovery from e-waste leachates.
Not available
S-EPMC12616540 | biostudies-literature
Proteomics2D-LC/MS/MS analysis of Escherichia coli during exposure an abrupt downshift in water activity
2D-LC/MS/MS analysis was used to examine time-dependent changes in proteome of E. coli O157:H7 strain Sakai upon an abrupt downshift in water activity (aw) (i.e., from aw 0.993 to aw 0.967) at a constant temperature of 35°C. Bacterial cells were harvested before hyperosmotic shift, and 0 (i.e. immed...
ORGANISM(S): Escherichia coli 
2014-04-14 | PXD000541 | Pride
Physiology Stress response 2d-lc/ms/ms Water activity stress E. coli 
Proteomics2D-LC/MS/MS analysis of Escherichia coli during exposure to an abrupt temperature downshift
2D-LC/MS/MS analysis was used to examine time-dependent changes in proteome of E. coli O157:H7 strain Sakai upon an abrupt downshift in temperature (i.e., from 35°C to 14°C). Cell cultures were harvested at 30, 90, 160, and 330 min post-temperature downshift. It also should be noted that these time ...
ORGANISM(S): Escherichia coli 
2019-11-25 | PXD000573 | Pride
Physiology Stress response 2d-lc/ms/ms E. coli Cold stress 
ProteomicsDifferential proteome analysis of Escherichia coli grown on acetate vs. glucose
Relative protein abundances of Escherichia coli growing exponentially on minimal medium with acetate or glucose as the sole carbon source were investigated in a quantitative shotgun proteome analysis with TMT6-plex isobaric tags. Peptides were separated by high resolution high/low pH 2D-LC, using an...
ORGANISM(S): Escherichia coli 
2016-10-11 | PXD003863 | Pride
Tmt Isobaric High/low ph 2d-lc 
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