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Items: 3

1.

Chaperone saturation mediates translation and protein folding efficiency

(Submitter supplied) Whether the emergence of a nascent protein from the ribosome and the formation of structural elements are synchronized has been a longstanding question. Paradoxically, kinetically efficient translation can induce mis-folding and aggregation despite the presence of molecular chaperones, which in Escherichia coli are induced by unfolded protein via σ32. The molecular mechanisms mediating translation efficiency and protein folding efficiency remain poorly understood. more...
Organism:
Escherichia coli; Escherichia coli str. K-12 substr. MG1655
Type:
Other; Expression profiling by high throughput sequencing
Platforms:
GPL18956 GPL18133
30 Samples
Download data: TSV
Series
Accession:
GSE104303
ID:
200104303
2.

Illumina HiSeq 2500 (Escherichia coli str. K-12 substr. MG1655)

Organism:
Escherichia coli str. K-12 substr. MG1655
30 Series
530 Samples
Download data
Platform
Accession:
GPL18956
ID:
100018956
3.

pACYC177 plasmid / WT Luciferase rep 2

Organism:
Escherichia coli str. K-12 substr. MG1655
Source name:
pACYC177 plasmid / WT Luciferase rep 2
Platform:
GPL18956
Series:
GSE104303
Download data
Sample
Accession:
GSM2794758
ID:
302794758
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db=gds|term=GSM2794758[Accession]|query=1|qty=3|blobid=MCID_67595ea0df415c74f8b621b7|ismultiple=true|min_list=5|max_list=20|def_tree=20|def_list=|def_view=|url=/Taxonomy/backend/subset.cgi?|trace_url=/stat?
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