Type | Description |
---|---|
Definition | chaperonin GroEL |
Date | Results | Publications |
---|---|---|
2019-01-05 10:16:00 | While GroEL and GroES increases the folding rate of PepQ by over 15-fold, the slow spontaneous folding of PepQ is not caused by aggregation. | 28665408 |
2018-01-27 10:42:00 | study confirmed the altered GroEL dependence of green fluorescent protein variants with in vitro folding assays; mutations at positions predicted to be highly frustrated were found to correlate with decreased GroEL dependence; conversely, mutations at positions with low frustration were found to correlate with increased GroEL dependence | 29066625 |
2016-05-14 10:49:00 | Data suggest that neither DnaK nor GroEL singly can modulate sigma32 stability in vivo; there is ordered network between them, where GroEL acts upstream of DnaK. | 26545493 |
2014-06-28 12:45:00 | In the case of GroEL, individualisation of monomers thus leads to individualisation of homomultimeric protein complexes, effectively providing the prerequisites for evolving an orthogonal intracellular GroEL folding machine. | 24151180 |
2014-04-19 10:05:00 | Evidence is provided for an interaction between GroESL and CspC that results in enhanced, temperature-dependent proteolysis of the latter. | 24148697 |
Type | IDs |
---|---|
Synonymous | ECK4137, groEL, mopA |
Gene |
UniProtKB-ID:
CH60_ECOLI
UniprotKB:
P0A6F5
UniParc:
UPI0000000ED4
EMBL:
M11294,
X07850,
AP009048,
U14003,
U00096,
X07899
EnsemblGenome:
b4143,
BAE78145
KO:
eco:b4143,
ecj:JW4103
|
Nucleutide sequences |
EMBL-CDS:
AAA23934.1,
AAC77103.1,
CAA30739.1,
CAA30698.1,
AAA97042.1,
BAE78145.1
EnsemblGenome_TRS:
AAC77103,
BAE78145
|
Protein sequencees |
EnsemblGenome_PRO:
BAE78145,
AAC77103
RefSeq:
NP_418567.1
|
Others |
UniRef100:
UniRef100_A1AJ51
UniRef90:
UniRef90_Q0T9P8
UniRef50:
UniRef50_P0C0Z7
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
---|---|---|---|---|---|---|---|---|
Refseq |
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