Type | Description |
---|---|
Definition | elastase LasB |
Date | Results | Publications |
---|---|---|
2020-06-27 11:56:00 | LasB, PIV, and LasA are activated postsecretionally in a cascading manner in which the initial activation of LasB was controlled tightly by quorum sensing (QS) at the protein level in addition to the well-known transcriptional control of these proteases by QS | 31727738 |
2020-05-30 10:46:00 | In order to check the presence of other chemical groups on modified lysines identified on LasB and CbpD, we used 1- and 2- dimensional gel electrophoresis approaches to target lysine modified by 7 other modifications: butyrylation, crotonylation, dimethylation, malonylation, methylation, propionylation, and trimethylation. | 30672296 |
2019-09-21 12:18:00 | There is no relationship among elastase gene (lasB) presence, antibiotic resistance, and biofilm formation in P. aeruginosa strains isolated from burn patients. | 30274028 |
2019-04-06 11:35:00 | Using a model Proteobacterium, P. aeruginosa, which expresses the gluten-degrading protease elastase (LasB), and its isogenic non-functional lasB mutant19, study in mouse Celiac disease model shows an elastase-dependent inflammatory response mediated by the protease-activated receptor-2 (PAR-2) pathway. | 30867416 |
2016-02-20 11:16:00 | This study represents a systematic mutational analyses of salt bridges in the model metalloprotease PAE and provides important insights into the structure-function relationship of enzymes | 25815820 |
Type | IDs |
---|---|
Gene |
UniProtKB-ID:
ELAS_PSEAE
UniprotKB:
P14756
UniParc:
UPI0000129E46
EMBL:
AB029328,
M19472,
AE004091,
M24531
EnsemblGenome:
PA3724
KO:
pae:PA3724
|
Nucleutide sequences |
EMBL-CDS:
AAA25811.1,
AAG07111.1,
AAB36615.1,
BAB79621.1
EnsemblGenome_TRS:
AAG07111
|
Protein sequencees |
EnsemblGenome_PRO:
AAG07111
RefSeq:
NP_252413.1
|
Others |
UniRef100:
UniRef100_P14756
UniRef90:
UniRef90_P14756
UniRef50:
UniRef50_P14756
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
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Refseq |
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