scholarly article | Q13442814 |
P2093 | author name string | Y Ishii | |
F Amano | |||
P2860 | cites work | The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system | Q24603386 |
The ATP-dependent HslVU/ClpQY protease participates in turnover of cell division inhibitor SulA in Escherichia coli | Q33992303 | ||
Redundant in vivo proteolytic activities of Escherichia coli Lon and the ClpYQ (HslUV) protease. | Q33992310 | ||
Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli | Q34384407 | ||
Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli | Q34448690 | ||
Protein degradation in Escherichia coli: the lon gene controls the stability of sulA protein | Q34708350 | ||
HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome | Q34733264 | ||
Regulation of SOS mutagenesis by proteolysis | Q34734770 | ||
Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY. | Q34737150 | ||
Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli. | Q34737513 | ||
Functional dissection of a cell-division inhibitor, SulA, of Escherichia coli and its negative regulation by Lon. | Q34740784 | ||
Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis | Q34756168 | ||
Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH) | Q35198523 | ||
Interaction between FtsZ and inhibitors of cell division | Q35611409 | ||
Differential protease-mediated turnover of H-NS and StpA revealed by a mutation altering protein stability and stationary-phase survival of Escherichia coli | Q35631720 | ||
Inhibition of FtsZ polymerization by SulA, an inhibitor of septation in Escherichia coli | Q35974127 | ||
Capsule synthesis in Escherichia coli K-12 is regulated by proteolysis | Q36230246 | ||
Cell-division control in Escherichia coli: specific induction of the SOS function SfiA protein is sufficient to block septation | Q36273121 | ||
Protease La from Escherichia coli hydrolyzes ATP and proteins in a linked fashion | Q36307516 | ||
Role of sulA and sulB in filamentation by lon mutants of Escherichia coli K-12. | Q36308395 | ||
The mechanism and functions of ATP-dependent proteases in bacterial and animal cells | Q36736334 | ||
ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions | Q36831491 | ||
A cell division inhibitor SulA of Escherichia coli directly interacts with FtsZ through GTP hydrolysis | Q38296823 | ||
Overproduction and purification of Lon protease from Escherichia coli using a maltose-binding protein fusion system | Q38303109 | ||
Evolution of the enterobacterial sulA gene: a component of the SOS system encoding an inhibitor of cell division | Q48352394 | ||
An inducible DNA replication–cell division coupling mechanism in E. coli | Q59050563 | ||
Selectivity of intracellular proteolysis: protein substrates activate the ATP-dependent protease (La) | Q69991883 | ||
Degradation in vitro of bacteriophage lambda N protein by Lon protease from Escherichia coli | Q70023877 | ||
Overproduction and purification of SulA fusion protein in Escherichia coli and its degradation by Lon protease in vitro | Q71880744 | ||
Regulatory role of C-terminal residues of SulA in its degradation by Lon protease in Escherichia coli | Q73731954 | ||
Recognition, targeting, and hydrolysis of the lambda O replication protein by the ClpP/ClpX protease | Q77726447 | ||
ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli | Q78144063 | ||
P433 | issue | Pt 2 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 473-80 | |
P577 | publication date | 2001-09-01 | |
P1433 | published in | Biochemical Journal | Q864221 |
P1476 | title | Regulation of SulA cleavage by Lon protease by the C-terminal amino acid of SulA, histidine | |
P478 | volume | 358 |
Q37059315 | Crystallization and preliminary X-ray diffraction analysis of the α subdomain of Lon protease from Brevibacillus thermoruber |
Q37413548 | Degrons in protein substrates program the speed and operating efficiency of the AAA+ Lon proteolytic machine. |
Q34651849 | Distinct quaternary structures of the AAA+ Lon protease control substrate degradation. |
Q37027096 | Engineering fluorescent protein substrates for the AAA+ Lon protease. |
Q36743161 | Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates |
Q42845384 | Ligand-controlled proteolysis of the Escherichia coli transcriptional regulator ZntR |
Q27003208 | Multitasking in the mitochondrion by the ATP-dependent Lon protease |
Q42732678 | Polyphosphate, cyclic AMP, guanosine tetraphosphate, and c-di-GMP reduce in vitro Lon activity |
Q37595861 | Proteolysis in the SOS response and metal homeostasis in Escherichia coli. |
Q41949884 | RamA, which controls expression of the MDR efflux pump AcrAB-TolC, is regulated by the Lon protease |
Q34809787 | Recognition of misfolded proteins by Lon, a AAA(+) protease |
Q39217558 | Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity. |
Q39832015 | Sequential recognition of two distinct sites in sigma(S) by the proteolytic targeting factor RssB and ClpX. |
Q41840280 | The Copper Efflux Regulator CueR Is Subject to ATP-Dependent Proteolysis in Escherichia coli. |
Q50798960 | The DNA-binding protease, CND41, and the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase in senescent leaves of tobacco. |
Q34616752 | The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease |
Q40403943 | Versatile modes of peptide recognition by the ClpX N domain mediate alternative adaptor-binding specificities in different bacterial species |
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