Results 111 to 120 of about 3,616 (191)
Queueing up for enzymatic processing: correlated signaling through coupled degradation
Molecular Systems Biology, 2011 High‐throughput technologies have led to the generation of complex wiring diagrams as a post‐sequencing paradigm for depicting the interactions between vast and diverse cellular species. While these diagrams are useful for analyzing biological systems on
Natalie A Cookson +6 more
doaj +1 more source
Investigating Degradation Machinery of Human ClpXP in Acute Myeloid Leukemia [PDF]
Mitochondrial ClpXP is a serine protease complex located within the mitochondrial matrix, playing a crucial role in maintaining mitochondrial protein quality and homeostasis.
Feng, Yue
core +1 more source
FliT selectively enhances proteolysis of FlhC Subunit in FlhD4C2 complex by an ATP-dependent protease, ClpXP [PDF]
, 2014 pre-printWe previously reported that the ClpXP ATP-dependent pro-tease specifically recognizes and degrades the flagellar master transcriptional activator complex, FlhD 4C2, to negatively control flagellar biogenesis. The flagellum-related protein, FliT,
Sato, Y.; Takaya, A.; Mouslim, C.; Yamamoto, T. +1 more
core
eLife, 2019 Most AAA+ remodeling motors denature proteins by pulling on the peptide termini of folded substrates, but it is not well-understood how motors produce grip when resisting a folded domain.
Tristan A Bell +2 more
doaj +1 more source
, 2018 The AAA+ protease ClpXP has long been established as the cellular rescue system that degrades ssrA-tagged proteins resulting from stalled ribosomes. Until recently, in all of these studies soluble proteins were used as model substrates, since the ClpXP ...
Zhaoshuai Wang +9 more
core +1 more source
ClpXP and ClpAP control the Escherichia coli division protein ZapC by proteolysis
Microbiology, 2016 The bacterial FtsZ-ring is an essential cytokinetic structure under tight spatiotemporal regulation. In Escherichia coli, FtsZ polymerization and assembly into the Z-ring is controlled on multiple levels through interactions with positive and negative regulators.
Monika S, Buczek +2 more
openaire +2 more sources
Hydantoin analogs inhibit the fully assembled ClpXP protease without affecting the individual peptidase and chaperone domains. [PDF]
, 2019 Proteolysis mediated by ClpXP is a crucial cellular process linked to bacterial pathogenesis. The development of specific inhibitors has largely focused on ClpP.
Korotkov, Vadim S +2 more
core +1 more source
A Finely Tuned Molecular Motor: Mechanochemistry and Power Efficiency in the AAA+ Protease Machine ClpXP [PDF]
, 2016 Molecular motors transduce chemical energy –usually from ATP hydrolysis– into directed motion and mechanical work, which is used to perform key functions in almost every cellular process.
Rodriguez Aliaga, Piere
core
, 2018 The rise of antibiotic resistant bacteria, such as multidrug-resistant Staphylococcus aureus, calls for novel treatment solutions. Targeting of bacterial virulence represents one potential strategy, with the ClpXP protease complex of S.
Fetzer, Christian
core
Investigation of ClpXP Protease Mechanism of Function and its Interaction with the Folding Chaperone Trigger Factor [PDF]
, 2013 The major chaperones identified in Escherichia coli that assist in protein folding include trigger factor (TF), DnaK/DnaJ/GrpE and GroEL/GroES systems. The main ATP-dependent proteases are ClpXP, ClpAP, HslUV, Lon, and FtsH.
Yu, Angela Yeou Hsiung
core