Results 61 to 70 of about 171,782 (185)

Self-resistance mechanism to acyldepsipeptide antibiotics in the Streptomyces producer

open access: yesmBio
Clp proteases are ubiquitous in bacteria and play an important role in regulatory proteolysis and in maintaining protein homeostasis within the bacterial cell. They consist of a tetradecameric, proteolytic ClpP core and associated AAA+ Clp-ATPases.
Dhana Thomy   +6 more
doaj   +1 more source

LAPTM5 Downregulation‐Driven VAMP8 Phosphorylation Impairs Autophagosome‐Lysosome Fusion and Aggravates Septic Acute Lung Injury

open access: yesAdvanced Science, EarlyView.
LAPTM5 functions as a critical molecular scaffold bridging PGAM5 and VAMP to facilitate PGAM5‐mediated dephosphorylation of VAMP8. This cascade promotes autophagosome‐lysosome fusion, restores impaired autophagic flux, and clears damaged mitochondria, thereby mitigating cellular oxidative stress and systemic inflammation.
Lang Jiang   +12 more
wiley   +1 more source

Protein Unfolding and Degradation by the CLP Family of Proteases

open access: yesMicroscopy and Microanalysis, 1998
Abstract ATP-dependent proteases play a major role in regulatory protein degradation in both prokaryotic and eukaryotic cells. ATP-dependent proteases in E. coli fall into two classes. The first class requires the interaction of structurally separate proteases with an ATPase, whereas in the second class both the protease and ATPase are ...
Martin Kessel   +5 more
openaire   +1 more source

Lactylation of HSC70 Impairs Chaperone‐Mediated Autophagy to Promote Pyrin Inflammasome‐Dependent PANoptosis in Macrophages During Sepsis

open access: yesAdvanced Science, EarlyView.
In sepsis, lactate accumulation drives HSC70 K561 lactylation, which impairs chaperone‐mediated autophagy and blocks CUX1 degradation. Accumulated CUX1 transcriptionally upregulates Pyrin, triggering PANoptosis in macrophages and exacerbating inflammatory storm and organ injury.
Ying Chen   +10 more
wiley   +1 more source

A practical approach to the global analysis of CLP programs [PDF]

open access: yes, 1993
This paper presents and illustrates with an example a practical approach to the dataflow analysis of programs written in constraint logic programming (CLP) languages using abstract interpretation. It is first argued that, from the framework point of view,
Hermenegildo, Manuel V.   +3 more
core  

Structural Insights into Bortezomib-Induced Activation of the Caseinolytic Chaperone-Protease System in Mycobacterium tuberculosis

open access: yesNature Communications
The caseinolytic protease (Clp) system has recently emerged as a promising anti-tuberculosis target. The anti-cancer drug bortezomib exhibits potent anti-mycobacterial activity and binds to Mycobacterium tuberculosis (Mtb) Clp protease complexes.
Biao Zhou   +21 more
doaj   +1 more source

Improved biocontrol performance of acid-tolerant Pseudomonas koreensis CLP-23 against Ralstonia solanacearum causing tobacco wilt

open access: yesBiological Control
Pseudomonas koreensis, a subgroup of the P. fluorescens complex, is a potential plant growth-promoting rhizobacterium. The aim of this study was to evaluate the biocontrol effects of Pseudomonas koreensis CLP-23 against R.
Guozheng Zhang   +6 more
doaj   +1 more source

Bioinformatic identification of ClpI, a distinct class of Clp unfoldases in Actinomycetota

open access: yesFrontiers in Microbiology, 2023
All clades of bacteria possess Hsp100/Clp family unfoldase enzymes that contribute to aspects of protein quality control. In Actinomycetota, these include ClpB, which functions as an independent chaperone and disaggregase, and ClpC, which cooperates with
Jialiu Jiang   +2 more
doaj   +1 more source

Bacterial Geosmin Biosynthesis is Compartmentalized Inside a Two‐Component Protein Shell

open access: yesAdvanced Science, EarlyView.
This study reports the discovery that geosmin biosynthesis is compartmentalized inside a two‐component protein shell in many bacteria. Sequestration of geosmin synthase inside a Family 2B encapsulin nanocompartment improves geosmin yield and increases enzyme stability as compared to the free enzyme.
Asif Fazal   +3 more
wiley   +1 more source

A role for the Clp protease in activating Mu-mediated DNA rearrangements [PDF]

open access: yesJournal of Bacteriology, 1993
Bacteriophage Mu, one of the best-characterized mobile genetic elements, can be used effectively to answer fundamental questions about the regulation of biochemical machinery for DNA rearrangement. Previous studies of Mu virulence have implicated the Clp protease in repressor inactivation (V. Geuskens, A. Mhammedi-Alaoui, L. Desmet, and A.
openaire   +2 more sources

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