Mostrando 181 - 200 Resultados de 2,845 Para Buscar '"CLP"', tiempo de consulta: 0.31s Limitar resultados
  1. 181
    “…Antibiotic acyldepsipeptides (ADEPs) deregulate ClpP, the proteolytic core of the bacterial Clp protease, thereby inhibiting its native functions and concomitantly activating it for uncontrolled proteolysis of nonnative substrates. …”
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    Cell Division Protein FtsZ Is Unfolded for N-Terminal Degradation by Antibiotic-Activated ClpP
  2. 182
    “…To identify transcriptional regulators with a changed expression in cells devoid of ClpXP activity, RNA sequencing was performed. The RNAseq analysis revealed a number of global virulence regulators that might act downstream of ClpXP, to control expression of tst and other virulence genes. …”
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    A Functional ClpXP Protease is Required for Induction of the Accessory Toxin Genes, tst, sed, and sec
  3. 183
    “…BACKGROUND: The degradation of intracellular proteins plays an essential role in plant responses to stressful environments. ClpS1 and E3 ubiquitin ligase function as adaptors for selecting target substrates in caseinolytic peptidase (Clp) proteases pathways and the 26S proteasome system, respectively. …”
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    TaClpS1, negatively regulates wheat resistance against Puccinia striiformis f. sp. tritici
  4. 184
    “…RESULTS: The serum and liver IL-27 expression levels were elevated in WT mice after CLP-induced severe infection, which were consistent with the changes in HE scores in the liver tissue. …”
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    Gadolinium Chloride Inhibits the Production of Liver Interleukin-27 and Mitigates Liver Injury in the CLP Mouse Model
  5. 185
    “…The ClpB–DnaK bichaperone system reactivates aggregated cellular proteins and is essential for survival of bacteria, fungi, protozoa, and plants under stress. …”
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    Repurposing p97 inhibitors for chemical modulation of the bacterial ClpB–DnaK bichaperone system
  6. 186
    por Bouchnak, Imen, van Wijk, Klaas J.
    Publicado 2021
    “…Recent progress and breakthroughs in identifying Clp protease structures, substrates, substrate adaptors (e.g., NblA/B, ClpS, ClpF), and degrons are highlighted. …”
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    Structure, function, and substrates of Clp AAA+ protease systems in cyanobacteria, plastids, and apicoplasts: A comparative analysis
  7. 187
    “…The binding mode of nepetin and ClpP was further investigated by molecular docking, and it was found that Ser-22 and Gln-47 of ClpP residues were found to be involved in the binding of nepetin to ClpP. …”
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    Nepetin reduces virulence factors expression by targeting ClpP against MRSA-induced pneumonia infection
  8. 188
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    Correction to “Mitochondrial Protease ClpP Is a Target for the Anticancer Compounds ONC201 and Related Analogues”
  9. 189
    “…Protein homeostasis is tightly regulated by protein quality control systems such as chaperones and proteases. In cyanobacteria, the ClpXP proteolytic complex is regarded as a representative proteolytic system and consists of a hexameric ATPase ClpX and a tetradecameric peptidase ClpP. …”
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    Proteomic analysis of the regulatory networks of ClpX in a model cyanobacterium Synechocystis sp. PCC 6803
  10. 190
    “…Clp1 was mainly located in the nucleus and partly in the vesicles. …”
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    The Plant Homeodomain Protein Clp1 Regulates Fungal Development, Virulence, and Autophagy Homeostasis in Magnaporthe oryzae
  11. 191
    “…The unfoldase ClpC1 is one of the most exciting drug targets against tuberculosis. …”
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    Structure of the drug target ClpC1 unfoldase in action provides insights on antibiotic mechanism of action
  12. 192
    “…Our findings demonstrated that both the CLP and lipopolysaccharide LPS methods could induce septic heart dysfunction within 24 h. …”
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    Comparative Analysis of Whole Transcriptome Profiles in Septic Cardiomyopathy: Insights from CLP- and LPS-Induced Mouse Models
  13. 193
    “…Chemo-activation of mitochondrial ClpP exhibits promising anticancer properties. However, we are currently unaware of any studies using selective and potent ClpP activators in lung squamous cell carcinoma. …”
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    Selective activator of human ClpP triggers cell cycle arrest to inhibit lung squamous cell carcinoma
  14. 194
    “…Finally, we show that NOA1 is a new substrate of the mitochondrial matrix protease complex ClpXP. Our results uncovered an unexpected, mandatory detour of NOA1 through the nucleolus before uptake into mitochondria. …”
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    NOA1, a Novel ClpXP Substrate, Takes an Unexpected Nuclear Detour Prior to Mitochondrial Import
  15. 195
    “…BACKGROUND: The caseinolytic protease (Clp) is crucial for chloroplast biogenesis and proteostasis. …”
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    Characterization of the accessory protein ClpT1 from Arabidopsis thaliana: oligomerization status and interaction with Hsp100 chaperones
  16. 196
    “…Polymicrobial sepsis was induced by cecal ligation and puncture (CLP), and SB216763 was used to inhibit GSK-3β in C57BL/6 mice. …”
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    GSK-3β Inhibition Attenuates CLP-Induced Liver Injury by Reducing Inflammation and Hepatic Cell Apoptosis
  17. 197
    “…The key feature is its highly divergent clpP1 gene, normally considered essential in chloroplast genomes. …”
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    The Complete Sequence of the Acacia ligulata Chloroplast Genome Reveals a Highly Divergent clpP1 Gene
  18. 198
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    hCLP46 increases Smad3 protein stability via inhibiting its ubiquitin-proteasomal degradation
  19. 199
    “…Mimosoid plastomes harbor additional interesting features, including loss of clpP intron1 in Inga, accelerated rates of evolution in clpP for Acacia and Inga, and dN/dS ratios consistent with neutral and positive selection for several genes. …”
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    Mimosoid legume plastome evolution: IR expansion, tandem repeat expansions, and accelerated rate of evolution in clpP
  20. 200
    “…Two stoichiometries are revealed for the heptameric rings: 4ClpP1 + 3ClpP2 and 3ClpP1 + 4ClpP2. When combined in the double ring the stoichiometries are (4ClpP1 + 3ClpP2) + (3ClpP1 + 4ClpP2) and 2 × (3ClpP1 + 4ClpP2) with a low population of a 2 × (4ClpP1 + 3ClpP2) tetradecamer. …”
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    Dual stoichiometry and subunit organization in the ClpP1/P2 protease from the cyanobacterium Synechococcus elongatus
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