Mostrando 201 - 220 Resultados de 2,845 Para Buscar '"CLP"', tiempo de consulta: 0.40s Limitar resultados
  1. 201
    “…Clp ATPases are powerful ring shaped nanomachines which participate in the degradation pathway of the protein quality control system, coupling the energy from ATP hydrolysis to threading substrate proteins (SP) through their narrow central pore. …”
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    Coarse-Grained Simulations of Topology-Dependent Mechanisms of Protein Unfolding and Translocation Mediated by ClpY ATPase Nanomachines
  2. 202
    “…Consistent with this assumption, the clpX ltaS double mutants did not produce LTA, and genetic analyses confirmed that LTA becomes nonessential in the absence of the ClpX chaperone. …”
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    The Cell Wall Polymer Lipoteichoic Acid Becomes Nonessential in Staphylococcus aureus Cells Lacking the ClpX Chaperone
  3. 203
    “…The components of the contracted tail sheath are then recycled by the ClpV AAA(+) ATPase for a new cycle of tail elongation. …”
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    Structure and specificity of the Type VI secretion system ClpV-TssC interaction in enteroaggregative Escherichia coli
  4. 204
    “…Instead, we report that a LON-ClpP proteolytic quality control axis extinguishes ROS in depolarized mitochondria by degrading the complex I ROS-generating domain. …”
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    A LON-ClpP Proteolytic Axis Degrades Complex I to Extinguish ROS Production in Depolarized Mitochondria
  5. 205
    por Yee, Michelle, Gopal, Pooja, Dick, Thomas
    Publicado 2017
    “…Eight of the nine resistant strains harbored missense mutations in the unfoldase ClpC1 associated with the caseinolytic protease complex.…”
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    Missense Mutations in the Unfoldase ClpC1 of the Caseinolytic Protease Complex Are Associated with Pyrazinamide Resistance in Mycobacterium tuberculosis
  6. 206
    “…While the majority of bacterial organisms utilize only a single ClpP, Listeria monocytogenes expresses two isoforms (LmClpP1 and LmClpP2). …”
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    Insights into ClpXP proteolysis: heterooligomerization and partial deactivation enhance chaperone affinity and substrate turnover in Listeria monocytogenes
  7. 207
    “…We showed that compound 1 inhibits the mycobacterial caseinolytic proteases P1 and P2 (ClpP1P2) and exhibits bactericidal activity, and we established compound 1 and ClpP1P2 as an attractive lead/target couple. …”
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    Towards Selective Mycobacterial ClpP1P2 Inhibitors with Reduced Activity against the Human Proteasome
  8. 208
    “…ClpXP is composed of a proteolytic subunit, ClpP, and a chaperone-like subunit, ClpX. …”
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    Drosophila protease ClpXP specifically degrades DmLRPPRC1 controlling mitochondrial mRNA and translation
  9. 209
    “…Surprisingly, our studies showed that purified ClpXP added to the TX-TL system has very low proteolytic activity. …”
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    Optimization of ClpXP activity and protein synthesis in an E. coli extract-based cell-free expression system
  10. 210
    “…Recent data suggest that the HSP100 family member, ClpB, is involved in T6SS disassembly in the subspecies Francisella novicida. …”
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    ClpB mutants of Francisella tularensis subspecies holarctica and tularensis are defective for type VI secretion and intracellular replication
  11. 211
    “…ClpC1 hexamers couple the energy of ATP hydrolysis to unfold and, subsequently, translocate specific protein substrates into the associated ClpP protease. …”
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    Mycobacterium tuberculosis ClpC1 N-Terminal Domain Is Dispensable for Adaptor Protein-Dependent Allosteric Regulation
  12. 212
    “…The ClpP protease is found in all kingdoms of life, from bacteria to humans. …”
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    Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis
  13. 213
    “…Prompted by the conservation of ClpP from bacteria to humans, we found that the imipridones also activate ClpP from Escherichia coli, Bacillus subtilis, and Staphylococcus aureus in biochemical and genetic assays. …”
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    Imipridone Anticancer Compounds Ectopically Activate the ClpP Protease and Represent a New Scaffold for Antibiotic Development
  14. 214
    “…Animal experiments also confirmed the protection of S5 in CLP mice was dependent on activation of macrophage autophagy. …”
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    Typically inhibiting USP14 promotes autophagy in M1-like macrophages and alleviates CLP-induced sepsis
  15. 215
    “…Bacterial ClpB is an ATP-dependent disaggregase that belongs to the Hsp100/Clp subfamily of the AAA+ ATPases and cooperates with the DnaK chaperone system in the reactivation of aggregated proteins, as well as promotes bacterial survival under adverse environmental conditions, including thermal and oxidative stresses. …”
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    AAA+ Molecular Chaperone ClpB in Leptospira interrogans: Its Role and Significance in Leptospiral Virulence and Pathogenesis of Leptospirosis
  16. 216
    “…[Image: see text] The genomic analysis of Leptospira reveals a trigger factor (TF) encoding gene (tig) to be colocalized along with the clpP1 and clpX. The TF is a crouching dragon-like protein known to be a ribosome-associated chaperone that is involved in cotranslational protein folding in bacteria in an ATP-independent mode. …”
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    Trigger Factor in Association with the ClpP1P2 Heterocomplex of Leptospira Promotes Protease/Peptidase Activity
  17. 217
    “…This study is aimed at evaluating the effects of βS on the biomarkers of inflammation and liver function in cecal ligation and puncture- (CLP-) induced septic rats. METHODS: Thirty male Wistar rats were divided equally into six groups as follows: sham, CLP, CLP+dexamethasone (DX, 0.2 mg/kg), CLP+βS (1 mg/kg), CLP+imipenem (IMI, 20 mg/kg), and CLP+IMI (20 mg/kg)+βS (1 mg/kg). …”
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    β-Sitosterol Alters the Inflammatory Response in CLP Rat Model of Sepsis by Modulation of NFκB Signaling
  18. 218
    “…Using a yeast two-hybrid screen, we found that OsClpR1 interacted with OsClpP4, OsClpP5, OsClpP2, and OsClpS1. …”
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    Plastid caseinolytic protease OsClpR1 regulates chloroplast development and chloroplast RNA editing in rice
  19. 219
    “…The M. tuberculosis (Mtb) ClpB is a protein disaggregase that helps to rejuvenate the bacterial cell. …”
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    Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system
  20. 220
    “…ClpB belongs to the cellular disaggretase machinery involved in rescuing misfolded or aggregated proteins during heat or other cellular shocks. …”
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    Reconstruction of Three-Dimensional Conformations of Bacterial ClpB from High-Speed Atomic-Force-Microscopy Images
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