, 2023 Multiple sequence alignment in FASTA format of clpC enzymes from ...
Karl Schmitz (14569274)
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Revista Jurídica Austral, 2023 En este artículo se analiza la noción jurídica de “plataforma continental”, incluida su extensión más allá de las 200 millas marinas. Asimismo, se examina el rol de la Comisión de Límites de la Plataforma Continental (CLPC) en cuanto órgano creado por ...
Ada Inés Sánchez Echevarría +1 more
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Microbiology Spectrum, 2022 Resistance to antibiotics is an increasing problem and necessitates novel antibacterial therapies. The polyketide antibiotics cervimycin A to D are natural products of Streptomyces tendae HKI 0179 with promising activity against multidrug-resistant ...
Alina Dietrich +18 more
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MdfA is a novel ClpC adaptor protein that functions in the developing <i>Bacillus subtilis</i> spore. [PDF]
Genes DevBacterial protein degradation machinery consists of chaperone-protease complexes that play vital roles in bacterial growth and development and have sparked interest as novel antimicrobial targets. ClpC-ClpP (ClpCP) is one such chaperone-protease complex,
Massoni SC +20 more
europepmc +2 more sources
eLife, 2017 Ring-forming AAA+ chaperones exert ATP-fueled substrate unfolding by threading through a central pore. This activity is potentially harmful requiring mechanisms for tight repression and substrate-specific activation.
Marta Carroni +10 more
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Induction of the CtsR regulon improves Xylanase production in Bacillus subtilis
Microbial Cell Factories, 2023 Background The bacterium Bacillus subtilis is extensively used for the commercial production of enzymes due to its efficient protein secretion capacity.
Biwen Wang +2 more
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Role of the MecA adaptor protein in regulation of the AAA + chaperone ClpC of Bacillus subtilis [PDF]
, 2004 ClpC, a member of the AAA+ protein superfamily from Bacillus subtilis, is forming with ClpP a proteolytic system, that is part of the protein quality control system and involved in general proteolysis of misfolded and aggregated proteins.
Schlothauer, Tilman
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Structural insights into the activity regulation of full-length non-structural protein 1 from SARS-CoV-2 and substrate recruitment by the hexameric MecA–ClpC complex [PDF]
, 2023 Since the outbreak of the COVID-19 pandemic in December 2019, SARS-CoV-2 has generated awareness for the requirement of novel antiviral drugs that target new proteins.
Wang, Ying
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The C-terminus of ClpC1 of Mycobacterium tuberculosis is crucial for its oligomerization and function. [PDF]
PLoS ONE, 2012 Mycobacterium tuberculosis ClpC1 is a member of the Hsp100/Clp AAA+ family of ATPases. The primary sequence of ClpC1 contains two N-terminal domains and two nucleotide binding domains (NBD).
Divya Bajaj, Janendra K Batra
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Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilis [PDF]
, 1997 Development of genetic competence in Bacillus subtilis is controlled by the competence-specific transcription factor ComK. ComK activates transcription of itself and several other genes required for competence. The activity of ComK is controlled by other
Hamoen, L. W. +3 more
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