Results 121 to 130 of about 5,899 (155)

Regulation of proteolysis of the sigma factor RpoS by the Gac-Rsm signal transduction system in <i>Azotobacter vinelandii</i>. [PDF]

Microbiology (Reading)
Rojo-Rodríguez JB, Moreno S, Espin G.
europepmc   +1 more source

Cryo-EM structures of human ClpXP reveal mechanisms of assembly and proteolytic activation. [PDF]

Nat Commun
Chen W, Lander GC, Yang J.
europepmc   +1 more source

An open axial channel of the AAA ClpXP protease enhances degradation of specific classes of protein substrates. [PDF]

Protein Sci
Lyu Y, Bolstad I, Davis JH, Sauer RT, Ghanbarpour A.   +4 more
europepmc   +1 more source

The Effect of <i>clpP</i> Gene Disruption on Cell Morphology, Growth, and the Ability to Synthesize Cellulose of <i>Komagataeibacter xylinus</i> E₂₅. [PDF]

Int J Mol Sci
Jędrzejczak-Krzepkowska M, Ludwicka K, Bielecki S.   +2 more
europepmc   +1 more source

The depletion of serine beta-lactamase-like protein (LACTB) ameliorates metabolic dysfunction-associated steatotic liver disease by reducing ubiquitin-mediated degradation of carnitine palmitoyltransferase 2. [PDF]

Diabetes Obes Metab
Shi W, Liu X, Wang N, Zhang Q, Gao J, Guan C, Li Y, Yang C, Bi S, Zou X, Zhong X.   +10 more
europepmc   +1 more source

Subunit-specific isotope labelling of heteromeric complexes using cell-free protein expression: application to the 760 kDa ClpXP molecular machine. [PDF]

RSC Chem Biol
Audibert A, Vermot A, Trauchessec M, Giandoreggio K, Fenel D, Le Roy A, Tymen C, Moscatello B, Gandy L, Mas C, Imbert L, Boisbouvier J.   +11 more
europepmc   +1 more source

Recent Advances in the Structural Studies of the Proteolytic ClpP/ClpX Molecular Machine. [PDF]

Biomolecules
Audibert A, Boisbouvier J, Vermot A.
europepmc   +1 more source

Dynamic Oligomerization Processes and Functional Characterization of Bacterial ClpP Protease

YAKUGAKU ZASSHI
openaire   +1 more source

Some of the next articles are maybe not open access.

Related searches:

Dynamics of the ClpP serine protease: A model for self-compartmentalized proteases

Critical Reviews in Biochemistry and Molecular Biology, 2014
ClpP is a highly conserved serine protease present in most bacterial species and in the mitochondria of mammalian cells. It forms a cylindrical tetradecameric complex arranged into two stacked heptamers. The two heptameric rings of ClpP enclose a roughly spherical proteolytic chamber of about 51 Å in diameter with 14 Ser-His-Asp proteolytic active ...
Walid Houry, Adedeji Ologbenla, Kaiyin Liu   +2 more
exaly   +3 more sources

Selective Activation of Human Caseinolytic Protease P (ClpP)

Angewandte Chemie - International Edition, 2018
AbstractCaseinolytic protease P (ClpP) is the proteolytic component of the ClpXP protein degradation complex. Eukaryotic ClpP was recently found to act within the mitochondria‐specific unfolded protein response (UPRmt). However, its detailed function and dedicated regulation remain largely unexplored.
Leonhard M Kick, Matthias Stahl, Klaus Richter   +2 more
exaly   +3 more sources