Results 161 to 170 of about 7,556 (201)

Detection of Brucella spp. from milk by quantitative PCR as a monitoring method for brucellosis in cattle in Mongolia. [PDF]

BMC Vet Res
Naranchimeg B, Chantsal B, Sandagdorj B, Bolormaa T, Ulzii-Orshikh P, Altanchimeg A, Ganzorig S, Batbaatar V, Horiuchi M, Nyam-Osor P.   +9 more
europepmc   +1 more source

Calcium Channels and Modulators as Potential Therapeutic Targets for Contraceptives and Male Fertility: A Scoping Review. [PDF]

Open Access J Contracept
Twambaze MF, Adebayo IA, Odoma S, Alagbonsi AI.   +3 more
europepmc   +1 more source

Imipridones ONC201/ONC206 + RT/TMZ triple (IRT) therapy reduces intracranial tumor burden, prolongs survival in orthotopic IDH-WT GBM mouse model, and suppresses MGMT. [PDF]

Oncotarget
Zhou L, Zhang L, Zhang J, Wu LJ, Zhang S, George A, Hahn M, Safran HP, Chen CC, Seyhan AA, Wong ET, El-Deiry WS.   +11 more
europepmc   +1 more source

Raphin-1 mediates the survival and sensitivity to radiation of pediatric-type diffuse high-grade glioma via phosphorylated eukaryotic initiation factor 2α-dependent and -independent processes. [PDF]

Mol Oncol
Eytan K, Leitner M, Toren A, Paglin S, Yalon M.   +4 more
europepmc   +1 more source

Some of the next articles are maybe not open access.

Related searches:

The Clpx G298D Mutation in Clpx-EPP Reveals That Clpx Regulates the Mitochondria Enzymes in Erythroid Heme Synthesis Via Distinct Mechanisms

Blood, 2023
Terminally differentiating red cells synthesize large quantities of heme for hemoglobin production, requiring tight coordination between mitochondrial iron import and synthesis of photosensitive protoporphyrin IX (PPIX). PPIX causes erythropoietic porphyria from loss of function mutations in FECH, or gain of function mutations in ALAS2.
Yvette Y. Yien, Samantha Gillis, Mark Perfetto, Hector Bergonia   +3 more
openaire   +1 more source

ClpX-Mediated Remodeling of Mu Transpososomes [PDF]

Molecular Cell, 2001
Tania A Baker
exaly   +2 more sources

Communication between ClpX and ClpP during substrate processing and degradation

Nature Structural and Molecular Biology, 2004
In the ClpXP compartmental protease, ring hexamers of the AAA(+) ClpX ATPase bind, denature and then translocate protein substrates into the degradation chamber of the double-ring ClpP(14) peptidase. A key question is the extent to which functional communication between ClpX and ClpP occurs and is regulated during substrate processing.
Tania A Baker, Robert T Sauer
exaly   +3 more sources

ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein Substrates [PDF]

Cell, 2011
AAA(+) unfoldases denature and translocate polypeptides into associated peptidases. We report direct observations of mechanical, force-induced protein unfolding by the ClpX unfoldase from E. coli, alone, and in complex with the ClpP peptidase. ClpX hydrolyzes ATP to generate mechanical force and translocate polypeptides through its central pore ...
Gheorghe Chistol, Maurizio Righini, Andreas Martin   +2 more
exaly   +3 more sources

ClpX/P-Dependent Degradation of Novel Substrates in Streptococcus mutans

Journal of Bacteriology, 2022
ClpX/P is a major intracellular proteolytic complex that is responsible for protein quality control in the cell. ClpX, an AAA+ ATPase, distinguishes the potential substrates by recognizing short motifs at the C-terminal end of proteins and delivers the substrates for degradation by ClpP protease.
Vivek Gurung, Indranil Biswas
openaire   +2 more sources

Human and mouse mitochondrial orthologs of bacterial ClpX

Mammalian Genome, 2000
We have determined the cDNA sequence and exon/intron structure of the human CLPX gene encoding a human ortholog of the E. coli ClpX chaperone and protease subunit. The CLPX gene comprises 14 exons and encodes a 633-amino acid-long precursor polypeptide.
Corydon, T J, Wilsbech, M, Jespersgaard, C, Andresen, B S, Borglum, A D, Pedersen, S, Bolund, L, Gregersen, N, Bross, P   +8 more
openaire   +3 more sources