Results 101 to 110 of about 393,592 (390)
Aggresome formation is a protective cellular response to counteract proteasome dysfunction by sequestering misfolded proteins and reducing proteotoxic stress.
Chenliang Zhang+5 more
doaj +1 more source
Peptide size dependent active transport in the proteasome
We investigate the transport of proteins inside the proteasome and propose an active transport mechanism based on a spatially asymmetric interaction potential of peptide chains.
Poeschel, Thorsten, Zaikin, Alexei
core +1 more source
Mifepristone increases mRNA translation rate, triggers the unfolded protein response, increases autophagic flux, and kills ovarian cancer cells in combination with proteasome or lysosome inhibitors [PDF]
The synthetic steroid mifepristone blocks the growth of ovarian cancer cells, yet the mechanism driving such effect is not entirely understood. Unbiased genomic and proteomic screenings using ovarian cancer cell lines of different genetic backgrounds and
Callegari, Eduardo A.+13 more
core +1 more source
Proteasomes in human spermatozoa [PDF]
In the present study we describe the localization of proteasomes in human spermatozoa by means of immunolabelling with different monoclonal and polyclonal antibodies detected by confocal microscopy. Western blotting confirmed the specificity of the antibodies and has shown that proteasomes are present in spermatozoa and in seminal fluid. In spermatozoa
Wojcik, C.+4 more
openaire +4 more sources
FEM1B enhances TRAIL‐induced apoptosis in T lymphocytes and monocytes
FEM1B facilitates TRAIL‐induced apoptosis through distinct mechanisms in T lymphocytes and monocytes. In T lymphocytes, FEM1B engages with TRAF2, leading to a reduction in TRAF2 expression, which subsequently lessens TRAF2's inhibitory influence on caspase‐8.
Chenbo Yang+5 more
wiley +1 more source
Proteasome Activation as a New Therapeutic Approach To Target Proteotoxic Disorders.
Proteasomes are multienzyme complexes that maintain protein homeostasis (proteostasis) and important cellular functions through the degradation of misfolded, redundant, and damaged proteins.
Evert Njomen, J. Tepe
semanticscholar +1 more source
The E3 ubiquitin ligase, RNF219, suppresses CNOT6L expression to exhibit antiproliferative activity
We identified RNF219 as a CCR4‐NOT complex‐interacting E3 ubiquitin ligase that targets the CCR4‐NOT subunit CNOT6L for ubiquitination. RNF219 directly binds to the DUF3819 domain of CNOT1 through its putative α‐helix spanning amino acids 521–542. Our findings also suggest that antiproliferative activity of RNF219 is at least partially mediated by ...
Shou Soeda+9 more
wiley +1 more source
Introduction Mutations in pre‐mRNA processing factor 31 (PRPF31), a core protein of the spliceosomal tri‐snRNP complex, cause autosomal‐dominant retinitis pigmentosa (adRP).
Maria Georgiou+19 more
doaj +1 more source
Prion degradation pathways: Potential for therapeutic intervention [PDF]
Prion diseases are fatal neurodegenerative disorders. Pathology is closely linked to the misfolding of native cellular PrP(C) into the disease-associated form PrP(Sc) that accumulates in the brain as disease progresses. Although treatments have yet to be
Goold, R, McKinnon, C, Tabrizi, SJ
core +1 more source
ABSTRACT C‐truncating variants in the charged multivesicular body protein 2B (CHMP2B) gene are a rare cause of frontotemporal lobar degeneration (FTLD), previously identified only in Denmark, Belgium, and China. We report a novel CHMP2B splice‐site variant (c.35‐1G>A) associated with familial FTLD in Spain. The cases were two monozygotic male twins who
Sara Rubio‐Guerra+17 more
wiley +1 more source