Mitochondrial Microproteins: Emerging Regulators in Neurodevelopment and Neurodegeneration
Mitochondrial microproteins have emerged as critical regulators of mitochondrial function. Neurons are highly dependent on mitochondria to sustain their function. Mitochondrial microproteins can be deregulated and can contribute to the pathogenesis of neurodegenerative disorders. Mitochondrial microproteins are involved in neuronal development. However,
Nada Borghol+2 more
wiley +1 more source
Exploring the roles of snoRNA-induced ribosome heterogeneity in equine osteoarthritis. [PDF]
Chabronova A+6 more
europepmc +1 more source
Studies on the role of polyamines associated with the ribosomes from Bacillus stearothermophilus [PDF]
Lewis Stevens, Marcelle R. Morrison
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When the Clock Is Ticking: The Role of Mitotic Duration in Cell Fate Determination
Recently, several studies identified mechanisms by which cells measure mitotic duration and how this influences cell fate, leading to normal cell cycle progression or G1 arrest. In light of drug‐resistant cancer cells that continue proliferating even after mitotic errors, understanding these mechanisms opens the door for new potential therapeutic ...
Cornelia Sala, Elmar Schiebel
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Impact of Gemin5 in protein synthesis: phosphoresidues of the dimerization domain regulate ribosome binding. [PDF]
Abellan S+3 more
europepmc +1 more source
Preparation of ribosome-free membranes from rat liver microsomes by means of lithium chloride [PDF]
Timothy Scott‐Burden, Å.O. Hawtrey
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Photocaged dinucleoside tetraphosphates can be incorporated into mRNA by T7 RNA polymerase. Subsequent irradiation with light activates 5′ cap interactions and translation. These 5′ cap analogs are useful tools to probe the functions of naturally occurring dinucleoside tetraphosphates and their role in bacteria and mammalian cells.
Cedrik Kühling+5 more
wiley +1 more source
MEMBRANE-BOUND RIBOSOMES IN KIDNEY [PDF]
G. C. Priestley, Ronald A. Malt
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TRiC Is a Structural Component of Mammalian Sperm Axonemes
ABSTRACT The TRiC chaperonin is responsible for folding ~5%–10% of the proteome in eukaryotic cells. Our recent cryo‐electron microscopy studies of axonemes from diverse mammalian cell types led to the surprising discovery that a fully assembled TRiC chaperonin is a structural component of mammalian sperm flagella, where it is tethered to the radial ...
Alan Brown+3 more
wiley +1 more source
Carrot and stick: how RNase R contributes to function and destruction of the translation machinery. [PDF]
Paternoga H, Dimitrova-Paternoga L.
europepmc +1 more source