Results 161 to 170 of about 26,049 (207)
Injury then recovery markedly rewires the DNA methylome in aged skeletal muscle.The addition of senolytics during muscle regeneration decelerates DNAmAGE more than regeneration alone as well as targets collagen remodeling and stem cell function‐related genes.
Toby L. Chambers+16 more
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Schematic diagram illustrating the protective role of protein disulphide isomerase (PDI) against DNA damage via non‐homologous end‐joining (NHEJ), which repairs double stranded DNA breaks (DSBs). Induction of DNA damage results in the formation of γH2AX and p53‐binding protein 1 foci during NHEJ repair of DSBs.
Sina Shadfar+12 more
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Microglia Single‐Cell RNA‐Seq Enables Robust and Applicable Markers of Biological Aging
This study develops computational approaches to translate single‐cell based transcriptomic signatures of microglia into aging clocks, or machine learning models of age. These models can be broadly applied to new single‐cell or bulk RNA‐sequencing datasets to gain novel biological insights and evaluate how environmental inputs (such as stress) affect ...
Natalie Stanley+4 more
wiley +1 more source
hTERT Increases TRF2 to Induce Telomere Compaction and Extend Cell Replicative Lifespan
In contrast to the dogma that a subset of short telomeres initiates senescence, hTERT variants unable to maintain telomere length block senescence by stabilizing TRF2 via inhibiting upstream E3 ubiquitin ligases. This noncanonical hTERT function also compacts telomeres and blocks senescence‐associated DNA damage signaling. Cancer cells expressing hTERT
Nancy Adam+15 more
wiley +1 more source
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The Cullin-RING Ubiquitin-Protein Ligases
Annual Review of Plant Biology, 2011The posttranslational addition of ubiquitin (Ub) helps control the half-life, localization, and action of many intracellular plant proteins. A primary function is the degradation of ubiquitylated proteins by the 26S proteasome, which in turn plays important housekeeping and regulatory roles by removing aberrant polypeptides and various normal short ...
Zhihua Hua, Richard D. Vierstra
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Ubiquitin–protein ligases in muscle wasting
The International Journal of Biochemistry & Cell Biology, 2005Muscle wasting occurs when rates of protein degradation outstrip rates of protein synthesis. Accelerated rates of protein degradation develop in atrophying muscle largely through activation of the ubiquitin-proteasome pathway. The complexity of the ubiquitination process, however, has hampered our understanding of how this pathway is activated in ...
Stewart H. Lecker+2 more
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Ubiquitin-Protein Ligases - Novel Therapeutic Targets?
Current Protein and Peptide Science, 2004Intracellular protein degradation is a tightly regulated process that in many cases is controlled by protein ubiquitylation. The ubiquitin pathway is a major route by which cells not only remove normal proteins at the appropriate time but also abnormally folded normal or mutant, cytoplasmic and membrane, proteins.
Philip A. Robinson, Helen C. Ardley
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Identification of the ubiquitin–protein ligase that recognizes oxidized IRP2
Nature Cell Biology, 2003The ubiquitin system is involved in several basic cellular functions. Ubiquitination is carried out by a cascade of three reactions catalysed by the E1, E2 and E3 enzymes. Among these, the E3 ubiquitin-protein ligases have a pivotal role in determining the specificity of the system by recognizing the target substrates through defined targeting motifs ...
Nagahiro Minato+11 more
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Role of Ubiquitin Protein Ligases in the Pathogenesis of Polyglutamine Diseases
Neurochemical Research, 2007The accumulation of intracellular protein deposits as inclusion bodies is the common pathological hallmark of most age related neurodegenerative disorders including polyglutamine diseases. Appearances of aggregates of the misfolded mutant disease proteins suggest that the cells are unable to efficiently degrade them, and failure of clearance leads to ...
Priyanka Dikshit, Nihar Ranjan Jana
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Progress in regulation of activity and stability of ubiquitin protein ligase MDM2
Hereditas (Beijing), 2009The ubiquitin protein ligase (E3) MDM2 (Murine double minute 2) possesses oncogenic activities. Overexpression of this protein enhances degradation and inactivation of the tumor suppressor p53. At least 7% of all human tumors exhibit inappropriate amplification of mdm2, whereas p53 gene remains in its wild-type configuration.
Jing NIE+2 more
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