Results 31 to 40 of about 267,857 (250)
Oxidatively Modified Proteins: Cause and Control of Diseases
Applied Sciences, 2020 Proteins succumb to numerous post-translational modifications (PTMs). These relate to enzymatic or non-enzymatic reactions taking place in either the intracellular or extracellular compartment.
Ramona Clemen, Sander Bekeschus
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Post-translational modifications on the retinoblastoma protein
Journal of Biomedical Science, 2022 The retinoblastoma protein (pRb) functions as a cell cycle regulator controlling G1 to S phase transition and plays critical roles in tumour suppression. It is frequently inactivated in various tumours.
Linbin Zhou +6 more
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Potential protein post-translational modification in ERp57: A phenotype marker for male fertility
Journal of Human Reproductive Sciences, 2010 Background : In protein expression, post-translational modification is an important process. It is also an important process in human reproductive science. ERp57 is a molecule that is mentioned for post-translational modification. ERp57 is a component of
Viroj Wiwanitkit
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Post-translational modification of RAS proteins
Current Opinion in Structural Biology, 2021 Mutations of RAS genes drive cancer more frequently than any other oncogene. RAS proteins integrate signals from a wide array of receptors and initiate downstream signaling through pathways that control cellular growth. RAS proteins are fundamentally binary molecular switches in which the off/on state is determined by the binding of GDP or GTP ...
Sharon L, Campbell, Mark R, Philips
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Post-translational modifications of EZH2 in cancer
Cell & Bioscience, 2020 Enhancer of zeste homolog 2 (EZH2), as a main component of Polycomb Repressive Complex 2, catalyzes histone H3K27me3 to silence its target gene expression. EZH2 upregulation results in cancer development and poor prognosis of cancer patients.
Zhongwei Li +8 more
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Post-translational modifications in circadian rhythms [PDF]
Trends in Biochemical Sciences, 2009 The pace has quickened in circadian biology research. In particular, an abundance of results focused on post-translational modifications (PTMs) is sharpening our view of circadian molecular clockworks. PTMs affect nearly all aspects of clock biology; in some cases they are essential for clock function and in others, they provide layers of regulatory ...
Arun, Mehra +3 more
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Reciprocal control of viral infection and phosphoinositide dynamics
FEBS Letters, EarlyView.Phosphoinositides, although scarce, regulate key cellular processes, including membrane dynamics and signaling. Viruses exploit these lipids to support their entry, replication, assembly, and egress. The central role of phosphoinositides in infection highlights phosphoinositide metabolism as a promising antiviral target.
Marie Déborah Bancilhon, Bruno Mesmin
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Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?
FEBS Letters, EarlyView.This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes +3 more
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Targeting DNA-Protein Crosslinks via Post-Translational Modifications
Frontiers in Molecular Biosciences, 2022 Covalent binding of proteins to DNA forms DNA-protein crosslinks (DPCs), which represent cytotoxic DNA lesions that interfere with essential processes such as DNA replication and transcription.
Xueyuan Leng, Julien P. Duxin
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FEBS Letters, EarlyView.This study reveals how the mitochondrial protein Slm35 is regulated in Saccharomyces cerevisiae. The authors identify stress‐responsive DNA elements and two upstream open reading frames (uORFs) in the 5′ untranslated region of SLM35. One uORF restricts translation, and its mutation increases Slm35 protein levels and mitophagy.
Hernán Romo‐Casanueva +5 more
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