Results 301 to 310 of about 101,614 (324)
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Selective degradation of p62 by autophagy
Seminars in Immunopathology, 2010The autophagy-lysosome pathway is a highly conserved bulk degradation system in eukaryotes. During starvation, cytoplasmic constituents are non-selectively degraded by autophagy, and the resulting amino acids are utilized for cell survival. By taking advantage of mouse genetics, many physiological functions of mammalian autophagy have been uncovered ...
Yoshinobu, Ichimura, Masaaki, Komatsu
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1995
Abstract The amino-terminal half of p62 contains a domain with predicted RNA binding properties (Wong etal. 1992). This domain is highly related to a domain found in the Artemia hnRNP protein GRP33. In the C-terminal domain, a region containing 12 arginine-glycine pairs was identified: this is a characteristic of other RNA binding ...
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Abstract The amino-terminal half of p62 contains a domain with predicted RNA binding properties (Wong etal. 1992). This domain is highly related to a domain found in the Artemia hnRNP protein GRP33. In the C-terminal domain, a region containing 12 arginine-glycine pairs was identified: this is a characteristic of other RNA binding ...
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p62, an autophagy hero or culprit?
Nature Cell Biology, 2010The p62 protein recognizes toxic cellular waste, which is then scavenged by a sequestration process known as self-eating or autophagy. Lack of autophagy leads to accumulation of p62, which is not good for liver cells, as it induces a cellular stress response that leads to disease.
Tor Erik, Rusten, Harald, Stenmark
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p62/SQSTM1 analysis in frontotemporal lobar degeneration
Neurobiology of Aging, 2015Mutations in the gene p62/SQSTM1 have been reported as a relatively rare cause of frontotemporal lobar degeneration (FTLD). To establish whether this was the case for cases of FTLD from the United Kingdom, we sequenced the sequenced the entire open reading frame of this gene in a large cohort of patients.
Miller, L +10 more
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Limiting inflammation with p62
Science Signaling, 2016Without the adaptor protein p62, macrophages produce tissue-damaging amounts of the proinflammatory cytokine IL-1β.
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Analysis of nuclear pore protein p62 glycosylation
Biochemistry, 1995Glycoprotein components of the nuclear pore are essential for nuclear transport and are modified by both glycosylation and phosphorylation. The function and control of these post-translational modifications are poorly understood. Glycosylation of the major rat nuclear pore glycoprotein, p62, was examined in vitro using recombinant p62 as a substrate ...
W A, Lubas +3 more
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