Biochemical and Biophysical Research Communications
Regular ArticleApoptosis Induced by Human Fas-Associated Factor 1, hFAF1, Requires Its Ubiquitin Homologous Domain, but Not the Fas-Binding Domain
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XIAP Interacts with and Regulates the Activity of FAF1
2017, Biochimica et Biophysica Acta - Molecular Cell ResearchCitation Excerpt :In contrast, the present analyses suggest that XIAP inhibits FAF1-induced cell death. Overexpression of FAF1 sensitizes HeLa and other cell lines to cell death (present results and [32,33,35,49,50]) through the activation of caspase-8 and the subsequent activation of effector caspases. Our experiments with HeLa cells showed that when co-expressed with XIAP, FAF1 is no longer able to induce cell death, even under Fas/CD95 stimulation.
New perspectives on the mutated NGLY1 enigma
2015, Medical HypothesesCitation Excerpt :ArrayExpress public resource for microarray data [6] showed co-expression of NGLY1 and FAF1 proteins in 24 human body tissues, with FAF1-to-NGLY1 ratio being highest (more than 3:1) in skeletal muscle and brain tissues (https://www.ebi.ac.uk/gxa/experiments/E-MTAB-513). FAF1 is an apoptosis-potentiating protein, but the full scope of its functions is not known yet [7,8]. The fact that NGLY1 binds FAF1 through its PUB domain (a protein module of unknown function linked to the ubiquitin–proteasome system) that functions as an AAA ATPase complex p97 binding module [9] makes FAF1 a possible degradation substrate for the ERAD complex.
High entomotoxicity and mechanism of the fungal GalNAc/Gal-specific Rhizoctonia solani lectin in pest insects
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2008, Journal of Biological Chemistry
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