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10.1007/s00775-018-1538-8 http://scihub22266oqcxt.onion/10.1007/s00775-018-1538-8 C6006223!6006223!29435647     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29435647&cmd=llinks): Failed to open stream: HTTP request failed! 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The unique fold and lability of the 2Fe-2S clusters of NEET proteins mediate their key functions in health and disease |pdf=|usr=}}{{29435647}} gab.com Text The unique fold and lability of the 2Fe-2S clusters of NEET proteins mediate their key functions in health and disease JO: J Biol Inorg Chem http://www.kidney.de/pget.php?&tw=1&pmid=29435647 #FOAvip Abstract: NEET proteins comprise a new class of [2Fe-2S] cluster proteins. In human, three genes encode for NEET proteins: cisd1 encodes mitoNEET (mNT), cisd2 encodes the Nutrient-deprivation autophagy factor-1 (NAF-1) and cisd3 encodes MiNT (Miner2). These recently discovered proteins play key roles in many processes related to normal metabolism and disease. Indeed, NEET proteins are involved in iron, Fe-S, and reactive oxygen homeostasis in cells and play an important role in regulating apoptosis and autophagy. mNT and NAF-1 are homodimeric and reside on the outer mitochondrial membrane. NAF-1 also resides in the membranes of the ER associated mitochondrial membranes (MAM) and the ER. MiNT is a monomer with distinct asymmetry in the molecular surfaces surrounding the clusters. Unlike its paralogs mNT and NAF-1, it resides within the mitochondria. NAF-1 and mNT share similar backbone folds to the plant homodimeric NEET protein (At-NEET), while MiNT?s backbone fold resembles a bacterial MiNT protein. Despite the variation of amino acid composition among these proteins, all NEET proteins retained their unique CDGSH domain harboring their unique 3Cys:1His [2Fe-2S] cluster coordination through evolution. The coordinating exposed His was shown to convey the lability to the NEET proteins? [2Fe-2S] clusters. In this minireview, we discuss the NEET fold and its structural elements. Special attention is given to the unique lability of the NEETs? [2Fe-2S] cluster and the implication of the latter to the NEET proteins? cellular and systemic function in health and disease. Graphical abstract: Twit Text FOAVip The unique fold and lability of the 2Fe-2S clusters of NEET proteins mediate their key functions in health and disease ????J Biol Inorg Chem http://www.kidney.de/pget.php?&tw=1&pmid=29435647 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29435647 #FOAvip English Wikipedia <ref>{{Cite pmid|29435647}}</ref> The unique fold and lability of the 2Fe-2S clusters of NEET proteins mediate their key functions in health and disease #MMPMID29435647 Karmi O; Marjault HB; Pesce L; Carloni P; Onuchic JN; Jennings PA; Mittler R; Nechushtai R J Biol Inorg Chem 2018[]; 23 (4): 599-612 PMID29435647show ga Abstract: NEET proteins comprise a new class of [2Fe-2S] cluster proteins. In human, three genes encode for NEET proteins: cisd1 encodes mitoNEET (mNT), cisd2 encodes the Nutrient-deprivation autophagy factor-1 (NAF-1) and cisd3 encodes MiNT (Miner2). These recently discovered proteins play key roles in many processes related to normal metabolism and disease. Indeed, NEET proteins are involved in iron, Fe-S, and reactive oxygen homeostasis in cells and play an important role in regulating apoptosis and autophagy. mNT and NAF-1 are homodimeric and reside on the outer mitochondrial membrane. NAF-1 also resides in the membranes of the ER associated mitochondrial membranes (MAM) and the ER. MiNT is a monomer with distinct asymmetry in the molecular surfaces surrounding the clusters. Unlike its paralogs mNT and NAF-1, it resides within the mitochondria. NAF-1 and mNT share similar backbone folds to the plant homodimeric NEET protein (At-NEET), while MiNT?s backbone fold resembles a bacterial MiNT protein. Despite the variation of amino acid composition among these proteins, all NEET proteins retained their unique CDGSH domain harboring their unique 3Cys:1His [2Fe-2S] cluster coordination through evolution. The coordinating exposed His was shown to convey the lability to the NEET proteins? [2Fe-2S] clusters. In this minireview, we discuss the NEET fold and its structural elements. Special attention is given to the unique lability of the NEETs? [2Fe-2S] cluster and the implication of the latter to the NEET proteins? cellular and systemic function in health and disease. Graphical abstract: äThe unique fold and lability of the 2Fe-2S clusters of NEET proteins(epmc).pdf DeepDyve Pubget Overpricing