Pub. Date : 2021 Nov
PMID : 34403688
17 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Recently, we elucidated the molecular mechanism of SARM1 activation, demonstrating that SARM1 is a metabolic sensor regulated by the levels of NAD+ and its precursor, nicotinamide mononucleotide (NMN), via their competitive binding to an allosteric site within the SARM1 N-terminal ARM domain. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 2 | Recently, we elucidated the molecular mechanism of SARM1 activation, demonstrating that SARM1 is a metabolic sensor regulated by the levels of NAD+ and its precursor, nicotinamide mononucleotide (NMN), via their competitive binding to an allosteric site within the SARM1 N-terminal ARM domain. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 3 | Recently, we elucidated the molecular mechanism of SARM1 activation, demonstrating that SARM1 is a metabolic sensor regulated by the levels of NAD+ and its precursor, nicotinamide mononucleotide (NMN), via their competitive binding to an allosteric site within the SARM1 N-terminal ARM domain. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 4 | However, with injury or disease the levels of the NAD+ biosynthetic enzyme NMNAT2 drop, increasing the NMN/ NAD+ ratio and thereby promoting NMN binding to the SARM1 allosteric site, which in turn induces a conformational change activating the SARM1 NAD+ hydrolase. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 5 | However, with injury or disease the levels of the NAD+ biosynthetic enzyme NMNAT2 drop, increasing the NMN/ NAD+ ratio and thereby promoting NMN binding to the SARM1 allosteric site, which in turn induces a conformational change activating the SARM1 NAD+ hydrolase. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 6 | However, with injury or disease the levels of the NAD+ biosynthetic enzyme NMNAT2 drop, increasing the NMN/ NAD+ ratio and thereby promoting NMN binding to the SARM1 allosteric site, which in turn induces a conformational change activating the SARM1 NAD+ hydrolase. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 7 | Hence, NAD+ metabolites both regulate the activation of SARM1 and, in turn, are regulated by the SARM1 NAD+ hydrolase. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 8 | Hence, NAD+ metabolites both regulate the activation of SARM1 and, in turn, are regulated by the SARM1 NAD+ hydrolase. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 9 | Hence, NAD+ metabolites both regulate the activation of SARM1 and, in turn, are regulated by the SARM1 NAD+ hydrolase. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 10 | Hence, NAD+ metabolites both regulate the activation of SARM1 and, in turn, are regulated by the SARM1 NAD+ hydrolase. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 11 | This dual upstream and downstream role for NAD+ metabolites in SARM1 function has hindered mechanistic understanding of axoprotective mechanisms that manipulate the NAD+ metabolome. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 12 | We find that these approaches not only lead to a decrease in the levels of the SARM1 activator NMN, but also an increase in the levels of the NAD+ precursor nicotinic acid mononucleotide (NaMN). | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 13 | Together, these results demonstrate that the SARM1 allosteric pocket can bind a diverse set of metabolites including NMN, NAD+, and NaMN to monitor cellular NAD+ homeostasis and regulate SARM1 NAD+ hydrolase activity. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 14 | Together, these results demonstrate that the SARM1 allosteric pocket can bind a diverse set of metabolites including NMN, NAD+, and NaMN to monitor cellular NAD+ homeostasis and regulate SARM1 NAD+ hydrolase activity. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 15 | Together, these results demonstrate that the SARM1 allosteric pocket can bind a diverse set of metabolites including NMN, NAD+, and NaMN to monitor cellular NAD+ homeostasis and regulate SARM1 NAD+ hydrolase activity. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 16 | Together, these results demonstrate that the SARM1 allosteric pocket can bind a diverse set of metabolites including NMN, NAD+, and NaMN to monitor cellular NAD+ homeostasis and regulate SARM1 NAD+ hydrolase activity. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |
| 17 | Together, these results demonstrate that the SARM1 allosteric pocket can bind a diverse set of metabolites including NMN, NAD+, and NaMN to monitor cellular NAD+ homeostasis and regulate SARM1 NAD+ hydrolase activity. | NAD | sterile alpha and TIR motif containing 1 | Homo sapiens |