PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16807375-0 2006 Regulation of mouse hepatic alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase, a key enzyme in the tryptophan-nicotinamide adenine dinucleotide pathway, by hepatocyte nuclear factor 4alpha and peroxisome proliferator-activated receptor alpha. NAD 128-161 amino carboxymuconate semialdehyde decarboxylase Mus musculus 28-95 16807375-2 2006 alpha-Amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD) is the key enzyme regulating de novo synthesis of NAD from l-tryptophan (Trp), designated the Trp-NAD pathway. NAD 126-129 amino carboxymuconate semialdehyde decarboxylase Mus musculus 0-67 16807375-2 2006 alpha-Amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD) is the key enzyme regulating de novo synthesis of NAD from l-tryptophan (Trp), designated the Trp-NAD pathway. NAD 126-129 amino carboxymuconate semialdehyde decarboxylase Mus musculus 69-74 16807375-2 2006 alpha-Amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD) is the key enzyme regulating de novo synthesis of NAD from l-tryptophan (Trp), designated the Trp-NAD pathway. NAD 174-177 amino carboxymuconate semialdehyde decarboxylase Mus musculus 0-67 16807375-2 2006 alpha-Amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD) is the key enzyme regulating de novo synthesis of NAD from l-tryptophan (Trp), designated the Trp-NAD pathway. NAD 174-177 amino carboxymuconate semialdehyde decarboxylase Mus musculus 69-74 34089817-5 2021 Supplementation of a specific inhibitor (TES-1025) of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD), a rate-limiting enzyme of NAD+de novo synthesis pathway, promoted SIRT1 activity, increased mtDNA contents and enhanced AMPK expression, thus significantly reduced hair cells loss and deformation. NAD 157-161 amino carboxymuconate semialdehyde decarboxylase Mus musculus 123-128 30356218-3 2018 Here we show that alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD), the enzyme that limits spontaneous cyclization of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde in the de novo NAD+ synthesis pathway, controls cellular NAD+ levels via an evolutionarily conserved mechanism in Caenorhabditis elegans and mouse. NAD 214-218 amino carboxymuconate semialdehyde decarboxylase Mus musculus 87-92 30356218-3 2018 Here we show that alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD), the enzyme that limits spontaneous cyclization of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde in the de novo NAD+ synthesis pathway, controls cellular NAD+ levels via an evolutionarily conserved mechanism in Caenorhabditis elegans and mouse. NAD 256-260 amino carboxymuconate semialdehyde decarboxylase Mus musculus 87-92 30356218-4 2018 Genetic and pharmacological inhibition of ACMSD boosts de novo NAD+ synthesis and sirtuin 1 activity, ultimately enhancing mitochondrial function. NAD 63-67 amino carboxymuconate semialdehyde decarboxylase Mus musculus 42-47 30356218-7 2018 In summary, we identify ACMSD as a key modulator of cellular NAD+ levels, sirtuin activity and mitochondrial homeostasis in kidney and liver. NAD 61-65 amino carboxymuconate semialdehyde decarboxylase Mus musculus 24-29