2.1.2.3	malfunction	growth deficiency phenotypes (in un-supplemented M9 minimal medium containing thymidine) are direct consequences of the gene deletions	-, 757625	
2.1.2.3	malfunction	inhibition of the enzyme results in depletion of purine nucleotides	736619	
2.1.2.3	malfunction	insulin stimulation and enzyme ATIC knockdown readily increase the level of AMP-activated protein kinase-Thr172 phosphorylation in insulin receptor complexes. Enzyme ATIC, protein-tyrosine phosphatase-like A domain-containing protein 1, and AMP-activated protein kinase knockdown affects insulin receptor internalization in HEK-293 cells	736802	
2.1.2.3	malfunction	insulin stimulation and enzyme ATIC knockdown readily increase the level of AMPK-Thr172 phosphorylation in insulin receptor complexes	736802	
2.1.2.3	malfunction	the ATIC rs2372536 GG enzyme genotype is associated with improved clinical remission in juvenile idiopathic arthritis during methotrexate therapy, only one of the ATIC single nucleotide polymorphisms show any trend toward methotrexate response in an independent cohort of North American juvenile idiopathic arthritis children	737222	
2.1.2.3	metabolism	aminoimidazolecarboxamide ribotide transformylase is involved in the de novo purine nucleotide biosynthesis	719415	
2.1.2.3	metabolism	aminoimidazolecarboxamide ribotide transformylase is involved in the de novo purine nucleotide biosynthesis. No enzyme complex that generates 10-formyl-5,6,7,8-tetrahydrofolate and immediately channels or furnishes it to AICAR transformylase is needed because the first oxidation product of 10-formyl-5,6,7,8-tetrahydrofolate is 10-formyl-7,8-dihydrofolate that is utilized by this transformylase	719415	
2.1.2.3	metabolism	last and rate-limiting enzyme of the de novo purine synthesis pathway	736802	
2.1.2.3	metabolism	last enzyme of the de novo purine synthesis pathway. The enzyme plays a central role in insulin signaling and the Golgi/endosomes protein network	757662	
2.1.2.3	metabolism	the 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) transformylase/inosine monophosphate (IMP) cyclohydrolase (ATIC) catalyzes final two steps of purine nucleotide de novo biosynthetic pathway. The cell proliferation activity of the enzyme is observed where it promotes proliferation and viability of NIH 3T3 and RIN-5F cells, exhibits in vitro wound healing in NIH 3T3 fibroblast cells, and rescues RIN-5F cells from the cytotoxic effects of palmitic acid and high glucose	756701