PMC:6562565 / 12161-13215 JSONTXT

{"project":"MyTest","denotations":[{"id":"31244820-15747061-35365346","span":{"begin":271,"end":274},"obj":"15747061"},{"id":"31244820-11734617-35365347","span":{"begin":365,"end":368},"obj":"11734617"},{"id":"31244820-11734617-35365348","span":{"begin":452,"end":455},"obj":"11734617"},{"id":"31244820-11734617-35365349","span":{"begin":827,"end":830},"obj":"11734617"},{"id":"31244820-16497986-35365350","span":{"begin":1044,"end":1047},"obj":"16497986"},{"id":"31244820-15130776-35365351","span":{"begin":1049,"end":1052},"obj":"15130776"}],"namespaces":[{"prefix":"_base","uri":"https://www.uniprot.org/uniprot/testbase"},{"prefix":"UniProtKB","uri":"https://www.uniprot.org/uniprot/"},{"prefix":"uniprot","uri":"https://www.uniprot.org/uniprotkb/"}],"text":"Of the four classes of Gα proteins characterized to date, namely Gαs, Gαi, Gαq/11, Gα12/13, only Gαs and Gαi directly influence the activity of adenylyl cyclases (AC), enzymes that catalyze the cyclization of intracellular ATP into cyclic adenosine monophosphate (cAMP) (114). In terms of function, triggering of the Gαs-coupled A2AR and A2BR promotes AC activity (115). In contrast, stimulation of the Gαi-paired A1R and A3R inhibits cAMP generation (115). Although modulation of intracellular cAMP content constitutes a crucial aspect of extracellular adenosine-exerted regulation, stimulation of its receptors induces a variety of cAMP-independent biochemical effects, such as A1R/Gαi, A2BR/Gαq/11, A3R/Gαq/11-induced stimulation of phospholipase C (PLC) activity and A1R/Gαi, A2AR, A2BR/Gq/11, A3R-mediated ERK activation (115). Finally, elevation of extracellular adenosine levels induces receptor-independent boosting of AMP-activated protein kinase (AMPK) via intracellular transfer of this nucleoside followed by its conversion to AMP (116, 117)."}

{"project":"TEST0","denotations":[{"id":"31244820-236-243-3849494","span":{"begin":271,"end":274},"obj":"[\"15747061\"]"},{"id":"31244820-88-95-3849495","span":{"begin":365,"end":368},"obj":"[\"11734617\"]"},{"id":"31244820-81-88-3849496","span":{"begin":452,"end":455},"obj":"[\"11734617\"]"},{"id":"31244820-231-238-3849497","span":{"begin":827,"end":830},"obj":"[\"11734617\"]"},{"id":"31244820-211-218-3849498","span":{"begin":1044,"end":1047},"obj":"[\"16497986\"]"},{"id":"31244820-216-223-3849499","span":{"begin":1049,"end":1052},"obj":"[\"15130776\"]"}],"text":"Of the four classes of Gα proteins characterized to date, namely Gαs, Gαi, Gαq/11, Gα12/13, only Gαs and Gαi directly influence the activity of adenylyl cyclases (AC), enzymes that catalyze the cyclization of intracellular ATP into cyclic adenosine monophosphate (cAMP) (114). In terms of function, triggering of the Gαs-coupled A2AR and A2BR promotes AC activity (115). In contrast, stimulation of the Gαi-paired A1R and A3R inhibits cAMP generation (115). Although modulation of intracellular cAMP content constitutes a crucial aspect of extracellular adenosine-exerted regulation, stimulation of its receptors induces a variety of cAMP-independent biochemical effects, such as A1R/Gαi, A2BR/Gαq/11, A3R/Gαq/11-induced stimulation of phospholipase C (PLC) activity and A1R/Gαi, A2AR, A2BR/Gq/11, A3R-mediated ERK activation (115). Finally, elevation of extracellular adenosine levels induces receptor-independent boosting of AMP-activated protein kinase (AMPK) via intracellular transfer of this nucleoside followed by its conversion to AMP (116, 117)."}

{"project":"2_test","denotations":[{"id":"31244820-15747061-35365346","span":{"begin":271,"end":274},"obj":"15747061"},{"id":"31244820-11734617-35365347","span":{"begin":365,"end":368},"obj":"11734617"},{"id":"31244820-11734617-35365348","span":{"begin":452,"end":455},"obj":"11734617"},{"id":"31244820-11734617-35365349","span":{"begin":827,"end":830},"obj":"11734617"},{"id":"31244820-16497986-35365350","span":{"begin":1044,"end":1047},"obj":"16497986"},{"id":"31244820-15130776-35365351","span":{"begin":1049,"end":1052},"obj":"15130776"}],"text":"Of the four classes of Gα proteins characterized to date, namely Gαs, Gαi, Gαq/11, Gα12/13, only Gαs and Gαi directly influence the activity of adenylyl cyclases (AC), enzymes that catalyze the cyclization of intracellular ATP into cyclic adenosine monophosphate (cAMP) (114). In terms of function, triggering of the Gαs-coupled A2AR and A2BR promotes AC activity (115). In contrast, stimulation of the Gαi-paired A1R and A3R inhibits cAMP generation (115). Although modulation of intracellular cAMP content constitutes a crucial aspect of extracellular adenosine-exerted regulation, stimulation of its receptors induces a variety of cAMP-independent biochemical effects, such as A1R/Gαi, A2BR/Gαq/11, A3R/Gαq/11-induced stimulation of phospholipase C (PLC) activity and A1R/Gαi, A2AR, A2BR/Gq/11, A3R-mediated ERK activation (115). Finally, elevation of extracellular adenosine levels induces receptor-independent boosting of AMP-activated protein kinase (AMPK) via intracellular transfer of this nucleoside followed by its conversion to AMP (116, 117)."}