Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "Within the cardiac isoform's amino-terminal extension, serines are present at residues 23 and 24 (Ser23/Ser24), which serve as substrates for protein kinase A (PKA), which is activated in response to ?-adrenergic stimulation of the heart (3). Several investigations report that PKA-mediated phosphorylation of cTnI results in a reduction in myofilament Ca2+ sensitivity (4), an increase in cross-bridge cycling (5), and increased binding of cTnI to the thin filament. Cardiac TnI is also a substrate for protein kinase C (PKC) phosphorylation at Ser43/Ser45 and Thr144 (position 143 in the human protein) (6). However, the substrate specificity of these sites is not absolute, since PKC can phosphorylate the PKA sites (7-9). " ?g. }

• _5 value "Within the cardiac isoform's amino-terminal extension, serines are present at residues 23 and 24 (Ser23/Ser24), which serve as substrates for protein kinase A (PKA), which is activated in response to ?-adrenergic stimulation of the heart (3). Several investigations report that PKA-mediated phosphorylation of cTnI results in a reduction in myofilament Ca2+ sensitivity (4), an increase in cross-bridge cycling (5), and increased binding of cTnI to the thin filament. Cardiac TnI is also a substrate for protein kinase C (PKC) phosphorylation at Ser43/Ser45 and Thr144 (position 143 in the human protein) (6). However, the substrate specificity of these sites is not absolute, since PKC can phosphorylate the PKA sites (7-9). " provenance.
• _5 value "Within the cardiac isoform's amino-terminal extension, serines are present at residues 23 and 24 (Ser23/Ser24), which serve as substrates for protein kinase A (PKA), which is activated in response to ?-adrenergic stimulation of the heart (3). Several investigations report that PKA-mediated phosphorylation of cTnI results in a reduction in myofilament Ca2+ sensitivity (4), an increase in cross-bridge cycling (5), and increased binding of cTnI to the thin filament. Cardiac TnI is also a substrate for protein kinase C (PKC) phosphorylation at Ser43/Ser45 and Thr144 (position 143 in the human protein) (6). However, the substrate specificity of these sites is not absolute, since PKC can phosphorylate the PKA sites (7-9). " provenance.
• _5 value "Within the cardiac isoform's amino-terminal extension, serines are present at residues 23 and 24 (Ser23/Ser24), which serve as substrates for protein kinase A (PKA), which is activated in response to ?-adrenergic stimulation of the heart (3). Several investigations report that PKA-mediated phosphorylation of cTnI results in a reduction in myofilament Ca2+ sensitivity (4), an increase in cross-bridge cycling (5), and increased binding of cTnI to the thin filament. Cardiac TnI is also a substrate for protein kinase C (PKC) phosphorylation at Ser43/Ser45 and Thr144 (position 143 in the human protein) (6). However, the substrate specificity of these sites is not absolute, since PKC can phosphorylate the PKA sites (7-9). " provenance.
• _5 value "Within the cardiac isoform's amino-terminal extension, serines are present at residues 23 and 24 (Ser23/Ser24), which serve as substrates for protein kinase A (PKA), which is activated in response to ?-adrenergic stimulation of the heart (3). Several investigations report that PKA-mediated phosphorylation of cTnI results in a reduction in myofilament Ca2+ sensitivity (4), an increase in cross-bridge cycling (5), and increased binding of cTnI to the thin filament. Cardiac TnI is also a substrate for protein kinase C (PKC) phosphorylation at Ser43/Ser45 and Thr144 (position 143 in the human protein) (6). However, the substrate specificity of these sites is not absolute, since PKC can phosphorylate the PKA sites (7-9). " provenance.
• _5 value "Within the cardiac isoform's amino-terminal extension, serines are present at residues 23 and 24 (Ser23/Ser24), which serve as substrates for protein kinase A (PKA), which is activated in response to ?-adrenergic stimulation of the heart (3). Several investigations report that PKA-mediated phosphorylation of cTnI results in a reduction in myofilament Ca2+ sensitivity (4), an increase in cross-bridge cycling (5), and increased binding of cTnI to the thin filament. Cardiac TnI is also a substrate for protein kinase C (PKC) phosphorylation at Ser43/Ser45 and Thr144 (position 143 in the human protein) (6). However, the substrate specificity of these sites is not absolute, since PKC can phosphorylate the PKA sites (7-9). " provenance.
• _5 value "Within the cardiac isoform's amino-terminal extension, serines are present at residues 23 and 24 (Ser23/Ser24), which serve as substrates for protein kinase A (PKA), which is activated in response to ?-adrenergic stimulation of the heart (3). Several investigations report that PKA-mediated phosphorylation of cTnI results in a reduction in myofilament Ca2+ sensitivity (4), an increase in cross-bridge cycling (5), and increased binding of cTnI to the thin filament. Cardiac TnI is also a substrate for protein kinase C (PKC) phosphorylation at Ser43/Ser45 and Thr144 (position 143 in the human protein) (6). However, the substrate specificity of these sites is not absolute, since PKC can phosphorylate the PKA sites (7-9). " provenance.
• _5 value "Within the cardiac isoform's amino-terminal extension, serines are present at residues 23 and 24 (Ser23/Ser24), which serve as substrates for protein kinase A (PKA), which is activated in response to ?-adrenergic stimulation of the heart (3). Several investigations report that PKA-mediated phosphorylation of cTnI results in a reduction in myofilament Ca2+ sensitivity (4), an increase in cross-bridge cycling (5), and increased binding of cTnI to the thin filament. Cardiac TnI is also a substrate for protein kinase C (PKC) phosphorylation at Ser43/Ser45 and Thr144 (position 143 in the human protein) (6). However, the substrate specificity of these sites is not absolute, since PKC can phosphorylate the PKA sites (7-9). " provenance.
• _5 value "Within the cardiac isoform's amino-terminal extension, serines are present at residues 23 and 24 (Ser23/Ser24), which serve as substrates for protein kinase A (PKA), which is activated in response to ?-adrenergic stimulation of the heart (3). Several investigations report that PKA-mediated phosphorylation of cTnI results in a reduction in myofilament Ca2+ sensitivity (4), an increase in cross-bridge cycling (5), and increased binding of cTnI to the thin filament. Cardiac TnI is also a substrate for protein kinase C (PKC) phosphorylation at Ser43/Ser45 and Thr144 (position 143 in the human protein) (6). However, the substrate specificity of these sites is not absolute, since PKC can phosphorylate the PKA sites (7-9). " provenance.