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PubMed:6150036 JSONTXT 23 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-85 Sentence denotes Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon.
T1 0-85 Sentence denotes Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon.
T2 86-227 Sentence denotes Caldesmon, a major calmodulin- and actin-binding protein of smooth muscle (Sobue, K., Muramoto, Y., Fujita, M., and Kakiuchi, S. (1981) Proc.
T2 86-227 Sentence denotes Caldesmon, a major calmodulin- and actin-binding protein of smooth muscle (Sobue, K., Muramoto, Y., Fujita, M., and Kakiuchi, S. (1981) Proc.
T3 228-233 Sentence denotes Natl.
T3 228-233 Sentence denotes Natl.
T4 234-239 Sentence denotes Acad.
T4 234-239 Sentence denotes Acad.
T5 240-244 Sentence denotes Sci.
T5 240-244 Sentence denotes Sci.
T6 245-247 Sentence denotes U.
T6 245-247 Sentence denotes U.
T7 248-250 Sentence denotes S.
T7 248-250 Sentence denotes S.
T8 251-253 Sentence denotes A.
T8 251-253 Sentence denotes A.
T9 254-396 Sentence denotes 78, 5652-5655), has been obtained in highly purified form from chicken gizzard by a modification of a previously published procedure (Ngai, P.
T9 254-396 Sentence denotes 78, 5652-5655), has been obtained in highly purified form from chicken gizzard by a modification of a previously published procedure (Ngai, P.
T10 397-415 Sentence denotes K., Carruthers, C.
T10 397-415 Sentence denotes K., Carruthers, C.
T11 416-433 Sentence denotes A., and Walsh, M.
T11 416-433 Sentence denotes A., and Walsh, M.
T12 434-452 Sentence denotes P. (1984) Biochem.
T12 434-452 Sentence denotes P. (1984) Biochem.
T13 453-455 Sentence denotes J.
T13 453-455 Sentence denotes J.
T14 456-729 Sentence denotes 218, 863-870) and was found to cause a significant inhibition of both superprecipitation and actin-activated myosin Mg2+-ATPase activity in a system reconstituted from the purified contractile and regulatory proteins without influencing the phosphorylation state of myosin.
T14 456-729 Sentence denotes 218, 863-870) and was found to cause a significant inhibition of both superprecipitation and actin-activated myosin Mg2+-ATPase activity in a system reconstituted from the purified contractile and regulatory proteins without influencing the phosphorylation state of myosin.
T15 730-810 Sentence denotes This inhibitory effect was seen both in the presence and absence of tropomyosin.
T15 730-810 Sentence denotes This inhibitory effect was seen both in the presence and absence of tropomyosin.
T16 811-985 Sentence denotes A Ca2+-and calmodulin-dependent kinase which catalyzed phosphorylation of caldesmon was identified in chicken gizzard; this kinase is distinct from myosin light-chain kinase.
T16 811-985 Sentence denotes A Ca2+-and calmodulin-dependent kinase which catalyzed phosphorylation of caldesmon was identified in chicken gizzard; this kinase is distinct from myosin light-chain kinase.
T17 986-1176 Sentence denotes Caldesmon prepared by calmodulin-Sepharose affinity chromatography was contaminated with caldesmon kinase activity and was unable to inhibit actomyosin ATPase activity or superprecipitation.
T17 986-1176 Sentence denotes Caldesmon prepared by calmodulin-Sepharose affinity chromatography was contaminated with caldesmon kinase activity and was unable to inhibit actomyosin ATPase activity or superprecipitation.
T18 1177-1274 Sentence denotes Phosphatase activity capable of dephosphorylating caldesmon was also identified in smooth muscle.
T18 1177-1274 Sentence denotes Phosphatase activity capable of dephosphorylating caldesmon was also identified in smooth muscle.
T19 1275-1473 Sentence denotes These results indicate that caldesmon can inhibit smooth muscle actomyosin ATPase activity in vitro, and this function may itself be subject to regulation by reversible phosphorylation of caldesmon.
T19 1275-1473 Sentence denotes These results indicate that caldesmon can inhibit smooth muscle actomyosin ATPase activity in vitro, and this function may itself be subject to regulation by reversible phosphorylation of caldesmon.