> top > projects > sentences > docs > PubMed:7929081 > annotations

PubMed:7929081 JSONTXT 22 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-141 Sentence denotes Type II regulatory subunit (RII) of the cAMP-dependent protein kinase interaction with A-kinase anchor proteins requires isoleucines 3 and 5.
T1 0-141 Sentence denotes Type II regulatory subunit (RII) of the cAMP-dependent protein kinase interaction with A-kinase anchor proteins requires isoleucines 3 and 5.
T2 142-307 Sentence denotes Compartmentalization of the type II cAMP-dependent protein kinase is maintained by association of the regulatory subunit (RII) with A-Kinase Anchor Proteins (AKAPs).
T2 142-307 Sentence denotes Compartmentalization of the type II cAMP-dependent protein kinase is maintained by association of the regulatory subunit (RII) with A-Kinase Anchor Proteins (AKAPs).
T3 308-338 Sentence denotes In previous studies (Scott, J.
T3 308-338 Sentence denotes In previous studies (Scott, J.
T4 339-353 Sentence denotes D., Stofko, R.
T4 339-353 Sentence denotes D., Stofko, R.
T5 354-370 Sentence denotes E., McDonald, J.
T5 354-370 Sentence denotes E., McDonald, J.
T6 371-384 Sentence denotes R., Comer, J.
T6 371-384 Sentence denotes R., Comer, J.
T7 385-400 Sentence denotes D., Vitalis, E.
T7 385-400 Sentence denotes D., Vitalis, E.
T8 401-429 Sentence denotes A., and Mangili J. (1990) J.
T8 401-429 Sentence denotes A., and Mangili J. (1990) J.
T9 430-435 Sentence denotes Biol.
T9 430-435 Sentence denotes Biol.
T10 436-441 Sentence denotes Chem.
T10 436-441 Sentence denotes Chem.
T11 442-599 Sentence denotes 265, 21561-21566) we have shown that dimerization of RII alpha was required for interaction with the cytoskeletal component microtubule-associated protein 2.
T11 442-599 Sentence denotes 265, 21561-21566) we have shown that dimerization of RII alpha was required for interaction with the cytoskeletal component microtubule-associated protein 2.
T12 600-751 Sentence denotes In this report we show that the localization and dimerization domains of RII alpha are contained within the first thirty residues of each RII protomer.
T12 600-751 Sentence denotes In this report we show that the localization and dimerization domains of RII alpha are contained within the first thirty residues of each RII protomer.
T13 752-881 Sentence denotes RII des-5 (an amino-terminal deletion mutant lacking residues 1-5) was unable to bind AKAPs but retained the ability to dimerize.
T13 752-881 Sentence denotes RII des-5 (an amino-terminal deletion mutant lacking residues 1-5) was unable to bind AKAPs but retained the ability to dimerize.
T14 882-1002 Sentence denotes RII alpha I3A,I5A (a mutant where isoleucines 3 and 5 were replaced with alanine) was unable to bind a variety of AKAPs.
T14 882-1002 Sentence denotes RII alpha I3A,I5A (a mutant where isoleucines 3 and 5 were replaced with alanine) was unable to bind a variety of AKAPs.
T15 1003-1151 Sentence denotes Mutation of both isoleucines decreased AKAP binding without affecting dimerization, cAMP binding, or the overall secondary structure of the protein.
T15 1003-1151 Sentence denotes Mutation of both isoleucines decreased AKAP binding without affecting dimerization, cAMP binding, or the overall secondary structure of the protein.
T16 1152-1344 Sentence denotes Measurement of RII alpha I3A,I5A interaction with the human thyroid AKAP, Ht 31, by two independent methods suggests that mutation of isoleucines 3 and 5 decreases affinity by at least 6-fold.
T16 1152-1344 Sentence denotes Measurement of RII alpha I3A,I5A interaction with the human thyroid AKAP, Ht 31, by two independent methods suggests that mutation of isoleucines 3 and 5 decreases affinity by at least 6-fold.
T17 1345-1512 Sentence denotes Therefore, we propose that two isoleucine side chains on each RII protomer are principle sites of contact with the conserved amphipathic helix binding domain on AKAPs.
T17 1345-1512 Sentence denotes Therefore, we propose that two isoleucine side chains on each RII protomer are principle sites of contact with the conserved amphipathic helix binding domain on AKAPs.