| 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. |