> top > projects > sentences > docs > PubMed:16407284 > annotations
sentences Home  

PubMed:16407284 JSONTXT 26 Projects

Annnotations TAB TSV DIC JSON TextAE

Id Subject Object Predicate Lexical cue
T1 0-67 Sentence denotes Blockade of NFAT activation by the second calcineurin binding site.
T2 68-178 Sentence denotes Activation of NFAT transcription factors requires their dephosphorylation by the phosphatase calcineurin (CN).
T3 179-215 Sentence denotes NFATs contain two CN binding motifs:
T4 216-261 Sentence denotes PxIxIT and CnBP-B/CNBR2 (which we call LxVP).
T5 262-399 Sentence denotes Here we carry out a detailed comparative analysis of the CN binding activity displayed by the PxIxIT and LxVP sites from different NFATs.
T6 400-554 Sentence denotes Dose-response CN binding experiments with GST fusion proteins of NFATc1 and NFATc2 showed that NFATc1 binds CN in vitro more efficiently than does NFATc2.
T7 555-809 Sentence denotes This difference in binding appears to be caused by the different CN binding potencies of the corresponding LxVP sites; thus while the LxVPc2 peptide fused to GST did not bind CN, GST-LxVPc1 bound it more efficiently than did GST-PxIxITc1 or GST-PxIxITc2.
T8 810-951 Sentence denotes Furthermore, an NFATc2 chimera protein containing the LxVP motif from NFATc1 interacted with CN much more potently than did wild-type NFATc2.
T9 952-1098 Sentence denotes Free peptides spanning the LxVP motifs from NFATc1, c3 or c4 displaced CN from GST-NFATc1 and GST-NFATc2 more efficiently than any PxIxIT peptide.
T10 1099-1202 Sentence denotes PxIxITc2 and LxVPc1 peptides were each able to cross-compete GST-LxVPc1-CN and GST-PxIxITc2-CN binding.
T11 1203-1332 Sentence denotes In contrast with PxIxITc2, the LxVP peptide not only blocked CN-NFAT binding but also inhibited CN phosphatase activity in vitro.
T12 1333-1428 Sentence denotes Furthermore, exogenous LxVPc1 blocked NFATc2 phosphorylation and nuclear translocation in vivo.
T13 1429-1641 Sentence denotes These results suggest a model in which the different CN binding characteristics of the PxIxIT and LxVP sites enable different NFAT members to influence each others activities in cells where they are co-expressed.