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PubMed:12034713 JSONTXT

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sentences

Id Subject Object Predicate Lexical cue
T1 0-65 Sentence denotes Structural independence of the two EF-hand domains of caltractin.
T2 66-282 Sentence denotes Caltractin (centrin) is a member of the calmodulin subfamily of EF-hand Ca2+-binding proteins that is an essential component of microtubule-organizing centers in many organisms ranging from yeast and algae to humans.
T3 283-425 Sentence denotes The protein contains two homologous EF-hand Ca2+-binding domains linked by a flexible tether; each domain is capable of binding two Ca2+ ions.
T4 426-580 Sentence denotes In an effort to search for domain-specific functional properties of caltractin, the two isolated domains were subcloned and expressed in Escherichia coli.
T5 581-726 Sentence denotes Ca2+ binding affinities and the Ca2+ dependence of biophysical properties of the isolated domains were monitored by UV, CD, and NMR spectroscopy.
T6 727-872 Sentence denotes Comparisons to the corresponding results for the intact protein showed that the two domains function independently of each other in these assays.
T7 873-1125 Sentence denotes Titration of a peptide fragment from the yeast Kar1p protein to the isolated domains and intact caltractin shows that the two domains interact in a Ca2+-dependent manner, with the C-terminal domain binding much more strongly than the N-terminal domain.
T8 1126-1360 Sentence denotes Measurements of the macroscopic Ca2+ binding constants show that only the N-terminal domain has sufficient apparent Ca2+ affinity in vitro (1-10 microm) to be classified as a traditional calcium sensor in signal transduction pathways.
T9 1361-1663 Sentence denotes However, investigation of the microscopic Ca2+ binding events in the C-terminal domain by NMR spectroscopy revealed that the observed macroscopic binding constant likely results from binding to two sites with very different affinities, one in the micromolar range and the other in the millimolar range.
T10 1664-1791 Sentence denotes Thus, the C-terminal domain appears to also be capable of sensing Ca2+ signals but is activated by the binding of a single ion.

Glycosmos6-MAT

Id Subject Object Predicate Lexical cue
T1 38-42 http://purl.obolibrary.org/obo/MAT_0000091 denotes hand
T2 133-137 http://purl.obolibrary.org/obo/MAT_0000091 denotes hand
T3 322-326 http://purl.obolibrary.org/obo/MAT_0000091 denotes hand

NCBITAXON

Id Subject Object Predicate Lexical cue db_id
T1 563-579 OrganismTaxon denotes Escherichia coli 562

Anatomy-UBERON

Id Subject Object Predicate Lexical cue uberon_id
T1 38-42 Body_part denotes hand http://purl.obolibrary.org/obo/UBERON_0002398
T2 133-137 Body_part denotes hand http://purl.obolibrary.org/obo/UBERON_0002398
T3 194-205 Body_part denotes microtubule http://purl.obolibrary.org/obo/GO_0005874
T4 233-242 Body_part denotes organisms http://purl.obolibrary.org/obo/UBERON_0000468
T5 322-326 Body_part denotes hand http://purl.obolibrary.org/obo/UBERON_0002398

Anatomy-MAT

Id Subject Object Predicate Lexical cue mat_id
T1 38-42 Body_part denotes hand http://purl.obolibrary.org/obo/MAT_0000091
T2 133-137 Body_part denotes hand http://purl.obolibrary.org/obo/MAT_0000091
T3 322-326 Body_part denotes hand http://purl.obolibrary.org/obo/MAT_0000091