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PubMed:7822274 JSONTXT 22 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-70 Sentence denotes Structural analysis of myosin heavy chain kinase A from Dictyostelium.
T1 0-70 Sentence denotes Structural analysis of myosin heavy chain kinase A from Dictyostelium.
T2 71-237 Sentence denotes Evidence for a highly divergent protein kinase domain, an amino-terminal coiled-coil domain, and a domain homologous to the beta-subunit of heterotrimeric G proteins.
T2 71-237 Sentence denotes Evidence for a highly divergent protein kinase domain, an amino-terminal coiled-coil domain, and a domain homologous to the beta-subunit of heterotrimeric G proteins.
T3 238-384 Sentence denotes We report here the cloning and characterization of the gene encoding the 130-kDa myosin heavy chain kinase (MHCK A) from the amoeba Dictyostelium.
T3 238-384 Sentence denotes We report here the cloning and characterization of the gene encoding the 130-kDa myosin heavy chain kinase (MHCK A) from the amoeba Dictyostelium.
T4 385-680 Sentence denotes Previous studies have shown that purified MHCK A phosphorylates threonines in the carboxyl-terminal tail portion of the Dictyostelium myosin II heavy chain and that phosphorylation of these sites is critical in regulating the assembly and disassembly of myosin II filaments in vitro and in vivo.
T4 385-680 Sentence denotes Previous studies have shown that purified MHCK A phosphorylates threonines in the carboxyl-terminal tail portion of the Dictyostelium myosin II heavy chain and that phosphorylation of these sites is critical in regulating the assembly and disassembly of myosin II filaments in vitro and in vivo.
T5 681-1046 Sentence denotes Biochemical analysis of MHCK A, together with analysis of the primary sequence, suggests that the amino-terminal approximately 500 amino acids form an alpha-helical coiled-coil domain and that residues from position approximately 860 to the carboxyl terminus (residue 1146) form a domain with significant similarity to the beta-subunit of heterotrimeric G proteins.
T5 681-1046 Sentence denotes Biochemical analysis of MHCK A, together with analysis of the primary sequence, suggests that the amino-terminal approximately 500 amino acids form an alpha-helical coiled-coil domain and that residues from position approximately 860 to the carboxyl terminus (residue 1146) form a domain with significant similarity to the beta-subunit of heterotrimeric G proteins.
T6 1047-1177 Sentence denotes No part of the MHCK A sequence displays significant similarity to the catalytic domain of conventional eukaryotic protein kinases.
T6 1047-1177 Sentence denotes No part of the MHCK A sequence displays significant similarity to the catalytic domain of conventional eukaryotic protein kinases.
T7 1178-1439 Sentence denotes However, both native and recombinant MHCK A displayed autophosphorylation activity following renaturation from SDS gels, and MHCK A expressed in Escherichia coli phosphorylated purified Dictyostelium myosin, confirming that MHCK A is a bona fide protein kinase.
T7 1178-1439 Sentence denotes However, both native and recombinant MHCK A displayed autophosphorylation activity following renaturation from SDS gels, and MHCK A expressed in Escherichia coli phosphorylated purified Dictyostelium myosin, confirming that MHCK A is a bona fide protein kinase.
T8 1440-1578 Sentence denotes Cross-linking studies demonstrated that native MHCK A is a multimer, consistent with the presence of an amino-terminal coiled-coil domain.
T8 1440-1578 Sentence denotes Cross-linking studies demonstrated that native MHCK A is a multimer, consistent with the presence of an amino-terminal coiled-coil domain.
T9 1579-1683 Sentence denotes Southern blot analysis indicates that MHCK A is encoded by a single gene that has no detectable introns.
T9 1579-1683 Sentence denotes Southern blot analysis indicates that MHCK A is encoded by a single gene that has no detectable introns.