| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-104 |
Sentence |
denotes |
Characterization of the in vitro reconstituted cyclin A or B1-dependent cdk2 and cdc2 kinase activities. |
| T2 |
105-233 |
Sentence |
denotes |
Human cyclins A and B1 were assembled with the cdk2 or cdc2 protein to reconstitute their respective kinase activities in vitro. |
| T3 |
234-357 |
Sentence |
denotes |
Both cyclins complemented either cdk2 or cdc2, yielding kinase activities that supported the phosphorylation of histone H1. |
| T4 |
358-681 |
Sentence |
denotes |
Activation of cdk2-catalyzed H1 kinase activity by cyclin A required a 10-min preincubation of the two components, whereas cdc2 kinase supported phosphate incorporation without a detectable time lag upon the addition of cyclin B1, suggesting a slower association rate of cdk2 with cyclin A compared with cdc2 and cyclin B1. |
| T5 |
682-859 |
Sentence |
denotes |
Both cdk2 and cyclin A, as well as cdc2 and cyclin B1, formed stable complexes in the absence of ATP and substrate that could be isolated after glycerol gradient centrifugation. |
| T6 |
860-968 |
Sentence |
denotes |
Incubation of the isolated complexes with ATP and histone H1 supported the phosphorylation of the substrate. |
| T7 |
969-1117 |
Sentence |
denotes |
Cyclin A-activated cdk2 or cdc2 phosphorylated p107, a pRB-related cellular protein, 10 times more effectively than the cyclin B1-complexed kinases. |
| T8 |
1118-1198 |
Sentence |
denotes |
This was most likely due to a direct association of cyclin A with p107 (Ewen, M. |
| T9 |
1199-1289 |
Sentence |
denotes |
E., Faha, B., Harlow, E., and Livingston, D. (1992) Science 255, 85-87; Faha, B., Ewen, M. |
| T10 |
1290-1365 |
Sentence |
denotes |
E., Tsai, L.-H., Livingston, D., and Harlow, E. (1992) Science 255, 87-90). |
| T11 |
1366-1628 |
Sentence |
denotes |
The reconstituted cdc2-cyclin B1 complex incorporated 4-5-fold more phosphate into the p34 subunit of the three-subunit (p70, p34, and p14) human single-stranded DNA-binding protein (also called RP-A), a DNA replication and DNA repair factor, than cdc2-cyclin A. |
| T12 |
1629-1738 |
Sentence |
denotes |
No detectable phosphorylation of the p34 protein was observed with cdk2 complexed with either cyclin B1 or A. |
| T13 |
1739-1897 |
Sentence |
denotes |
These data indicate that both cyclins as well as the catalytic subunits are important factors in controlling the rate of phosphorylation of a given substrate. |
| T14 |
1898-2029 |
Sentence |
denotes |
The cyclin-activated cdc2 family kinases may target their cellular substrates through cyclin-mediated protein-protein interactions. |
| T1 |
0-104 |
Sentence |
denotes |
Characterization of the in vitro reconstituted cyclin A or B1-dependent cdk2 and cdc2 kinase activities. |
| T2 |
105-233 |
Sentence |
denotes |
Human cyclins A and B1 were assembled with the cdk2 or cdc2 protein to reconstitute their respective kinase activities in vitro. |
| T3 |
234-357 |
Sentence |
denotes |
Both cyclins complemented either cdk2 or cdc2, yielding kinase activities that supported the phosphorylation of histone H1. |
| T4 |
358-681 |
Sentence |
denotes |
Activation of cdk2-catalyzed H1 kinase activity by cyclin A required a 10-min preincubation of the two components, whereas cdc2 kinase supported phosphate incorporation without a detectable time lag upon the addition of cyclin B1, suggesting a slower association rate of cdk2 with cyclin A compared with cdc2 and cyclin B1. |
| T5 |
682-859 |
Sentence |
denotes |
Both cdk2 and cyclin A, as well as cdc2 and cyclin B1, formed stable complexes in the absence of ATP and substrate that could be isolated after glycerol gradient centrifugation. |
| T6 |
860-968 |
Sentence |
denotes |
Incubation of the isolated complexes with ATP and histone H1 supported the phosphorylation of the substrate. |
| T7 |
969-1117 |
Sentence |
denotes |
Cyclin A-activated cdk2 or cdc2 phosphorylated p107, a pRB-related cellular protein, 10 times more effectively than the cyclin B1-complexed kinases. |
| T8 |
1118-1198 |
Sentence |
denotes |
This was most likely due to a direct association of cyclin A with p107 (Ewen, M. |
| T9 |
1199-1289 |
Sentence |
denotes |
E., Faha, B., Harlow, E., and Livingston, D. (1992) Science 255, 85-87; Faha, B., Ewen, M. |
| T10 |
1290-1365 |
Sentence |
denotes |
E., Tsai, L.-H., Livingston, D., and Harlow, E. (1992) Science 255, 87-90). |
| T11 |
1366-1628 |
Sentence |
denotes |
The reconstituted cdc2-cyclin B1 complex incorporated 4-5-fold more phosphate into the p34 subunit of the three-subunit (p70, p34, and p14) human single-stranded DNA-binding protein (also called RP-A), a DNA replication and DNA repair factor, than cdc2-cyclin A. |
| T12 |
1629-1738 |
Sentence |
denotes |
No detectable phosphorylation of the p34 protein was observed with cdk2 complexed with either cyclin B1 or A. |
| T13 |
1739-1897 |
Sentence |
denotes |
These data indicate that both cyclins as well as the catalytic subunits are important factors in controlling the rate of phosphorylation of a given substrate. |
| T14 |
1898-2029 |
Sentence |
denotes |
The cyclin-activated cdc2 family kinases may target their cellular substrates through cyclin-mediated protein-protein interactions. |