| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10762495 | Biochemical and Biophysical Research Communications | 2011 | 6 Pages |
Abstract
⺠DIP1-c is a dimer in solution using analytical ultracentrifugation. ⺠DIP1-c interacts physically with ADAT, a tRNA deaminase. ⺠DIP1-c interaction with ADAT is not altered by the presence of pre-tRNAAla. ⺠DIP1-c binds with high affinity to insect pre-tRNAAla.
Keywords
tRNAAdenosine Deaminase that acts on RNAtRNAAlaTranscription and translationUltrabithoraxdsRNA-binding proteinUbxssRNARNAPdsRBDADARdsRNADouble-stranded RNA-binding domainGSTDIP1single-stranded RNAdouble-stranded RNAanalytical ultracentrifugationRNA polymeraseHigh affinityequilibrium dissociation constantTnTGel retardationMicroRNAMiRNAglutathione S-transferase
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Authors
Daniel J. Jr., Kathleen S. Matthews,