Found: 7
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Mobilization of a splicing factor through a nuclear kinase–kinase complex.
- Published in:
- Biochemical Journal, 2018, v. 475, n. 3, p. 677, doi. 10.1042/BCJ20170672
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- Article
Nuclear protein kinase CLK1 uses a non-traditional docking mechanism to select physiological substrates.
- Published in:
- Biochemical Journal, 2015, v. 472, n. 3, p. 329, doi. 10.1042/BJ20150903
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- Article
Conserved proline-directed phosphorylation regulates SR protein conformation and splicing function.
- Published in:
- Biochemical Journal, 2015, v. 466, n. 2, p. 311, doi. 10.1042/BJ20141373
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- Article
N-terminus of the protein kinase CLK1 induces SR protein hyperphosphorylation.
- Published in:
- Biochemical Journal, 2014, v. 462, n. 1, p. 143, doi. 10.1042/BJ20140494
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- Article
SRPK1 regulates RNA binding in a pre‐spliceosomal complex using a catalytic bypass mechanism.
- Published in:
- FEBS Journal, 2022, v. 289, n. 23, p. 7428, doi. 10.1111/febs.16560
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- Article
A conserved sequence motif bridges two protein kinases for enhanced phosphorylation and nuclear function of a splicing factor.
- Published in:
- FEBS Journal, 2021, v. 288, n. 2, p. 566, doi. 10.1111/febs.15351
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- Article
C6 pyridinium ceramide influences alternative pre-mRNA splicing by inhibiting protein phosphatase-1.
- Published in:
- Nucleic Acids Research, 2012, v. 40, n. 9, p. 4025, doi. 10.1093/nar/gkr1289
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- Article