PQBP-1/Npw38, a Nuclear Protein Binding to the Polyglutamine Tract, Interacts with U5-15kD/dim1p via the Carboxyl-Terminal Domain
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference14 articles.
1. PQBP-1, a novel polyglutamine tract-binding protein, inhibits transcription activation by Brn-2 and affects cell survival
2. Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kd protein
3. Fission Yeast dim1+ Encodes a Functionally Conserved Polypeptide Essential for Mitosis
4. Presenilin 1 Binds to Amyloid Precursor Protein Directly
5. The Schizosaccharomyces pombe dim1 + Gene Interacts with the Anaphase-Promoting Complex or Cyclosome (APC/C) Component lid1 + and Is Required for APC/C Function
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1. Molecular consequences of PQBP1 deficiency, involved in the X-linked Renpenning syndrome;Molecular Psychiatry;2023-11-29
2. Splicing Modulators Are Involved in Human Polyglutamine Diversification via Protein Complexes Shuttling between Nucleus and Cytoplasm;International Journal of Molecular Sciences;2023-06-01
3. PQBP1 regulates striatum development through balancing striatal progenitor proliferation and differentiation;Cell Reports;2023-03
4. The role of PQBP1 in neural development and function;Biochemical Society Transactions;2023-02-23
5. In Silico Analysis of Cellular Interactors of PQBP1 for Potential Drug Repurposing;Drug Repurposing for Emerging Infectious Diseases and Cancer;2023
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