ArticleActa biochimica et biophysica Sinica2024
The P124A mutation of SRP14 alters its migration on SDS-PAGE without impacting its function.
Article in Acta biochimica et biophysica Sinica, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 3 citations in OpenAlex.
- Optimized Multi-Epitope Norovirus Vaccines Induce Robust Humoral and Cellular Responses in Mice.Vaccines · 2025Article
- The Structural Proteins of Thermophilic Bacteriophage P23-77: Expression and Characterization.International journal of molecular sciences · 2025Article
- Design, Co-Expression, and Evaluation for Assembly of the Structural Proteins from Thermophilic Bacteriophage ΦIN93.International journal of molecular sciences · 2025Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
SRP14 is a crucial protein subunit of the signal recognition particle (SRP), a ribonucleoprotein complex essential for co-translational translocation to the endoplasmic reticulum. During our investigation of SRP14 expression across diverse cell lines, we observe variations in its migration on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), with some cells exhibiting slower migration and others migrating faster. However, the cause of this phenomenon remains elusive. Our research rules out alternative splicing as the cause and, instead, identifies the presence of a P124A mutation in SRP14 (SRP14
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