Protein Processing, Post-Translational
"Protein Processing, Post-Translational" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
| Descriptor ID |
D011499
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| MeSH Number(s) |
G02.111.660.871.790.600 G02.111.691.600 G03.734.871.790.600 G05.308.670.600
|
| Concept/Terms |
Protein Processing, Post-Translational- Protein Processing, Post-Translational
- Posttranslational Protein Processing
- Processing, Posttranslational Protein
- Protein Processing, Posttranslational
- Posttranslational Modifications
- Modification, Posttranslational
- Modifications, Posttranslational
- Posttranslational Modification
- Post-Translational Modifications
- Modification, Post-Translational
- Modifications, Post-Translational
- Post Translational Modifications
- Post-Translational Modification
- Post-Translational Protein Processing
- Post Translational Protein Processing
- Processing, Post-Translational Protein
- Amino Acid Modification, Post-Translational
- Amino Acid Modification, Post Translational
- Post-Translational Amino Acid Modification
- Post Translational Amino Acid Modification
- Posttranslational Amino Acid Modification
- Amino Acid Modification, Posttranslational
- Post-Translational Protein Modification
- Modification, Post-Translational Protein
- Modifications, Post-Translational Protein
- Post Translational Protein Modification
- Post-Translational Protein Modifications
- Protein Modifications, Post-Translational
- Protein Processing, Post Translational
- Protein Modification, Post-Translational
- Protein Modification, Post Translational
|
Below are MeSH descriptors whose meaning is more general than "Protein Processing, Post-Translational".
Below are MeSH descriptors whose meaning is more specific than "Protein Processing, Post-Translational".
This graph shows the total number of publications written about "Protein Processing, Post-Translational" by people in this website by year, and whether "Protein Processing, Post-Translational" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2013 | 1 | 0 | 1 |
| 2016 | 3 | 1 | 4 |
| 2017 | 0 | 1 | 1 |
| 2020 | 1 | 0 | 1 |
| 2024 | 0 | 3 | 3 |
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Below are the most recent publications written about "Protein Processing, Post-Translational" by people in Profiles.
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Deconstructing fibrin(ogen) structure. J Thromb Haemost. 2025 Feb; 23(2):368-380.
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APE-Gen2.0: Expanding Rapid Class I Peptide-Major Histocompatibility Complex Modeling to Post-Translational Modifications and Noncanonical Peptide Geometries. J Chem Inf Model. 2024 03 11; 64(5):1730-1750.
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Regulating Androgen Receptor Function in Prostate Cancer: Exploring the Diversity of Post-Translational Modifications. Cells. 2024 Jan 19; 13(2).
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Acetylation of histone H3K27 signals the transcriptional elongation for estrogen receptor alpha. Commun Biol. 2020 04 07; 3(1):165.
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The PAS domains of the major sporulation kinase in Bacillus subtilis play a role in tetramer formation that is essential for the?autokinase activity. Microbiologyopen. 2017 08; 6(4).
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Lysyl Hydroxylase 2 Is Secreted by Tumor Cells and Can Modify Collagen in the Extracellular Space. J Biol Chem. 2016 Dec 09; 291(50):25799-25808.
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Selective Modulation of Protein Kinase C a over Protein Kinase C e by Curcumin and Its Derivatives in CHO-K1 Cells. Biochemistry. 2016 Apr 12; 55(14):2135-43.
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SUMOylated ORC2 Recruits a Histone Demethylase to Regulate Centromeric Histone Modification and Genomic Stability. Cell Rep. 2016 Apr 05; 15(1):147-157.
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Isolation of In Vivo SUMOylated Chromatin-Bound Proteins. Methods Mol Biol. 2016; 1475:205-16.
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Triggering sporulation in Bacillus subtilis with artificial two-component systems reveals the importance of proper Spo0A activation dynamics. Mol Microbiol. 2013 Oct; 90(1):181-94.