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
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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
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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 |
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2008 | 0 | 1 | 1 |
2014 | 1 | 0 | 1 |
2015 | 1 | 0 | 1 |
2016 | 0 | 1 | 1 |
2019 | 1 | 1 | 2 |
2020 | 0 | 1 | 1 |
2021 | 0 | 1 | 1 |
2024 | 0 | 1 | 1 |
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Below are the most recent publications written about "Protein Processing, Post-Translational" by people in Profiles.
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Exploring therapeutic potential of Rutin by investigating its cyclin-dependent kinase 6 inhibitory activity and binding affinity. Int J Biol Macromol. 2024 Apr; 264(Pt 2):130624.
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Submission for Special Issue: The Role of Platelet Activation in the Pathophysiology of HIV, Tuberculosis, and Pneumococcal Disease. Bedaquiline Suppresses ADP-Mediated Activation of Human Platelets In Vitro via Interference With Phosphatidylinositol 3-Kinase. Front Immunol. 2020; 11:621148.
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Plant-based production of highly potent anti-HIV antibodies with engineered posttranslational modifications. Sci Rep. 2020 04 10; 10(1):6201.
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Risk of developing cerebral ß-amyloid plaques with posttranslational modification among HIV-infected adults. AIDS. 2019 11 15; 33(14):2157-2166.
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N-glycosylation and homodimeric folding significantly enhance the immunoreactivity of Mycobacterium tuberculosis virulence factor CFP32 when produced in the yeast Pichia pastoris. Biochem Biophys Res Commun. 2019 08 27; 516(3):845-850.
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Smoking and Air Pollution as Pro-Inflammatory Triggers for the Development of Rheumatoid Arthritis. Nicotine Tob Res. 2016 07; 18(7):1556-65.
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Cleavage of the moaX-encoded fused molybdopterin synthase from Mycobacterium tuberculosis is necessary for activity. BMC Microbiol. 2015 Feb 06; 15:22.
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OS-9 facilitates turnover of nonnative GRP94 marked by hyperglycosylation. Mol Biol Cell. 2014 Aug 01; 25(15):2220-34.
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Targeting histone deacetylases for the treatment of disease. J Cell Mol Med. 2009 May; 13(5):826-52.