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.
To see the data from this visualization as text,
click here.
Year | Major Topic | Minor Topic | Total |
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1994 | 0 | 2 | 2 |
1995 | 1 | 2 | 3 |
1996 | 2 | 3 | 5 |
1998 | 0 | 1 | 1 |
1999 | 1 | 2 | 3 |
2000 | 0 | 1 | 1 |
2002 | 3 | 2 | 5 |
2003 | 0 | 3 | 3 |
2004 | 4 | 6 | 10 |
2005 | 1 | 4 | 5 |
2006 | 5 | 8 | 13 |
2007 | 1 | 5 | 6 |
2008 | 3 | 3 | 6 |
2009 | 2 | 3 | 5 |
2010 | 3 | 2 | 5 |
2011 | 3 | 4 | 7 |
2012 | 5 | 4 | 9 |
2013 | 6 | 5 | 11 |
2014 | 3 | 6 | 9 |
2015 | 1 | 6 | 7 |
2016 | 6 | 2 | 8 |
2017 | 2 | 4 | 6 |
2018 | 5 | 1 | 6 |
2019 | 1 | 2 | 3 |
2020 | 1 | 2 | 3 |
2021 | 1 | 3 | 4 |
2023 | 0 | 2 | 2 |
2024 | 1 | 4 | 5 |
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Below are the most recent publications written about "Protein Processing, Post-Translational" by people in Profiles.
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Vaishnav MS, Kumari N, Srikanta S, Simha V, Krishnaswamy PR, Balaram P, Bhat N. Albumin Oxidation and Albumin Glycation Discordance During Type 2 Diabetes Therapy: Biological and Clinical Implications. Metab Syndr Relat Disord. 2024 Jun; 22(5):372-384.
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Neal CL, Kronert WA, Camillo JRT, Suggs JA, Huxford T, Bernstein SI. Aging-affiliated post-translational modifications of skeletal muscle myosin affect biochemical properties, myofibril structure, muscle function, and proteostasis. Aging Cell. 2024 06; 23(6):e14134.
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Fern?ndez-Coto DL, Gil J, Ayala G, Encarnaci?n-Guevara S. Dynamics of Mitochondrial Proteome and Acetylome in Glioblastoma Cells with Contrasting Metabolic Phenotypes. Int J Mol Sci. 2024 Mar 19; 25(6).
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Hu H, Hu W, Guo AD, Zhai L, Ma S, Nie HJ, Zhou BS, Liu T, Jia X, Liu X, Yao X, Tan M, Chen XH. Spatiotemporal and direct capturing global substrates of lysine-modifying enzymes in living cells. Nat Commun. 2024 Feb 17; 15(1):1465.
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Barylko B, Taylor CA, Wang J, Earnest S, Stippec S, Binns DD, Brautigam CA, Jameson DM, DeMartino GN, Cobb MH, Albanesi JP. Mimicking Protein Kinase C Phosphorylation Inhibits Arc/Arg3.1 Palmitoylation and Its Interaction with Nucleic Acids. Int J Mol Sci. 2024 Jan 08; 25(2).
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Du Y, Chen C, Zhou G, Cai Z, Man Q, Liu B, Wang WC. Perfluorooctanoic acid disrupts thyroid-specific genes expression and regulation via the TSH-TSHR signaling pathway in thyroid cells. Environ Res. 2023 Dec 15; 239(Pt 1):117372.
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Rodriguez G, Martinez GS, Negrete OD, Sun S, Guo W, Xie Y, Li L, Xiao C, Ross JA, Kirken RA. JAK3 Y841 Autophosphorylation Is Critical for STAT5B Activation, Kinase Domain Stability and Dimer Formation. Int J Mol Sci. 2023 Jul 25; 24(15).
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Bao Y, Wang L, Sun J. Post-translational knockdown and post-secretional modification of EsxA determine contribution of EsxA membrane permeabilizing activity for mycobacterial intracellular survival. Virulence. 2021 12; 12(1):312-328.
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Estrada A, Rodriguez AC, Rodriguez G, Grant AH, Ayala-Marin YM, Arrieta AJ, Kirken RA. Phosphorylation of CrkL S114 induced by common gamma chain cytokines and T-cell receptor signal transduction. Sci Rep. 2021 08 20; 11(1):16951.
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Toro TB, Swanier JS, Bezue JA, Broussard CG, Watt TJ. Lysine Deacetylase Substrate Selectivity: A Dynamic Ionic Interaction Specific to KDAC8. Biochemistry. 2021 08 24; 60(33):2524-2536.