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 |
|---|
| 1996 | 1 | 0 | 1 | | 1997 | 0 | 4 | 4 | | 1998 | 1 | 3 | 4 | | 1999 | 2 | 3 | 5 | | 2000 | 3 | 6 | 9 | | 2001 | 3 | 2 | 5 | | 2002 | 1 | 6 | 7 | | 2003 | 1 | 8 | 9 | | 2004 | 3 | 7 | 10 | | 2005 | 3 | 5 | 8 | | 2006 | 4 | 7 | 11 | | 2007 | 3 | 3 | 6 | | 2008 | 2 | 6 | 8 | | 2009 | 6 | 6 | 12 | | 2010 | 4 | 4 | 8 | | 2011 | 3 | 8 | 11 | | 2012 | 6 | 12 | 18 | | 2013 | 6 | 12 | 18 | | 2014 | 5 | 9 | 14 | | 2015 | 4 | 10 | 14 | | 2016 | 13 | 13 | 26 | | 2017 | 7 | 16 | 23 | | 2018 | 3 | 9 | 12 | | 2019 | 6 | 12 | 18 | | 2020 | 5 | 9 | 14 | | 2021 | 6 | 6 | 12 | | 2022 | 0 | 3 | 3 | | 2023 | 0 | 8 | 8 | | 2024 | 3 | 5 | 8 | | 2025 | 3 | 10 | 13 | | 2026 | 2 | 2 | 4 |
To return to the timeline, click here.
Below are the most recent publications written about "Protein Processing, Post-Translational" by people in Profiles.
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Panja S, Nagaraj RH. Deamidation Promotes AGE-Modifications in Human Lens ?S-Crystallin. Biochemistry. 2026 Jun 16; 65(12):1957-1965.
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Staab-Weijnitz CA, Merl-Pham J, Hennen E, Onursal C, Cabeza-Boeddinghaus N, Kandhari K, Stremlau M, Behr J, Hilgendorff A, Bächinger HP, Hauck SM, Vanacore R, Hansen KC, Basak T. Prolyl-3-hydroxylase 1 is a central regulator of collagen post-translational modifications and the collagen biosynthetic network. J Biol Chem. 2026 May; 302(5):111422.
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Sachs R, Ogi Y, Prekeris R. TPGS1 regulates central spindle microtubule glutamylation and remodeling during telophase and abscission. EMBO Rep. 2026 Apr; 27(8):1944-1963.
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Bui S, Reineberg A, Jones D, Na CL, Kitzmiller J, Rodriguez LR, Murthy A, Iyer S, Cooper C, Chroneos R, Tomer Y, Mulugeta S, Weaver TE, Kotton DN, Alysandratos KD, Whitsett JA, Beers MF. Divergent pathways of surfactant protein C maturation for disease-associated isoforms. J Biol Chem. 2026 Mar; 302(3):111252.
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Zhang Z, Uribe I, Davis KA, McPherson RL, Larson GP, Badiee M, Tran V, Ledwith MP, Feltman EM, Yú S, Caì Y, Chang CY, Yang X, Ma Z, Chang P, Kuhn JH, Leung AKL, Mehle A. Global remodeling of ADP-ribosylation by PARP1 suppresses influenza A virus infection. Nat Commun. 2025 Dec 17; 16(1):11176.
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Keele GR, Dzieciatkowska M, Hay AM, Vincent M, O'Connor C, Stephenson D, Reisz JA, Nemkov T, Hansen KC, Page GP, Zimring JC, Churchill GA, D'Alessandro A. Genetic architecture of the murine red blood cell proteome reveals central role of hemoglobin beta cysteine 93 in maintaining redox balance. Cell Genom. 2026 Mar 11; 6(3):101069.
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Marunde MR, Popova IK, Hall NW, Vaidya A, Bone JR, Boone BA, Brown PJ, Ezell RJ, Firestone TM, Fuchs HA, Gibson E, Gillespie ZB, Gloor SL, Hickman AR, Howard SA, Husby NL, Hsiung VT, Johnstone AL, Khan LF, Krajewski K, Lee AS, McAnarney ET, Maier KE, Maryanski DN, McCuiston JL, Noll KE, Novitzky K, Patteson EF, Rodriguez KL, Sanchez JC, Schachner LF, Smith CE, Sun L, Taylor HF, Watson R, Willis HE, Musselman CA, Venters BJ, Cheek MA, Meiners MJ, Sun ZW, Kelleher NL, Cowles MW, Weinzapfel EN, Keogh MC, Burg JM. Nucleosome context regulates chromatin reader preference. Nucleic Acids Res. 2025 Oct 28; 53(20).
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Keogh MC, Almouzni G, Andrews AJ, Armache KJ, Arrowsmith CH, Baek SH, Bedford MT, Bernstein E, Côté J, David Y, Denu JM, Fierz B, Garcia BA, Glass KC, Gozani O, Helin K, Henikoff S, Jensen ON, Josefowicz SZ, Kelleher NL, Kutateladze TG, Lindner HH, Lu C, Luger K, Mallick P, Musselman CA, Muir TW, Pa?a-Tolic L, Schneider R, Shi X, Shi Y, Sidoli S, Smith LM, Tyler JK, Wolberger C, Workman JL, Strahl BD, Young NL. A needed nomenclature for nucleosomes. Mol Cell. 2025 Oct 02; 85(19):3554-3561.
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Morrison EJ, Rissland OS. The generation and consequences of N-terminal proteoform diversity. Cell Rep. 2025 Sep 23; 44(9):116275.
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Vanauberg D, Schulz C, Raab S, Fuentes-GarcÍa G, Cadart E, Lemaire Q, Olivier-Van Stichelen S, Bray F, Brysbaert G, Rossez Y, Hardivillé S, Lefebvre T. O-GlcNAcylation of fatty acid synthase is required for its proper subcellular localization, expression level, and activity. J Biol Chem. 2025 08; 301(8):110497.
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