 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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| 1993 | 0 | 3 | 3 | | 1994 | 2 | 4 | 6 | | 1995 | 2 | 1 | 3 | | 1996 | 1 | 2 | 3 | | 1997 | 1 | 4 | 5 | | 1998 | 1 | 2 | 3 | | 1999 | 3 | 3 | 6 | | 2000 | 3 | 7 | 10 | | 2001 | 2 | 2 | 4 | | 2002 | 1 | 6 | 7 | | 2003 | 1 | 8 | 9 | | 2004 | 3 | 7 | 10 | | 2005 | 3 | 3 | 6 | | 2006 | 5 | 6 | 11 | | 2007 | 3 | 4 | 7 | | 2008 | 3 | 8 | 11 | | 2009 | 4 | 7 | 11 | | 2010 | 5 | 5 | 10 | | 2011 | 3 | 8 | 11 | | 2012 | 4 | 13 | 17 | | 2013 | 7 | 11 | 18 | | 2014 | 4 | 8 | 12 | | 2015 | 6 | 10 | 16 | | 2016 | 10 | 13 | 23 | | 2017 | 9 | 12 | 21 | | 2018 | 2 | 7 | 9 | | 2019 | 6 | 9 | 15 | | 2020 | 2 | 8 | 10 | | 2021 | 5 | 7 | 12 | | 2022 | 0 | 3 | 3 | | 2023 | 0 | 2 | 2 |
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Below are the most recent publications written about "Protein Processing, Post-Translational" by people in Profiles.
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Kulik L, Renner B, Laskowski J, Thurman JM, Michael Holers V. Highly pathogenic natural monoclonal antibody B4-IgM recognizes a post-translational modification comprised of acetylated N-terminal methionine followed by aspartic or glutamic acid. Mol Immunol. 2023 05; 157:112-128.
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Kant S, Sun Y, Pancholi V. StkP- and PhpP-Mediated Posttranslational Modifications Modulate the S. pneumoniae Metabolism, Polysaccharide Capsule, and Virulence. Infect Immun. 2023 04 18; 91(4):e0029622.
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Wethekam LC, Moore JK. Microtubule cytoskeleton: Revealing new readers of?the tubulin code. Curr Biol. 2022 09 26; 32(18):R960-R962.
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Johnson NR. Tau acetylation reduces its autophagic degradation and is a targetable pathway for human tauopathies. Bioessays. 2022 06; 44(6):e2200062.
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Shepard JD, Freitas BT, Rodriguez SE, Scholte FEM, Baker K, Hutchison MR, Longo JE, Miller HC, O'Boyle BM, Tandon A, Zhao P, Grimsey NJ, Wells L, Bergeron ?, Pegan SD. The Structure and Immune Regulatory Implications of the Ubiquitin-Like Tandem Domain Within an Avian 2'-5' Oligoadenylate Synthetase-Like Protein. Front Immunol. 2021; 12:794664.
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Iragavarapu AG, Yao L, Kasinath V. Structural insights into the interactions of Polycomb Repressive Complex 2 with chromatin. Biochem Soc Trans. 2021 12 17; 49(6):2639-2653.
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Jennings EQ, Fritz KS, Galligan JJ. Biochemical genesis of enzymatic and non-enzymatic post-translational modifications. Mol Aspects Med. 2022 08; 86:101053.
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Vann KR, Vishweshwaraiah YL, Dokholyan NV, Kutateladze TG. Searching for methyllysine-binding aromatic cages. Biochem J. 2021 10 15; 478(19):3613-3619.
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Kumar R, Theiss AL, Venuprasad K. ROR?t protein modifications and IL-17-mediated inflammation. Trends Immunol. 2021 11; 42(11):1037-1050.
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Roffers-Agarwal J, Lidberg KA, Gammill LS. The lysine methyltransferase SETD2 is a dynamically expressed regulator of early neural crest development. Genesis. 2021 10; 59(10):e23448.
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