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.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

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
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".

Biological Sciences [G]
Chemical Phenomena [G02]
Biochemical Phenomena [G02.111]
Peptide Biosynthesis [G02.111.660]
Protein Biosynthesis [G02.111.660.871]
Protein Modification, Translational [G02.111.660.871.790]
Protein Processing, Post-Translational [G02.111.660.871.790.600]
Protein Modification, Translational [G02.111.691]
Protein Processing, Post-Translational [G02.111.691.600]
Metabolism [G03]
Peptide Biosynthesis [G03.734]
Protein Biosynthesis [G03.734.871]
Protein Modification, Translational [G03.734.871.790]
Protein Processing, Post-Translational [G03.734.871.790.600]
Genetic Phenomena [G05]
Gene Expression Regulation [G05.308]
Protein Modification, Translational [G05.308.670]
Protein Processing, Post-Translational [G05.308.670.600]

Below are MeSH descriptors whose meaning is related to "Protein Processing, Post-Translational".

Below are MeSH descriptors whose meaning is more specific than "Protein Processing, Post-Translational".

publications

Timeline | Most Recent

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.

Bar chart showing 151 publications over 27 distinct years, with a maximum of 13 publications in 2006

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
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

Below are the most recent publications written about "Protein Processing, Post-Translational" by people in Profiles.

Vaishnav MS, Kumari N, Srikanta S, Simha V, Krishnaswamy PR, Bhat N. Truncated Albumins as Novel Surrogate Biomarkers in Diabetes Therapy: Epiphenomena and Potential Clinical Applications. Metab Syndr Relat Disord. 2024 Dec; 22(10):743-752.

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Qin M, Fan W, Li L, Xu T, Zhang H, Chen F, Man J, Kombe AJK, Zhang J, Shi Y, Yao X, Yang Z, Hou Z, Ruan K, Liu D. PRMT1 and TDRD3 promote stress granule assembly by rebuilding the protein-RNA interaction network. Int J Biol Macromol. 2024 Oct; 277(Pt 3):134411.

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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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