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 200 publications over 29 distinct years, with a maximum of 13 publications in 2015 and 2017

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

Year	Major Topic	Minor Topic	Total
1996	0	4	4
1997	1	4	5
1998	3	6	9
1999	4	3	7
2000	2	9	11
2001	0	8	8
2002	1	7	8
2003	1	4	5
2004	3	7	10
2005	1	1	2
2006	1	3	4
2007	1	10	11
2008	4	2	6
2009	2	6	8
2010	1	4	5
2011	4	6	10
2012	4	6	10
2013	3	9	12
2014	1	6	7
2015	4	9	13
2016	2	5	7
2017	5	8	13
2018	4	1	5
2019	0	4	4
2020	2	3	5
2021	2	1	3
2022	1	1	2
2023	1	2	3
2024	0	3	3

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

Ko YH, Lokareddy RK, Doll SG, Yeggoni DP, Girdhar A, Mawn I, Klim JR, Rizvi NF, Meyers R, Gillilan RE, Guo L, Cingolani G. Single Acetylation-mimetic Mutation in TDP-43 Nuclear Localization Signal Disrupts Importin a1/? Signaling. J Mol Biol. 2024 10 15; 436(20):168751.

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Seitz A, Busch M, Kroemer J, Schneider A, Simon S, Jungmann A, Katus HA, Most P, Ritterhoff J. S100A1's single cysteine is an indispensable redox switch for the protection against diastolic calcium waves in cardiomyocytes. Am J Physiol Heart Circ Physiol. 2024 07 01; 327(1):H000.

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Meyer GA, Ferey JLA, Sanford JA, Fitzgerald LS, Greenberg AE, Svensson K, Greenberg MJ, Schenk S. Insights into posttranslational regulation of skeletal muscle contractile function by the acetyltransferases, p300 and CBP. J Appl Physiol (1985). 2024 06 01; 136(6):1559-1567.

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Pelham JF, Mosier AE, Altshuler SC, Rhodes ML, Kirchhoff CL, Fall WB, Mann C, Baik LS, Chiu JC, Hurley JM. Conformational changes in the negative arm of the circadian clock correlate with dynamic interactomes involved in post-transcriptional regulation. Cell Rep. 2023 04 25; 42(4):112376.

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Kaji H, Kaji A. Recollection of How We Came Across the Protein Modification with Amino Acids by Aminoacyl tRNA-Protein Transferase. Methods Mol Biol. 2023; 2620:15-20.

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Kaji H, Kaji A. Correlated Measurement of Endogenous ATE1 Activity on Native Acceptor Proteins in Tissues and Cultured Cells to Detect Cellular Aging. Methods Mol Biol. 2023; 2620:41-50.

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Ashton AW, Dhanjal HK, Rossner B, Mahmood H, Patel VI, Nadim M, Lota M, Shahid F, Li Z, Joyce D, Pajkos M, Doszt?nyi Z, Jiao X, Pestell RG. Acetylation of nuclear receptors in health and disease: an update. FEBS J. 2024 01; 291(2):217-236.

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Gavali S, Ross KE, Cowart J, Chen C, Wu CH. iPTMnet RESTful API for Post-translational Modification Network Analysis. Methods Mol Biol. 2022; 2499:187-204.

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Trefely S, Huber K, Liu J, Noji M, Stransky S, Singh J, Doan MT, Lovell CD, von Krusenstiern E, Jiang H, Bostwick A, Pepper HL, Izzo L, Zhao S, Xu JP, Bedi KC, Rame JE, Bogner-Strauss JG, Mesaros C, Sidoli S, Wellen KE, Snyder NW. Quantitative subcellular acyl-CoA analysis reveals distinct nuclear metabolism and isoleucine-dependent histone propionylation. Mol Cell. 2022 01 20; 82(2):447-462.e6.

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Yi M, Niu M, Xu L, Luo S, Wu K. Regulation of PD-L1 expression in the tumor microenvironment. J Hematol Oncol. 2021 01 07; 14(1):10.

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