 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) |
G02.111.087.675.871.790.600 G02.111.087.693.600 G02.149.115.675.871.790.600 G02.149.115.693.600 G03.495.770.871.790.600 G05.355.315.670.600
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| Concept/Terms |
Protein Processing, Post-Translational- Protein Processing, Post-Translational
- Processing, Post-Translational Protein
- Post-Translational Protein Processing
- Post Translational Protein Processing
- Protein Processing, Post Translational
- Protein Modification, Post-Translational
- Protein Modification, Post Translational
- 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 Modification
- Modification, Post-Translational Protein
- Modifications, Post-Translational Protein
- Post Translational Protein Modification
- Post-Translational Protein Modifications
- Protein Modifications, Post-Translational
- Posttranslational Protein Processing
- Processing, Posttranslational Protein
Amino Acid Modification, Post-Translational- Amino Acid Modification, Post-Translational
- Amino Acid Modification, Post Translational
- Posttranslational Amino Acid Modification
- Amino Acid Modification, Posttranslational
- Post-Translational Amino Acid Modification
- Post Translational Amino Acid Modification
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Below are MeSH descriptors whose meaning is more general than "Protein Processing, Post-Translational".
- Biological Sciences [G]
- Chemical Phenomena [G02]
- Biochemical Phenomena [G02.111]
- Biochemical Processes [G02.111.087]
- Peptide Biosynthesis [G02.111.087.675]
- Protein Biosynthesis [G02.111.087.675.871]
- Protein Modification, Translational [G02.111.087.675.871.790]
- Protein Processing, Post-Translational [G02.111.087.675.871.790.600]
- Protein Modification, Translational [G02.111.087.693]
- Protein Processing, Post-Translational [G02.111.087.693.600]
- Chemical Processes [G02.149]
- Biochemical Processes [G02.149.115]
- Peptide Biosynthesis [G02.149.115.675]
- Protein Biosynthesis [G02.149.115.675.871]
- Protein Modification, Translational [G02.149.115.675.871.790]
- Protein Processing, Post-Translational [G02.149.115.675.871.790.600]
- Protein Modification, Translational [G02.149.115.693]
- Protein Processing, Post-Translational [G02.149.115.693.600]
- Metabolic Phenomena [G03]
- Metabolism [G03.495]
- Peptide Biosynthesis [G03.495.770]
- Protein Biosynthesis [G03.495.770.871]
- Protein Modification, Translational [G03.495.770.871.790]
- Protein Processing, Post-Translational [G03.495.770.871.790.600]
- Genetic Phenomena [G05]
- Genetic Processes [G05.355]
- Gene Expression Regulation [G05.355.315]
- Protein Modification, Translational [G05.355.315.670]
- Protein Processing, Post-Translational [G05.355.315.670.600]
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 |
|---|
| 2007 | 0 | 1 | 1 | | 2008 | 1 | 0 | 1 | | 2013 | 1 | 0 | 1 | | 2014 | 1 | 1 | 2 | | 2021 | 0 | 1 | 1 |
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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Lutz PE, Chay MA, Pacis A, Chen GG, Aouabed Z, Maffioletti E, Th?roux JF, Grenier JC, Yang J, Aguirre M, Ernst C, Redensek A, van Kempen LC, Yalcin I, Kwan T, Mechawar N, Pastinen T, Turecki G. Non-CG methylation and multiple histone profiles associate child abuse with immune and small GTPase dysregulation. Nat Commun. 2021 02 18; 12(1):1132.
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Majnik AV, Lane RH. The relationship between early-life environment, the epigenome and the microbiota. Epigenomics. 2015 Oct; 7(7):1173-84.
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Light N, Adoue V, Ge B, Chen SH, Kwan T, Pastinen T. Interrogation of allelic chromatin states in human cells by high-density ChIP-genotyping. Epigenetics. 2014 Sep; 9(9):1238-51.
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Harihar S, Pounds KM, Iwakuma T, Seidah NG, Welch DR. Furin is the major proprotein convertase required for KISS1-to-Kisspeptin processing. PLoS One. 2014; 9(1):e84958.
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Menden H, Tate E, Hogg N, Sampath V. LPS-mediated endothelial activation in pulmonary endothelial cells: role of Nox2-dependent IKK-? phosphorylation. Am J Physiol Lung Cell Mol Physiol. 2013 Mar 15; 304(6):L445-55.
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Terzian T, Suh YA, Iwakuma T, Post SM, Neumann M, Lang GA, Van Pelt CS, Lozano G. The inherent instability of mutant p53 is alleviated by Mdm2 or p16INK4a loss. Genes Dev. 2008 May 15; 22(10):1337-44.
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Iwakuma T, Lozano G. Crippling p53 activities via knock-in mutations in mouse models. Oncogene. 2007 Apr 02; 26(15):2177-84.
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MacLennan NK, James SJ, Melnyk S, Piroozi A, Jernigan S, Hsu JL, Janke SM, Pham TD, Lane RH. Uteroplacental insufficiency alters DNA methylation, one-carbon metabolism, and histone acetylation in IUGR rats. Physiol Genomics. 2004 Jun 17; 18(1):43-50.
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Abate C, Baker SJ, Lees-Miller SP, Anderson CW, Marshak DR, Curran T. Dimerization and DNA binding alter phosphorylation of Fos and Jun. Proc Natl Acad Sci U S A. 1993 Jul 15; 90(14):6766-70.
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Curran T, Abate C, Baker S, Kerppola T, Xanthoudakis S. The regulation of c-fos: too much is never enough. Adv Second Messenger Phosphoprotein Res. 1993; 28:271-7.
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