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
|
| 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".
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,
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2003 | 0 | 1 | 1 |
| 2004 | 1 | 0 | 1 |
| 2007 | 2 | 3 | 5 |
| 2008 | 0 | 1 | 1 |
| 2010 | 1 | 0 | 1 |
| 2012 | 0 | 2 | 2 |
| 2013 | 0 | 1 | 1 |
| 2014 | 0 | 3 | 3 |
| 2016 | 3 | 0 | 3 |
| 2018 | 0 | 1 | 1 |
| 2020 | 0 | 1 | 1 |
| 2021 | 0 | 1 | 1 |
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Below are the most recent publications written about "Protein Processing, Post-Translational" by people in Profiles.
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Calcium-dependent cytosolic phospholipase A2 activation is implicated in neuroinflammation and oxidative stress associated with ApoE4. Mol Neurodegener. 2021 04 16; 16(1):26.
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Sialylation and fucosylation modulate inflammasome-activating eIF2 Signaling and microbial translocation during HIV infection. Mucosal Immunol. 2020 09; 13(5):753-766.
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The human brainome: network analysis identifies HSPA2 as a novel Alzheimer’s disease target. Brain. 2018 09 01; 141(9):2721-2739.
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Characterization of Post-Translational Modifications to Calsequestrins of Cardiac and Skeletal Muscle. Int J Mol Sci. 2016 Sep 13; 17(9).
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The epigenome in Alzheimer's disease: current state and approaches for a new path to gene discovery and understanding disease mechanism. Acta Neuropathol. 2016 10; 132(4):503-14.
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Oxidative Stress Promotes Peroxiredoxin Hyperoxidation and Attenuates Pro-survival Signaling in Aging Chondrocytes. J Biol Chem. 2016 Mar 25; 291(13):6641-54.
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S-nitrosoglutathione reductase-dependent PPAR? denitrosylation participates in MSC-derived adipogenesis and osteogenesis. J Clin Invest. 2015 Apr; 125(4):1679-91.
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Role of Runx2 in crosstalk between Mek/Erk and PI3K/Akt signaling in MCF-10A cells. J Cell Biochem. 2014 Dec; 115(12):2208-17.
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Critical roles for nitric oxide and ERK in the completion of prosurvival autophagy in 4OHTAM-treated estrogen receptor-positive breast cancer cells. Cancer Lett. 2014 Oct 28; 353(2):290-300.
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Proteomic profiling of nitrosative stress: protein S-oxidation accompanies S-nitrosylation. ACS Chem Biol. 2014 Mar 21; 9(3):821-30.