 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 |
|---|
| 1988 | 1 | 0 | 1 | | 1990 | 0 | 1 | 1 | | 1992 | 0 | 1 | 1 | | 1996 | 1 | 0 | 1 | | 1997 | 1 | 0 | 1 | | 2002 | 0 | 1 | 1 | | 2004 | 0 | 2 | 2 | | 2005 | 1 | 0 | 1 | | 2006 | 1 | 0 | 1 | | 2008 | 0 | 1 | 1 | | 2009 | 2 | 1 | 3 | | 2010 | 0 | 3 | 3 | | 2011 | 0 | 2 | 2 | | 2012 | 1 | 1 | 2 | | 2013 | 0 | 2 | 2 | | 2014 | 1 | 2 | 3 | | 2015 | 2 | 1 | 3 | | 2016 | 3 | 0 | 3 | | 2017 | 1 | 0 | 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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Rietz A, Li H, Quist KM, Cherry JJ, Lorson CL, Burnett BG, Kern NL, Calder AN, Fritsche M, Lusic H, Boaler PJ, Choi S, Xing X, Glicksman MA, Cuny GD, Androphy EJ, Hodgetts KJ. Discovery of a Small Molecule Probe That Post-Translationally Stabilizes the Survival Motor Neuron Protein for the Treatment of Spinal Muscular Atrophy. J Med Chem. 2017 Jun 08; 60(11):4594-4610.
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Chen Y, Guo H, Terajima M, Banerjee P, Liu X, Yu J, Momin AA, Katayama H, Hanash SM, Burns AR, Fields GB, Yamauchi M, Kurie JM. Lysyl Hydroxylase 2 Is Secreted by Tumor Cells and Can Modify Collagen in the Extracellular Space. J Biol Chem. 2016 Dec 09; 291(50):25799-25808.
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Huang C, Cheng J, Bawa-Khalfe T, Yao X, Chin YE, Yeh ET. SUMOylated ORC2 Recruits a Histone Demethylase to Regulate Centromeric Histone Modification and Genomic Stability. Cell Rep. 2016 Apr 05; 15(1):147-57.
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Kanan Y, Al-Ubaidi MR. Identification of Tyrosine O Sulfated Proteins in Cow Retina and the 661W Cell Line. Adv Exp Med Biol. 2016; 854:649-54.
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Stuck MW, Conley SM, Naash MI. Retinal Degeneration Slow (RDS) Glycosylation Plays a Role in Cone Function and in the Regulation of RDS·ROM-1 Protein Complex Formation. J Biol Chem. 2015 Nov 13; 290(46):27901-13.
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Yu H, Chen K, Wu J, Yang Z, Shi L, Barlow LL, Aronoff DM, Garey KW, Savidge TC, von Rosenvinge EC, Kelly CP, Feng H. Identification of toxemia in patients with Clostridium difficile infection. PLoS One. 2015; 10(4):e0124235.
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Kanan Y, Al-Ubaidi MR. Role of tyrosine-sulfated proteins in retinal structure and function. Exp Eye Res. 2015 Apr; 133:126-31.
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Dao AT, Zagaar MA, Alkadhi KA. Moderate Treadmill Exercise Protects Synaptic Plasticity of the Dentate Gyrus and Related Signaling Cascade in a Rat Model of Alzheimer's Disease. Mol Neurobiol. 2015 Dec; 52(3):1067-1076.
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Kanan Y, Siefert JC, Kinter M, Al-Ubaidi MR. Complement factor H, vitronectin, and opticin are tyrosine-sulfated proteins of the retinal pigment epithelium. PLoS One. 2014; 9(8):e105409.
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Kanan Y, Brobst D, Han Z, Naash MI, Al-Ubaidi MR. Fibulin 2, a tyrosine O-sulfated protein, is up-regulated following retinal detachment. J Biol Chem. 2014 May 09; 289(19):13419-33.
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