Amino Acid Substitution
"Amino Acid Substitution" 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.
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
Descriptor ID |
D019943
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MeSH Number(s) |
E05.393.420.601.035 G05.355.600.109
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Concept/Terms |
Amino Acid Substitution- Amino Acid Substitution
- Amino Acid Substitutions
- Substitution, Amino Acid
- Substitutions, Amino Acid
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Below are MeSH descriptors whose meaning is more general than "Amino Acid Substitution".
Below are MeSH descriptors whose meaning is more specific than "Amino Acid Substitution".
This graph shows the total number of publications written about "Amino Acid Substitution" by people in this website by year, and whether "Amino Acid Substitution" 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 |
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1999 | 0 | 2 | 2 | 2001 | 0 | 2 | 2 | 2003 | 0 | 2 | 2 | 2004 | 0 | 1 | 1 | 2005 | 1 | 2 | 3 | 2006 | 0 | 1 | 1 | 2008 | 0 | 3 | 3 | 2009 | 1 | 1 | 2 | 2010 | 0 | 2 | 2 | 2011 | 0 | 1 | 1 | 2014 | 1 | 0 | 1 | 2015 | 0 | 2 | 2 | 2016 | 0 | 1 | 1 | 2018 | 0 | 3 | 3 | 2019 | 0 | 1 | 1 |
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Below are the most recent publications written about "Amino Acid Substitution" by people in Profiles.
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Komatsu TE, Hodowanec AC, Colberg-Poley AM, Pikis A, Singer ME, O'Rear JJ, Donaldson EF. In-depth genomic analyses identified novel letermovir resistance-associated substitutions in the cytomegalovirus UL56 and UL89 gene products. Antiviral Res. 2019 09; 169:104549.
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Jo S, Fonseca TL, Bocco BMLC, Fernandes GW, McAninch EA, Bolin AP, Da Concei??o RR, Werneck-de-Castro JP, Ignacio DL, Egri P, N?meth D, Fekete C, Bernardi MM, Leitch VD, Mannan NS, Curry KF, Butterfield NC, Bassett JHD, Williams GR, Gereben B, Ribeiro MO, Bianco AC. Type 2 deiodinase polymorphism causes ER stress and hypothyroidism in the brain. J Clin Invest. 2019 01 02; 129(1):230-245.
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Lin DM, Javidiparsijani S, Vardouniotis A, Buckingham L, Reddy SB, Gattuso P. Ectopic Thyroid Tissue: Immunohistochemistry and Molecular Analysis. Appl Immunohistochem Mol Morphol. 2018 Nov/Dec; 26(10):734-739.
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McAninch EA, Rajan KB, Evans DA, Jo S, Chaker L, Peeters RP, Bennett DA, Mash DC, Bianco AC. A Common DIO2 Polymorphism and Alzheimer Disease Dementia in African and European Americans. J Clin Endocrinol Metab. 2018 05 01; 103(5):1818-1826.
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S?ndergaard MT, Liu Y, Larsen KT, Nani A, Tian X, Holt C, Wang R, Wimmer R, Van Petegem F, Fill M, Chen SR, Overgaard MT. The Arrhythmogenic Calmodulin p.Phe142Leu Mutation Impairs C-domain Ca2+ Binding but Not Calmodulin-dependent Inhibition of the Cardiac Ryanodine Receptor. J Biol Chem. 2017 01 27; 292(4):1385-1395.
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Lewis KM, Ronish LA, R?os E, Kang C. Characterization of Two Human Skeletal Calsequestrin Mutants Implicated in Malignant Hyperthermia and Vacuolar Aggregate Myopathy. J Biol Chem. 2015 Nov 27; 290(48):28665-74.
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McAninch EA, Jo S, Preite NZ, Farkas E, Moh?csik P, Fekete C, Egri P, Gereben B, Li Y, Deng Y, Patti ME, Zevenbergen C, Peeters RP, Mash DC, Bianco AC. Prevalent polymorphism in thyroid hormone-activating enzyme leaves a genetic fingerprint that underlies associated clinical syndromes. J Clin Endocrinol Metab. 2015 Mar; 100(3):920-33.
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Russell TA, Blizinsky KD, Cobia DJ, Cahill ME, Xie Z, Sweet RA, Duan J, Gejman PV, Wang L, Csernansky JG, Penzes P. A sequence variant in human KALRN impairs protein function and coincides with reduced cortical thickness. Nat Commun. 2014 Sep 16; 5:4858.
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Leung MY, Cohen FS. Increasing hydrophobicity of residues in an anti-HIV-1 Env peptide synergistically improves potency. Biophys J. 2011 Apr 20; 100(8):1960-8.
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Tasaki S, Nagasaki M, Kozuka-Hata H, Semba K, Gotoh N, Hattori S, Inoue J, Yamamoto T, Miyano S, Sugano S, Oyama M. Phosphoproteomics-based modeling defines the regulatory mechanism underlying aberrant EGFR signaling. PLoS One. 2010 Nov 10; 5(11):e13926.
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