alpha-Crystallins
"alpha-Crystallins" 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.
A subclass of crystallins that provides the majority of refractive power and translucency to the lens (LENS, CRYSTALLINE) in VERTEBRATES. Alpha-crystallins also act as molecular chaperones that bind to denatured proteins, keep them in solution and thereby maintain the translucency of the lens. The proteins exist as large oligomers that are formed from ALPHA-CRYSTALLIN A CHAIN and ALPHA-CRYSTALLIN B CHAIN subunits.
Descriptor ID |
D038201
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MeSH Number(s) |
D12.776.306.366.100 D12.776.580.157
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Concept/Terms |
alpha-Crystallins- alpha-Crystallins
- alpha Crystallins
- Crystallins, alpha
- alpha-Crystallin
- alpha Crystallin
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Below are MeSH descriptors whose meaning is more general than "alpha-Crystallins".
Below are MeSH descriptors whose meaning is more specific than "alpha-Crystallins".
This graph shows the total number of publications written about "alpha-Crystallins" by people in this website by year, and whether "alpha-Crystallins" 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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2003 | 1 | 0 | 1 | 2006 | 0 | 1 | 1 | 2007 | 1 | 0 | 1 | 2015 | 1 | 2 | 3 | 2019 | 1 | 0 | 1 |
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Below are the most recent publications written about "alpha-Crystallins" by people in Profiles.
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Nandi SK, Nahomi RB, Harris PS, Michel CR, Fritz KS, Nagaraj RH. The absence of SIRT3 and SIRT5 promotes the acetylation of lens proteins and improves the chaperone activity of a-crystallin in mouse lenses. Exp Eye Res. 2019 05; 182:1-9.
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Mueller NH, Fogueri U, Pedler MG, Montana K, Petrash JM, Ammar DA. Impact of Subunit Composition on the Uptake of a-Crystallin by Lens and Retina. PLoS One. 2015; 10(9):e0137659.
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Panda AK, Nandi SK, Chakraborty A, Nagaraj RH, Biswas A. Differential role of arginine mutations on the structure and functions of a-crystallin. Biochim Biophys Acta. 2016 Jan; 1860(1 Pt B):199-210.
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Nagaraj RH, Nahomi RB, Mueller NH, Raghavan CT, Ammar DA, Petrash JM. Therapeutic potential of a-crystallin. Biochim Biophys Acta. 2016 Jan; 1860(1 Pt B):252-7.
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Nahomi RB, DiMauro MA, Wang B, Nagaraj RH. Identification of peptides in human Hsp20 and Hsp27 that possess molecular chaperone and anti-apoptotic activities. Biochem J. 2015 Jan 01; 465(1):115-25.
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Nandi SK, Rehna EA, Panda AK, Shiburaj S, Dharmalingam K, Biswas A. A S52P mutation in the 'a-crystallin domain' of Mycobacterium leprae HSP18 reduces its oligomeric size and chaperone function. FEBS J. 2013 Dec; 280(23):5994-6009.
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Sasikala V, Rooban BN, Sahasranamam V, Abraham A. Rutin ameliorates free radical mediated cataract by enhancing the chaperone activity of a-crystallin. Graefes Arch Clin Exp Ophthalmol. 2013 Jul; 251(7):1747-55.
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Rooban BN, Sasikala V, Sahasranamam V, Abraham A. Analysis on the alterations of lens proteins by Vitex negundo in selenite cataract models. Mol Vis. 2011; 17:1239-48.
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Barton KA, Hsu CD, Petrash JM. Interactions between small heat shock protein alpha-crystallin and galectin-related interfiber protein (GRIFIN) in the ocular lens. Biochemistry. 2009 May 12; 48(18):3956-66.
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Puttaiah S, Biswas A, Staniszewska M, Nagaraj RH. Methylglyoxal inhibits glycation-mediated loss in chaperone function and synthesis of pentosidine in alpha-crystallin. Exp Eye Res. 2007 May; 84(5):914-21.
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