Crystallins
"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 heterogeneous family of water-soluble structural proteins found in cells of the vertebrate lens. The presence of these proteins accounts for the transparency of the lens. The family is composed of four major groups, alpha, beta, gamma, and delta, and several minor groups, which are classed on the basis of size, charge, immunological properties, and vertebrate source. Alpha, beta, and delta crystallins occur in avian and reptilian lenses, while alpha, beta, and gamma crystallins occur in all other lenses.
Descriptor ID |
D003459
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MeSH Number(s) |
D12.776.306.366
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Concept/Terms |
Crystallins- Crystallins
- Lens Proteins
- Proteins, Lens
- Crystallin
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Below are MeSH descriptors whose meaning is more general than "Crystallins".
Below are MeSH descriptors whose meaning is more specific than "Crystallins".
This graph shows the total number of publications written about "Crystallins" by people in this website by year, and whether "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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1995 | 0 | 1 | 1 | 1996 | 0 | 1 | 1 | 1997 | 0 | 1 | 1 | 1998 | 1 | 0 | 1 | 1999 | 0 | 3 | 3 | 2000 | 1 | 0 | 1 | 2001 | 2 | 0 | 2 | 2002 | 0 | 1 | 1 | 2005 | 0 | 1 | 1 | 2008 | 1 | 0 | 1 | 2009 | 1 | 0 | 1 | 2010 | 3 | 0 | 3 | 2011 | 1 | 1 | 2 | 2012 | 1 | 0 | 1 | 2013 | 2 | 0 | 2 | 2014 | 1 | 0 | 1 | 2015 | 1 | 0 | 1 | 2016 | 1 | 0 | 1 | 2018 | 1 | 0 | 1 | 2019 | 1 | 1 | 2 | 2020 | 0 | 1 | 1 | 2021 | 1 | 0 | 1 | 2023 | 1 | 0 | 1 | 2024 | 0 | 1 | 1 | 2025 | 1 | 0 | 1 |
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Below are the most recent publications written about "Crystallins" by people in Profiles.
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Panja S, Rankenberg J, Michel C, Cooksley G, Glomb MA, Nagaraj RH. Proximal cysteine residues in proteins promote Ne-carboxyalkylation of lysine residues by a-dicarbonyl compounds. J Biol Chem. 2025 Apr; 301(4):108377.
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Panja S, Nahomi RB, Rankenberg J, Michel CR, Nagaraj RH. Thiol-Mediated Enhancement of Ne-Acetyllysine Formation in Lens Proteins. ACS Chem Biol. 2024 07 19; 19(7):1495-1505.
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Panja S, Nahomi RB, Rankenberg J, Michel CR, Gaikwad H, Nam MH, Nagaraj RH. Aggrelyte-2 promotes protein solubility and decreases lens stiffness through lysine acetylation and disulfide reduction: Implications for treating presbyopia. Aging Cell. 2023 04; 22(4):e13797.
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Lo YH, Zhou J, Rana A, Morrill D, Gentry C, Enders B, Yu YS, Sun CY, Shapiro DA, Falcone RW, Kapteyn HC, Murnane MM, Gilbert PUPA, Miao J. X-ray linear dichroic ptychography. Proc Natl Acad Sci U S A. 2021 01 19; 118(3).
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DeSisto J, O'Rourke R, Jones HE, Pawlikowski B, Malek AD, Bonney S, Guimiot F, Jones KL, Siegenthaler JA. Single-Cell Transcriptomic Analyses of the Developing Meninges Reveal Meningeal Fibroblast Diversity and Function. Dev Cell. 2020 07 06; 54(1):43-59.e4.
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Nahomi RB, Nandi SK, Rakete S, Michel C, Fritz KS, Nagaraj RH. Lysine malonylation and propionylation are prevalent in human lens proteins. Exp Eye Res. 2020 01; 190:107864.
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Nandi SK, Rakete S, Nahomi RB, Michel C, Dunbar A, Fritz KS, Nagaraj RH. Succinylation Is a Gain-of-Function Modification in Human Lens aB-Crystallin. Biochemistry. 2019 03 05; 58(9):1260-1274.
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Nam MH, Nagaraj RH. Matrix-bound AGEs enhance TGF?2-mediated mesenchymal transition of lens epithelial cells via the noncanonical pathway: implications for secondary cataract formation. Biochem J. 2018 04 23; 475(8):1427-1440.
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Nahomi RB, Pantcheva MB, Nagaraj RH. aB-crystallin is essential for the TGF-?2-mediated epithelial to mesenchymal transition of lens epithelial cells. Biochem J. 2016 05 15; 473(10):1455-69.
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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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