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FEBS Letters, ISSN 0014-5793, 02/2012, Volume 586, Issue 4, pp. 330 - 336
► How can destabilizing mutations of lens γ-crystallin cause cataract? ► Cataract-causing mutations stabilize an unfolding intermediate of γD-crystallin. ►... 
Cataract | Chaperone | Small heat-shock protein | β-Crystallin | αB-crystallin phosphorylation | α-Crystallin | γD-crystallin | Bimane fluorescence | Denaturant unfolding | sHSP | T4 lysozyme | αB-D3 | T4L | small heat-shock proteins | guanidine hydrochloride | wild type | GdnHCl | αB-crystallin S19D/S45D/S59D | alpha B-crystallin phosphorylation | HEREDITARY CATARACT | MECHANISM | gamma D-crystallin | B-CRYSTALLIN | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | A-CRYSTALLIN | T4 LYSOZYME | alpha-Crystallin | 2-MODE BINDING | P23T MUTANT | CELL BIOLOGY | beta-Crystallin | HEAT-SHOCK PROTEINS | BIOPHYSICS | TRANSPARENCY | Recombinant Proteins - metabolism | gamma-Crystallins - genetics | Humans | Mutant Proteins - genetics | Lens, Crystalline - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Recombinant Proteins - genetics | Cataract - metabolism | Unfolded Protein Response | alpha-Crystallins - metabolism | Thermodynamics | Animals | gamma-Crystallins - chemistry | gamma-Crystallins - metabolism | Cataract - congenital | Mutant Proteins - chemistry | Lens, Crystalline - chemistry | Protein Binding | Cataract - genetics | Mice | Index Medicus | bimane fluorescence | chaperone | cataract | small heat-shock protein | β-crystallin | denaturant unfolding | α-crystallin
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 05/2013, Volume 288, Issue 18, pp. 13022 - 13035
Journal Article
PLOS ONE, ISSN 1932-6203, 12/2015, Volume 10, Issue 12, pp. e0144621 - e0144621
Interaction among crystallins is required for the maintenance of lens transparency. Deamidation is one of the most common post-translational modifications in... 
AGE-DEPENDENT DEAMIDATION | HUMAN LENS | MULTIDISCIPLINARY SCIENCES | GAMMA-D-CRYSTALLIN | BOVINE LENS | HUMAN SENILE CATARACTOGENESIS | SURFACE-PLASMON RESONANCE | BACKBONE CLEAVAGE | CHAPERONE-LIKE ACTIVITY | HEAT-SHOCK-PROTEIN | FUNCTIONAL-PROPERTIES | alpha-Crystallin B Chain - genetics | beta-Crystallin A Chain - metabolism | Crystallins - metabolism | Humans | Protein Multimerization | alpha-Crystallin B Chain - metabolism | Green Fluorescent Proteins - genetics | Transfection | alpha-Crystallin B Chain - chemistry | Escherichia coli - metabolism | Amides - metabolism | Binding Sites | Crystallins - chemistry | Genes, Reporter | Recombinant Proteins - metabolism | Green Fluorescent Proteins - metabolism | Gene Expression | Mutagenesis, Site-Directed | Bacterial Proteins - genetics | Lens, Crystalline - metabolism | Recombinant Proteins - chemistry | Crystallins - genetics | Recombinant Proteins - genetics | Escherichia coli - genetics | Lens, Crystalline - chemistry | Protein Binding | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | Protein Processing, Post-Translational | HeLa Cells | Mutation | beta-Crystallin A Chain - genetics | Luminescent Proteins - metabolism | beta-Crystallin A Chain - chemistry | Cataracts | Transparency | Fluorescence | Hydrophobicity | Molecular weight | Strong interactions (field theory) | Oligomers | Post-translation | Aging | Fluorescence resonance energy transfer | Crystal structure | Binding | Heat shock proteins | Optometry | Crystallinity | Adhesion | Mutants | Crystallin | Microscopy | Affinity | Surface plasmon resonance | Resonance | Energy transfer | Apoptosis | Index Medicus
Journal Article
Journal Article