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humans (549) 549
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alpha-crystallin b chain - genetics (341) 341
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biochemistry & molecular biology (259) 259
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proteins (228) 228
alpha-crystallin (215) 215
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heat shock proteins (158) 158
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cell biology (140) 140
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alpha-crystallin b chain - chemistry (114) 114
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alpha-crystallin a chain - metabolism (88) 88
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crystallin (88) 88
heat-shock-protein (88) 88
eye diseases (87) 87
protein folding (87) 87
b-crystallin (86) 86
lens, crystalline - metabolism (85) 85
phosphorylation (81) 81
base sequence (79) 79
multidisciplinary sciences (77) 77
a-crystallin (75) 75
molecular chaperones - metabolism (75) 75
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medicine (73) 73
molecular chaperones (73) 73
blotting, western (72) 72
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middle aged (72) 72
reverse transcriptase polymerase chain reaction (72) 72
alpha b-crystallin (71) 71
alpha-crystallin a chain - chemistry (71) 71
protein structure, tertiary (71) 71
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small heat shock proteins (64) 64
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crystal structure (57) 57
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protein structure, secondary (56) 56
sequence alignment (56) 56
aggregation (55) 55
protein conformation (55) 55
recombinant proteins - metabolism (55) 55
rna, messenger - metabolism (55) 55
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immunohistochemistry (54) 54
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lens (47) 47
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Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 05/2013, Volume 288, Issue 18, pp. 13022 - 13035
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 12/2017, Volume 494, Issue 1-2, pp. 402 - 408
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 04/2014, Volume 9, Issue 4, pp. e95507 - e95507
alpha A-crystallin and alpha B-crystallin are members of the small heat shock protein family and function as molecular chaperones and major lens structural... 
AUTOSOMAL-DOMINANT CATARACT | EPITHELIAL-CELLS | AGE-RELATED-CHANGES | MULTIDISCIPLINARY SCIENCES | MOUSE MODEL | COMPARATIVE PROTEOMIC ANALYSIS | GAMMA-CRYSTALLIN | BETA-CRYSTALLIN | EYE LENS | MASS-SPECTROMETRY | HEAT-SHOCK-PROTEIN | alpha-Crystallin B Chain - genetics | Crystallins - metabolism | Calpain - metabolism | Gelsolin - metabolism | Lens, Crystalline - metabolism | alpha-Crystallin B Chain - metabolism | Crystallins - genetics | Calpain - genetics | Mice, Knockout | alpha-Crystallin A Chain - genetics | Muscle Proteins - genetics | Animals | Eye Proteins - metabolism | alpha-Crystallin A Chain - metabolism | Mice, Mutant Strains | Mass Spectrometry | Intermediate Filament Proteins - genetics | Muscle Proteins - metabolism | Gelsolin - genetics | Mice | Eye Proteins - genetics | Intermediate Filament Proteins - metabolism | Cataracts | Cytochrome | Glutamate dehydrogenase | Creatine kinase | Genomics | Filensin | Acidification | Biochemistry | Chaperones | Kinases | Creatine | Degradation | Proteins | Spectrometry | Phosphoglycerate mutase | Actin | Histones | Hemoglobin | Gelsolin | Age | Phosphopyruvate hydratase | Crystal structure | Structural proteins | Heat shock proteins | Crosslinking | Calpain | Abundance | Crystallinity | Substrates | Medicine | Cytochrome c | Crystallin | Proteomics | Scientific imaging | In vivo methods and tests | Genetic engineering | Mutation | Mass spectrometry | Lenses | Heat shock | Index Medicus
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
PLoS ONE, ISSN 1932-6203, 01/2012, Volume 7, Issue 1, pp. e30257 - e30257
Methylglyoxal (MGO) is an alpha-dicarbonyl compound present ubiquitously in the human body. MGO reacts with arginine residues in proteins and forms adducts... 
HUMAN LENS PROTEINS | B-CRYSTALLIN | MAILLARD REACTION | MULTIDISCIPLINARY SCIENCES | MOLECULAR CHAPERONE | POSTTRANSLATIONAL MODIFICATIONS | ALPHA-A-CRYSTALLIN | HEAT-SHOCK-PROTEIN-27 | METHYLGLYOXAL MODIFICATION | NONOCULAR TISSUES | N-TERMINAL REGION | alpha-Crystallin B Chain - genetics | HSP27 Heat-Shock Proteins - chemistry | Molecular Chaperones - metabolism | Imidazoles - chemistry | Molecular Sequence Data | alpha-Crystallin B Chain - metabolism | Molecular Chaperones - chemistry | alpha-Crystallin A Chain - genetics | HSP27 Heat-Shock Proteins - genetics | Thermodynamics | alpha-Crystallin A Chain - metabolism | alpha-Crystallin B Chain - chemistry | Arginine - genetics | Protein Binding - drug effects | Molecular Structure | Circular Dichroism | Imidazoles - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Pyruvaldehyde - pharmacology | Electrophoresis, Polyacrylamide Gel | Molecular Chaperones - genetics | Recombinant Proteins - chemistry | Spectrometry, Fluorescence | Binding Sites - genetics | Arginine - chemistry | Sequence Homology, Amino Acid | Protein Structure, Secondary - drug effects | HSP27 Heat-Shock Proteins - metabolism | Kinetics | Mutation | alpha-Crystallin A Chain - chemistry | Arginine - metabolism | Protein Structure, Tertiary - drug effects | Proteins | Physiological aspects | Heat shock proteins | Arginine | Protein binding | Cataracts | Residues | Structural stability | Amino acids | Biochemistry | Small heat shock proteins | Biopolymers | Aging | Age | Crystal structure | Adducts | Alanine | Tertiary structure | Crystallinity | Crystallin | Hsp27 protein | Alzheimers disease | Protein interaction | Pyruvaldehyde | Protein structure | Binding sites | Heat shock | Structure-function relationships | Index Medicus
Journal Article