X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (1195) 1195
humans (701) 701
animals (697) 697
alpha-crystallin b chain - metabolism (506) 506
biochemistry & molecular biology (358) 358
alpha-crystallin (294) 294
alpha-crystallin b chain - genetics (290) 290
proteins (272) 272
mice (265) 265
male (210) 210
female (187) 187
molecular sequence data (181) 181
alpha-b-crystallin (180) 180
amino acid sequence (177) 177
cell biology (177) 177
heat shock proteins (171) 171
rats (171) 171
alpha-crystallin a chain - metabolism (159) 159
mutation (158) 158
alpha-crystallin b chain - chemistry (156) 156
protein binding (152) 152
heat-shock proteins (151) 151
lens, crystalline - metabolism (151) 151
ophthalmology (145) 145
expression (143) 143
phosphorylation (142) 142
apoptosis (137) 137
molecular chaperone (135) 135
molecular chaperones - metabolism (129) 129
oxidative stress (128) 128
b-crystallin (126) 126
cells, cultured (117) 117
blotting, western (113) 113
heat-shock proteins - metabolism (113) 113
biophysics (111) 111
cattle (111) 111
heat-shock-protein (110) 110
a-crystallin (108) 108
sense organs (108) 108
article (107) 107
crystallin (101) 101
protein folding (99) 99
research article (98) 98
cataract (96) 96
cataract - metabolism (96) 96
alpha-crystallin a chain - genetics (95) 95
αb-crystallin (95) 95
eye diseases (94) 94
middle aged (94) 94
molecular chaperones (93) 93
alpha-crystallin a chain - chemistry (92) 92
alpha b-crystallin (90) 90
disease models, animal (90) 90
chaperone (88) 88
neurosciences (87) 87
adult (85) 85
analysis (85) 85
gene expression (85) 85
molecular chaperones - chemistry (85) 85
α-crystallin (83) 83
crystallins - metabolism (82) 82
immunohistochemistry (81) 81
lens (80) 80
protein conformation (80) 80
time factors (80) 80
aggregation (79) 79
stress (79) 79
protein structure, tertiary (78) 78
aged (77) 77
heat-shock proteins - genetics (73) 73
alpha-crystallins - metabolism (72) 72
temperature (72) 72
models, molecular (71) 71
cataract - genetics (70) 70
reverse transcriptase polymerase chain reaction (70) 70
in-vitro (68) 68
multidisciplinary sciences (68) 68
medicine (67) 67
small heat shock proteins (67) 67
chaperone-like activity (66) 66
alpha-crystallins - chemistry (65) 65
circular dichroism (65) 65
proteomics (65) 65
heat-shock proteins, small - metabolism (64) 64
recombinant proteins - metabolism (64) 64
protein structure, secondary (63) 63
mice, transgenic (62) 62
electrophoresis, polyacrylamide gel (60) 60
protein (60) 60
rna, messenger - metabolism (60) 60
base sequence (59) 59
binding sites (59) 59
cell line (59) 59
protein structure, quaternary (59) 59
science (59) 59
biology (58) 58
recombinant proteins - chemistry (57) 57
cells (56) 56
activation (55) 55
hot temperature (54) 54
more...
Language Language
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 05/2013, Volume 288, Issue 18, pp. 13022 - 13035
Journal Article
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, 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, 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, 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
PLOS ONE, ISSN 1932-6203, 09/2015, Volume 10, Issue 9, pp. e0137659 - e0137659
Journal Article