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Neuron, ISSN 0896-6273, 03/2012, Volume 73, Issue 5, pp. 951 - 961
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 04/2014, Volume 9, Issue 4, pp. e95768 - e95768
Autosomal dominant congenital stationary night blindness (adCSNB) is caused by mutations in three genes of the rod phototransduction cascade, rhodopsin (RHO),... 
MOLECULAR-MECHANISM | RHODOPSIN GENE | HETEROZYGOUS MISSENSE MUTATION | CGMP-PHOSPHODIESTERASE | ALPHA-SUBUNIT | MULTIDISCIPLINARY SCIENCES | RECESSIVE RETINITIS-PIGMENTOSA | GAF-A DOMAIN | CATALYTIC SUBUNITS | CYCLIC-GMP PHOSPHODIESTERASE | OUTER SEGMENTS | Night Blindness - metabolism | Humans | Night Blindness - etiology | Heterotrimeric GTP-Binding Proteins - metabolism | Cyclic Nucleotide Phosphodiesterases, Type 6 - genetics | Light Signal Transduction - genetics | Genetic Diseases, X-Linked - etiology | Heterotrimeric GTP-Binding Proteins - genetics | Myopia - metabolism | Genetic Diseases, X-Linked - genetics | Light Signal Transduction - physiology | Night Blindness - genetics | Cyclic Nucleotide Phosphodiesterases, Type 6 - metabolism | Animals, Genetically Modified | Xenopus laevis | Catalytic Domain - genetics | Genetic Diseases, X-Linked - metabolism | Myopia - etiology | Catalytic Domain - physiology | Eye Diseases, Hereditary - genetics | Myopia - genetics | Animals | Eye Diseases, Hereditary - etiology | Mutation | Eye Diseases, Hereditary - metabolism | Neurosciences | Night | Genomics | Genes | Transgenic | Transducin | Retina | Activation | Rods | Nyctalopia | Substitutes | Rodents | Cyclic GMP | Physiology | Catalysis | Deoxyribonucleic acid--DNA | Phosphodiesterase | Tyrosine | Enzymes | Rhodopsin | Congenital diseases | Desensitization | Biophysics | Phototransduction | Plasmids | Pedigree | Blindness | Photoreceptors | Genetic testing | Stationary night blindness | Catalytic subunits | Index Medicus | Deoxyribonucleic acid | DNA
Journal Article
Plant Cell, ISSN 1040-4651, 04/2011, Volume 23, Issue 4, pp. 1449 - 1467
The GENOMES UNCOUPLED4 (GUN4) protein stimulates chlorophyll biosynthesis by activating Mg-chelatase, the enzyme that commits protoporphyrin IX to chlorophyll... 
MONOMETHYL ESTER CYCLASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MAGNESIUM CHELATASE | TETRAPYRROLE BIOSYNTHESIS | NUCLEAR GENE-EXPRESSION | PLANT SCIENCES | CELL BIOLOGY | H-SUBUNIT | THYLAKOID MEMBRANES | STRESS RESPONSES | PROTOPORPHYRIN-IX | SINGLET OXYGEN | CHLOROPLAST BIOGENESIS | Arabidopsis - enzymology | Suppression, Genetic - drug effects | Reactive Oxygen Species - pharmacology | Protoporphyrins - pharmacology | Intracellular Signaling Peptides and Proteins - metabolism | Porphyrins - metabolism | Lyases - metabolism | Protein Subunits - metabolism | Arabidopsis Proteins - metabolism | Suppression, Genetic - radiation effects | Arabidopsis - radiation effects | Light | Plants, Genetically Modified | Protein Binding - drug effects | Chloroplasts - radiation effects | Protein Binding - radiation effects | Intracellular Membranes - radiation effects | Chloroplasts - drug effects | Arabidopsis Proteins - genetics | Gene Expression Regulation, Plant - radiation effects | Arabidopsis - drug effects | Photoperiod | Mutation - genetics | Chloroplasts - metabolism | Arabidopsis - genetics | Gene Expression Regulation, Plant - drug effects | Genes, Plant - genetics | Alleles | Intracellular Membranes - drug effects | Intracellular Membranes - metabolism | Chlorophyll - biosynthesis | Arabidopsis thaliana | Chlorophyll | Plant physiology | Plant genetics | Physiological aspects | Genetic aspects | Biosynthesis | Research | Porphyrins | Index Medicus | s
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 04/2005, Volume 280, Issue 15, pp. 14485 - 14491
The small heat shock protein, alpha-crystallin, plays a key role in maintaining lens transparency by chaperoning structurally compromised proteins. This is of... 
HEAT-SHOCK PROTEINS | HUMAN LENS CRYSTALLINS | AGE-RELATED-CHANGES | B-CRYSTALLIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | C-TERMINAL REGION | LIGHT-SCATTERING | CALPAIN LP82 | BOVINE LENS | EYE LENS | POSTTRANSLATIONAL MODIFICATION
Journal Article
Journal Article