Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Gene Ontology annotation through association of InterPro records with GO terms
A conserved role of αA-crystallin in the development of the zebrafish embryonic lens.
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Morpholino knockdown of the three alpha-crystallins produced lens abnormalities.
"we have carried out morpholino-mediated knockdown of"
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A maternal/zygotic alphaA-crystallin knockout line shows a more consistent and severe lens phenotype.
"A more consistent and severe lens phenotype was evident in maternal/zygotic"
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The role of alpha-crystallins in lens development is conserved from mammals to zebrafish.
"These findings demonstrate that the role of"
Functional validation of hydrophobic adaptation to physiological temperature in the small heat shock protein αA-crystallin.
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Chaperone-like activity was assayed as prevention of chemically induced aggregation of insulin and lactalbumin.
"ability to prevent the chemically induced aggregation of insulin and/or lactalbumin"
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Altering hydrophobicity of specific zebrafish residues changed chaperone-like activity and thermal stability.
"Altering hydrophobicity of specific zebrafish"
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Small heat shock proteins prevent stress- and disease-induced protein aggregation.
"Small heat shock proteins (sHsps) maintain cellular homeostasis by preventing stress and disease-induced protein aggregation"
Zebrafish alpha-crystallins: protein structure and chaperone-like activity compared to their mammalian orthologs.
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Chaperone-like activity was measured as prevention of chemically induced aggregation between 25 and 40 degrees C.
"The chaperone-like activities of zebrafish and human alpha-crystallins were compared by assaying their ability to prevent the chemically induced aggregation of several target proteins at temperatures between 25 degrees C and 40 degrees C"
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Zebrafish alphaA-crystallin is far more active than zebrafish alphaB-crystallin.
"The chaperone-like activities of the two zebrafish alpha-crystallins were highly divergent, with alphaA-crystallin showing much greater activity than alphaB-crystallin"
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alphaA-crystallin is a lens-specific chaperone-like molecule in both zebrafish and mammals.
"alphaA-crystallin serves a similar physiological function in both zebrafish and mammals as a lens specific chaperone-like molecule"
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Zebrafish crystallins denature at lower temperatures than mammalian ones.
"The denaturation temperatures of zebrafish crystallins were lower than those of mammals."
AlphaA-crystallin expression prevents gamma-crystallin insolubility and cataract formation in the zebrafish cloche mutant lens.
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AlphaA-crystallin is a chaperone that protects proteins from misfolding and insolubility.
"AlphaA-crystallin is a chaperone that protects proteins from misfolding and becoming insoluble"
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Overexpression rescued the cloche lens phenotype, solubilizing gamma-crystallin and restoring transparency and fibre-cell differentiation.
"Overexpression of exogenous alphaA-crystallin rescued the cloche lens phenotype, including solubilization of gamma-crystallin, increased lens transparency and induction of lens fiber cell differentiation"
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AlphaA-crystallin expression is required for normal lens development.
"these results indicate that alphaA-crystallin expression is required for normal lens development"
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Crystallins are the major structural proteins of the zebrafish lens.
"Crystallins are the major structural proteins in mouse, human and zebrafish lens"
Sequence and spatial expression of zebrafish (Danio rerio) alphaA-crystallin.
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High lens expression and very low expression in liver and spleen.
"We detected high expression of zebrafish alphaA-crystallin in the lens and very low expression in liver and spleen"
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Zebrafish alphaA-crystallin has a physiologically limited role outside the lens.
"These data suggest that zebrafish alphaA-crystallin plays a physiologically limited role outside of the zebrafish lens, similar to its mammalian orthologues"
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Residues important for chaperone function are largely shared with mammalian alphaA-crystallin.
"Few amino acids identified as being functionally important to chaperone function differ between zebrafish and mammalian alphaA-crystallin"
UniProtKB entry Q8UUZ6 for Danio rerio cryaa
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Cytoplasmic and nuclear localization (rule-based).
"SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus"
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Member of the small heat shock protein (HSP20) family.
"Belongs to the small heat shock protein (HSP20) family."
Falcon deep research report on zebrafish cryaa (alpha-A crystallin)
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No direct experimental evidence exists for the subcellular localization of zebrafish Cryaa, including nuclear association; the zebrafish evidence is cell-type, not compartment, resolved.
"I did **not** find direct experimental evidence specifying Cryaa’s **subcellular localization** (e.g., cytosolic vs membrane‑bound fractions, nuclear association) in zebrafish lens cells"