Lens alpha-crystallin: chaperone-like properties.

No abstract is available for this paper.

• Publication year

  1998

• Venue

  Methods in Enzymology

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/S0076-6879(98)90032-5PMID 9534176
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• THE ISOLATION AND CHARACTERIZATION OF DISTINCT MACROMOLECULAR FRACTIONS

  2005cited by this paper
• Immobilization of the C-terminal Extension of Bovine αA-Crystallin Reduces Chaperone-like Activity*

  1996cited by this paper
• Spatial and temporal activity of the αB‐crystallin/small heat shock protein gene promoter in transgenic mice

  1996cited by this paper
• Supervising the fold: functional principles of molecular chaperones

  1996cited by this paper
• Interaction of alpha-crystallin with spin-labeled peptides.

  1995cited by this paper
• Temperature dependent chaperone‐like activity of alpha‐crystallin

  1995cited by this paper
• The mutation Asp69-->Ser affects the chaperone-like activity of alpha A-crystallin.

  1995cited by this paper
• On the thermal stability of alpha-crystallin: a new insight from infrared spectroscopy.

  1995cited by this paper
• Temperature‐induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α‐crystallin

  1995cited by this paper
• Reduced Chaperone-like Activity of αAins-crystallin, an Alternative Splicing Product Containing a Large Insert Peptide (*)

  1995cited by this paper
• The Mutation Asp69→Ser Affects the Chaperone‐Like Activity of αA‐Crystallin

  1995cited by this paper
• The chaperone activity of bovine alpha crystallin. Interaction with other lens crystallins in native and denatured states.

  1994cited by this paper
• Expression of the α‐Crystallin/Small Heat‐Shock Protein/Molecular Chaperone Genes in the Lens and other Tissues

  1994cited by this paper
• Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology.

  1994cited by this paper
• Hsc70, immunoglobulin heavy chain binding protein, and Hsp90 differ in their ability to stimulate transport of precursor proteins into mammalian microsomes.

  1993cited by this paper
• The C-terminal region of alpha-crystallin: involvement in protection against heat-induced denaturation.

  1993cited by this paper
• Evolution of the alpha-crystallin/small heat-shock protein family.

  1993cited by this paper
• Alpha-crystallin, a molecular chaperone, forms a stable complex with carbonic anhydrase upon heat denaturation.

  1993cited by this paper
• Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones.

  1993cited by this paper
• Expression and aggregation of recombinant alpha A-crystallin and its two domains.

  1992cited by this paper
• Alpha-crystallin can function as a molecular chaperone.

  1992cited by this paper
• Expression and aggregation of recombinant αA-crystallin and its two domains

  1992cited by this paper
• Alpha B-crystallin is a small heat shock protein.

  1991cited by this paper
• GroE facilitates refolding of citrate synthase by suppressing aggregation.

  1991cited by this paper
• Reverse-phase HPLC analysis of human alpha crystallin.

  1991cited by this paper
• alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues.

  1989cited by this paper
• Enzyme/crystallins: gene sharing as an evolutionary strategy.

  1989cited by this paper
• αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissues

  1989cited by this paper
• Isolation of alpha-crystallin subunits by gel filtration.

  1987cited by this paper
• Fast protein liquid chromatography-chromatofocusing of bovine and chicken alpha-crystallin subunits under denaturing conditions.

  1987cited by this paper
• Fast protein liquid chromatography-chromatofocusing of bovine and chicken α-crystallin subunits under denaturing conditions

  1987cited by this paper
• Calf lens alpha-crystallin quaternary structure. A three-layer tetrahedral model.

  1986cited by this paper
• Calf lens ?-crystallin quaternary structure *1A three-layer tetrahedral model

  1986cited by this paper
• Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin.

  1982cited by this paper
• One-step separation of the subunits of alpha-crystallin by chromatofocusing in 6 M urea.

  1981cited by this paper
• One-step separation of the subunits of α-crystallin by chromatofocusing in 6 m urea

  1981cited by this paper
• Intracellular degradation of alpha-crystallin. Fractionation and characterization of degraded alpha A-chains.

  1974cited by this paper
• Intracellular Carboxy-Terminal Degradation of the αA Chain of α-Crystallin

  1974cited by this paper
• Intracellular carboxy-terminal degradation of the alpha A chain of alpha-crystallin.

  1974cited by this paper
• Intracellular Degradation of α-Crystallin

  1974cited by this paper

• Impact of crowding on aggregation of UV-irradiated βL-crystallin and chaperone like activity of α-crystallin depends of the nature of a crowding agent.

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• Lipid and Cholesterol Peroxidation Leads to α-Crystallin Membrane Aggregation and Cataract Formation

  2025cites this paper
• Effect of lens crystallins aggregation on cataract formation.

  2025cites this paper
• Cholesterol and Q147E Deamidation Modulates αA-Crystallin Membrane Binding Elucidating Protective Role of Lens Membrane Composition Changes With Aging

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• Exploring the significance of potassium homeostasis in copper ion binding to human αB-Crystallin.

  2024cites this paper
• Cholesterol Content Regulates the Interaction of αA-, αB-, and α-Crystallin with the Model of Human Lens-Lipid Membranes

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• Single-molecule observations of human small heat shock proteins in complex with aggregation-prone client proteins

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• Modulation of Alpha-Crystallin-Membrane Association by Phospholipid Acyl Chain Length and Degree of Unsaturation

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• The 18th amino acid glycine plays an essential role in maintaining the structural stabilities of γS-crystallin linking with congenital cataract.

  2023cites this paper
• Human γS-Crystallin Mutation F10_Y11delinsLN in the First Greek Key Pair Destabilizes and Impairs Tight Packing Causing Cortical Lamellar Cataract

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• An AFM Approach Applied in a Study of α-Crystallin Membrane Association: New Insights into Lens Hardening and Presbyopia Development

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• Binding of Alpha-Crystallin to Cortical and Nuclear Lens Lipid Membranes Derived from a Single Lens

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• The Effect of Oxidized Dopamine on the Structure and Molecular Chaperone Function of the Small Heat-Shock Proteins, αB-Crystallin and Hsp27

  2021cites this paper
• Cholesterol and cholesterol bilayer domains inhibit binding of Alpha-crystallin to the membranes made of the major phospholipids of eye lens fiber cell plasma membranes.

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• Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation

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• Isomerization of Asp is essential for assembly of amyloid-like fibrils of αA-crystallin-derived peptide

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• βB2 W151R mutant is prone to degradation, aggregation and exposes the hydrophobic side chains in the fourth Greek key motif.

  2020cites this paper
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  2020cites this paper
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• Interaction of alpha-crystallin with four major phospholipids of eye lens membranes.

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• Proteinaceous Transformers: Structural and Functional Variability of Human sHsps

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• Effect of cataract-associated mutations in the N-terminal domain of αB-crystallin (HspB5).

  2020cites this paper
• Structural and Functional Peculiarities of α-Crystallin

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• A single Asp isomer substitution in an αA-crystallin-derived peptide induces a large change in peptide properties.

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  2019cites this paper
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  2019cites this paper
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  2018cites this paper
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