Studies of the Denaturation Patterns of Bovine Alpha-Crystallin Using an Ionic Denaturant, Guanidine Hydrochloride and a Non-Ionic Denaturant, Urea

This publication has 39 references indexed in Scilit:

• The small heat-shock protein, αb-crystallin, has a variable quaternary structure
  Journal of Molecular Biology, 1998
• Analysis of the Factors Involved in the Loss and Restoration of the Chaperone-like Function of α-Crystallin
  Biochemical and Biophysical Research Communications, 1997
• Evolution of a protein superfamily: Relationships between vertebrate lens crystallins and microorganism dormancy proteins
  Journal of Molecular Evolution, 1990
• αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissues
  Biochemical and Biophysical Research Communications, 1989
• Specific dissociation of αB subunits from α-crystallin
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
• Calf lens α-crystallin quaternary structure
  Journal of Molecular Biology, 1986
• Steric Exclusion Liquid Chromatography Studies in Urea on the Denaturation of the Bovine Eye Lens Protein α-Crystallin
  Journal of Liquid Chromatography, 1986
• A Model for the Architecture of α-Crystallin
  Ophthalmic Research, 1979
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970
• Effect of Light Scattering on Ultraviolet Difference Spectra¹
  Journal of the American Chemical Society, 1960