Formation of βA3/βB2-crystallin mixed complexes: involvement of N- and C-terminal extensions

[1]  P. Wingfield,et al.  Association properties of betaB2- and betaA3-crystallin: ability to form dimers. , 1997, Protein engineering.

[2]  D. Moss,et al.  X-ray diffraction and structure of crystallins , 1997, Progress in Retinal and Eye Research.

[3]  W. D. de Jong,et al.  The elusive role of the N-terminal extension of beta A3- and beta A1-crystallin. , 1996, Protein engineering.

[4]  R. Glockshuber,et al.  Dimerization of βB2‐crystallin: The role of the linker peptide and the N‐ and C‐terminal extensions , 1994, Protein science : a publication of the Protein Society.

[5]  J. Carver,et al.  A 1H NMR Spectroscopic Comparison of γs- and γB-crystallins , 1994 .

[6]  C. Slingsby,et al.  Formation and crystallization of the eye lens heterodimer beta B2-beta B3-crystallin. , 1994, Experimental eye research.

[7]  Hao‐Chia Chen,et al.  βA3/Al-crystallin association: role of the N-terminal arm , 1994 .

[8]  J. Carver,et al.  1H‐NMR spectroscopy of βB2‐crystallin from bovine eye lens , 1993 .

[9]  J. Carver,et al.  1H‐NMR spectroscopy of bovine lens β‐crystallin , 1993 .

[10]  M. Morris,et al.  Determination of the parameters of self-association by direct fitting of the omega function. , 1985, Biophysical chemistry.

[11]  W. Quax,et al.  beta s‐Crystallin: structure and evolution of a distinct member of the beta gamma‐superfamily. , 1985, The EMBO journal.

[12]  W. D. de Jong,et al.  Aggregation behavior of the bovine beta-crystallin Bp chain studied by limited proteolysis. , 1983, Biochimica et biophysica acta.

[13]  M. M. Bradford.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[14]  B. Milthorpe,et al.  The direct analysis of sedimentation equilibrium results obtained with polymerizing systems. , 1975, Biophysical chemistry.

[15]  H. Aarts,et al.  The evolution of lenticular proteins: the β- and γ-crystallin super gene family , 1988 .

[16]  C. A. Schwartz,et al.  Purification of a heat-stable beta-crystallin polypeptide of the bovine lens. , 1981, Current eye research.