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1 noid-binding protein (IRBP), human IRBP, and alpha A-crystallin).
2 to degradation was comparable to that of wt alpha A-crystallin.
3 d with mutation of Arg-116 to Cys (R116C) in alpha A-crystallin.
4 milar to those of the equivalent sequence in alpha A-crystallin.
5 H, mouse 1.8-kb IRBP, human 1.3-kb IRBP, and alpha A-crystallin.
6 hway (UPP) in degrading C-terminal truncated alpha A-crystallins.
7 re used to characterize the wt and truncated alpha A-crystallins.
9 corresponding to a minor component of rodent alpha A-crystallin, alpha Ains-crystallin, had decreased
11 e prepared a tryptophan-free mutant of human alpha A-crystallin and assessed the conformation of ther
13 uence-specific structural similarity between alpha A-crystallin and HSP 27 and the first identificati
15 ticular, the structure of rhodanese bound to alpha A-crystallin appears to be considerably more nativ
17 e molecular basis of cataract formation, rat alpha A-crystallin cDNA was cloned into pET-23d(+), and
18 lpha B-crystallin precedes the expression of alpha A-crystallin during murine ocular development.
19 deamidated forms of each tryptic fragment of alpha-A crystallin from the fetal-embryonic region of le
21 e to the generation of a highly oligomerized alpha A-crystallin having a modified structure and decre
23 data demonstrate that C-terminal cleavage of alpha A-crystallin not only alters its conformation and
27 s and FGF receptors in lens development, the alpha A-crystallin promoter was used to target expressio
28 uman PDGF-A in the lens under the control of alpha A-crystallin promoter were generated by pronuclear
31 ut fails to bind to a point mutation in the (alpha)A-crystallin promoter that has been shown previous
33 ere expressed in E. coli and the recombinant alpha A-crystallins purified by Sephacryl size-exclusion
34 llins revealed that C-terminal truncation of alpha A-crystallin resulted in only subtle changes in se
35 opic analyses of wt and C-terminal truncated alpha A-crystallins revealed that C-terminal truncation
36 crystallin was much more susceptible than wt alpha A-crystallin to degradation in both lens fiber and
37 During subsequent development of the lens, alpha A crystallin transcripts are most abundant in the
41 tides, corresponding to tryptic fragments of alpha-A crystallin, were synthesized with either the exp
42 ic promoter of delta-crystallin enhancer and alpha A-crystallin, which is active at embryonic day 12.
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