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1 xpression of the lens differentiation marker beta-crystallin.
2 nd EGF increased the expression of alpha and beta crystallins.
3 ng potential interactions between alpha- and beta-crystallins.
4 rin, c-Maf, Prox1, and alphaA-, alphaB-, and beta-crystallins.
5 he monomer-monomer interface conserved among beta-crystallins.
6 tallin to prevent thermal destabilization of beta-crystallins.
7 ferences in the relative solubilities of the beta-crystallins.
8 ber cell-specific proteins including MIP and beta-crystallins.
9 ion of higher molecular weight aggregates of beta-crystallins.
10 nsed nuclei, and express fiber-cell-specific beta-crystallins.
11 d Akt phosphorylation, and the expression of beta-crystallins.
12 including Prox1, p57(KIP2), aquaporin 0 and beta-crystallins.
14 he principal differences among the different beta-crystallin aggregates was the presence of betaA4 in
15 gation, the components of the three sizes of beta-crystallin aggregates, beta1 (approximately 150,000
17 ggest that partial degradation of alpha- and beta-crystallins and increased acidity of gamma-crystall
18 monstrate a decreased solubility of specific beta-crystallins and post-translational modifications th
19 nd unambiguous identification of the various beta-crystallins and their modified forms by mass spectr
20 including manganese-SOD, alphaA crystallin, beta crystallin, and four proteins were downregulated, i
21 cell counting, the expression of alpha-SMA, beta-crystallin, and ICAM-1 by Western blot and immunocy
23 gen (PCNA), alpha-smooth muscle actin (SMA), beta-crystallin, and intercellular adhesion molecule (IC
27 As major constituents of the mammalian lens, beta-crystallins associate into dimers, tetramers, and h
28 a K d of 1.1 muM, indicating that these two beta-crystallins associate predominantly into heterotetr
31 alphaB-crystallin, aldehyde dehydrogenase 1, betaS-crystallin, betaB2-crystallin, and G3PDH, and UV-a
33 etaB1-crystallin, a major component of large beta-crystallin complexes (beta-high), with itself and w
34 ularly difficult to characterize because the beta-crystallins comprise several proteins of similar st
36 ue 328 kDa protein in DKO lenses, containing beta-crystallin, demonstrating aggregation of beta-cryst
40 eate the effects of loss of terminal arms on beta-crystallin function, the sensitivity of purified re
41 y markers D22S420 and D22S1163, contains the beta-crystallin gene cluster including the genes CRYBA4,
43 tor, p300, and recruited a repressor, Sp3 to beta-crystallin gene promoters, to negatively regulate t
44 e region on chromosome 22q that includes two beta crystallin genes (CRYBB2, CRYBB3) and one pseudogen
45 protein quantification showed that alpha and beta crystallin genes were downregulated at both transcr
46 .5, do not express (&agr;)A- and all of the (beta)-crystallin genes, and display inappropriately high
47 f directly activates many if not all of the (beta)-crystallin genes, and suggest a model for coordina
48 tionship between the expression of Pax-6 and beta-crystallin genes within the developing chicken lens
49 the AIM1 gene shows remarkable similarity to beta-crystallin genes, with homologous introns delineati
51 formed by the interactions of the human lens beta-crystallins have been particularly difficult to cha
53 allin when complexed with its target protein beta-crystallin in both normal and heavy-water-based sol
54 eta-crystallin, demonstrating aggregation of beta-crystallin in the absence of alpha-crystallins.
58 nding the solubilities of different forms of beta-crystallins is important to elucidating the mechani
59 betaB2-crystallin, the major component of beta-crystallin, is a dimer at low concentrations but ca
60 ained, were N-terminally acetylated, and all beta-crystallins lacked an initial methionine, except fo
61 ssed higher IgM autoantibodies against alpha beta crystallin, lipopolysaccharide, heat-shock cognate
62 alpha-smooth muscle actin (alpha-SMA) and a beta-crystallin (markers of stellate cell activation) me
64 tures, a weak interaction between alpha- and beta-crystallin occurs, and beta-crystallin is located i
65 known about the solubilities of the various beta-crystallins or the effects of post-translational mo
67 of the biophysical consequences of a mutant beta-crystallin protein that is associated with human in
72 ha-crystallin on its own and when mixed with beta-crystallin was 69 +/- 1 A at 35 degrees C and incre
73 ls expression of lens-specific genes such as beta-crystallins, was positively regulated by SUMO1 but
74 ur understanding of the interactions between beta-crystallins, we characterized the association of be
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