ライフサイエンスコーパス: beta-crystallin

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.

13 The size of the beta-crystallin aggregate correlated with the length of

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

16 which bind to CBP/p300, failed to upregulate beta-crystallin and gamma-crystallin expression.

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

22 n capsular bags and expression of alpha-SMA, beta-crystallin, and ICAM-1.

23 gen (PCNA), alpha-smooth muscle actin (SMA), beta-crystallin, and intercellular adhesion molecule (IC

24 In summary, we showed that alpha and beta crystallins are expressed in the retina predominant

25 Beta-crystallins are major protein constituents of the m

26 The human lens proteins beta-crystallins are subdivided into acidic (betaA1-beta

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

29 When present alone, each beta-crystallin associates into homodimers; however, no

30 Thus, while each purified beta-crystallin associates only into homodimers and unde

31 ction: higher levels of dermatopontin (DPT), beta-crystallin B1 (CRYBB1), interleukin-18-binding prot

32 alphaB-crystallin, aldehyde dehydrogenase 1, betaS-crystallin, betaB2-crystallin, and G3PDH, and UV-a

33 Analysis of the beta-crystallins by high performance liquid chromatograp

34 etaB1-crystallin, a major component of large beta-crystallin complexes (beta-high), with itself and w

35 ularly difficult to characterize because the beta-crystallins comprise several proteins of similar st

36 expression of the schizophrenia-related gene beta crystallin (Crybb1).

37 ue 328 kDa protein in DKO lenses, containing beta-crystallin, demonstrating aggregation of beta-cryst

38 ation occurs within N-terminal extensions of beta-crystallins during lens maturation.

39 f the three most common vertebrate subtypes, beta-crystallins exhibit the widest degree of polydisper

40 sed cell proliferation and uniquely affected beta-crystallin expression.

41 mbined with SB, altered LECs' morphology and beta-crystallin expression.

42 eate the effects of loss of terminal arms on beta-crystallin function, the sensitivity of purified re

43 y markers D22S420 and D22S1163, contains the beta-crystallin gene cluster including the genes CRYBA4,

44 mapped dominant pulverulent cataract to the beta-crystallin gene cluster on chromosome 22q11.2.

45 tor, p300, and recruited a repressor, Sp3 to beta-crystallin gene promoters, to negatively regulate t

46 e region on chromosome 22q that includes two beta crystallin genes (CRYBB2, CRYBB3) and one pseudogen

47 protein quantification showed that alpha and beta crystallin genes were downregulated at both transcr

48 .5, do not express (&agr;)A- and all of the (beta)-crystallin genes, and display inappropriately high

49 f directly activates many if not all of the (beta)-crystallin genes, and suggest a model for coordina

50 tionship between the expression of Pax-6 and beta-crystallin genes within the developing chicken lens

51 the AIM1 gene shows remarkable similarity to beta-crystallin genes, with homologous introns delineati

52 o a region of chromosome 22 containing three beta-crystallin genes.

53 formed by the interactions of the human lens beta-crystallins have been particularly difficult to cha

54 ndicated that the cells expressing alpha and beta crystallins in the GCL are RGCs.

55 allin when complexed with its target protein beta-crystallin in both normal and heavy-water-based sol

56 eta-crystallin, demonstrating aggregation of beta-crystallin in the absence of alpha-crystallins.

57 betaB2 is the most abundant beta-crystallin in the human lens and is important in fo

58 The beta-crystallins included the gene products of betaB2, b

59 tween alpha- and beta-crystallin occurs, and beta-crystallin is located in the fenestrations.

60 nding the solubilities of different forms of beta-crystallins is important to elucidating the mechani

61 betaB2-crystallin, the major component of beta-crystallin, is a dimer at low concentrations but ca

62 ained, were N-terminally acetylated, and all beta-crystallins lacked an initial methionine, except fo

63 ssed higher IgM autoantibodies against alpha beta crystallin, lipopolysaccharide, heat-shock cognate

64 alpha-smooth muscle actin (alpha-SMA) and a beta-crystallin (markers of stellate cell activation) me

65 The long N-terminal extensions of beta-crystallins may influence both homo- and heteromole

66 ur results support that specific isoforms of beta-crystallin modulate polydispersity through multiple

67 tures, a weak interaction between alpha- and beta-crystallin occurs, and beta-crystallin is located i

68 oncentrations of divalent cations dissociate beta-crystallin oligomers, reduce polydispersity, and sh

69 known about the solubilities of the various beta-crystallins or the effects of post-translational mo

70 To investigate this, we first characterized beta-crystallin polydispersity and then established a me

71 oderm results in the formation of Prox-1 and beta-crystallin-positive ectopic lentoid bodies.

72 of the biophysical consequences of a mutant beta-crystallin protein that is associated with human in

73 corner impairs the folding and solubility of beta-crystallin proteins.

74 All beta-crystallins studied demonstrated fast reversible mo

75 h degree of structural complexity within the beta-crystallin subtype and what the role of this featur

76 As the lens ages, beta-crystallins tend to undergo proteolytic cleavage of

77 Loss of beta-crystallin terminal arms appears to increase their

78 ha-crystallin on its own and when mixed with beta-crystallin was 69 +/- 1 A at 35 degrees C and incre

79 ls expression of lens-specific genes such as beta-crystallins, was positively regulated by SUMO1 but

80 ur understanding of the interactions between beta-crystallins, we characterized the association of be

81 smic gamma-crystallin, whereas no changes in beta-crystallin were observed.

82 In this study, the solubilities of beta-crystallins were examined.

83 Other beta-crystallins were present only as hetero-oligomers.