ライフサイエンスコーパス: lens protein

1 of GR (6.32 +/- 0.22 vs. 0.39 +/- 0.01 mU/mg lens protein).

2 dentify a novel, highly abundant and soluble lens protein.

3 und alphaB-crystallin, an abundant cytosolic lens protein.

4 erformed using the water soluble fraction of lens proteins.

5 em as major Maillard reaction cross-links in lens proteins.

6 ured methylglyoxal-derived products in human lens proteins.

7 o protect against nonspecific aggregation of lens proteins.

8 the addition of either a chelating agent or lens proteins.

9 eatment of the buffer, or by the addition of lens proteins.

10 ain a macromolecular profile of the abundant lens proteins.

11 lts in proteolysis of crystallins, the major lens proteins.

12 oxygen, possibly initiating the glycation of lens proteins.

13 r affinity purification of interacting human lens proteins.

14 products identical with those of aging human lens proteins.

15 tion and kynurenine-mediated modification of lens proteins.

16 entration of antigen when reacted with human lens proteins.

17 sponding incorporation of radioactivity into lens proteins.

18 ines to photooxidize ASC and to form AGEs in lens proteins.

19 rofile of a proteolytic digest of aged human lens proteins.

20 oduced more pentosidine on BLP than did aged lens proteins.

21 rotein) when compared with aged normal human lens proteins (261 +/- 93 pmol/mg of WISS protein or 23

22 a significant enhancement of K2P in cataract lens proteins (613 +/- 362 pmol/mg of water-insoluble so

23 alpha-Crystallin, the major lens protein, acts as a molecular chaperone by preventin

24 terol as a key molecule in the prevention of lens protein aggregation and points to a novel strategy

25 Abeta promoted lens protein aggregation that showed protofibrils, biref

26 Lens Abeta might promote regionally-specific lens protein aggregation, extracerebral amyloid formatio

27 receptors, gamma amino butyric acid and the lens protein alpha B crystallin, have intriguing and dis

28 family, was determined in the context of the lens protein alphaA-crystallin by systematic application

29 lens-specific transcription factor, and the lens protein, alphaA-crystallin were regulated by BMP re

30 n APH protein levels were >2.6% of the total lens protein and the specific activity, assayed using Ac

31 stress to restore the vital functions of the lens proteins and enzymes.

32 nteresting evolutionary link between the eye lens proteins and the ancestral intermediate filament pr

33 the baking of foods, would occur between the lens proteins and the highly reactive oxidation products

34 romophore from the enzymatic digest of human lens proteins and the identification of its chemical str

35 rly characterize the spatial distribution of lens proteins and their modifications in lens sections.

36 isulfide bonds between cysteinyl residues of lens proteins and thiols such as glutathione and cystein

37 ithine and lysine cyclodeaminases, marsupial lens proteins and, in man, a thyroid hormone-binding pro

38 te for future studies to determine how human lens proteins are altered during aging and cataract form

39 Human and other mammalian lens proteins are composed of three major crystallins: a

40 of the gamma crystallins, a family of ocular lens proteins, are involved in the aggregation and phase

41 Eye lens proteins arose separately and make up a diverse gro

42 UVA irradiation with 2 mg/ml human lens protein as sensitizer oxidized 1 mM ASA after sever

43 s through the large-scale aggregation of eye lens proteins as a result of ageing or congenital mutati

44 graphy/mass spectrometry and were present in lens protein at concentrations of 0.02-0.2 and 0.1-0.8 m

45 th the cataractogenic aggregation of soluble lens proteins at the membrane surface.

46 demonstration of MIP interaction with other lens proteins at the molecular level and raise the possi

47 The human lens proteins beta-crystallins are subdivided into acidi

48 ity in human alphaB crystallin using natural lens proteins, beta(H) crystallin and gammaD crystallin,

49 cetylarginine + N-alpha-acetyllysine, bovine lens proteins (BLP), and lysozyme; the amounts measured

50 The precise mechanisms by which lens proteins both prevent aggregation and maintain lens

51 resulted from an improper folding status of lens proteins caused by Sep15 deficiency.

52 uced light-scattering, measured in vitro for lens proteins, correlated with increasing age and catara

53 The 2-DE proteome maps of mouse lens proteins created in this study, using immobilized p

54 the 330-nm absorbing peaks in an aged human lens protein digest.

55 Enzyme-digested cataractous lens proteins displayed 3OHKYN-derived modifications.

56 at lenses grown in organ culture showed that lens proteins do not have an increase in methylglyoxal-m

57 ulted in the incorporation of ascorbate into lens proteins during the ensuing 24 hours in the dark.

58 Lens protein extract was incubated in vitro with ASA or

59 Anaerobic UVA irradiation of aged human lens proteins for 2 hours with [U-(14)C]ascorbate result

60 gammaD-Crys) is a two-domain, beta-sheet eye lens protein found in the lens nucleus.

61 gammaS-crystallin is a major human lens protein found in the outer region of the eye lens,

62 Young, old, and cataractous human lens protein fractions were glycated with ascorbic acid

63 Lens proteins from 10-week old chickens were separated b

64 Lens proteins from aged lenses (from donors 65 to 80 yea

65 was investigated in dura mater collagen and lens proteins from dogs that were diabetic for 5 years.

66 Lens proteins from mice of increasing age or different s

67 e lens nucleus is critical for protection of lens proteins from the effects of oxidative stress and f

68 with proteolytic processing of the abundant lens protein gamma-crystallin, leading to its aggregatio

69 The structural eye lens protein gammaD-crystallin is a major component of c

70 ractions in the natively monomeric human eye lens protein gammad-crystallin, whose aggregation leads

71 tigate the aggregation propensity of the eye-lens protein gammaS-crystallin.

72 selection of the Greek key fold as the major lens protein in all vertebrates.

73 t into the factors essential for maintaining lens proteins in a single homogeneous phase, thereby ena

74 ne fractions and proteoliposomes composed of lens proteins in phosphatidylcholine/sphingomyelin/chole

75 ures) suggest that gene-targeting studies of lens proteins in which the 129 strain was used as a sour

76 hat selectively degrades damaged or abnormal lens proteins, including C-terminally truncated alphaA-c

77 Nontransgenic mouse lens proteins incubated with purified wt-APH in vitro re

78 Our studies indicate that 3OHKYN modifies lens proteins independent of glycation to form products

79 and aggregation studies to investigate Abeta-lens protein interactions.

80 gammaS) is an important human and bovine eye lens protein involved in maintaining the transparency of

81 tallin, originally described as a structural lens protein, is now known to be a member of the small h

82 efractive index, and bis-ANS fluorescence of lens proteins isolated from the alphaA-R49C mouse lenses

83 tion of tryptophan residues represents a new lens protein modification that can explain galectin-3 in

84 nificant biomarker for assessing the role of lens protein modifications during aging and in the patho

85 encoding gamma-B crystallin, a mammalian eye-lens protein, modulate the rates of translation and cotr

86 e modification by glutathiolation can render lens proteins more susceptible to degradation by the ubi

87 alpha-crystallin, a major lens protein of approximately 800 kDa with subunits of a

88 alpha-Crystallin, a major lens protein of approximately 800 kDa with subunits of a

89 , will be useful for comparison with maps of lens proteins of mice with cataracts so that cataract-sp

90 J3-crystallin, one of the three major eye-lens proteins of the cubomedusan jellyfish (Tripedalia c

91 eye due to light scattering of precipitated lens proteins or aberrant cellular debris.

92 glycation end products (AGEs) contribute to lens protein pigmentation and cross-linking during aging

93 Oxidation of lens proteins plays a central role in the formation of a

94 ns that are associated with the yellowing of lens protein prevented most of the UV-B from reaching th

95 With this method we found that diabetic lens proteins produced more pentosidine on BLP than did

96 the major degradation product bound to human lens proteins provides in vivo evidence for the non-oxid

97 act activity through the increase in soluble lens protein, reduced glutathione, catalase and SOD acti

98 Application of this approach to lens proteins resulted in the largest set of PTMs report

99 may exist between beaded filaments and other lens proteins/structures) suggest that gene-targeting st

100 be useful in providing protection for other lens proteins super-aggregating.

101 consensus sequences from the major intrinsic lens protein superfamily; a "touchdown" PCR protocol acc

102 es occur at a much higher rate in brunescent lens proteins than in either nuclear cataractous or norm

103 istently stronger reactions with cataractous lens proteins than those from noncataractous lenses, and

104 Human gammaD-crystallin is an eye lens protein that aggregates into amyloid fibrils under

105 ystallin (HgammaD-Crys) is a very stable eye lens protein that must remain soluble and folded through

106 Human betaB1-crystallin is a major eye-lens protein that undergoes in vivo truncation at the N-

107 We used proteomic analysis to identify lens proteins that change in abundance after deletion of

108 ents the aggregation and insolubilization of lens proteins that occur during the process of aging.

109 roteins were identified; including truncated lens proteins that would be difficult to assign to an im

110 major role in maintaining the homeostasis of lens protein thiols thus protecting against oxidative st

111 During aging, human lens proteins undergo several post-translational modific

112 of intact betaB1-crystallin protein to total lens protein was significantly reduced.

113 Furthermore, the total amount of lens proteins was 60% less than normal in the Pax6 trans

114 The abundance of endogenous and transgenic lens proteins was estimated by quantitative Western blot

115 n-Trp) fluorescence of porcine and human eye lens proteins was identified by Mass Spectrometry (MS) a

116 VA irradiation in the presence of aged human lens proteins, was measured in the absence of oxygen by

117 Brunescent cataractous lens proteins were digested by enzymes, the digest was s

118 Pentosidine concentrations in serum and lens proteins were much lower than argpyrimidine concent

119 Water-soluble lens proteins were separated by 2-DE and identified by t

120 Lens proteins, which do not turn over, provide a useful

121 ent incorporation of [U-(14)C]ascorbate into lens proteins with a water-insoluble (WI) fraction in vi