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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 oduced more pentosidine on BLP than did aged 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 erformed using the water soluble fraction of lens proteins.
9  the addition of either a chelating agent or lens proteins.
10 eatment of the buffer, or by the addition of lens proteins.
11 ms mediating the turnover and homeostasis of lens proteins.
12 ines to photooxidize ASC and to form AGEs in lens proteins.
13 ain a macromolecular profile of the abundant lens proteins.
14 lts in proteolysis of crystallins, the major lens proteins.
15 oxygen, possibly initiating the glycation of lens proteins.
16 r affinity purification of interacting human lens proteins.
17 products identical with those of aging human lens proteins.
18 tion and kynurenine-mediated modification of lens proteins.
19 entration of antigen when reacted with human lens proteins.
20 proteins or decrease the levels of insoluble lens proteins.
21 sponding incorporation of radioactivity into lens proteins.
22 rofile of a proteolytic digest of aged human lens proteins.
23 rotein) when compared with aged normal human lens proteins (261 +/- 93 pmol/mg of WISS protein or 23
24 a significant enhancement of K2P in cataract lens proteins (613 +/- 362 pmol/mg of water-insoluble so
25                  alpha-Crystallin, the major lens protein, acts as a molecular chaperone by preventin
26 terol as a key molecule in the prevention of lens protein aggregation and points to a novel strategy
27                               Abeta promoted lens protein aggregation that showed protofibrils, biref
28 Lens Abeta might promote regionally-specific lens protein aggregation, extracerebral amyloid formatio
29  receptors, gamma amino butyric acid and the lens protein alpha B crystallin, have intriguing and dis
30 al role in minimizing the aggregation of the lens protein alphaA-crystallin (CRYAA) during rewarming.
31 family, was determined in the context of the lens protein alphaA-crystallin by systematic application
32  lens-specific transcription factor, and the lens protein, alphaA-crystallin were regulated by BMP re
33 n APH protein levels were >2.6% of the total lens protein and the specific activity, assayed using Ac
34 stress to restore the vital functions of the lens proteins and enzymes.
35 nteresting evolutionary link between the eye lens proteins and the ancestral intermediate filament pr
36 the baking of foods, would occur between the lens proteins and the highly reactive oxidation products
37 romophore from the enzymatic digest of human lens proteins and the identification of its chemical str
38 rly characterize the spatial distribution of lens proteins and their modifications in lens sections.
39 isulfide bonds between cysteinyl residues of lens proteins and thiols such as glutathione and cystein
40 ithine and lysine cyclodeaminases, marsupial lens proteins and, in man, a thyroid hormone-binding pro
41 te for future studies to determine how human lens proteins are altered during aging and cataract form
42                    Human and other mammalian lens proteins are composed of three major crystallins: a
43 of the gamma crystallins, a family of ocular lens proteins, are involved in the aggregation and phase
44                                          Eye lens proteins arose separately and make up a diverse gro
45           UVA irradiation with 2 mg/ml human lens protein as sensitizer oxidized 1 mM ASA after sever
46 s through the large-scale aggregation of eye lens proteins as a result of ageing or congenital mutati
47 graphy/mass spectrometry and were present in lens protein at concentrations of 0.02-0.2 and 0.1-0.8 m
48 th the cataractogenic aggregation of soluble lens proteins at the membrane surface.
49  demonstration of MIP interaction with other lens proteins at the molecular level and raise the possi
50                                              Lens proteins become increasingly cross-linked through n
51 ation of aqueous solutions of the bovine eye lens protein beta(H) crystallin from dilute conditions u
52                                    The human lens proteins beta-crystallins are subdivided into acidi
53 ity in human alphaB crystallin using natural lens proteins, beta(H) crystallin and gammaD crystallin,
54 cetylarginine + N-alpha-acetyllysine, bovine lens proteins (BLP), and lysozyme; the amounts measured
55              The precise mechanisms by which lens proteins both prevent aggregation and maintain lens
56  resulted from an improper folding status of lens proteins caused by Sep15 deficiency.
57 uced light-scattering, measured in vitro for lens proteins, correlated with increasing age and catara
58              The 2-DE proteome maps of mouse lens proteins created in this study, using immobilized p
59  the 330-nm absorbing peaks in an aged human lens protein digest.
60                  Enzyme-digested cataractous lens proteins displayed 3OHKYN-derived modifications.
61 at lenses grown in organ culture showed that lens proteins do not have an increase in methylglyoxal-m
62 ulted in the incorporation of ascorbate into lens proteins during the ensuing 24 hours in the dark.
63                                              Lens protein extract was incubated in vitro with ASA or
64      Anaerobic UVA irradiation of aged human lens proteins for 2 hours with [U-(14)C]ascorbate result
65 gammaD-Crys) is a two-domain, beta-sheet eye lens protein found in the lens nucleus.
66           gammaS-crystallin is a major human lens protein found in the outer region of the eye lens,
67            Young, old, and cataractous human lens protein fractions were glycated with ascorbic acid
68                                              Lens proteins from 10-week old chickens were separated b
69                                              Lens proteins from aged lenses (from donors 65 to 80 yea
70  was investigated in dura mater collagen and lens proteins from dogs that were diabetic for 5 years.
71                                              Lens proteins from mice of increasing age or different s
72 e lens nucleus is critical for protection of lens proteins from the effects of oxidative stress and f
73 perature and pressure on the LLPS of the eye-lens protein gamma-crystallin using UV/vis and IR absorp
74  with proteolytic processing of the abundant lens protein gamma-crystallin, leading to its aggregatio
75                 Here, we investigate the eye-lens protein gammaB-crystallin in the ribosomal exit tun
76                           The structural eye lens protein gammaD-crystallin is a major component of c
77 ractions in the natively monomeric human eye lens protein gammad-crystallin, whose aggregation leads
78 oligomers in delaying the aggregation of the lens protein gammaD-crystallin.
79                                 The fish eye lens protein gammaM7-crystallin (gammaM7) is found in vi
80 tigate the aggregation propensity of the eye-lens protein gammaS-crystallin.
81 selection of the Greek key fold as the major lens protein in all vertebrates.
82 t into the factors essential for maintaining lens proteins in a single homogeneous phase, thereby ena
83 ne fractions and proteoliposomes composed of lens proteins in phosphatidylcholine/sphingomyelin/chole
84 ures) suggest that gene-targeting studies of lens proteins in which the 129 strain was used as a sour
85 hat selectively degrades damaged or abnormal lens proteins, including C-terminally truncated alphaA-c
86 asured the (14)N/(15)N-peptide ratios of 248 lens proteins, including Crystallin, Aquaporin, Collagen
87                          Nontransgenic mouse lens proteins incubated with purified wt-APH in vitro re
88    Our studies indicate that 3OHKYN modifies lens proteins independent of glycation to form products
89 and aggregation studies to investigate Abeta-lens protein interactions.
90 gammaS) is an important human and bovine eye lens protein involved in maintaining the transparency of
91 tallin, originally described as a structural lens protein, is now known to be a member of the small h
92 efractive index, and bis-ANS fluorescence of lens proteins isolated from the alphaA-R49C mouse lenses
93 tion of tryptophan residues represents a new lens protein modification that can explain galectin-3 in
94 nificant biomarker for assessing the role of lens protein modifications during aging and in the patho
95 encoding gamma-B crystallin, a mammalian eye-lens protein, modulate the rates of translation and cotr
96 e modification by glutathiolation can render lens proteins more susceptible to degradation by the ubi
97 he biochemical and biophysical properties of lens proteins needed to maintain transparency, refractio
98                    alpha-Crystallin, a major lens protein of approximately 800 kDa with subunits of a
99                    alpha-crystallin, a major lens protein of approximately 800 kDa with subunits of a
100 , will be useful for comparison with maps of lens proteins of mice with cataracts so that cataract-sp
101    J3-crystallin, one of the three major eye-lens proteins of the cubomedusan jellyfish (Tripedalia c
102 ides in nanostructured granules, we find the lens protein Omega- crystallin interfacing tightly with
103  eye due to light scattering of precipitated lens proteins or aberrant cellular debris.
104 rol failed to increase the levels of soluble lens proteins or decrease the levels of insoluble lens p
105  glycation end products (AGEs) contribute to lens protein pigmentation and cross-linking during aging
106                                 Oxidation of lens proteins plays a central role in the formation of a
107 ns that are associated with the yellowing of lens protein prevented most of the UV-B from reaching th
108      With this method we found that diabetic lens proteins produced more pentosidine on BLP than did
109 the major degradation product bound to human lens proteins provides in vivo evidence for the non-oxid
110 g before ARC presents, we postulate that the lens protein PTMs contribute to a "cataractogenic load"
111 act activity through the increase in soluble lens protein, reduced glutathione, catalase and SOD acti
112              Application of this approach to lens proteins resulted in the largest set of PTMs report
113 , in vitro rat lens studies along with human lens protein solubilization studies were conducted.
114 may exist between beaded filaments and other lens proteins/structures) suggest that gene-targeting st
115  be useful in providing protection for other lens proteins super-aggregating.
116 consensus sequences from the major intrinsic lens protein superfamily; a "touchdown" PCR protocol acc
117 anied by a lack of protein turnover, leaving lens proteins susceptible to a number of damaging modifi
118 es occur at a much higher rate in brunescent lens proteins than in either nuclear cataractous or norm
119 istently stronger reactions with cataractous lens proteins than those from noncataractous lenses, and
120            Human gammaD-crystallin is an eye lens protein that aggregates into amyloid fibrils under
121 ystallin (HgammaD-Crys) is a very stable eye lens protein that must remain soluble and folded through
122       Human betaB1-crystallin is a major eye-lens protein that undergoes in vivo truncation at the N-
123       We used proteomic analysis to identify lens proteins that change in abundance after deletion of
124 ents the aggregation and insolubilization of lens proteins that occur during the process of aging.
125 igh-molecular-weight aggregates of human eye lens proteins that scatter light, causing lens opacity.
126 roteins were identified; including truncated lens proteins that would be difficult to assign to an im
127 major role in maintaining the homeostasis of lens protein thiols thus protecting against oxidative st
128 i-cataractogenic activity or bind aggregated lens protein to dissolve cataracts.
129                          During aging, human lens proteins undergo several post-translational modific
130 of intact betaB1-crystallin protein to total lens protein was significantly reduced.
131             Furthermore, the total amount of lens proteins was 60% less than normal in the Pax6 trans
132   The abundance of endogenous and transgenic lens proteins was estimated by quantitative Western blot
133 n-Trp) fluorescence of porcine and human eye lens proteins was identified by Mass Spectrometry (MS) a
134 VA irradiation in the presence of aged human lens proteins, was measured in the absence of oxygen by
135                       Brunescent cataractous lens proteins were digested by enzymes, the digest was s
136      Pentosidine concentrations in serum and lens proteins were much lower than argpyrimidine concent
137                                Water-soluble lens proteins were separated by 2-DE and identified by t
138                                              Lens proteins, which do not turn over, provide a useful
139 ent incorporation of [U-(14)C]ascorbate into lens proteins with a water-insoluble (WI) fraction in vi

 
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