ライフサイエンスコーパス: alpha-crystallin

1 ll heat shock protein (HSP) homolog of human alpha-crystallin.

2 e understanding of the chaperone function of alpha-crystallin.

3 ozyme (T4L) and the small heat shock protein alpha-crystallin.

4 ymmetric pattern of contacts between T4L and alpha-crystallin.

5 3-crystallin peptides and in the presence of alpha-crystallin.

6 motif upstream of the hypoxic response gene alpha-crystallin.

7 ondary and tertiary structure of MG-modified alpha-crystallin.

8 (CLA) and subunit exchange of membrane bound alpha-crystallin.

9 brane binding capacity as compared to native alpha-crystallin.

10 gressive increase in membrane association of alpha-crystallin.

11 perone function showing the robust nature of alpha-crystallin.

12 tually exclusive sites for these proteins in alpha-crystallin.

13 ole determinant of the chaperone function of alpha-crystallin.

14 ified alpha-crystallin or ascorbate-modified alpha-crystallin.

15 from lens extracts as one multimeric entity, alpha-crystallin.

16 ndance O-GlcNAc-modified peptide from bovine alpha-crystallin.

17 ase dramatically alters its interaction with alpha-crystallin.

18 tallin substrate species recognized by human alpha-crystallin.

19 had no effect on chaperone-like activity of alpha-crystallin.

20 the background of wild-type endogenous mouse alpha-crystallins.

21 wo-mode nature of the binding process by the alpha-crystallins.

22 nt, similar to the exchange reactions of the alpha-crystallins.

23 egation of beta-crystallin in the absence of alpha-crystallins.

24 he major lenticular structural proteins, the alpha-crystallins.

25 pproach to treating cataracts by stabilizing alpha-crystallins.

26 r cells marked by the expression of PAX6 and alpha-crystallins.

27 ryptic fragment and intact protein of bovine alpha-crystallin A chain to localize the single site of

28 h phosphorylated and unphosphorylated bovine alpha-crystallin A chain whole protein ions were subject

29 A tryptic digest of the bovine alpha-crystallin A chain yielded a phosphopeptide contai

30 Alpha-crystallin, a large lenticular protein complex mad

31 alpha-Crystallin, a major lens protein of approximately

32 Alpha-crystallin, a molecular chaperone and lens structu

33 Alpha-crystallin, a ubiquitous molecular chaperone, is f

34 In contrast to wild-type, modified alpha-crystallins accumulated in HLE B3 cells.

35 ded acr1, which encodes the virulence factor alpha-crystallin (Acr) 1, a protein that has been report

36 acterium tuberculosis has two members of the alpha-crystallin (Acr) family of molecular chaperones.

37 The M. tuberculosis alpha-crystallin (acr) gene is powerfully and rapidly in

38 mRNA synthesis increased for alpha-crystallin (acr), rv2626c, and rv2623 and decrease

39 The overall results suggest that alpha-crystallin acts to stabilize denaturing proteins s

40 tion, the formation of high molecular weight alpha-crystallin aggregates, and the progressive increas

41 Addition of exogenous alpha-crystallin (alphaA+ alphaB) was ineffective in pre

42 The chaperone proteins, alpha-crystallins, also possess antiapoptotic properties

43 or the formation of a stable complex between alpha-crystallin and betaB2-crystallin as a consequence

44 The binding interaction between alpha-crystallin and GRIFIN is enhanced up to 5-fold in

45 roduct can enhance the chaperone function of alpha-crystallin and Hsp27 and suggest that such modific

46 ecular weight complexes (HMWCs) comprised of alpha-crystallin and other lens crystallins accumulate.

47 ate the mechanism of the interaction between alpha-crystallin and substrate proteins, we determined t

48 family of small heat-shock proteins (sHsp) (alpha-crystallin and Synechocystis HSP17) have stabilizi

49 ure of the intermediate states recognized by alpha-crystallin and the conformations that are stably b

50 Molecular images of the two subunits of alpha-crystallin and their modifications over approximat

51 tterns were observed for the two subunits of alpha-crystallin and their modified forms.

52 the conformation-sensitive amide I bands of alpha-crystallin and unlabeled substrate proteins.

53 ed enzymes are no longer associated with the alpha-crystallin, and ATP is required for re-activation.

54 lphaB-crystallin, human HSP27, bovine native alpha-crystallin, and the complex of alphaB-crystallin a

55 Such truncated alpha-crystallins appear to contribute to an increased l

56 in HGD-alpha mixtures, as the proportion of alpha-crystallin approaches that in the lens nucleus.

57 hat heat-destabilized conformers captured by alpha-crystallin are characterized by a high proportion

58 In the absence of ATP, sHSPs such as alpha-crystallin are more efficient than HSP70 in preven

59 g overexpressed, the molecular properties of alpha-crystallins are disrupted by diabetes and contribu

60 The small heat shock proteins (sHSPs) and alpha-crystallins are highly effective, ATP-independent

61 alpha-Crystallins are small heat shock proteins that reg

62 heat shock proteins (sHSPs) and the related alpha-crystallins are ubiquitous chaperones linked to ne

63 sHsps) and the structurally related eye lens alpha-crystallins are ubiquitous stress proteins that ex

64 ediates may be related to the functioning of alpha-crystallins as chaperone-like molecules.

65 s the most monodisperse, while HSP27 and the alpha-crystallin assemblies are more polydisperse.

66 P-induced structural changes of native human alpha-crystallin assemblies were determined by hydrogen-

67 Asymmetric reconstructions for the alpha-crystallin assemblies, with an additional mass sel

68 l symmetry for HSP16.5 than for HSP27 or the alpha-crystallin assemblies.

69 can be interpreted in terms of a model where alpha-crystallin binds at least two conformationally dis

70 Calf lens alpha-crystallin binds GRIFIN with relatively high affin

71 alpha-Crystallin binds the various betaB2-crystallin mut

72 cted at high ionic strength, suggesting that alpha-crystallin binds to the fiber cell plasma membrane

73 hat less re-activation was observed when the alpha-crystallin-bound enzyme was treated with heat-shoc

74 However, the alpha-crystallin-bound enzymes regain activity on intera

75 gain insight into the secondary structure of alpha-crystallin-bound species, an understanding which h

76 We found that chemical modification of alpha-crystallin by a physiological alpha-dicarbonyl com

77 we determined the melittin-binding sites in alpha-crystallin by cross-linking studies.

78 ly map the age-related changes of human lens alpha-crystallin by MALDI imaging mass spectrometry incl

79 s strongly reduces the chaperone function of alpha-crystallins by reducing their solubility and disru

80 Under stress, sHSPs such as alpha-crystallin can act as chaperones binding partially

81 Here it is demonstrated that alpha-crystallin can bind to partially denatured enzymes

82 A similar role has been proposed for ATP in alpha-crystallin chaperone activity.

83 The results suggest that the alpha-crystallin chaperone peptides could be used as the

84 n to nonreplicating persistence (NRP) is the alpha-crystallin chaperone protein homologue (Acr).

85 Using alpha-crystallin chaperone variants lacking tryptophans,

86 stallins were used to simulate reduced total alpha-crystallin chaperone-like activity in vivo.

87 esis that the physical properties of a mixed alpha-crystallin complex may hold particular relevance f

88 oss-linking, GRIFIN subunits copurified with alpha-crystallin complexes during size exclusion chromat

89 Membrane-associated alpha-crystallin complexes have measurably reduced CLA c

90 nd subsequent precipitation of the saturated alpha-crystallin complexes in the developing lens of aff

91 binding does not alter the time required for alpha-crystallin complexes to reach subunit exchange equ

92 Alpha-crystallins comprise 35% of soluble proteins in th

93 alpha-Crystallin consists of two subunits, alphaA and al

94 D) and (b) reconstituted heteroaggregates of alpha-crystallin containing (i) wild type alphaA (WT-alp

95 The reconstituted alpha-crystallin containing alphaA-R116C and alphaB-wt h

96 faces, and lower chaperone activity than the alpha-crystallin containing alphaA-wt and alphaB-wt.

97 These findings demonstrate that both alpha-crystallins contribute to persistent infection wit

98 blished the beta3-beta8-beta9 surface of the alpha crystallin core domain as an interface for complex

99 The alpha crystallin core domain contained four interactive

100 6, and Ser-138 on the exposed surface of the alpha crystallin core domain could account for the effec

101 ITSSLS(138)), which is on the surface of the alpha crystallin core domain of human alphaB crystallin,

102 xposed residues of the beta8 sequence in the alpha crystallin core domain was independent of complex

103 and (131)LTITSSLSDGV(141), belonging to the alpha crystallin core domain were synthesized as peptide

104 tion, 3HK and 3HAA fostered copper-dependent alpha-crystallin cross-linking.

105 we identified a class of molecules that bind alpha-crystallins (cryAA and cryAB) and reversed their a

106 tudy was to investigate whether 19 to 20-mer alpha-crystallin-derived mini-chaperone peptides (alpha-

107 Cellular uptake of fluorescein-labeled, alpha-crystallin-derived mini-peptides and recombinant f

108 Alpha-crystallin did not have a strong effect on the GTP

109 nding of the hydrophobic protein melittin to alpha-crystallin diminishes its chaperone-like activity

110 Conversely, the abundance of native alpha-crystallin diminishes with age and cataract develo

111 cently reported structure of the homodimeric alpha-crystallin domain (ACD) and C-terminal IXI motif i

112 While the alpha-crystallin domain (ACD) dimer of sHSPs is the univ

113 information reveals that a central conserved alpha-crystallin domain (ACD) forms dimeric building blo

114 sHsps contain a structurally conserved alpha-crystallin domain (ACD) of about 100 amino acid re

115 Within the conserved alpha-crystallin domain both substrates also bind the be

116 terminal truncation and six mutations in the alpha-crystallin domain destabilized the sHsp oligomer a

117 The disease mutant R120G alpha-crystallin domain dimer was found to be more stabl

118 gle amino acid substitutions within the core alpha-crystallin domain displayed a modest decrease in c

119 cular chaperones, all containing a conserved alpha-crystallin domain flanked by variable N- and C-ter

120 copy is related to recent EPR studies of the alpha-crystallin domain fold and dimer interface of alph

121 Here, crystal structures of excised alpha-crystallin domain from rat Hsp20 and that from hum

122 t, whereas the Y118D mutation in the central alpha-crystallin domain impairs alphaA-crystallin's abil

123 ction clearly required interactions with the alpha-crystallin domain in addition to the N-terminal ar

124 This protein also contains the alpha-crystallin domain in its C-terminal half, a hallma

125 We hypothesize that the alpha-crystallin domain in other sHSPs may have a simila

126 We show that the alpha-crystallin domain is the elementary Cu(II)-binding

127 ognizes conserved determinants in the folded alpha-crystallin domain itself.

128 results strongly suggest that Hspb8 and its alpha-crystallin domain might act as pleiotropic prosurv

129 ent does not alter the fold of the conserved alpha-crystallin domain nor does it disturb the interfac

130 teractions along a conserved sequence in the alpha-crystallin domain of alphaA-crystallin, heat-shock

131 The mutations at sites within the core alpha-crystallin domain of alphaB-crystallin identify re

132 demonstrate that subunit interactions in the alpha-crystallin domain of mammalian small heat-shock pr

133 to the beta3 and beta4 region present in the alpha-crystallin domain of sHSP 16.5.

134 In total, these data imply that the core alpha-crystallin domain of the sHSPs is a platform for f

135 IDM2 encodes an alpha-crystallin domain protein in the nucleus.

136 g the histone acetyltransferase IDM1 and the alpha-crystallin domain proteins IDM2 and IDM3.

137 omain but also tethered by contacts with the alpha-crystallin domain shell.

138 reviously solved structures, a total of four alpha-crystallin domain structures are now available, gi

139 ed of the Hsp16.9 N-terminal arm and Hsp18.1 alpha-crystallin domain supports the model that a dimeri

140 stigate the role of the conserved C-terminal alpha-crystallin domain versus the variable N-terminal a

141 of mutants within and N-terminal to the core alpha-crystallin domain were similar to wild-type alphaB

142 16.5 changes its orientation relative to the alpha-crystallin domain which enables alternative packin

143 XaHspA monomer structures mainly consist of alpha-crystallin domain with disordered N- and C-termina

144 ins form large cytosolic assemblies from an "alpha-crystallin domain" (ACD) flanked by sequence exten

145 t for a C-terminal approximately 90-residue "alpha-crystallin domain".

146 Four mutations are located in the Hsp20-alpha-crystallin domain, and one mutation is in the C-te

147 and are defined by a conserved beta-sandwich alpha-crystallin domain, flanked by variable N- and C-te

148 An alpha-crystallin domain, typically conserved in small he

149 nd Tyr(122), located near or within the core alpha-crystallin domain, were shielded from the action o

150 uctural elements by wrapping them around the alpha-crystallin domain.

151 he junction of the N-terminal region and the alpha-crystallin domain.

152 titutions within and N-terminal to the core "alpha-crystallin" domain of the small heat-shock protein

153 ified four residues located within the core "alpha-crystallin" domain, Lys(82), Lys(103), Arg(116), a

154 between these proteins containing the core 'alpha-crystallin' domain are much closer.

155 regation in vitro, and it contains the core 'alpha-crystallin' domain found in all sHsps.

156 ctions along this interface persist when the alpha-crystallin domains are expressed in isolation.

157 Sequence differences in the alpha-crystallin domains between metazoans and non-metaz

158 dimers formed by domain swapping between the alpha-crystallin domains, adding to evidence that the sm

159 no report to date has studied the effect of alpha-crystallin expression on tubulin/microtubule assem

160 c, which encodes Acr2, a novel member of the alpha-crystallin family of molecular chaperones.

161 dii, Hsp30/bag1, and both are members of the alpha-crystallin family of proteins that can serve as mo

162 s response protein and a member of the Hsp20/alpha-crystallin family.

163 gh its crystal structure reveals the typical alpha-crystallin fold.

164 LC MS/MS analysis of MG-modified alpha-crystallin following chymotryptic digestion reveal

165 tiary structure was distinctly different for alpha-crystallin formed from alphaA-R116C and alphaB-wt.

166 but a protein of approximately 28 kDa in the alpha-crystallin fraction displayed the greatest immunor

167 binding of beta- and gamma-crystallin to the alpha-crystallin fraction was observed in alphaA-R49C he

168 opy and compared with those of reconstituted alpha-crystallin from alphaB-wt and wild-type alphaA-cry

169 and biophysical properties of reconstituted alpha-crystallin from different proportions of wild-type

170 crease in fluorescence yield upon binding to alpha-crystallin from mutant as compared with the wild-t

171 Both native alpha-crystallin from mutant lens and recombinant alphaA

172 A major stress protein, alpha-crystallin, functions as a chaperone.

173 Whole eye lens and alpha-crystallin gels and solutions were investigated us

174 tact lens was very similar to the pattern of alpha-crystallin gels at near-physiological concentratio

175 In the alpha-crystallin gels, a moderate increase in both the s

176 cells because they showed high expression of alpha-crystallin genes but low expression of beta- and g

177 change in abundance after deletion of these alpha-crystallin genes.

178 The alpha-crystallin glass transition could have implication

179 of the small heat shock protein superfamily, alpha-crystallin has a chaperone-like ability to recogni

180 The alpha-crystallins have chaperone-like activity in mainta

181 lin and (b) the presence of WT-alphaB in the alpha-crystallin heteroaggregate leads to packing-induce

182 ibed M. tuberculosis genes acr/hspX/Rv2031c (alpha-crystallin homolog) and Rv2032/acg (acr-coregulate

183 omoters, including acr (also known as hspX) (alpha-crystallin homolog), are upregulated in shallow st

184 including hspX, senX3 and mtrA, encoding the alpha-crystallin homologue, a two-component sensor kinas

185 hermore, purified antigen 85 ABC complex and alpha-crystallin (HspX), two major cell wall antigens pr

186 that have been shown to differentially bind alpha-crystallin in a manner that reflects their free-en

187 dy we investigated the chaperone function of alpha-crystallin in a more physiological system in which

188 Bovine lens alpha-crystallin in solution can be modeled as a fenestr

189 egation was observed despite the presence of alpha-crystallin in the assay.

190 To identify potential binding partners for alpha-crystallin in the intact ocular lens, we conducted

191 The molecular chaperone function of alpha-crystallin in the lens prevents the aggregation an

192 gammaB-I4F mutant proteins interacting with alpha-crystallin in the lens.

193 is that GRIFIN is a novel binding partner of alpha-crystallin in the lens.

194 have weak affinity to the resident chaperone alpha-crystallin in vitro To better understand the mecha

195 roprotective effect of the overexpression of alpha-crystallins in retinal neurons in culture.

196 ng changes in the chaperone-like activity of alpha-crystallins in vitro, little is known about how th

197 ted from Synechocystis thylakoids, HSP17 and alpha-crystallin increase the molecular order in the flu

198 aract formation the amount of membrane-bound alpha-crystallin increases significantly while high mole

199 r with immunoaffinity-purified argpyrimidine-alpha-crystallin indicates that 50-60% of the increased

200 that E. coli Lon degrades variants of human alpha-crystallin, indicating that Lon recognizes conserv

201 doylphosphatidylethanolamine, both HSP17 and alpha-crystallin inhibit the formation of inverted hexag

202 issimilar proteins--i.e., heterologous gamma-alpha crystallin interactions--primarily due to the chan

203 netration peptides (CPP) to enhance entry of alpha-crystallins into lens-derived cells.

204 e, the alphaA subunit (alphaA-crystallin) of alpha crystallin is thought to be "lens-specific" as onl

205 Alpha-crystallin is a member of the family of small heat

206 Eye lens alpha-crystallin is a member of the small heat shock pro

207 alpha-Crystallin is a member of the small heat-shock pro

208 model in which increased membrane binding of alpha-crystallin is an integral step in the pathogenesis

209 understand the mechanism by which increased alpha-crystallin is bound to the membrane of old and cat

210 esults therefore indicate that in whole lens alpha-crystallin is capable of maintaining its structura

211 orts the view that the chaperone activity of alpha-crystallin is dependent on the presence of surface

212 Binding to alpha-crystallin is detected through changes in the emis

213 es have shown that the chaperone activity of alpha-crystallin is significantly affected in diabetic r

214 Thus, total chaperone-like activity of alpha-crystallins is important for maintaining lens tran

215 m binding to GRIFIN was studied using native alpha-crystallin isolated from calf lenses as well as ol

216 Double heterozygous alpha-crystallin knock-out alphaA(+/-) alphaB(+/-) mice

217 ATP interaction with lens alpha-crystallins leading to enhanced chaperone activity

218 (acr, Rv2031c) gene, which encodes a 16-kDa alpha-crystallin-like protein that is a major antigen.

219 uced aggregation of tubulin, suggesting that alpha-crystallin may affect microtubule assembly by main

220 Recent studies suggest that alpha-crystallin may also interact with a variety of pro

221 We hypothesize replenishing lens alpha-crystallin may delay or prevent cataract.

222 Intriguingly, these data suggest that alpha-crystallin may interact with MAPs to inhibit aggre

223 Augmentation of the chaperone function of alpha-crystallin might have evolved to protect the lens

224 -crystallin-derived mini-chaperone peptides (alpha-crystallin mini-chaperone) are antiapoptotic, and

225 The entry mechanism in hfRPE cells for alpha-crystallin mini-peptides was investigated.

226 id-liquid phase separation behavior of E107A-alpha-crystallin mixtures compared to HGD-alpha-crystall

227 7A-alpha-crystallin mixtures compared to HGD-alpha-crystallin mixtures, and the light-scattering inte

228 of hydrophobicity of proteins, increased in alpha-crystallin modified by low concentrations of MG (2

229 her small heat shock proteins including lens alpha-crystallin mutants linked to congenital cataract.

230 The physicochemical properties of alpha-crystallin obtained from mouse lenses with the Y11

231 attractive force involves the recognition by alpha-crystallins of modified proteins prone to unfoldin

232 d the effects of structural modifications of alpha-crystallin on chaperone activity, but little is kn

233 The radius of gyration of alpha-crystallin on its own and when mixed with beta-cry

234 d redox activity in comparison to unmodified alpha-crystallin or ascorbate-modified alpha-crystallin.

235 nd required the downstream expression of the alpha-crystallin ortholog HSP-16.48 Using a combination

236 /ml), so it is reasonable to assume that the alpha-crystallin pattern dominates the pattern of the in

237 These studies suggest that alpha-crystallin plays a role in suppressing caspase act

238 SDS-PAGE analysis showed that alpha-crystallin prevented heat-induced aggregation of t

239 Intracellular alpha-crystallin protected against the decrease in ouaba

240 o lens biology enhances the understanding of alpha-crystallin protein processing in aging and disease

241 urs in vitro, resulting in production of the alpha-crystallin protein, occurs in vivo as well.

242 acterized and found to contain lens-specific alpha-crystallin protein.

243 e determined by immunoblotting for TTase and alpha-crystallin proteins and by immunohistochemistry fo

244 For alpha-crystallin proteins, the sites that undergo the gr

245 synthase as substrates compared to the other alpha-crystallin proteins.

246 We interpret the alpha-crystallin reconstructions to be average represent

247 nfection genes encoding isocitrate lyase and alpha-crystallin, respectively.

248 Localization of melittin-binding sites in alpha-crystallin resulted in the identification of RTLGP

249 The different distributions of alpha-crystallin revealed in this study provide new lead

250 3HK- or 3HAA-modifed alpha-crystallin showed enhanced redox activity in compa

251 Intact alpha-crystallin signals were detected primarily in the

252 Induction of metallothioneins and alpha-crystallin/small heat shock proteins by different

253 tallothioneins (Ig, If, Ih, Ie, and IIa) and alpha-crystallin/small heat-shock (alphaA-crystallin, al

254 tallothioneins (Ig, If, Ih, Ie, and IIa) and alpha-crystallin/small heat-shock genes (alphaA-crystall

255 litatively similar results were observed for alpha-crystallin solutions at a variety of lower concent

256 ons, and analysis show that aqueous eye lens alpha-crystallin solutions exhibit a glass transition at

257 X-ray scattering liquid structure data from alpha-crystallin solutions over an extended range of pro

258 s of dilute and concentrated bovine eye lens alpha-crystallin solutions, using small-angle X-ray scat

259 imyristoylphosphatidylserine, both HSP17 and alpha-crystallin strongly stabilize the liquid-crystalli

260 ach subunit and/or ATP causes a more compact alpha-crystallin structure.

261 toichiometry of 0.25 +/- 0.01 GRIFIN monomer/alpha-crystallin subunit.

262 The ability of alpha-crystallin subunits to function as molecular chape

263 Molecular images of modified and unmodified alpha-crystallin subunits were obtained from mass spectr

264 ignificance of the modified forms of the two alpha-crystallin subunits.

265 es light scattering measurements showed that alpha-crystallin suppressed tubulin assembly in vitro.

266 rotein aggregation models for cataract, with alpha-crystallin suppressing aggregation of damaged or u

267 The amount of alpha-crystallin that binds to the membrane increases un

268 ltiple truncation products were observed for alpha-crystallin that increased in abundance, both with

269 alpha-Crystallin, the major protein component of the ver

270 alpha-Crystallin, the major protein component of vertebr

271 in the oxidative damage of proteins, such as alpha-crystallin, through interactions with redox-active

272 The ability of alpha-crystallin to detect subtle changes in the populat

273 mmaB, the gammaB-I4F mutant protein binds to alpha-crystallin to form high molecular weight complexes

274 of this chaperone activity is the ability of alpha-crystallin to prevent thermal destabilization of b

275 on binding that depend on the molar ratio of alpha-crystallin to T4L.

276 A) was evaluated by measuring the ability of alpha-crystallins to suppress chemically-induced protein

277 of an approach toward a glass transition at alpha-crystallin volume fractions near 58%.

278 Bovine lens alpha-crystallin was immobilized on EAH-Sepharose gel an

279 alpha-Crystallin was incorporated in the cells on reseal

280 llin in a more physiological system in which alpha-crystallin was incorporated into red cell 'ghosts'

281 As no significant phosphorylation of alpha-crystallin was observed during the renaturation, t

282 When inactive luciferase bound to alpha-crystallin was treated with reticulocyte lysate, a

283 tress after overexpression and knock-down of alpha-crystallins was used to measure their neuroprotect

284 o MjHsp16.5 subunits, as other sHsps such as alpha-crystallin were not structurally compatible and co

285 To evaluate protein uptake, labeled alpha-crystallins were incubated with HLE B3 cells and m

286 e changes to the chaperone-like abilities of alpha-crystallins were observed in alphaB-crystallin mod

287 haA-wt with alphaB-wt, and the reconstituted alpha-crystallins were true heteroaggregates of two inte

288 alphaB(+/-) mice with a decreased amount of alpha-crystallins were used to simulate reduced total al

289 easure the radius of gyration of bovine lens alpha-crystallin when complexed with its target protein

290 in was also observed despite the presence of alpha-crystallin (which has anti-aggregating properties)

291 entrations of the small heat shock chaperone alpha-crystallin, which suppresses aggregation of model

292 Incubation of alpha-crystallin with DL-glyceraldehyde and arginine-mod

293 n of highly oligomerized heteroaggregates of alpha-crystallin with modified structure.

294 interaction of the small heat-shock protein alpha-Crystallin with two substrates: destabilized mutan

295 otypes are modulated by interactions between alpha-crystallins with altered chaperone-like activities

296 ity and disrupting the normal interaction of alpha-crystallins with Bax.

297 alpha-Crystallins with different chaperone-like activiti

298 ent with a model in which the interaction of alpha-crystallins with substrates is not solely triggere

299 old particular relevance for the function of alpha-crystallin within the lens.

300 o be two subunits of one multimeric protein, alpha-crystallin, within the ocular lens.