ライフサイエンスコーパス: alpha-crystallin

1 had no effect on chaperone-like activity of 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 ll heat shock protein (HSP) homolog of human alpha-crystallin.

6 3-crystallin peptides and in the presence of alpha-crystallin.

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

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

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

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

11 gressive increase in membrane association of alpha-crystallin.

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

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

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

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

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

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

18 ase dramatically alters its interaction with alpha-crystallin.

19 tallin substrate species recognized by human alpha-crystallin.

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

21 pproach to treating cataracts by stabilizing alpha-crystallins.

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

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

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

25 egation of beta-crystallin in the absence of 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 allins in age-related cataracts are bound by alpha-crystallin and form light-scattering HMW aggregate

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

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

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

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

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

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

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

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

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

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

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

60 alpha-Crystallins are small heat shock proteins that reg

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

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

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

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

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

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

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

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

69 alpha-Crystallin binds the various betaB2-crystallin mut

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

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

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

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

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

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

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

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

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

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

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

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

82 Using alpha-crystallin chaperone variants lacking tryptophans,

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

84 d suggest that AGE-mediated cross-linking of alpha-crystallin-client complexes could contribute to le

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

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

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

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

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

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

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

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

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

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

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

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

97 The alpha crystallin core domain contained four interactive

98 6, and Ser-138 on the exposed surface of the alpha crystallin core domain could account for the effec

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

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

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

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

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

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

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

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

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

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

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

110 l-known binding groove within the structured alpha-crystallin domain (ACD) and to sites within the en

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

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

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

114 osphorylation motif around Ser16, and a core alpha-crystallin domain (ACD) responsible for dimerisati

115 The structured core of the protein, the alpha-crystallin domain (ACD), forms dimers and can prev

116 n about sHSP structure beyond its structured alpha-crystallin domain (ACD), which is flanked by disor

117 ics, and function of HSP27 and its conserved alpha-crystallin domain (ACD).

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

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

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

121 sHSPs comprise a conserved alpha-crystallin domain flanked by variable N- and C-ter

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

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

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

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

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

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

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

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

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

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

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

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 We conclude that although the isolated alpha-crystallin domain retains some chaperone activity

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

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

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

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

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 sHSPs share an 'alpha-crystallin domain' with a beta-sandwich structure

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

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

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

150 e a diverse chaperone family that shares the alpha-crystallin domain, which is flanked by variable, d

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

176 The alpha-crystallin glass transition could have implication

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

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

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

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

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

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

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

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

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

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

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

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

189 alpha-Crystallin in the lens binds to other proteins and

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

226 7A-alpha-crystallin mixtures compared to HGD-alpha-crystallin mixtures, and the light-scattering inte

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

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

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

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

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

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

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

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

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

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

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

238 Intracellular alpha-crystallin protected against the decrease in ouaba

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

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

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

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

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

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

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

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

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

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

249 3HK- or 3HAA-modifed alpha-crystallin showed enhanced redox activity in compa

250 Intact alpha-crystallin signals were detected primarily in the

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

269 alpha-Crystallin, the major protein component of vertebr

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

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

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

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

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

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

276 consequences of amino acid isomerization in alpha-crystallins using mass spectrometry, molecular dyn

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.