195 related articles for article (PubMed ID: 16488470)
21. The cataract-causing mutation G98R in human alphaA-crystallin leads to folding defects and loss of chaperone activity.
Singh D; Raman B; Ramakrishna T; Rao ChM
Mol Vis; 2006 Nov; 12():1372-9. PubMed ID: 17149363
[TBL] [Abstract][Full Text] [Related]
22. Productive interaction of chaperones with substrate protein domains allows correct folding of the downstream GFP domain.
Zhang A; Cantor EJ; Barshevsky T; Chong S
Gene; 2005 Apr; 350(1):25-31. PubMed ID: 15780997
[TBL] [Abstract][Full Text] [Related]
23. Small heat-shock proteins function in the insoluble protein complex.
Jiao W; Li P; Zhang J; Zhang H; Chang Z
Biochem Biophys Res Commun; 2005 Sep; 335(1):227-31. PubMed ID: 16055090
[TBL] [Abstract][Full Text] [Related]
24. A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins.
Grousl T; Ungelenk S; Miller S; Ho CT; Khokhrina M; Mayer MP; Bukau B; Mogk A
J Cell Biol; 2018 Apr; 217(4):1269-1285. PubMed ID: 29362223
[TBL] [Abstract][Full Text] [Related]
25. Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue.
Xu X; Kanbara K; Azakami H; Kato A
J Biochem; 2004 May; 135(5):615-8. PubMed ID: 15173200
[TBL] [Abstract][Full Text] [Related]
26. The excised heat-shock domain of alphaB crystallin is a folded, proteolytically susceptible trimer with significant surface hydrophobicity and a tendency to self-aggregate upon heating.
Kundu B; Shukla A; Chaba R; Guptasarma P
Protein Expr Purif; 2004 Aug; 36(2):263-71. PubMed ID: 15249049
[TBL] [Abstract][Full Text] [Related]
27. Fusion tags and chaperone co-expression modulate both the solubility and the inclusion body features of the recombinant CLIPB14 serine protease.
Schrödel A; Volz J; de Marco A
J Biotechnol; 2005 Oct; 120(1):2-10. PubMed ID: 16023240
[TBL] [Abstract][Full Text] [Related]
28. Association of partially folded lens betaB2-crystallins with the alpha-crystallin molecular chaperone.
Evans P; Slingsby C; Wallace BA
Biochem J; 2008 Feb; 409(3):691-9. PubMed ID: 17937660
[TBL] [Abstract][Full Text] [Related]
29. Soybean disease resistance protein RHG1-LRR domain expressed, purified and refolded from Escherichia coli inclusion bodies: preparation for a functional analysis.
Afzal AJ; Lightfoot DA
Protein Expr Purif; 2007 Jun; 53(2):346-55. PubMed ID: 17287130
[TBL] [Abstract][Full Text] [Related]
30. A model for heterooligomer formation in the heat shock response of Escherichia coli.
Healy EF
Biochem Biophys Res Commun; 2012 Apr; 420(3):639-43. PubMed ID: 22450329
[TBL] [Abstract][Full Text] [Related]
31. Characterization of a sHsp of Schizosaccharomyces pombe, SpHsp15.8, and the implication of its functional mechanism by comparison with another sHsp, SpHsp16.0.
Sugino C; Hirose M; Tohda H; Yoshinari Y; Abe T; Giga-Hama Y; Iizuka R; Shimizu M; Kidokoro S; Ishii N; Yohda M
Proteins; 2009 Jan; 74(1):6-17. PubMed ID: 18543332
[TBL] [Abstract][Full Text] [Related]
32. Purification and characterization of two small heat shock proteins from Anabaena sp. PCC 7120.
Liu X; Huang W; Li M; Wu Q
IUBMB Life; 2005 Jun; 57(6):449-54. PubMed ID: 16012054
[TBL] [Abstract][Full Text] [Related]
33. Expression and purification of HtpX-like small heat shock integral membrane protease of an unknown organism related to Methylobacillus flagellatus.
Siddiqui AA; Jalah R; Sharma YD
J Biochem Biophys Methods; 2007 Jun; 70(4):539-46. PubMed ID: 17239953
[TBL] [Abstract][Full Text] [Related]
34. Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26.
White HE; Orlova EV; Chen S; Wang L; Ignatiou A; Gowen B; Stromer T; Franzmann TM; Haslbeck M; Buchner J; Saibil HR
Structure; 2006 Jul; 14(7):1197-204. PubMed ID: 16843901
[TBL] [Abstract][Full Text] [Related]
35. Role of the IXI/V motif in oligomer assembly and function of StHsp14.0, a small heat shock protein from the acidothermophilic archaeon, Sulfolobus tokodaii strain 7.
Saji H; Iizuka R; Yoshida T; Abe T; Kidokoro S; Ishii N; Yohda M
Proteins; 2008 May; 71(2):771-82. PubMed ID: 17979194
[TBL] [Abstract][Full Text] [Related]
36. Oligomeric Aip2p/Dld2p modifies the protein conformation of both properly folded and misfolded substrates in vitro.
Hachiya NS; Sakasegawa Y; Sasaki H; Jozuka A; Tsukita S; Kaneko K
Biochem Biophys Res Commun; 2004 Oct; 323(1):339-44. PubMed ID: 15351742
[TBL] [Abstract][Full Text] [Related]
37. Human and yeast Hsp110 chaperones exhibit functional differences.
Raviol H; Bukau B; Mayer MP
FEBS Lett; 2006 Jan; 580(1):168-74. PubMed ID: 16364315
[TBL] [Abstract][Full Text] [Related]
38. Purification and characterization of the chaperone-like Hsp26 from Saccharomyces cerevisiae.
Ferreira RM; de Andrade LR; Dutra MB; de Souza MF; Flosi Paschoalin VM; Silva JT
Protein Expr Purif; 2006 Jun; 47(2):384-92. PubMed ID: 16603379
[TBL] [Abstract][Full Text] [Related]
39. Chaperone-assisted refolding of Escherichia coli maltodextrin glucosidase.
Paul S; Punam S; Chaudhuri TK
FEBS J; 2007 Nov; 274(22):6000-10. PubMed ID: 17983358
[TBL] [Abstract][Full Text] [Related]
40. The chaperone-like protein alpha-crystallin dissociates insulin dimers and hexamers.
Rasmussen T; Kasimova MR; Jiskoot W; van de Weert M
Biochemistry; 2009 Oct; 48(39):9313-20. PubMed ID: 19715354
[TBL] [Abstract][Full Text] [Related]
[Previous] [Next] [New Search]