296 related articles for article (PubMed ID: 24043785)
21. Zebrafish alpha-crystallins: protein structure and chaperone-like activity compared to their mammalian orthologs.
Dahlman JM; Margot KL; Ding L; Horwitz J; Posner M
Mol Vis; 2005 Jan; 11():88-96. PubMed ID: 15692462
[TBL] [Abstract][Full Text] [Related]
22. Structural and functional aspects of hetero-oligomers formed by the small heat shock proteins αB-crystallin and HSP27.
Aquilina JA; Shrestha S; Morris AM; Ecroyd H
J Biol Chem; 2013 May; 288(19):13602-9. PubMed ID: 23532854
[TBL] [Abstract][Full Text] [Related]
23. Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αBa- and Rodent αA(ins)-Crystallin Encode Activated Chaperones.
Koteiche HA; Claxton DP; Mishra S; Stein RA; McDonald ET; Mchaourab HS
Biochemistry; 2015 Sep; 54(38):5949-58. PubMed ID: 26378715
[TBL] [Abstract][Full Text] [Related]
24. Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant.
Ahmad MF; Raman B; Ramakrishna T; Rao ChM
J Mol Biol; 2008 Jan; 375(4):1040-51. PubMed ID: 18061612
[TBL] [Abstract][Full Text] [Related]
25. Structural perturbation of alphaB-crystallin by zinc and temperature related to its chaperone-like activity.
Coi A; Bianucci AM; Bonomi F; Rasmussen P; Mura GM; Ganadu ML
Int J Biol Macromol; 2008 Apr; 42(3):229-34. PubMed ID: 18048095
[TBL] [Abstract][Full Text] [Related]
26. AlphaA-crystallin interacting regions in the small heat shock protein, alphaB-crystallin.
Sreelakshmi Y; Santhoshkumar P; Bhattacharyya J; Sharma KK
Biochemistry; 2004 Dec; 43(50):15785-95. PubMed ID: 15595834
[TBL] [Abstract][Full Text] [Related]
27. The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin.
Jovcevski B; Andrew Aquilina J; Benesch JLP; Ecroyd H
Cell Stress Chaperones; 2018 Sep; 23(5):827-836. PubMed ID: 29520626
[TBL] [Abstract][Full Text] [Related]
28. Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils.
Garvey M; Ecroyd H; Ray NJ; Gerrard JA; Carver JA
Biomolecules; 2017 Sep; 7(3):. PubMed ID: 28895938
[TBL] [Abstract][Full Text] [Related]
29. Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G alphaB-crystallin mutant.
Chávez Zobel AT; Loranger A; Marceau N; Thériault JR; Lambert H; Landry J
Hum Mol Genet; 2003 Jul; 12(13):1609-20. PubMed ID: 12812987
[TBL] [Abstract][Full Text] [Related]
30. Analysis of the alphaB-crystallin domain responsible for inhibiting tubulin aggregation.
Ohto-Fujita E; Fujita Y; Atomi Y
Cell Stress Chaperones; 2007; 12(2):163-71. PubMed ID: 17688195
[TBL] [Abstract][Full Text] [Related]
31. Mechanistic insights into the switch of αB-crystallin chaperone activity and self-multimerization.
Liu Z; Wang C; Li Y; Zhao C; Li T; Li D; Zhang S; Liu C
J Biol Chem; 2018 Sep; 293(38):14880-14890. PubMed ID: 30076220
[TBL] [Abstract][Full Text] [Related]
32. The Effect of Oxidized Dopamine on the Structure and Molecular Chaperone Function of the Small Heat-Shock Proteins, αB-Crystallin and Hsp27.
Hayashi J; Ton J; Negi S; Stephens DEKM; Pountney DL; Preiss T; Carver JA
Int J Mol Sci; 2021 Apr; 22(7):. PubMed ID: 33918165
[TBL] [Abstract][Full Text] [Related]
33. Structural and functional characterization of D109H and R69C mutant versions of human αB-crystallin: The biochemical pathomechanism underlying cataract and myopathy development.
Ghahramani M; Yousefi R; Krivandin A; Muranov K; Kurganov B; Moosavi-Movahedi AA
Int J Biol Macromol; 2020 Mar; 146():1142-1160. PubMed ID: 31678106
[TBL] [Abstract][Full Text] [Related]
34. Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.
Sprague-Piercy MA; Wong E; Roskamp KW; Fakhoury JN; Freites JA; Tobias DJ; Martin RW
Biochim Biophys Acta Gen Subj; 2020 Mar; 1864(3):129502. PubMed ID: 31812542
[TBL] [Abstract][Full Text] [Related]
35. Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in alphaB-crystallin.
Koteiche HA; McHaourab HS
J Biol Chem; 2003 Mar; 278(12):10361-7. PubMed ID: 12529319
[TBL] [Abstract][Full Text] [Related]
36. The multifaceted nature of αB-crystallin.
Hayashi J; Carver JA
Cell Stress Chaperones; 2020 Jul; 25(4):639-654. PubMed ID: 32383140
[TBL] [Abstract][Full Text] [Related]
37. Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin.
Gupta R; Srivastava OP
J Biol Chem; 2004 Oct; 279(43):44258-69. PubMed ID: 15284238
[TBL] [Abstract][Full Text] [Related]
38. The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.
Mainz A; Peschek J; Stavropoulou M; Back KC; Bardiaux B; Asami S; Prade E; Peters C; Weinkauf S; Buchner J; Reif B
Nat Struct Mol Biol; 2015 Nov; 22(11):898-905. PubMed ID: 26458046
[TBL] [Abstract][Full Text] [Related]
39. Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: a model aggregation assay for alpha-crystallin chaperone activity in vitro.
Reddy GB; Narayanan S; Reddy PY; Surolia I
FEBS Lett; 2002 Jul; 522(1-3):59-64. PubMed ID: 12095619
[TBL] [Abstract][Full Text] [Related]
40. Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure.
Aquilina JA; Benesch JL; Ding LL; Yaron O; Horwitz J; Robinson CV
J Biol Chem; 2004 Jul; 279(27):28675-80. PubMed ID: 15117944
[TBL] [Abstract][Full Text] [Related]
[Previous] [Next] [New Search]