213 related articles for article (PubMed ID: 22057845)
1. Roles of the N- and C-terminal sequences in Hsp27 self-association and chaperone activity.
Lelj-Garolla B; Mauk AG
Protein Sci; 2012 Jan; 21(1):122-33. PubMed ID: 22057845
[TBL] [Abstract][Full Text] [Related]
2. 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]
3. Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain.
McDonald ET; Bortolus M; Koteiche HA; Mchaourab HS
Biochemistry; 2012 Feb; 51(6):1257-68. PubMed ID: 22264079
[TBL] [Abstract][Full Text] [Related]
4. Chaperone activity of human small heat shock protein-GST fusion proteins.
Arbach H; Butler C; McMenimen KA
Cell Stress Chaperones; 2017 Jul; 22(4):503-515. PubMed ID: 28130664
[TBL] [Abstract][Full Text] [Related]
5. Specific sequences in the N-terminal domain of human small heat-shock protein HSPB6 dictate preferential hetero-oligomerization with the orthologue HSPB1.
Heirbaut M; Lermyte F; Martin EM; Beelen S; Sobott F; Strelkov SV; Weeks SD
J Biol Chem; 2017 Jun; 292(24):9944-9957. PubMed ID: 28487364
[TBL] [Abstract][Full Text] [Related]
6. Self-association and chaperone activity of Hsp27 are thermally activated.
Lelj-Garolla B; Mauk AG
J Biol Chem; 2006 Mar; 281(12):8169-74. PubMed ID: 16436384
[TBL] [Abstract][Full Text] [Related]
7. Identification of peptides in human Hsp20 and Hsp27 that possess molecular chaperone and anti-apoptotic activities.
Nahomi RB; DiMauro MA; Wang B; Nagaraj RH
Biochem J; 2015 Jan; 465(1):115-25. PubMed ID: 25332102
[TBL] [Abstract][Full Text] [Related]
8. Structural and functional specificity of small heat shock protein HspB1 and HspB4, two cellular partners of HspB5: role of the in vitro hetero-complex formation in chaperone activity.
Skouri-Panet F; Michiel M; Férard C; Duprat E; Finet S
Biochimie; 2012 Apr; 94(4):975-84. PubMed ID: 22210387
[TBL] [Abstract][Full Text] [Related]
9. Engineering of a Polydisperse Small Heat-Shock Protein Reveals Conserved Motifs of Oligomer Plasticity.
Mishra S; Chandler SA; Williams D; Claxton DP; Koteiche HA; Stewart PL; Benesch JLP; Mchaourab HS
Structure; 2018 Aug; 26(8):1116-1126.e4. PubMed ID: 29983375
[TBL] [Abstract][Full Text] [Related]
10. Structure and properties of G84R and L99M mutants of human small heat shock protein HspB1 correlating with motor neuropathy.
Nefedova VV; Sudnitsyna MV; Strelkov SV; Gusev NB
Arch Biochem Biophys; 2013 Oct; 538(1):16-24. PubMed ID: 23948568
[TBL] [Abstract][Full Text] [Related]
11. Wrapping the alpha-crystallin domain fold in a chaperone assembly.
Stamler R; Kappé G; Boelens W; Slingsby C
J Mol Biol; 2005 Oct; 353(1):68-79. PubMed ID: 16165157
[TBL] [Abstract][Full Text] [Related]
12. Characterization of human small heat shock protein HSPB1 α-crystallin domain localized mutants associated with hereditary motor neuron diseases.
Weeks SD; Muranova LK; Heirbaut M; Beelen S; Strelkov SV; Gusev NB
Sci Rep; 2018 Jan; 8(1):688. PubMed ID: 29330367
[TBL] [Abstract][Full Text] [Related]
13. Chaperone-like activity of alpha-crystallin and other small heat shock proteins.
Ganea E
Curr Protein Pept Sci; 2001 Sep; 2(3):205-25. PubMed ID: 12369933
[TBL] [Abstract][Full Text] [Related]
14. Role of the conserved SRLFDQFFG region of alpha-crystallin, a small heat shock protein. Effect on oligomeric size, subunit exchange, and chaperone-like activity.
Pasta SY; Raman B; Ramakrishna T; Rao ChM
J Biol Chem; 2003 Dec; 278(51):51159-66. PubMed ID: 14532291
[TBL] [Abstract][Full Text] [Related]
15. The Role of the Arginine in the Conserved N-Terminal Domain RLFDQxFG Motif of Human Small Heat Shock Proteins HspB1, HspB4, HspB5, HspB6, and HspB8.
Shatov VM; Weeks SD; Strelkov SV; Gusev NB
Int J Mol Sci; 2018 Jul; 19(7):. PubMed ID: 30036999
[TBL] [Abstract][Full Text] [Related]
16. Attempt to optimize some properties of fluorescent chimeras of human small heat shock protein HspB1 by modifying linker length and nature.
Datskevich PN; Muranova LK; Gusev NB
Biochemistry (Mosc); 2015 Jan; 80(1):67-73. PubMed ID: 25754041
[TBL] [Abstract][Full Text] [Related]
17. Local unfolding of the HSP27 monomer regulates chaperone activity.
Alderson TR; Roche J; Gastall HY; Dias DM; Pritišanac I; Ying J; Bax A; Benesch JLP; Baldwin AJ
Nat Commun; 2019 Mar; 10(1):1068. PubMed ID: 30842409
[TBL] [Abstract][Full Text] [Related]
18. The taming of small heat-shock proteins: crystallization of the alpha-crystallin domain from human Hsp27.
Baranova EV; Beelen S; Gusev NB; Strelkov SV
Acta Crystallogr Sect F Struct Biol Cryst Commun; 2009 Dec; 65(Pt 12):1277-81. PubMed ID: 20054128
[TBL] [Abstract][Full Text] [Related]
19. Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations.
Bova MP; McHaourab HS; Han Y; Fung BK
J Biol Chem; 2000 Jan; 275(2):1035-42. PubMed ID: 10625643
[TBL] [Abstract][Full Text] [Related]
20. Release of a disordered domain enhances HspB1 chaperone activity toward tau.
Baughman HER; Pham TT; Adams CS; Nath A; Klevit RE
Proc Natl Acad Sci U S A; 2020 Feb; 117(6):2923-2929. PubMed ID: 31974309
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
