141 related articles for article (PubMed ID: 34639138)
1. Oligomeric Structural Transition of HspB1 from Chinese Hamster.
Kurokawa N; Midorikawa R; Nakamura M; Noguchi K; Morishima K; Inoue R; Sugiyama M; Yohda M
Int J Mol Sci; 2021 Oct; 22(19):. PubMed ID: 34639138
[TBL] [Abstract][Full Text] [Related]
2. Functional and structural characterization of HspB1/Hsp27 from Chinese hamster ovary cells.
Sha E; Nakamura M; Ankai K; Yamamoto YY; Oka T; Yohda M
FEBS Open Bio; 2019 Oct; 9(10):1826-1834. PubMed ID: 31441240
[TBL] [Abstract][Full Text] [Related]
3. 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]
4. 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]
5. Structural instability caused by a mutation at a conserved arginine in the alpha-crystallin domain of Chinese hamster heat shock protein 27.
Chávez Zobel AT; Lambert H; Thériault JR; Landry J
Cell Stress Chaperones; 2005; 10(2):157-66. PubMed ID: 16038412
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1.
Chalova AS; Sudnitsyna MV; Semenyuk PI; Orlov VN; Gusev NB
Cell Stress Chaperones; 2014 Nov; 19(6):963-72. PubMed ID: 24898092
[TBL] [Abstract][Full Text] [Related]
8. Conditional Disorder in Small Heat-shock Proteins.
Alderson TR; Ying J; Bax A; Benesch JLP; Baldwin AJ
J Mol Biol; 2020 Apr; 432(9):3033-3049. PubMed ID: 32081587
[TBL] [Abstract][Full Text] [Related]
9. 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]
10. Multiple oligomeric structures of a bacterial small heat shock protein.
Mani N; Bhandari S; Moreno R; Hu L; Prasad BVV; Suguna K
Sci Rep; 2016 Apr; 6():24019. PubMed ID: 27053150
[TBL] [Abstract][Full Text] [Related]
11. It takes a dimer to tango: Oligomeric small heat shock proteins dissociate to capture substrate.
Santhanagopalan I; Degiacomi MT; Shepherd DA; Hochberg GKA; Benesch JLP; Vierling E
J Biol Chem; 2018 Dec; 293(51):19511-19521. PubMed ID: 30348902
[TBL] [Abstract][Full Text] [Related]
12. Crystal structures of Xanthomonas small heat shock protein provide a structural basis for an active molecular chaperone oligomer.
Hilario E; Martin FJ; Bertolini MC; Fan L
J Mol Biol; 2011 Apr; 408(1):74-86. PubMed ID: 21315085
[TBL] [Abstract][Full Text] [Related]
13. Chaperone-like activity of the N-terminal region of a human small heat shock protein and chaperone-functionalized nanoparticles.
Gliniewicz EF; Chambers KM; De Leon ER; Sibai D; Campbell HC; McMenimen KA
Proteins; 2019 May; 87(5):401-415. PubMed ID: 30684363
[TBL] [Abstract][Full Text] [Related]
14. The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli.
Jiao W; Qian M; Li P; Zhao L; Chang Z
J Mol Biol; 2005 Apr; 347(4):871-84. PubMed ID: 15769476
[TBL] [Abstract][Full Text] [Related]
15. HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus.
Lambert H; Charette SJ; Bernier AF; Guimond A; Landry J
J Biol Chem; 1999 Apr; 274(14):9378-85. PubMed ID: 10092617
[TBL] [Abstract][Full Text] [Related]
16. Tsp36, a tapeworm small heat-shock protein with a duplicated alpha-crystallin domain, forms dimers and tetramers with good chaperone-like activity.
Kappé G; Aquilina JA; Wunderink L; Kamps B; Robinson CV; Garate T; Boelens WC; de Jong WW
Proteins; 2004 Oct; 57(1):109-17. PubMed ID: 15326597
[TBL] [Abstract][Full Text] [Related]
17. A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization.
Haslbeck M; Ignatiou A; Saibil H; Helmich S; Frenzl E; Stromer T; Buchner J
J Mol Biol; 2004 Oct; 343(2):445-55. PubMed ID: 15451672
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. pH-dependent structural modulation is conserved in the human small heat shock protein HSBP1.
Clouser AF; Klevit RE
Cell Stress Chaperones; 2017 Jul; 22(4):569-575. PubMed ID: 28332148
[TBL] [Abstract][Full Text] [Related]
20. Mammalian HspB1 (Hsp27) is a molecular sensor linked to the physiology and environment of the cell.
Arrigo AP
Cell Stress Chaperones; 2017 Jul; 22(4):517-529. PubMed ID: 28144778
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
