232 related articles for article (PubMed ID: 36719917)
21. Proteinaceous Transformers: Structural and Functional Variability of Human sHsps.
Riedl M; Strauch A; Catici DAM; Haslbeck M
Int J Mol Sci; 2020 Jul; 21(15):. PubMed ID: 32751672
[TBL] [Abstract][Full Text] [Related]
22. N- and C-terminal regions of αB-crystallin and Hsp27 mediate inhibition of amyloid nucleation, fibril binding, and fibril disaggregation.
Selig EE; Zlatic CO; Cox D; Mok YF; Gooley PR; Ecroyd H; Griffin MDW
J Biol Chem; 2020 Jul; 295(29):9838-9854. PubMed ID: 32417755
[TBL] [Abstract][Full Text] [Related]
23. Effect of cataract-associated mutations in the N-terminal domain of αB-crystallin (HspB5).
Muranova LK; Strelkov SV; Gusev NB
Exp Eye Res; 2020 Aug; 197():108091. PubMed ID: 32533979
[TBL] [Abstract][Full Text] [Related]
24. The function of the beta3 interactive domain in the small heat shock protein and molecular chaperone, human alphaB crystallin.
Ghosh JG; Estrada MR; Houck SA; Clark JI
Cell Stress Chaperones; 2006; 11(2):187-97. PubMed ID: 16817325
[TBL] [Abstract][Full Text] [Related]
25. Cell biological roles of αB-crystallin.
Boelens WC
Prog Biophys Mol Biol; 2014 Jul; 115(1):3-10. PubMed ID: 24576798
[TBL] [Abstract][Full Text] [Related]
26. Arginine hydrochloride enhances the dynamics of subunit assembly and the chaperone-like activity of alpha-crystallin.
Srinivas V; Raman B; Rao KS; Ramakrishna T; Rao ChM
Mol Vis; 2005 Apr; 11():249-55. PubMed ID: 15827547
[TBL] [Abstract][Full Text] [Related]
27. 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]
28. HspB5 Chaperone Structure and Activity Are Modulated by Chemical-Scale Interactions in the ACD Dimer Interface.
Wang C; Teng L; Liu ZS; Kamalova A; McMenimen KA
Int J Mol Sci; 2023 Dec; 25(1):. PubMed ID: 38203641
[TBL] [Abstract][Full Text] [Related]
29. The Aggregation of αB-Crystallin under Crowding Conditions Is Prevented by αA-Crystallin: Implications for α-Crystallin Stability and Lens Transparency.
Grosas AB; Rekas A; Mata JP; Thorn DC; Carver JA
J Mol Biol; 2020 Sep; 432(20):5593-5613. PubMed ID: 32827531
[TBL] [Abstract][Full Text] [Related]
30. Impact of Subunit Composition on the Uptake of α-Crystallin by Lens and Retina.
Mueller NH; Fogueri U; Pedler MG; Montana K; Petrash JM; Ammar DA
PLoS One; 2015; 10(9):e0137659. PubMed ID: 26355842
[TBL] [Abstract][Full Text] [Related]
31. The Chaperone Activity and Substrate Spectrum of Human Small Heat Shock Proteins.
Mymrikov EV; Daake M; Richter B; Haslbeck M; Buchner J
J Biol Chem; 2017 Jan; 292(2):672-684. PubMed ID: 27909051
[TBL] [Abstract][Full Text] [Related]
32. The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.
Carver JA; Grosas AB; Ecroyd H; Quinlan RA
Cell Stress Chaperones; 2017 Jul; 22(4):627-638. PubMed ID: 28391594
[TBL] [Abstract][Full Text] [Related]
33. Some properties of three αB-crystallin mutants carrying point substitutions in the C-terminal domain and associated with congenital diseases.
Gerasimovich ES; Strelkov SV; Gusev NB
Biochimie; 2017 Nov; 142():168-178. PubMed ID: 28919577
[TBL] [Abstract][Full Text] [Related]
34. Chaperone-Like Activity of HSPB5: The Effects of Quaternary Structure Dynamics and Crowding.
Chebotareva NA; Roman SG; Borzova VA; Eronina TB; Mikhaylova VV; Kurganov BI
Int J Mol Sci; 2020 Jul; 21(14):. PubMed ID: 32668633
[TBL] [Abstract][Full Text] [Related]
35. [The recent progress on the role of alpha-crystallin as a molecular chaperone in cataractogenesis].
Yan H; Hui Y
Yan Ke Xue Bao; 2000 Jun; 16(2):91-6. PubMed ID: 12579912
[TBL] [Abstract][Full Text] [Related]
36. The small heat shock proteins αB-crystallin (HSPB5) and Hsp27 (HSPB1) inhibit the intracellular aggregation of α-synuclein.
Cox D; Ecroyd H
Cell Stress Chaperones; 2017 Jul; 22(4):589-600. PubMed ID: 28337642
[TBL] [Abstract][Full Text] [Related]
37. Acetylation of αA-crystallin in the human lens: effects on structure and chaperone function.
Nagaraj RH; Nahomi RB; Shanthakumar S; Linetsky M; Padmanabha S; Pasupuleti N; Wang B; Santhoshkumar P; Panda AK; Biswas A
Biochim Biophys Acta; 2012 Feb; 1822(2):120-9. PubMed ID: 22120592
[TBL] [Abstract][Full Text] [Related]
38. A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis.
Rajagopal P; Tse E; Borst AJ; Delbecq SP; Shi L; Southworth DR; Klevit RE
Elife; 2015 May; 4():. PubMed ID: 25962097
[TBL] [Abstract][Full Text] [Related]
39. Regions outside the alpha-crystallin domain of the small heat shock protein Hsp26 are required for its dimerization.
Chen J; Feige MJ; Franzmann TM; Bepperling A; Buchner J
J Mol Biol; 2010 Apr; 398(1):122-31. PubMed ID: 20171228
[TBL] [Abstract][Full Text] [Related]
40. α-Crystallin Domains of Five Human Small Heat Shock Proteins (sHsps) Differ in Dimer Stabilities and Ability to Incorporate Themselves into Oligomers of Full-Length sHsps.
Shatov VM; Muranova LK; Zamotina MA; Sluchanko NN; Gusev NB
Int J Mol Sci; 2023 Jan; 24(2):. PubMed ID: 36674601
[TBL] [Abstract][Full Text] [Related]
[Previous] [Next] [New Search]