163 related articles for article (PubMed ID: 16038412)
1. 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]
2. 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]
3. The IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies.
Pasta SY; Raman B; Ramakrishna T; Rao ChM
Mol Vis; 2004 Sep; 10():655-62. PubMed ID: 15448619
[TBL] [Abstract][Full Text] [Related]
4. HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cells.
Carra S; Sivilotti M; Chávez Zobel AT; Lambert H; Landry J
Hum Mol Genet; 2005 Jun; 14(12):1659-69. PubMed ID: 15879436
[TBL] [Abstract][Full Text] [Related]
5. Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimics.
Nagaraj RH; Panda AK; Shanthakumar S; Santhoshkumar P; Pasupuleti N; Wang B; Biswas A
PLoS One; 2012; 7(1):e30257. PubMed ID: 22272318
[TBL] [Abstract][Full Text] [Related]
6. Oligomeric structure and chaperone-like activity of Drosophila melanogaster mitochondrial small heat shock protein Hsp22 and arginine mutants in the alpha-crystallin domain.
Dabbaghizadeh A; Finet S; Morrow G; Moutaoufik MT; Tanguay RM
Cell Stress Chaperones; 2017 Jul; 22(4):577-588. PubMed ID: 28389817
[TBL] [Abstract][Full Text] [Related]
7. Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27.
Thériault JR; Lambert H; Chávez-Zobel AT; Charest G; Lavigne P; Landry J
J Biol Chem; 2004 May; 279(22):23463-71. PubMed ID: 15033973
[TBL] [Abstract][Full Text] [Related]
8. Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins.
Kumar LV; Ramakrishna T; Rao CM
J Biol Chem; 1999 Aug; 274(34):24137-41. PubMed ID: 10446186
[TBL] [Abstract][Full Text] [Related]
9. Site-directed mutations within the core "alpha-crystallin" domain of the small heat-shock protein, human alphaB-crystallin, decrease molecular chaperone functions.
Muchowski PJ; Wu GJ; Liang JJ; Adman ET; Clark JI
J Mol Biol; 1999 Jun; 289(2):397-411. PubMed ID: 10366513
[TBL] [Abstract][Full Text] [Related]
10. Rescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 Partners.
Hussein RM; Benjamin IJ; Kampinga HH
PLoS One; 2015; 10(5):e0126761. PubMed ID: 25961584
[TBL] [Abstract][Full Text] [Related]
11. Structure and function of small heat shock/alpha-crystallin proteins: established concepts and emerging ideas.
MacRae TH
Cell Mol Life Sci; 2000 Jun; 57(6):899-913. PubMed ID: 10950306
[TBL] [Abstract][Full Text] [Related]
12. 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]
13. 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]
14. 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]
15. The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1-10.
Kappé G; Franck E; Verschuure P; Boelens WC; Leunissen JA; de Jong WW
Cell Stress Chaperones; 2003; 8(1):53-61. PubMed ID: 12820654
[TBL] [Abstract][Full Text] [Related]
16. 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]
17. NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Carver JA; Lindner RA
Int J Biol Macromol; 1998; 22(3-4):197-209. PubMed ID: 9650074
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. Maintenance of chaperone-like activity despite mutations in a conserved region of murine lens alphaB crystallin.
Hepburne-Scott HW; Crabbe MJ
Mol Vis; 1999 Aug; 5():15. PubMed ID: 10445957
[TBL] [Abstract][Full Text] [Related]
20. The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteins.
Fontaine JM; Rest JS; Welsh MJ; Benndorf R
Cell Stress Chaperones; 2003; 8(1):62-9. PubMed ID: 12820655
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]