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Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones.
Van Montfort R, Slingsby C, Vierling E. Van Montfort R, et al. Among authors: vierling e. Adv Protein Chem. 2001;59:105-56. doi: 10.1016/s0065-3233(01)59004-x. Adv Protein Chem. 2001. PMID: 11868270 Review. No abstract available.
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. Santhanagopalan I, et al. Among authors: vierling e. J Biol Chem. 2018 Dec 21;293(51):19511-19521. doi: 10.1074/jbc.RA118.005421. Epub 2018 Oct 22. J Biol Chem. 2018. PMID: 30348902 Free PMC article.
Evidence for an essential function of the N terminus of a small heat shock protein in vivo, independent of in vitro chaperone activity.
Giese KC, Basha E, Catague BY, Vierling E. Giese KC, et al. Among authors: vierling e. Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18896-901. doi: 10.1073/pnas.0506169103. Epub 2005 Dec 19. Proc Natl Acad Sci U S A. 2005. PMID: 16365319 Free PMC article.
Chaperone activity of cytosolic small heat shock proteins from wheat.
Basha E, Lee GJ, Demeler B, Vierling E. Basha E, et al. Among authors: vierling e. Eur J Biochem. 2004 Apr;271(8):1426-36. doi: 10.1111/j.1432-1033.2004.04033.x. Eur J Biochem. 2004. PMID: 15066169
Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions.
Basha E, O'Neill H, Vierling E. Basha E, et al. Among authors: vierling e. Trends Biochem Sci. 2012 Mar;37(3):106-17. doi: 10.1016/j.tibs.2011.11.005. Epub 2011 Dec 14. Trends Biochem Sci. 2012. PMID: 22177323 Free PMC article.
Quaternary dynamics and plasticity underlie small heat shock protein chaperone function.
Stengel F, Baldwin AJ, Painter AJ, Jaya N, Basha E, Kay LE, Vierling E, Robinson CV, Benesch JL. Stengel F, et al. Among authors: vierling e. Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):2007-12. doi: 10.1073/pnas.0910126107. Epub 2010 Jan 19. Proc Natl Acad Sci U S A. 2010. PMID: 20133845 Free PMC article.
The N-terminal arm of small heat shock proteins is important for both chaperone activity and substrate specificity.
Basha E, Friedrich KL, Vierling E. Basha E, et al. Among authors: vierling e. J Biol Chem. 2006 Dec 29;281(52):39943-52. doi: 10.1074/jbc.M607677200. Epub 2006 Nov 7. J Biol Chem. 2006. PMID: 17090542
Mutants in a small heat shock protein that affect the oligomeric state. Analysis and allele-specific suppression.
Giese KC, Vierling E. Giese KC, et al. Among authors: vierling e. J Biol Chem. 2004 Jul 30;279(31):32674-83. doi: 10.1074/jbc.M404455200. Epub 2004 May 19. J Biol Chem. 2004. PMID: 15152007
The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions.
Basha E, Lee GJ, Breci LA, Hausrath AC, Buan NR, Giese KC, Vierling E. Basha E, et al. Among authors: vierling e. J Biol Chem. 2004 Feb 27;279(9):7566-75. doi: 10.1074/jbc.M310684200. Epub 2003 Dec 8. J Biol Chem. 2004. PMID: 14662763
Small heat-shock proteins regulate membrane lipid polymorphism.
Tsvetkova NM, Horváth I, Török Z, Wolkers WF, Balogi Z, Shigapova N, Crowe LM, Tablin F, Vierling E, Crowe JH, Vigh L. Tsvetkova NM, et al. Among authors: vierling e. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13504-9. doi: 10.1073/pnas.192468399. Epub 2002 Oct 4. Proc Natl Acad Sci U S A. 2002. PMID: 12368478 Free PMC article.
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