The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin
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[1] Alexander K. Buell,et al. Opposed Effects of Dityrosine Formation in Soluble and Aggregated α-Synuclein on Fibril Growth , 2017, Journal of molecular biology.
[2] F. Sobott,et al. Specific sequences in the N-terminal domain of human small heat-shock protein HSPB6 dictate preferential hetero-oligomerization with the orthologue HSPB1 , 2017, The Journal of Biological Chemistry.
[3] H. Ecroyd,et al. Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of Aggregation* , 2016, The Journal of Biological Chemistry.
[4] A. Dillin,et al. Walking the tightrope: proteostasis and neurodegenerative disease , 2016, Journal of neurochemistry.
[5] Yonghua Wang,et al. Active-State Structures of a Small Heat-Shock Protein Revealed a Molecular Switch for Chaperone Function. , 2015, Structure.
[6] B. Reif,et al. The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client , 2015, Nature Structural &Molecular Biology.
[7] E. Thornell,et al. Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis , 2015, Cellular and Molecular Life Sciences.
[8] Blagojce Jovcevski,et al. Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity. , 2015, Chemistry & biology.
[9] J. Carver,et al. Small heat-shock proteins: important players in regulating cellular proteostasis , 2015, Cellular and Molecular Life Sciences.
[10] S. Strelkov,et al. Dissecting the Functional Role of the N-Terminal Domain of the Human Small Heat Shock Protein HSPB6 , 2014, PloS one.
[11] W. Boelens,et al. Cell biological roles of αB-crystallin. , 2014, Progress in biophysics and molecular biology.
[12] Alexander K. Buell,et al. Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation , 2014, Proceedings of the National Academy of Sciences.
[13] PNAS Plus Significance Statements , 2014, Proceedings of the National Academy of Sciences.
[14] Johannes Buchner,et al. Regulated structural transitions unleash the chaperone activity of αB-crystallin , 2013, Proceedings of the National Academy of Sciences.
[15] Georg K. A. Hochberg,et al. C-terminal interactions mediate the quaternary dynamics of αB-crystallin , 2013, Philosophical Transactions of the Royal Society B: Biological Sciences.
[16] R. Klevit,et al. One size does not fit all: The oligomeric states of αB crystallin , 2013, FEBS letters.
[17] Amie M. Morris,et al. Structural and Functional Aspects of Hetero-oligomers Formed by the Small Heat Shock Proteins αB-Crystallin and HSP27* , 2013, The Journal of Biological Chemistry.
[18] M. Yohda,et al. Nonequivalence observed for the 16-meric structure of a small heat shock protein, SpHsp16.0, from Schizosaccharomyces pombe. , 2013, Structure.
[19] H. Ecroyd,et al. The small heat-shock protein αB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of α-lactalbumin. , 2012, The Biochemical journal.
[20] R. Klevit,et al. Binding determinants of the small heat shock protein, αB‐crystallin: recognition of the ‘IxI’ motif , 2012, The EMBO journal.
[21] Alice R. Clark,et al. sHSP in the eye lens: crystallin mutations, cataract and proteostasis. , 2012, The international journal of biochemistry & cell biology.
[22] C. Emanuelsson,et al. Probing the transient interaction between the small heat-shock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry , 2012, Cell Stress and Chaperones.
[23] H. Mchaourab,et al. Crystal structure of an activated variant of small heat shock protein Hsp16.5. , 2012, Biochemistry.
[24] H. Mchaourab,et al. Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain. , 2012, Biochemistry.
[25] P. Brundin,et al. Membrane interaction of α-synuclein in different aggregation states. , 2012, Journal of Parkinson's disease.
[26] John L Rubinstein,et al. The polydispersity of αB-crystallin is rationalized by an interconverting polyhedral architecture. , 2011, Structure.
[27] Johannes Buchner,et al. Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach , 2011, Proceedings of the National Academy of Sciences.
[28] L. Kay,et al. αB-crystallin polydispersity is a consequence of unbiased quaternary dynamics. , 2011, Journal of molecular biology.
[29] L. Kay,et al. Quaternary dynamics of αB-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus. , 2011, Journal of molecular biology.
[30] Andreas Bracher,et al. Molecular chaperones in protein folding and proteostasis , 2011, Nature.
[31] Rachel E. Klevit,et al. N-terminal domain of αB-crystallin provides a conformational switch for multimerization and structural heterogeneity , 2011, Proceedings of the National Academy of Sciences.
[32] M. Yohda,et al. Dimer structure and conformational variability in the N-terminal region of an archaeal small heat shock protein, StHsp14.0. , 2011, Journal of structural biology.
[33] Ronald Kühne,et al. Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers , 2010, Nature Structural &Molecular Biology.
[34] David Eisenberg,et al. Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function , 2010, Protein science : a publication of the Protein Society.
[35] E. Vierling,et al. Substrate binding site flexibility of the small heat shock protein molecular chaperones , 2009, Proceedings of the National Academy of Sciences.
[36] U. Andley. Effects of α-Crystallin on Lens Cell Function and Cataract Pathology , 2009 .
[37] P. Stewart,et al. Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins. , 2009, Biochemistry.
[38] R. Klevit,et al. alphaB-crystallin: a hybrid solid-state/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer. , 2009, Journal of molecular biology.
[39] C. Robinson,et al. Small Heat Shock Protein Activity Is Regulated by Variable Oligomeric Substructure* , 2008, Journal of Biological Chemistry.
[40] J. Carver,et al. The effect of small molecules in modulating the chaperone activity of αB‐crystallin against ordered and disordered protein aggregation , 2008, The FEBS journal.
[41] Richard I. Morimoto,et al. Adapting Proteostasis for Disease Intervention , 2008, Science.
[42] P. Stewart,et al. Cryoelectron Microscopy and EPR Analysis of Engineered Symmetric and Polydisperse Hsp16.5 Assemblies Reveals Determinants of Polydispersity and Substrate Binding* , 2006, Journal of Biological Chemistry.
[43] John I. Clark,et al. Structure-based analysis of the β8 interactive sequence of human αB crystallin , 2006 .
[44] Y. Sreelakshmi,et al. The interaction between alphaA- and alphaB-crystallin is sequence-specific. , 2006, Molecular vision.
[45] Carol V Robinson,et al. Phosphorylation of αB-Crystallin Alters Chaperone Function through Loss of Dimeric Substructure* , 2004, Journal of Biological Chemistry.
[46] M. Yohda,et al. Role of the N-terminal region of the crenarchaeal sHsp, StHsp14.0, in thermal-induced disassembly of the complex and molecular chaperone activity. , 2004, Biochemical and biophysical research communications.
[47] Christine Slingsby,et al. Polydispersity of a mammalian chaperone: Mass spectrometry reveals the population of oligomers in αB-crystallin , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[48] V. Subramaniam,et al. Dependence of α-synuclein aggregate morphology on solution conditions , 2002 .
[49] Christine Slingsby,et al. Crystal structure and assembly of a eukaryotic small heat shock protein , 2001, Nature Structural Biology.
[50] A. Tardieu,et al. alpha-Crystallin quaternary structure and interactive properties control eye lens transparency. , 1998, International journal of biological macromolecules.
[51] J. Buchner,et al. Structure and function of α-crystallins: Traversing from in vitro to in vivo. , 2016, Biochimica et biophysica acta.
[52] H. Kampinga,et al. The Multicolored World of the Human HSPB Family , 2015 .
[53] H. Ecroyd. Redefining the chaperone mechanism of sHsps: not just holdase chaperones , 2015 .
[54] J. Carver,et al. Crystallin proteins and amyloid fibrils , 2008, Cellular and Molecular Life Sciences.
[55] M. Bova,et al. Lens alpha-crystallin: chaperone-like properties. , 1998, Methods in enzymology.