Fibrillogenic propensity of the GroEL apical domain: A Janus‐faced minichaperone
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M. Vendruscolo | K. Makabe | K. Kuwajima | Jin Chen | P. Sormanni | Y. Goto | H. Yagi | Takashi Nakamura | Pietro Sormanni
[1] G. Fan,et al. Small heat shock protein AgsA forms dynamic fibrils , 2011, FEBS letters.
[2] Daichi Yamada,et al. Substrate Assignment of the (6-4) Photolyase Reaction by FTIR Spectroscopy , 2011 .
[3] Alexander K. Buell,et al. Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation. , 2011, Biophysical journal.
[4] Lingling Chen,et al. Stimulating the Substrate Folding Activity of a Single Ring GroEL Variant by Modulating the Cochaperonin GroES* , 2011, The Journal of Biological Chemistry.
[5] K. Makabe,et al. Dissecting a bimolecular process of MgATP²- binding to the chaperonin GroEL. , 2011, Journal of molecular biology.
[6] Y. Kawata,et al. Covalent Structural Changes in Unfolded GroES That Lead to Amyloid Fibril Formation Detected by NMR , 2011, The Journal of Biological Chemistry.
[7] E. Getzoff,et al. FTIR study of light-dependent activation and DNA repair processes of (6-4) photolyase. , 2011, Biochemistry.
[8] W. Taylor,et al. On the evolutionary origin of the chaperonins , 2011, Proteins.
[9] Michele Vendruscolo,et al. Amyloid-like Aggregates Sequester Numerous Metastable Proteins with Essential Cellular Functions , 2011, Cell.
[10] 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.
[11] Matthias J. Feige,et al. Regions outside the alpha-crystallin domain of the small heat shock protein Hsp26 are required for its dimerization. , 2010, Journal of molecular biology.
[12] David Eisenberg,et al. Identifying the amylome, proteins capable of forming amyloid-like fibrils , 2010, Proceedings of the National Academy of Sciences.
[13] Maria Trulsson,et al. alpha-Lactalbumin, engineered to be nonnative and inactive, kills tumor cells when in complex with oleic acid: a new biological function resulting from partial unfolding. , 2009, Journal of molecular biology.
[14] Michele Vendruscolo,et al. Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins , 2009, Proceedings of the National Academy of Sciences.
[15] J. Grason,et al. Setting the chaperonin timer: A two-stroke, two-speed, protein machine , 2008, Proceedings of the National Academy of Sciences.
[16] Michele Vendruscolo,et al. Prediction of aggregation-prone regions in structured proteins. , 2008, Journal of molecular biology.
[17] S. Radford,et al. Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly , 2008, Proceedings of the National Academy of Sciences.
[18] C. Dobson,et al. Characterisation of Amyloid Fibril Formation by Small Heat-shock Chaperone Proteins Human αA-, αB- and R120G αB-Crystallins , 2007 .
[19] Wenmiao Shu,et al. Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass , 2007, Proceedings of the National Academy of Sciences.
[20] Michele Vendruscolo,et al. Life on the edge: a link between gene expression levels and aggregation rates of human proteins. , 2007, Trends in biochemical sciences.
[21] C. Dobson,et al. Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins. , 2007, Journal of molecular biology.
[22] Flavio Seno,et al. Insight into the Structure of Amyloid Fibrils from the Analysis of Globular Proteins , 2006, PLoS Comput. Biol..
[23] C. Dobson,et al. Protein misfolding, functional amyloid, and human disease. , 2006, Annual review of biochemistry.
[24] K. Wüthrich,et al. GroEL‐GroES‐mediated protein folding , 2006, Chemical reviews.
[25] H. Rye,et al. GroEL-Mediated Protein Folding: Making the Impossible, Possible , 2006, Critical reviews in biochemistry and molecular biology.
[26] C. Dobson,et al. Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein. , 2005, Biochemistry.
[27] Amnon Horovitz,et al. Allosteric regulation of chaperonins. , 2005, Current opinion in structural biology.
[28] Y. Kawata,et al. Amyloid-like fibril formation of co-chaperonin GroES: nucleation and extension prefer different degrees of molecular compactness. , 2005, Journal of molecular biology.
[29] L. Serrano,et al. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins , 2004, Nature Biotechnology.
[30] L. Serrano,et al. A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins. , 2004, Journal of molecular biology.
[31] S. Lindquist,et al. Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[32] C. Dobson,et al. Amyloid Fibril Formation by Lens Crystallin Proteins and Its Implications for Cataract Formation* , 2004, Journal of Biological Chemistry.
[33] Y. Kawarabayasi,et al. Expression and biochemical characterization of two small heat shock proteins from the thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7 , 2004, Protein science : a publication of the Protein Society.
[34] Melissa S Kosinski-Collins,et al. In vitro unfolding, refolding, and polymerization of human γD crystallin, a protein involved in cataract formation , 2003, Protein science : a publication of the Protein Society.
[35] S. Radford,et al. Structural Plasticity and Noncovalent Substrate Binding in the GroEL Apical Domain , 2002, The Journal of Biological Chemistry.
[36] M. Hoshino,et al. Mapping the core of the β2-microglobulin amyloid fibril by H/D exchange , 2002, Nature Structural Biology.
[37] Johannes Buchner,et al. Molecular chaperones--cellular machines for protein folding. , 2002, Angewandte Chemie.
[38] C. Dobson,et al. Amyloid fibril formation by a helical cytochrome , 2001, FEBS letters.
[39] A. Fersht,et al. The binding of bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL. , 2001, Biochemistry.
[40] Christopher M. Dobson,et al. Amyloid fibrils from muscle myoglobin , 2001, Nature.
[41] A. Fersht,et al. Identification of substrate binding site of GroEL minichaperone in solution. , 1999, Journal of molecular biology.
[42] A. Fersht,et al. In vivo activities of GroEL minichaperones. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[43] A. Fersht,et al. Thermodynamic stability and folding of GroEL minichaperones. , 1998, Journal of molecular biology.
[44] H. Kagawa,et al. Chaperonin filaments: the archaeal cytoskeleton? , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[45] A. Fersht,et al. Chaperone activity and structure of monomeric polypeptide binding domains of GroEL. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[46] Leon D. Segal,et al. Functions , 1995 .
[47] Y. Kashi,et al. Residues in chaperonin GroEL required for polypeptide binding and release , 1994, Nature.
[48] J. Tamada,et al. Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[49] M. Hosokawa,et al. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. , 1989, Analytical biochemistry.