Fibrillogenic propensity of the GroEL apical domain: A Janus‐faced minichaperone

[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.