Conformational properties of the aggregation precursor state of HypF-N.

[1]  Sheena E. Radford,et al.  Folding versus aggregation: Polypeptide conformations on competing pathways , 2008, Archives of biochemistry and biophysics.

[2]  Walter Richter,et al.  Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's abeta(1-40) amyloid fibrils. , 2007, Journal of molecular biology.

[3]  R. Varadarajan,et al.  Identification and thermodynamic characterization of molten globule states of periplasmic binding proteins. , 2007, Biochemistry.

[4]  C. Gomes,et al.  Studies of the molten globule state of ferredoxin: Structural characterization and implications on protein folding and iron–sulfur center assembly , 2007, Proteins.

[5]  Atanas V Koulov,et al.  Functional amyloid--from bacteria to humans. , 2007, Trends in biochemical sciences.

[6]  E. Gazit Use of biomolecular templates for the fabrication of metal nanowires , 2007, The FEBS journal.

[7]  G. Choi,et al.  Intrinsically unstructured N‐terminal domain of bZIP transcription factor HY5 , 2006, Proteins.

[8]  M. Eftink Fluorescence techniques for studying protein structure. , 2006, Methods of biochemical analysis.

[9]  C. Dobson,et al.  Protein misfolding, functional amyloid, and human disease. , 2006, Annual review of biochemistry.

[10]  J. Torrent,et al.  High pressure modulates amyloid formation. , 2006, Protein and peptide letters.

[11]  M. J. Parker,et al.  Amyloid formation under physiological conditions proceeds via a native-like folding intermediate , 2006, Nature Structural &Molecular Biology.

[12]  S. Radford,et al.  Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. , 2005, Journal of molecular biology.

[13]  C. Dobson,et al.  Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates. , 2005, Journal of molecular biology.

[14]  V. Uversky,et al.  Protein dissection enhances the amyloidogenic properties of α‐lactalbumin , 2005 .

[15]  C. Dobson,et al.  Amyloid formation from HypF-N under conditions in which the protein is initially in its native state. , 2005, Journal of molecular biology.

[16]  Fabrizio Chiti,et al.  Investigating the Effects of Mutations on Protein Aggregation in the Cell* , 2005, Journal of Biological Chemistry.

[17]  Mireille Dumoulin,et al.  Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations. , 2005, Journal of molecular biology.

[18]  T. Ban,et al.  Critical balance of electrostatic and hydrophobic interactions is required for beta 2-microglobulin amyloid fibril growth and stability. , 2005, Biochemistry.

[19]  J. Schneider,et al.  Self-assembling peptides and proteins for nanotechnological applications. , 2004, Current opinion in structural biology.

[20]  V. Uversky,et al.  Conformational constraints for amyloid fibrillation: the importance of being unfolded. , 2004, Biochimica et biophysica acta.

[21]  V. Uversky,et al.  Role of Protein−Water Interactions and Electrostatics in α-Synuclein Fibril Formation† , 2004 .

[22]  K. Tsumoto,et al.  Engineering amyloidogenicity towards the development of nanofibrillar materials. , 2004, Trends in biotechnology.

[23]  S. Ferreira,et al.  Folding Intermediates of the Prion Protein Stabilized by Hydrostatic Pressure and Low Temperature* , 2003, Journal of Biological Chemistry.

[24]  E. Forest,et al.  Use of different proteases working in acidic conditions to improve sequence coverage and resolution in hydrogen/deuterium exchange of large proteins. , 2003, Rapid communications in mass spectrometry : RCM.

[25]  S. Radford,et al.  A systematic investigation into the effect of protein destabilisation on beta 2-microglobulin amyloid formation. , 2003, Journal of molecular biology.

[26]  A. Fontana,et al.  Partly folded states of members of the lysozyme/lactalbumin superfamily: A comparative study by circular dichroism spectroscopy and limited proteolysis , 2002, Protein science : a publication of the Protein Society.

[27]  Andreas Hoenger,et al.  De novo designed peptide-based amyloid fibrils , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[28]  F. Bossa,et al.  Contribution of Lys276 to the conformational flexibility of the active site of glutamate decarboxylase from Escherichia coli. , 2002, European journal of biochemistry.

[29]  V. Uversky,et al.  Conformational Prerequisites for α-Lactalbumin Fibrillation† , 2002 .

[30]  M. Bolognesi,et al.  Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain. , 2002, Journal of molecular biology.

[31]  V. Uversky Natively unfolded proteins: A point where biology waits for physics , 2002, Protein science : a publication of the Protein Society.

[32]  C. Dobson,et al.  Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N‐terminal domain , 2001, Protein science : a publication of the Protein Society.

[33]  R. Woody,et al.  A partially folded intermediate conformation is induced in pectate lyase C by the addition of 8‐anilino‐1‐naphthalenesulfonate (ANS) , 2001, Protein science : a publication of the Protein Society.

[34]  C. Dobson,et al.  Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain. , 2001, Journal of molecular biology.

[35]  V. Uversky,et al.  Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation* , 2001, The Journal of Biological Chemistry.

[36]  C. Ionescu-Zanetti,et al.  Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. , 2001, Biochemistry.

[37]  N. Sreerama,et al.  Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. , 2000, Analytical biochemistry.

[38]  N. Sreerama,et al.  Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. , 2000, Analytical biochemistry.

[39]  T D Kim,et al.  Thermal behavior of proteins: heat-resistant proteins and their heat-induced secondary structural changes. , 2000, Biochemistry.

[40]  L. Regan,et al.  A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[41]  L. Serpell,et al.  The protofilament substructure of amyloid fibrils. , 2000, Journal of molecular biology.

[42]  C M Dobson,et al.  Mutational analysis of the propensity for amyloid formation by a globular protein , 2000, The EMBO journal.

[43]  C. Dobson,et al.  Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. , 1999, Biochemistry.

[44]  V. Bhakuni,et al.  8-anilino-1-naphthalene sulfonic acid (ANS) induces folding of acid unfolded cytochrome c to molten globule state as a result of electrostatic interactions. , 1999, Biochemistry.

[45]  C. Dobson Protein misfolding, evolution and disease. , 1999, Trends in biochemical sciences.

[46]  I D Campbell,et al.  Amyloid fibril formation by an SH3 domain. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[47]  J. Kelly,et al.  The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. , 1998, Current opinion in structural biology.

[48]  L. Masotti,et al.  Intrinsic Fluorescence Properties and Structural Analysis of p13suc1 from Schizosaccharomyces pombe * , 1996, The Journal of Biological Chemistry.

[49]  M. Billeter,et al.  MOLMOL: a program for display and analysis of macromolecular structures. , 1996, Journal of molecular graphics.

[50]  O. Ptitsyn,et al.  Further evidence on the equilibrium "pre-molten globule state": four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature. , 1996, Journal of molecular biology.

[51]  O. Ptitsyn,et al.  "Partly folded" state, a new equilibrium state of protein molecules: four-state guanidinium chloride-induced unfolding of beta-lactamase at low temperature. , 1994, Biochemistry.

[52]  N. Puri,et al.  Spectrofluorimetric assessment of the surface hydrophobicity of proteins. , 1992, The Biochemical journal.

[53]  N. A. Rodionova,et al.  Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe , 1991, Biopolymers.

[54]  A. Fink,et al.  Mechanism of acid-induced folding of proteins. , 1990, Biochemistry.

[55]  T. Creighton Proteins: Structures and Molecular Properties , 1986 .

[56]  K. D. Collins,et al.  The Hofmeister effect and the behaviour of water at interfaces , 1985, Quarterly Reviews of Biophysics.

[57]  W. Kabsch,et al.  Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.

[58]  W. Ebeling,et al.  Proteinase K from Tritirachium album Limber. , 1974, European journal of biochemistry.

[59]  P. Picotti,et al.  Probing protein structure by limited proteolysis. , 2004, Acta biochimica Polonica.

[60]  Vladimir N Uversky,et al.  What does it mean to be natively unfolded? , 2002, European journal of biochemistry.

[61]  M. Tomiyama,et al.  Rhodobacter capsulatus HypF is involved in regulation of hydrogenase synthesis through the HupUV proteins. , 1998, European journal of biochemistry.

[62]  C. Blake,et al.  The structure of amyloid fibrils by electron microscopy and X-ray diffraction. , 1997, Advances in protein chemistry.

[63]  A. Dunker,et al.  Aromatic and Cystine Side-Chain Circular Dichroism in Proteins , 1996 .

[64]  G. Fasman Circular Dichroism and the Conformational Analysis of Biomolecules , 1996, Springer US.

[65]  R. Heinrikson [20] Applications of thermolysin in protein structural analysis , 1977 .

[66]  D. M. Blow,et al.  6 The Structure of Chymotrypsin , 1971 .

[67]  J. Fruton The specificity and mechanism of pepsin action. , 1970, Advances in enzymology and related areas of molecular biology.