Conformational properties of the aggregation precursor state of HypF-N.
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F. Chiti | A. Fontana | P. P. de Laureto | G. Calloni | S. Campioni | A. Relini | M. F. Mossuto | S. Torrassa
[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.