PubRank

Daniel P Raleigh

Author PubWeight™ 130.45‹?›

Top papers

Rank Title Journal Year PubWeight™‹?›
1 Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction. Nat Chem Biol 2011 2.39
2 Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution. Proc Natl Acad Sci U S A 2009 2.02
3 Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci 2005 1.91
4 Peptide models provide evidence for significant structure in the denatured state of a rapidly folding protein: the villin headpiece subdomain. Biochemistry 2004 1.89
5 Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. J Am Chem Soc 2003 1.82
6 The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity. Biochemistry 2010 1.63
7 The unfolded state of the villin headpiece helical subdomain: computational studies of the role of locally stabilized structure. J Mol Biol 2006 1.63
8 A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor. J Am Chem Soc 2007 1.59
9 Effect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain. Proc Natl Acad Sci U S A 2005 1.55
10 Residue specific resolution of protein folding dynamics using isotope-edited infrared temperature jump spectroscopy. Biochemistry 2007 1.51
11 A role for helical intermediates in amyloid formation by natively unfolded polypeptides? Phys Biol 2009 1.49
12 Characterizing a partially folded intermediate of the villin headpiece domain under non-denaturing conditions: contribution of His41 to the pH-dependent stability of the N-terminal subdomain. J Mol Biol 2005 1.47
13 The role of His-18 in amyloid formation by human islet amyloid polypeptide. Biochemistry 2005 1.46
14 Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor. Nat Chem 2012 1.39
15 A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides. Protein Eng Des Sel 2009 1.38
16 Multistate folding of the villin headpiece domain. J Mol Biol 2005 1.36
17 Recovery and purification of highly aggregation-prone disulfide-containing peptides: application to islet amyloid polypeptide. Anal Biochem 2005 1.36
18 Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state. J Mol Biol 2004 1.35
19 Rifampicin does not prevent amyloid fibril formation by human islet amyloid polypeptide but does inhibit fibril thioflavin-T interactions: implications for mechanistic studies of beta-cell death. Biochemistry 2008 1.32
20 Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP, a highly amyloidogenic and aggregation-prone polypeptide. Org Lett 2005 1.29
21 Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein. J Mol Biol 2002 1.28
22 Interpretation of p-cyanophenylalanine fluorescence in proteins in terms of solvent exposure and contribution of side-chain quenchers: a combined fluorescence, IR and molecular dynamics study. Biochemistry 2009 1.25
23 Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology. Biochemistry 2007 1.24
24 Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins. J Mol Biol 2005 1.21
25 The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors. Biochemistry 2010 1.21
26 Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: implications for the study of amyloid formation. Protein Sci 2002 1.20
27 Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet. Proc Natl Acad Sci U S A 2013 1.20
28 2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure. J Am Chem Soc 2011 1.20
29 Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human IAPP? J Mol Biol 2005 1.19
30 Azidohomoalanine: a conformationally sensitive IR probe of protein folding, protein structure, and electrostatics. Angew Chem Int Ed Engl 2010 1.17
31 Residue-specific, real-time characterization of lag-phase species and fibril growth during amyloid formation: a combined fluorescence and IR study of p-cyanophenylalanine analogs of islet amyloid polypeptide. J Mol Biol 2010 1.17
32 Rapid cooperative two-state folding of a miniature alpha-beta protein and design of a thermostable variant. J Mol Biol 2003 1.17
33 Strategies for extracting structural information from 2D IR spectroscopy of amyloid: application to islet amyloid polypeptide. J Phys Chem B 2009 1.16
34 Role of aromatic interactions in amyloid formation by peptides derived from human Amylin. Biochemistry 2004 1.14
35 Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols. Biochemistry 2012 1.13
36 Efficient microwave-assisted synthesis of human islet amyloid polypeptide designed to facilitate the specific incorporation of labeled amino acids. Org Lett 2010 1.13
37 Surface salt bridges, double-mutant cycles, and protein stability: an experimental and computational analysis of the interaction of the Asp 23 side chain with the N-terminus of the N-terminal domain of the ribosomal protein l9. Biochemistry 2003 1.12
38 Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding. Biochemistry 2007 1.12
39 Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J Mol Biol 2005 1.12
40 Denatured state effects and the origin of nonclassical phi values in protein folding. J Am Chem Soc 2006 1.10
41 Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity. FEBS Lett 2013 1.08
42 Two-dimensional infrared spectroscopy provides evidence of an intermediate in the membrane-catalyzed assembly of diabetic amyloid. J Phys Chem B 2009 1.07
43 Folding intermediate in the villin headpiece domain arises from disruption of a N-terminal hydrogen-bonded network. J Am Chem Soc 2007 1.07
44 Islet amyloid polypeptide toxicity and membrane interactions. Proc Natl Acad Sci U S A 2013 1.06
45 Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitors. J Am Chem Soc 2013 1.06
46 Exploiting the right side of the Ramachandran plot: substitution of glycines by D-alanine can significantly increase protein stability. J Am Chem Soc 2004 1.05
47 Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers. Protein Sci 2012 1.05
48 Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology. Curr Opin Struct Biol 2012 1.04
49 Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation. J Am Chem Soc 2010 1.04
50 Characterizing septum inhibition in Mycobacterium tuberculosis for novel drug discovery. Tuberculosis (Edinb) 2008 1.04
51 The fluorescent amino acid p-cyanophenylalanine provides an intrinsic probe of amyloid formation. Chembiochem 2008 1.03
52 Amyloid formation by pro-islet amyloid polypeptide processing intermediates: examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes. Biochemistry 2007 1.03
53 Deamidation accelerates amyloid formation and alters amylin fiber structure. J Am Chem Soc 2012 1.03
54 NMR characterization of a peptide model provides evidence for significant structure in the unfolded state of the villin headpiece helical subdomain. Biochemistry 2006 1.01
55 Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Arch Biochem Biophys 2007 1.01
56 Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II. Biochemistry 2006 1.00
57 The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation. J Mol Biol 2010 1.00
58 Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20. J Mol Biol 2011 1.00
59 Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain. Biochemistry 2007 0.99
60 Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects. Biochemistry 2012 0.99
61 Native like structure in the unfolded state of the villin headpiece helical subdomain, an ultrafast folding protein. Protein Sci 2009 0.98
62 A simple and economical method for the production of 13C,18O-labeled Fmoc-amino acids with high levels of enrichment: applications to isotope-edited IR studies of proteins. Org Lett 2007 0.98
63 Electrostatic interactions in the denatured state and in the transition state for protein folding: effects of denatured state interactions on the analysis of transition state structure. J Mol Biol 2006 0.98
64 Differential ordering of the protein backbone and side chains during protein folding revealed by site-specific recombinant infrared probes. J Am Chem Soc 2011 0.97
65 Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation. J Biol Chem 2010 0.96
66 Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure. Proc Natl Acad Sci U S A 2013 0.96
67 Characterization of large peptide fragments derived from the N-terminal domain of the ribosomal protein L9: definition of the minimum folding motif and characterization of local electrostatic interactions. Biochemistry 2002 0.95
68 Beyond the decoupling approximation in the model free approach for the interpretation of NMR relaxation of macromolecules in solution. J Am Chem Soc 2003 0.95
69 Contribution to stability and folding of a buried polar residue at the CARM1 methylation site of the KIX domain of CBP. Biochemistry 2003 0.94
70 Rational design of potent domain antibody inhibitors of amyloid fibril assembly. Proc Natl Acad Sci U S A 2012 0.94
71 The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure. Biochemistry 2009 0.93
72 Role of aromatic interactions in amyloid formation by islet amyloid polypeptide. Biochemistry 2013 0.93
73 pH-dependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9. J Mol Biol 2002 0.93
74 Direct characterization of the folded, unfolded and urea-denatured states of the C-terminal domain of the ribosomal protein L9. J Mol Biol 2005 0.93
75 Modulation of p-cyanophenylalanine fluorescence by amino acid side chains and rational design of fluorescence probes of alpha-helix formation. Biochemistry 2010 0.92
76 Analysis of core packing in a cooperatively folded miniature protein: the ultrafast folding villin headpiece helical subdomain. Biochemistry 2009 0.92
77 Partially folded equilibrium intermediate of the villin headpiece HP67 defined by 13C relaxation dispersion. J Biomol NMR 2009 0.92
78 Tuning protein autoinhibition by domain destabilization. Nat Struct Mol Biol 2011 0.92
79 phi-Values beyond the ribosomally encoded amino acids: kinetic and thermodynamic consequences of incorporating trifluoromethyl amino acids in a globular protein. J Am Chem Soc 2003 0.90
80 Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state for protein folding. J Mol Biol 2005 0.90
81 Raising the speed limit for β-hairpin formation. J Am Chem Soc 2012 0.89
82 Reconciling the solution and X-ray structures of the villin headpiece helical subdomain: molecular dynamics simulations and double mutant cycles reveal a stabilizing cation-pi interaction. Biochemistry 2007 0.89
83 Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: implications for amyloid formation. Biochemistry 2006 0.89
84 Design of a hyperstable protein by rational consideration of unfolded state interactions. J Am Chem Soc 2006 0.89
85 The unfolded state of NTL9 is compact in the absence of denaturant. Biochemistry 2006 0.88
86 Experimental characterization of the denatured state ensemble of proteins. Methods Mol Biol 2009 0.88
87 The low-pH unfolded state of the C-terminal domain of the ribosomal protein L9 contains significant secondary structure in the absence of denaturant but is no more compact than the low-pH urea unfolded state. Biochemistry 2008 0.87
88 The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9. J Mol Biol 2007 0.87
89 Nucleobindin 1 is a calcium-regulated guanine nucleotide dissociation inhibitor of G{alpha}i1. J Biol Chem 2010 0.86
90 Defining the molecular basis of amyloid inhibitors: human islet amyloid polypeptide-insulin interactions. J Am Chem Soc 2014 0.86
91 Domain-specific incorporation of noninvasive optical probes into recombinant proteins. J Am Chem Soc 2004 0.86
92 The denatured state ensemble contains significant local and long-range structure under native conditions: analysis of the N-terminal domain of ribosomal protein L9. Biochemistry 2013 0.85
93 Biophysical and functional analyses suggest that adenovirus E4-ORF3 protein requires higher-order multimerization to function against promyelocytic leukemia protein nuclear bodies. J Biol Chem 2012 0.85
94 Efficient high level expression of peptides and proteins as fusion proteins with the N-terminal domain of L9: application to the villin headpiece helical subdomain. Protein Expr Purif 2005 0.85
95 The cold denatured state of the C-terminal domain of protein L9 is compact and contains both native and non-native structure. J Am Chem Soc 2010 0.85
96 Ionic-strength-dependent effects in protein folding: analysis of rate equilibrium free-energy relationships and their interpretation. Biochemistry 2007 0.85
97 Rational modification of protein stability by targeting surface sites leads to complicated results. Proc Natl Acad Sci U S A 2013 0.84
98 Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry 2007 0.84
99 Inhibition of glycosaminoglycan-mediated amyloid formation by islet amyloid polypeptide and proIAPP processing intermediates. J Mol Biol 2010 0.84
100 Phi-value analysis for ultrafast folding proteins by NMR relaxation dispersion. J Am Chem Soc 2010 0.84
101 Mutational analysis of the ability of resveratrol to inhibit amyloid formation by islet amyloid polypeptide: critical evaluation of the importance of aromatic-inhibitor and histidine-inhibitor interactions. Biochemistry 2015 0.84
102 A critical assessment of putative gatekeeper interactions in the villin headpiece helical subdomain. J Mol Biol 2010 0.83
103 Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions. Proteins 2011 0.83
104 Temperature dependence of water interactions with the amide carbonyls of α-helices. Biochemistry 2012 0.81
105 Competition between intradomain and interdomain interactions: a buried salt bridge is essential for villin headpiece folding and actin binding. Biochemistry 2011 0.81
106 Kinetic isotope effects reveal the presence of significant secondary structure in the transition state for the folding of the N-terminal domain of L9. J Mol Biol 2007 0.81
107 Denatured state ensembles with the same radii of gyration can form significantly different long-range contacts. Biochemistry 2013 0.80
108 Ester to amide switch peptides provide a simple method for preparing monomeric islet amyloid polypeptide under physiologically relevant conditions and facilitate investigations of amyloid formation. J Am Chem Soc 2010 0.80
109 General strategy for the bioorthogonal incorporation of strongly absorbing, solvation-sensitive infrared probes into proteins. J Phys Chem B 2014 0.80
110 Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry. Analyst 2015 0.79
111 The ability of insulin to inhibit the formation of amyloid by pro-islet amyloid polypeptide processing intermediates is significantly reduced in the presence of sulfated glycosaminoglycans. Biochemistry 2014 0.79
112 pH-dependent stability of the human alpha-lactalbumin molten globule state: contrasting roles of the 6 - 120 disulfide and the beta-subdomain at low and neutral pH. Proteins 2003 0.79
113 Nucleobindin 1 caps human islet amyloid polypeptide protofibrils to prevent amyloid fibril formation. J Mol Biol 2012 0.79
114 Rational and computational design of stabilized variants of cyanovirin-N that retain affinity and specificity for glycan ligands. Biochemistry 2011 0.79
115 Cooperative cold denaturation: the case of the C-terminal domain of ribosomal protein L9. Biochemistry 2013 0.79
116 Temperature-dependent Hammond behavior in a protein-folding reaction: analysis of transition-state movement and ground-state effects. J Mol Biol 2008 0.78
117 Slow folding of a three-helix protein via a compact intermediate. Biochemistry 2005 0.78
118 Amyloid formation in heterogeneous environments: islet amyloid polypeptide glycosaminoglycan interactions. J Mol Biol 2012 0.77
119 A structural basis for the regulation of an H-NOX-associated cyclic-di-GMP synthase/phosphodiesterase enzyme by nitric oxide-bound H-NOX. Biochemistry 2014 0.77
120 A comparative study of the alpha-subdomains of bovine and human alpha-lactalbumin reveals key differences that correlate with molten globule stability. Protein Sci 2004 0.77
121 pH dependent thermodynamic and amide exchange studies of the C-terminal domain of the ribosomal protein L9: implications for unfolded state structure. Biochemistry 2006 0.77
122 Aspirin, diabetes, and amyloid: re-examination of the inhibition of amyloid formation by aspirin and ketoprofen. ACS Chem Biol 2014 0.76
123 Protein dissection experiments reveal key differences in the equilibrium folding of alpha-lactalbumin and the calcium binding lysozymes. Biochemistry 2004 0.76
124 Rationally designed, nontoxic, nonamyloidogenic analogues of human islet amyloid polypeptide with improved solubility. Biochemistry 2014 0.76
125 High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States. J Am Chem Soc 2016 0.76
126 Size-Dependent Relationships Between Protein Stability and Thermal Unfolding Temperature Have Important Implications for Analysis of Protein Energetics and High-Throughput Assays of Protein-Ligand Interactions. J Phys Chem B 2017 0.75
127 A Free Energy Barrier Caused by the Refolding of an Oligomeric Intermediate Controls the Lag Time of Amyloid Formation by hIAPP. J Am Chem Soc 2017 0.75