PubRank

Salvador Ventura

Author PubWeight™ 82.02‹?›

Top papers

Rank Title Journal Year PubWeight™‹?›
1 AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides. BMC Bioinformatics 2007 3.02
2 Amyloid-like properties of bacterial inclusion bodies. J Mol Biol 2005 1.90
3 Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins. Microb Cell Fact 2005 1.79
4 Prediction of "hot spots" of aggregation in disease-linked polypeptides. BMC Struct Biol 2005 1.34
5 Design, selection, and characterization of thioflavin-based intercalation compounds with metal chelating properties for application in Alzheimer's disease. J Am Chem Soc 2009 1.32
6 Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities. FEBS J 2006 1.29
7 Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin. Proc Natl Acad Sci U S A 2005 1.25
8 Amyloids in bacterial inclusion bodies. Trends Biochem Sci 2009 1.24
9 Inclusion bodies: specificity in their aggregation process and amyloid-like structure. Biochim Biophys Acta 2008 1.24
10 Protein aggregation: mechanisms and functional consequences. Int J Biochem Cell Biol 2012 1.20
11 Recent structural and computational insights into conformational diseases. Curr Med Chem 2008 1.12
12 Prion and non-prion amyloids of the HET-s prion forming domain. J Mol Biol 2007 1.11
13 Protein folding and aggregation in bacteria. Cell Mol Life Sci 2010 1.10
14 Folding of small disulfide-rich proteins: clarifying the puzzle. Trends Biochem Sci 2006 1.07
15 Amyloid fibril formation by a partially structured intermediate state of alpha-chymotrypsin. J Mol Biol 2004 1.06
16 Effect of temperature on protein quality in bacterial inclusion bodies. FEBS Lett 2006 1.05
17 Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates. J Biotechnol 2006 1.02
18 Detection of transient protein-protein interactions by bimolecular fluorescence complementation: the Abl-SH3 case. Proteomics 2007 1.02
19 AGGRESCAN: method, application, and perspectives for drug design. Methods Mol Biol 2012 1.01
20 Bacterial inclusion bodies of Alzheimer's disease β-amyloid peptides can be employed to study native-like aggregation intermediate states. Chembiochem 2011 1.01
21 Biological role of bacterial inclusion bodies: a model for amyloid aggregation. FEBS J 2011 1.01
22 Prediction of the aggregation propensity of proteins from the primary sequence: aggregation properties of proteomes. Biotechnol J 2011 0.99
23 Study and selection of in vivo protein interactions by coupling bimolecular fluorescence complementation and flow cytometry. Nat Protoc 2008 0.96
24 Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion. Microb Cell Fact 2009 0.95
25 Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains. BMC Genomics 2013 0.95
26 The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells. Microb Cell Fact 2006 0.95
27 Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases. PLoS Comput Biol 2009 0.94
28 Sulfated polysaccharides promote the assembly of amyloid beta(1-42) peptide into stable fibrils of reduced cytotoxicity. J Biol Chem 2008 0.93
29 Ile-phe dipeptide self-assembly: clues to amyloid formation. Biophys J 2006 0.93
30 Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation. Mol Biosyst 2012 0.92
31 Using bacterial inclusion bodies to screen for amyloid aggregation inhibitors. Microb Cell Fact 2012 0.92
32 Modulation of Abeta42 fibrillogenesis by glycosaminoglycan structure. FASEB J 2010 0.91
33 Protein aggregation profile of the bacterial cytosol. PLoS One 2010 0.90
34 PrionScan: an online database of predicted prion domains in complete proteomes. BMC Genomics 2014 0.90
35 Evolutionary selection for protein aggregation. Biochem Soc Trans 2012 0.89
36 Yeast prions form infectious amyloid inclusion bodies in bacteria. Microb Cell Fact 2012 0.88
37 Studies on bacterial inclusion bodies. Future Microbiol 2008 0.88
38 Linking amyloid protein aggregation and yeast survival. Mol Biosyst 2011 0.88
39 Protein complementation assays: approaches for the in vivo analysis of protein interactions. FEBS Lett 2009 0.87
40 Modeling amyloids in bacteria. Microb Cell Fact 2012 0.87
41 The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case. J Mol Biol 2008 0.87
42 Scrambled isomers as key intermediates in the oxidative folding of ligand binding module 5 of the low density lipoprotein receptor. J Biol Chem 2008 0.86
43 Human kallikrein 6 activity is regulated via an autoproteolytic mechanism of activation/inactivation. Biol Chem 2004 0.86
44 The effect of amyloidogenic peptides on bacterial aging correlates with their intrinsic aggregation propensity. J Mol Biol 2011 0.84
45 Amyloid-like protein inclusions in tobacco transgenic plants. PLoS One 2010 0.84
46 Thioflavin-T excimer formation upon interaction with amyloid fibers. Chem Commun (Camb) 2013 0.83
47 Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case. Antioxid Redox Signal 2011 0.83
48 Detecting and interfering protein interactions: towards the control of biochemical pathways. Curr Med Chem 2009 0.83
49 Native structure protects SUMO proteins from aggregation into amyloid fibrils. Biomacromolecules 2012 0.83
50 Direct interaction between a human digestive protease and the mucoadhesive poly(acrylic acid). Acta Crystallogr D Biol Crystallogr 2008 0.83
51 The role of protein sequence and amino acid composition in amyloid formation: scrambling and backward reading of IAPP amyloid fibrils. J Mol Biol 2010 0.83
52 Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli. Biotechnol J 2014 0.83
53 The aggregation properties of Escherichia coli proteins associated with their cellular abundance. Biotechnol J 2011 0.82
54 Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis. Int J Mol Sci 2013 0.82
55 Kinetic and thermodynamic stability of bacterial intracellular aggregates. FEBS Lett 2008 0.82
56 Monitoring the interference of protein-protein interactions in vivo by bimolecular fluorescence complementation: the DnaK case. Proteomics 2008 0.82
57 Temperature dependence of the aggregation kinetics of Sup35 and Ure2p yeast prions. Biomacromolecules 2011 0.82
58 Folding specificity induced by loop stiffness. Protein Sci 2003 0.82
59 N-terminal protein tails act as aggregation protective entropic bristles: the SUMO case. Biomacromolecules 2014 0.81
60 Deciphering the role of the thermodynamic and kinetic stabilities of SH3 domains on their aggregation inside bacteria. Proteomics 2010 0.81
61 Design and NMR conformational study of a beta-sheet peptide based on Betanova and WW domains. Protein Sci 2006 0.81
62 Characterizing the tick carboxypeptidase inhibitor: molecular basis for its two-domain nature. J Biol Chem 2006 0.81
63 Cross-β-sheet supersecondary structure in amyloid folds: techniques for detection and characterization. Methods Mol Biol 2013 0.81
64 Amyloids or prions? That is the question. Prion 2015 0.80
65 Protein aggregation propensity is a crucial determinant of intracellular inclusion formation and quality control degradation. Biochim Biophys Acta 2013 0.80
66 Secondary binding site of the potato carboxypeptidase inhibitor. Contribution to its structure, folding, and biological properties. Biochemistry 2004 0.79
67 Self-assembly of human latexin into amyloid-like oligomers. BMC Struct Biol 2007 0.79
68 Role of kinetic intermediates in the folding of leech carboxypeptidase inhibitor. J Biol Chem 2004 0.79
69 NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor. Structure 2005 0.78
70 Oxidative folding of leech-derived tryptase inhibitor via native disulfide-bonded intermediates. Antioxid Redox Signal 2008 0.78
71 Effect of the surface charge of artificial model membranes on the aggregation of amyloid β-peptide. Biochimie 2012 0.78
72 Designing out disulfide bonds of leech carboxypeptidase inhibitor: implications for its folding, stability and function. J Mol Biol 2009 0.78
73 About targets and causes in protein folding. J Biomol Struct Dyn 2013 0.78
74 Protein oxidative folding in the intermembrane mitochondrial space: more than protein trafficking. Curr Protein Pept Sci 2012 0.77
75 The mitochondrial intermembrane space oxireductase Mia40 funnels the oxidative folding pathway of the cytochrome c oxidase assembly protein Cox19. J Biol Chem 2014 0.77
76 Trifluoroethanol modulates amyloid formation by the all α-helical URN1 FF domain. Int J Mol Sci 2013 0.77
77 The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain. PLoS One 2013 0.77
78 Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor. J Biol Chem 2009 0.77
79 Zinc induced folding is essential for TIM15 activity as an mtHsp70 chaperone. Biochim Biophys Acta 2012 0.77
80 Protein aggregation profile of the human kinome. Front Physiol 2012 0.77
81 Characterization of amyloid-like properties in bacterial intracellular aggregates. Methods Mol Biol 2015 0.76
82 Protease inhibitors as models for the study of oxidative folding. Antioxid Redox Signal 2010 0.76
83 Association between foldability and aggregation propensity in small disulfide-rich proteins. Antioxid Redox Signal 2014 0.76
84 The NMR structures of the major intermediates of the two-domain tick carboxypeptidase inhibitor reveal symmetry in its folding and unfolding pathways. J Biol Chem 2008 0.76
85 Discovery of novel inhibitors of amyloid β-peptide 1-42 aggregation. J Med Chem 2012 0.76
86 Aggregation of the neuroblastoma-associated mutant (S120G) of the human nucleoside diphosphate kinase-A/NM23-H1 into amyloid fibrils. Naunyn Schmiedebergs Arch Pharmacol 2011 0.76
87 Oxidative folding in the mitochondrial intermembrane space in human health and disease. Int J Mol Sci 2013 0.75
88 Screening for amyloid aggregation: in-silico, in-vitro and in-vivo detection. Curr Protein Pept Sci 2014 0.75
89 Structure and dynamics of the potato carboxypeptidase inhibitor by 1H and 15N NMR. Proteins 2003 0.75
90 Molecular dynamics study of amyloid formation of two Abl-SH3 domain peptides. J Pept Sci 2006 0.75
91 Study of a major intermediate in the oxidative folding of leech carboxypeptidase inhibitor: contribution of the fourth disulfide bond. J Mol Biol 2005 0.75
92 Multiple β-sheet molecular dynamics of amyloid formation from two ABl-SH3 domain peptides. Biopolymers 2012 0.75
93 Oxidative protein folding: from the test tube to in vivo insights. Antioxid Redox Signal 2008 0.75
94 Dynamics study on single and multiple beta-sheets. Adv Exp Med Biol 2009 0.75