CHITI, FABRIZIO
 Distribuzione geografica
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Continente #
NA - Nord America 9.086
EU - Europa 7.735
AS - Asia 854
AF - Africa 24
OC - Oceania 9
SA - Sud America 6
Continente sconosciuto - Info sul continente non disponibili 1
Totale 17.715
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Nazione #
US - Stati Uniti d'America 9.064
PL - Polonia 4.346
IE - Irlanda 847
IT - Italia 710
SE - Svezia 690
HK - Hong Kong 374
DE - Germania 359
UA - Ucraina 300
FI - Finlandia 153
GB - Regno Unito 141
CN - Cina 131
VN - Vietnam 118
IN - India 92
CH - Svizzera 60
JO - Giordania 47
RU - Federazione Russa 41
TR - Turchia 40
ES - Italia 25
FR - Francia 23
CA - Canada 20
SG - Singapore 20
SC - Seychelles 15
BE - Belgio 14
KR - Corea 13
IR - Iran 12
NL - Olanda 10
RO - Romania 7
BR - Brasile 6
AU - Australia 5
BG - Bulgaria 5
CM - Camerun 4
NZ - Nuova Zelanda 4
MU - Mauritius 3
CZ - Repubblica Ceca 2
IL - Israele 2
JP - Giappone 2
AT - Austria 1
DK - Danimarca 1
EG - Egitto 1
EU - Europa 1
GT - Guatemala 1
IQ - Iraq 1
MX - Messico 1
PH - Filippine 1
TW - Taiwan 1
ZA - Sudafrica 1
Totale 17.715
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Città #
Warsaw 4.340
Fairfield 1.520
Dublin 847
Chandler 808
Ashburn 796
Woodbridge 712
Seattle 641
Cambridge 569
Houston 557
Wilmington 542
Jacksonville 488
Ann Arbor 253
Altamura 246
Hong Kong 217
Lawrence 217
Princeton 207
Florence 154
Boston 143
Boardman 141
Bremen 129
Dong Ket 106
San Diego 85
Pune 77
Beijing 74
Medford 68
Bern 56
Milan 47
Buffalo 43
Norwalk 38
Izmir 34
New York 30
Phoenix 30
Moscow 28
Auburn Hills 26
West Jordan 24
Barcelona 23
London 22
Shanghai 20
Andover 19
Hillsboro 18
Falls Church 17
Redwood City 16
Dearborn 15
Brussels 14
Toronto 14
Frankfurt Am Main 11
Singapore 11
Los Angeles 10
Seongnam 9
Castelliri 8
Naples 8
Salerno 8
Verona 8
Guangzhou 7
Philadelphia 7
Helsinki 5
Orenburg 5
Rome 5
Sofia 5
Washington 5
Chicago 4
Dallas 4
Krakow 4
Munich 4
Padova 4
Pisa 4
Poggio a Caiano 4
Prato 4
San Mateo 4
Serra 4
Siena 4
Tappahannock 4
Tehran 4
Timisoara 4
Cagliari 3
Carmignano 3
Chiswick 3
Dunedin 3
Fuzhou 3
Hefei 3
Laurel 3
Nanjing 3
Old Bridge 3
Ottawa 3
Perugia 3
Pittsburgh 3
Redmond 3
Venice 3
Wuhan 3
Xian 3
Americana 2
Brisbane 2
Bucharest 2
Caravaggio 2
Codroipo 2
Concord 2
Genova 2
Grodzisk Mazowiecki 2
Groningen 2
Hebei 2
Totale 14.707
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Nome #
(1)H, (13)C and (15)N resonance assignments of human muscle acylphosphatase 358
Insight into the structure of amyloid fibrils from the analysis of globular proteins 266
A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation 246
A causative link between the structure of aberrant protein oligomers and their toxicity 236
The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosis 235
Aggregation propensity of the human proteome 228
Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia 227
Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils 226
Patterns of cell death triggered in two different cell lines by HypF-N prefibrillar aggregates. 222
Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases 221
Quantification of the Relative Contributions of Loss-of function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies 219
TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells 217
The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain. 216
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity 211
Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy 209
Soluble Oligomers Require a Ganglioside to Trigger Neuronal Calcium Overload 209
Effect of molecular chaperones on aberrant protein oligomers in vitro: super- versus sub-stoichiometric chaperone concentrations 208
TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells 207
The contribution of acidic residues to the conformational stability of common-type acylphosphatase 203
Cloning, expression and characterization of a new human LMW-PTP isoform originating by alternative splicing 202
Chaperones in Neurodegeneration 201
Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions 200
TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells 197
Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicity 196
Toxic HypF-N oligomers selectively bind the plasma membrane to impair cell adhesion capability 193
Thermodynamics and kinetics of folding of common type acylphosphatase 185
Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Ther42 and Thr46 174
Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers 173
Single particle tracking to study the binding of protein misfolded oligomer to membrane ganglioside GM1 165
Molecular links between aberrant protein oligomers and neurodegeneration in Alzheimer’s disease 160
Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers 155
Capturing Aβ42 aggregation in the cell 146
Partial Failure of Proteostasis Systems Counteracting TDP-43 Aggregates in Neurodegenerative Diseases 145
Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes 141
Multistep Inhibition of α‑Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine 139
Protein misfolding, amyloid formation, and human disease: A summary of progress over the last decade 138
The toxicity of misfolded protein oligomers is independent of their secondary structure 131
The polyphenol Oleuropein aglycone hinders the growth of toxic transthyretin amyloid assemblies 121
Identification of Novel 1,3,5-Triphenylbenzene Derivative Compounds as Inhibitors of Hen Lysozyme Amyloid Fibril Formation 121
Probing the origin of the toxicity of oligomeric aggregates of α-synuclein with antibodies 114
Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: insights into the effect of pH on protein fibrillogenesis 111
Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases. 109
Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates 107
Amyloid Fibril Formation can Proceed from Different Conformations of a Partially Unfolded Protein 106
Isolation and characterization of soluble human full-length TDP-43 associated with neurodegeneration 106
Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity 105
Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. 104
Probing conformational changes of monomeric transthyretin with second derivative fluorescence 102
Prevention of amyloid-like aggregation as a driving force of protein evolution 98
The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity 98
Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity 96
Amyloid formation from HypF-N under conditions in which the protein is initially in its native state 95
Conformational properties of the aggregation precursor state of HypF-N 94
Amyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanism 93
Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase 93
Characterizing intermolecular interactions that initiate native-like protein aggregation. 93
A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state. 92
PROTEIN AGGREGATION STARTING FROM THE NATIVE GLOBULAR STATE 91
C-terminal region contributes to muscle acylphosphatase three-dimensional structure stabilisation 90
Mutational Analysis of the Aggregation-Prone and Disaggregation-Prone Regions of Acylphosphatase. 90
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers 90
A Complex Equilibrium among Partially Unfolded Conformations in Monomeric Transthyretin 89
EQUILIBRIUM COLLAPSE AND THE KINETIC 'FOLDABILITY' OF PROTEINS. 88
Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. 88
Protein misfolding, functional amyloid, and human disease 88
Sequence and structural determinants of amyloid fibril formation 88
A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells 88
Glycosaminoglycans (GAGs) Suppress the Toxicity of HypF-N Prefibrillar Aggregates 88
Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers 88
Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies 88
Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding. 87
Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N 87
SERS Detection of Amyloid Oligomers on Metallorganic-Decorated Plasmonic Beads 87
Searching for conditions to form stable protein oligomers with amyloid-like characteristics: The unexplored basic pH 86
Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation. 86
The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. 86
Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation. 84
Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway 84
Amyloid formation by globular proteins under native conditions 84
Nanoscopic insights into the surface conformation of neurotoxic amyloid b oligomers 84
Bis(indolyl)phenylmethane derivatives are effective small molecules for inhibition of amyloid fibril formation by hen lysozyme 84
Biological function in a non-native partially folded state of a protein. 83
Rationalization of the effects of mutations on peptide and protein aggregation rates 83
Investigating the effects of mutations on protein aggregation in the cell. 82
FRET studies of various conformational states adopted by transthyretin 82
Detection of populations of amyloid-like protofibrils with different physical properties. 81
Extracellular chaperones prevent Aβ42-induced toxicity in rat brains 81
Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro 81
Characterization of a novel Drosophila melanogaster acylphosphatase 81
Biophysical analysis of three novel profilin-1 variants associated with amyotrophic lateral sclerosis indicates a correlation between their aggregation propensity and the structural features of their globular state 81
Prefibrillar amyloid aggregates could be generic toxins in higher organisms 81
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases 80
The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution 80
Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis 80
Mutations of Profilin-1 Associated with Amyotrophic Lateral Sclerosis Promote Aggregation Due to Structural Changes of Its Native State 80
Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism 80
Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration and pH 79
Mutational analysis of the propensity for amyloid formation by a globular protein. 78
Prefibrillar amyloid protein aggregates share common features of cytotoxicity 77
Nanoscale Discrimination between Toxic and Nontoxic Protein Misfolded Oligomers with Tip-Enhanced Raman Spectroscopy 77
Totale 13.083
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Categoria #
all - tutte 45.946
article - articoli 0
book - libri 0
conference - conferenze 0
curatela - curatele 0
other - altro 0
patent - brevetti 0
selected - selezionate 0
volume - volumi 0
Totale 45.946
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Totale Lug Ago Sett Ott Nov Dic Gen Feb Mar Apr Mag Giu
2018/20191.419 0 0 0 0 0 0 0 0 0 296 621 502
2019/20204.470 349 436 127 380 527 513 453 576 428 241 360 80
2020/20212.886 228 274 156 361 131 346 119 249 224 417 125 256
2021/20221.296 78 157 102 34 46 58 63 82 56 74 232 314
2022/20233.784 322 615 194 406 301 686 512 162 362 29 117 78
2023/20241.291 61 180 212 76 99 255 59 267 24 58 0 0
Totale 17.974