CHITI, FABRIZIO
 Distribuzione geografica
Salva come PNG Salva come JPEG
Continente #
NA - Nord America 12.881
EU - Europa 10.257
AS - Asia 1.581
AF - Africa 63
OC - Oceania 9
SA - Sud America 8
Continente sconosciuto - Info sul continente non disponibili 1
Totale 24.800
Salva come PNG Salva come JPEG
Nazione #
US - Stati Uniti d'America 12.851
PL - Polonia 4.346
RU - Federazione Russa 2.409
IE - Irlanda 848
IT - Italia 755
SE - Svezia 692
SG - Singapore 448
HK - Hong Kong 375
DE - Germania 366
UA - Ucraina 306
CN - Cina 281
IN - India 224
FI - Finlandia 206
GB - Regno Unito 155
VN - Vietnam 118
CH - Svizzera 61
JO - Giordania 46
TR - Turchia 41
CI - Costa d'Avorio 38
CA - Canada 28
FR - Francia 27
ES - Italia 26
KR - Corea 24
NL - Olanda 20
SC - Seychelles 16
BE - Belgio 15
IR - Iran 13
BR - Brasile 7
RO - Romania 7
AU - Australia 5
BG - Bulgaria 5
AT - Austria 4
CM - Camerun 4
NZ - Nuova Zelanda 4
CZ - Repubblica Ceca 3
DK - Danimarca 3
MU - Mauritius 3
IL - Israele 2
JP - Giappone 2
LT - Lituania 2
PH - Filippine 2
AZ - Azerbaigian 1
CO - Colombia 1
EG - Egitto 1
EU - Europa 1
GE - Georgia 1
GT - Guatemala 1
IQ - Iraq 1
KG - Kirghizistan 1
LU - Lussemburgo 1
MX - Messico 1
TW - Taiwan 1
ZA - Sudafrica 1
Totale 24.800
Salva come PNG Salva come JPEG
Città #
Warsaw 4.340
Santa Clara 3.142
Fairfield 1.526
Dublin 848
Chandler 809
Ashburn 805
Woodbridge 717
Seattle 644
Cambridge 573
Houston 557
Wilmington 544
Jacksonville 495
Singapore 354
Ann Arbor 253
Altamura 248
Lawrence 218
Hong Kong 215
Princeton 208
Florence 163
Boardman 150
Boston 145
Mumbai 132
Bremen 129
Dong Ket 106
Moscow 86
San Diego 85
Beijing 77
Pune 75
Medford 68
Bern 56
Milan 53
Shanghai 53
Buffalo 43
Helsinki 39
Abidjan 38
Norwalk 38
Izmir 34
New York 30
Phoenix 30
Auburn Hills 27
Kent 27
Los Angeles 25
West Jordan 24
Barcelona 23
London 23
Andover 19
Hillsboro 18
Lappeenranta 18
Falls Church 17
Redwood City 16
Toronto 16
Yubileyny 16
Dearborn 15
Brussels 14
Seoul 12
Frankfurt Am Main 11
Guangzhou 10
Naples 9
Seongnam 9
Castelliri 8
Salerno 8
Verona 8
Philadelphia 7
Prato 6
Rome 6
Chicago 5
Orenburg 5
Perth 5
Peterborough 5
Sofia 5
Washington 5
Wuhan 5
Dallas 4
Fuzhou 4
Krakow 4
Livorno 4
Munich 4
Ottawa 4
Padova 4
Pisa 4
Poggio a Caiano 4
San Mateo 4
Serra 4
Shenzhen 4
Siena 4
Tappahannock 4
Tehran 4
Timisoara 4
Turin 4
Cagliari 3
Carmignano 3
Chiswick 3
Dunedin 3
Epsom 3
Falkenstein 3
Grenoble 3
Groningen 3
Hefei 3
Laurel 3
Nanjing 3
Totale 18.654
Salva come PNG Salva come JPEG
Nome #
(1)H, (13)C and (15)N resonance assignments of human muscle acylphosphatase 439
Insight into the structure of amyloid fibrils from the analysis of globular proteins 290
The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosis 285
A causative link between the structure of aberrant protein oligomers and their toxicity 282
A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation 281
Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils 271
Aggregation propensity of the human proteome 267
TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells 261
Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia 258
Patterns of cell death triggered in two different cell lines by HypF-N prefibrillar aggregates. 256
Quantification of the Relative Contributions of Loss-of function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies 253
Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases 252
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity 247
Soluble Oligomers Require a Ganglioside to Trigger Neuronal Calcium Overload 247
Effect of molecular chaperones on aberrant protein oligomers in vitro: super- versus sub-stoichiometric chaperone concentrations 244
TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells 243
TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells 242
Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy 240
Cloning, expression and characterization of a new human LMW-PTP isoform originating by alternative splicing 239
The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain. 238
Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions 231
Toxic HypF-N oligomers selectively bind the plasma membrane to impair cell adhesion capability 227
The contribution of acidic residues to the conformational stability of common-type acylphosphatase 221
Chaperones in Neurodegeneration 220
Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicity 215
Thermodynamics and kinetics of folding of common type acylphosphatase 208
Protein misfolding, amyloid formation, and human disease: A summary of progress over the last decade 203
Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers 199
Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Ther42 and Thr46 197
Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers 194
Single particle tracking to study the binding of protein misfolded oligomer to membrane ganglioside GM1 192
Partial Failure of Proteostasis Systems Counteracting TDP-43 Aggregates in Neurodegenerative Diseases 189
Molecular links between aberrant protein oligomers and neurodegeneration in Alzheimer’s disease 188
Capturing Aβ42 aggregation in the cell 184
The toxicity of misfolded protein oligomers is independent of their secondary structure 178
Multistep Inhibition of α‑Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine 172
Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes 166
Identification of Novel 1,3,5-Triphenylbenzene Derivative Compounds as Inhibitors of Hen Lysozyme Amyloid Fibril Formation 162
The polyphenol Oleuropein aglycone hinders the growth of toxic transthyretin amyloid assemblies 149
Isolation and characterization of soluble human full-length TDP-43 associated with neurodegeneration 149
Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity 148
Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates 145
Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity 145
Probing conformational changes of monomeric transthyretin with second derivative fluorescence 144
Nanoscopic insights into the surface conformation of neurotoxic amyloid b oligomers 143
The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity 141
Amyloid Fibril Formation can Proceed from Different Conformations of a Partially Unfolded Protein 140
Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: insights into the effect of pH on protein fibrillogenesis 139
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers 138
Probing the origin of the toxicity of oligomeric aggregates of α-synuclein with antibodies 137
PROTEIN AGGREGATION STARTING FROM THE NATIVE GLOBULAR STATE 136
Sequence and structural determinants of amyloid fibril formation 136
Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies 134
Characterizing intermolecular interactions that initiate native-like protein aggregation. 133
Amyloid formation from HypF-N under conditions in which the protein is initially in its native state 132
A Complex Equilibrium among Partially Unfolded Conformations in Monomeric Transthyretin 131
Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases. 129
Glycosaminoglycans (GAGs) Suppress the Toxicity of HypF-N Prefibrillar Aggregates 129
A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells 128
Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase 128
Mutations of Profilin-1 Associated with Amyotrophic Lateral Sclerosis Promote Aggregation Due to Structural Changes of Its Native State 127
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 126
A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state. 126
Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro 125
Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. 124
SERS Detection of Amyloid Oligomers on Metallorganic-Decorated Plasmonic Beads 124
Extracellular chaperones prevent Aβ42-induced toxicity in rat brains 123
Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N 123
Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers 123
FRET studies of various conformational states adopted by transthyretin 123
Biological function in a non-native partially folded state of a protein. 122
Nanoscale Discrimination between Toxic and Nontoxic Protein Misfolded Oligomers with Tip-Enhanced Raman Spectroscopy 121
Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism 121
Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. 118
C-terminal region contributes to muscle acylphosphatase three-dimensional structure stabilisation 117
Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus. 117
Prevention of amyloid-like aggregation as a driving force of protein evolution 116
Conformational properties of the aggregation precursor state of HypF-N 115
Bis(indolyl)phenylmethane derivatives are effective small molecules for inhibition of amyloid fibril formation by hen lysozyme 115
Protein misfolding, functional amyloid, and human disease 114
Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes 114
Structural differences between toxic and nontoxic HypF-N oligomers 114
Prediction of amyloid aggregation in vivo 113
Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state. 112
Amyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanism 112
Differential interactome and innate immune response activation of two structurally distinct misfolded protein oligomers 112
Very rapid amyloid fibril formation by a bacterial lipase in the absence of a detectable lag phase 111
Quantitative assessment of the degradation of aggregated TDP-43 mediated by the ubiquitin proteasome system and macroautophagy 111
Mutational Analysis of the Aggregation-Prone and Disaggregation-Prone Regions of Acylphosphatase. 111
EQUILIBRIUM COLLAPSE AND THE KINETIC 'FOLDABILITY' OF PROTEINS. 110
Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway 110
Searching for conditions to form stable protein oligomers with amyloid-like characteristics: The unexplored basic pH 110
Investigation of the effects of copper ions on protein aggregation using a model system. 110
Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation. 109
Characterization of a novel Drosophila melanogaster acylphosphatase 109
Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation. 109
The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. 109
Prefibrillar amyloid aggregates could be generic toxins in higher organisms 109
Rationalization of the effects of mutations on peptide and protein aggregation rates 108
Amyloid formation by globular proteins under native conditions 108
Totale 16.546
Salva come PNG Salva come JPEG
Categoria #
all - tutte 64.452
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 64.452
Salva come PNG Salva come JPEG


Totale Lug Ago Sett Ott Nov Dic Gen Feb Mar Apr Mag Giu
2019/20202.664 0 0 0 0 0 517 455 579 429 242 361 81
2020/20212.897 229 275 157 362 131 348 119 250 225 418 125 258
2021/20221.302 78 157 103 34 47 58 64 83 56 74 233 315
2022/20233.781 324 618 194 406 299 683 511 160 361 29 118 78
2023/20241.446 61 181 213 75 99 254 59 264 24 87 71 58
2024/20256.892 274 968 541 1.413 2.815 881 0 0 0 0 0 0
Totale 25.062