CHITI, FABRIZIO
 Distribuzione geografica
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Continente #
NA - Nord America 14.568
EU - Europa 11.752
AS - Asia 5.633
SA - Sud America 804
AF - Africa 142
OC - Oceania 142
Continente sconosciuto - Info sul continente non disponibili 3
Totale 33.044
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Nazione #
US - Stati Uniti d'America 14.455
PL - Polonia 4.360
RU - Federazione Russa 3.240
SG - Singapore 1.545
CN - Cina 1.386
HK - Hong Kong 1.003
IT - Italia 864
IE - Irlanda 860
SE - Svezia 703
BR - Brasile 659
KR - Corea 620
DE - Germania 499
VN - Vietnam 375
UA - Ucraina 314
IN - India 296
FI - Finlandia 279
GB - Regno Unito 206
AU - Australia 131
ID - Indonesia 100
CH - Svizzera 96
FR - Francia 95
NL - Olanda 94
CA - Canada 53
JO - Giordania 53
TR - Turchia 53
AR - Argentina 48
JP - Giappone 46
CI - Costa d'Avorio 40
ES - Italia 37
EC - Ecuador 30
MX - Messico 30
BD - Bangladesh 27
ZA - Sudafrica 26
BE - Belgio 18
IQ - Iraq 17
CO - Colombia 16
SC - Seychelles 16
IR - Iran 14
PY - Paraguay 14
UZ - Uzbekistan 14
CL - Cile 13
MA - Marocco 13
LT - Lituania 12
AT - Austria 11
BJ - Benin 11
NZ - Nuova Zelanda 11
SK - Slovacchia (Repubblica Slovacca) 11
PH - Filippine 10
RO - Romania 10
KE - Kenya 9
VE - Venezuela 9
AZ - Azerbaigian 8
BG - Bulgaria 8
EG - Egitto 8
IL - Israele 8
PE - Perù 8
AE - Emirati Arabi Uniti 7
PK - Pakistan 7
SA - Arabia Saudita 7
AL - Albania 6
CR - Costa Rica 6
CZ - Repubblica Ceca 6
HN - Honduras 6
KG - Kirghizistan 6
KZ - Kazakistan 6
DK - Danimarca 5
HU - Ungheria 5
PA - Panama 5
BO - Bolivia 4
CM - Camerun 4
TN - Tunisia 4
TT - Trinidad e Tobago 4
BA - Bosnia-Erzegovina 3
DO - Repubblica Dominicana 3
DZ - Algeria 3
MU - Mauritius 3
MY - Malesia 3
NG - Nigeria 3
NP - Nepal 3
PT - Portogallo 3
TH - Thailandia 3
UY - Uruguay 3
AM - Armenia 2
BH - Bahrain 2
GE - Georgia 2
JM - Giamaica 2
LU - Lussemburgo 2
XK - ???statistics.table.value.countryCode.XK??? 2
AO - Angola 1
BB - Barbados 1
BT - Bhutan 1
EU - Europa 1
GA - Gabon 1
GR - Grecia 1
GT - Guatemala 1
IS - Islanda 1
KH - Cambogia 1
KW - Kuwait 1
LA - Repubblica Popolare Democratica del Laos 1
LB - Libano 1
Totale 33.034
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Città #
Warsaw 4.354
Santa Clara 3.159
Fairfield 1.527
Ashburn 1.359
Singapore 1.011
Dublin 860
Hong Kong 842
Chandler 809
Woodbridge 717
Seattle 644
Seoul 607
Cambridge 575
Houston 562
Wilmington 546
Jacksonville 496
Hefei 426
Beijing 325
Ann Arbor 255
Altamura 248
Lawrence 218
Princeton 208
Florence 195
Buffalo 175
Los Angeles 160
Boston 156
Boardman 150
Moscow 147
Mumbai 138
Bremen 129
Melbourne 126
Munich 113
Dong Ket 106
The Dalles 101
Ho Chi Minh City 97
San Diego 87
Jakarta 86
Pune 75
Kent 72
Dallas 68
Medford 68
Milan 62
New York 59
Shanghai 57
Bern 56
Hanoi 53
Paris 52
Turku 51
São Paulo 50
Clifton 48
Helsinki 41
Abidjan 40
Lappeenranta 38
Norwalk 38
Izmir 34
Phoenix 34
London 30
Redondo Beach 30
Auburn Hills 27
Barcelona 26
Bengaluru 25
West Jordan 24
Council Bluffs 21
Tokyo 21
Toronto 21
Andover 19
Brooklyn 18
Chicago 18
Hillsboro 18
Falls Church 17
Rome 17
Basel 16
Brussels 16
Guangzhou 16
Redwood City 16
Yubileyny 16
Dearborn 15
Naples 15
Rio de Janeiro 15
Tianjin 15
Brasília 14
Tashkent 14
Groningen 13
Chennai 12
Delft 12
Denver 12
Manaus 12
Montreal 12
Amsterdam 11
Cotonou 11
Frankfurt Am Main 11
Matsuyama 11
Quito 11
Utrecht 11
Belo Horizonte 10
Frankfurt am Main 10
Haaksbergen 10
Orem 10
Shenzhen 10
Stockholm 10
Da Nang 9
Totale 23.418
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Nome #
(1)H, (13)C and (15)N resonance assignments of human muscle acylphosphatase 527
Protein misfolding, amyloid formation, and human disease: A summary of progress over the last decade 437
A causative link between the structure of aberrant protein oligomers and their toxicity 361
Insight into the structure of amyloid fibrils from the analysis of globular proteins 331
The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosis 326
Aggregation propensity of the human proteome 322
A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation 321
Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils 317
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity 297
Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia 292
Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases 292
Quantification of the Relative Contributions of Loss-of function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies 288
TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells 287
Soluble Oligomers Require a Ganglioside to Trigger Neuronal Calcium Overload 285
Cloning, expression and characterization of a new human LMW-PTP isoform originating by alternative splicing 283
Patterns of cell death triggered in two different cell lines by HypF-N prefibrillar aggregates. 282
Effect of molecular chaperones on aberrant protein oligomers in vitro: super- versus sub-stoichiometric chaperone concentrations 281
TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells 279
TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells 276
Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy 266
Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers 263
Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions 258
The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain. 254
Toxic HypF-N oligomers selectively bind the plasma membrane to impair cell adhesion capability 250
The contribution of acidic residues to the conformational stability of common-type acylphosphatase 241
Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicity 236
Chaperones in Neurodegeneration 235
Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Ther42 and Thr46 226
Thermodynamics and kinetics of folding of common type acylphosphatase 225
Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers 224
Multistep Inhibition of α‑Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine 221
The toxicity of misfolded protein oligomers is independent of their secondary structure 219
Molecular links between aberrant protein oligomers and neurodegeneration in Alzheimer’s disease 219
Partial Failure of Proteostasis Systems Counteracting TDP-43 Aggregates in Neurodegenerative Diseases 218
Single particle tracking to study the binding of protein misfolded oligomer to membrane ganglioside GM1 217
Capturing Aβ42 aggregation in the cell 209
Identification of Novel 1,3,5-Triphenylbenzene Derivative Compounds as Inhibitors of Hen Lysozyme Amyloid Fibril Formation 198
Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes 192
Isolation and characterization of soluble human full-length TDP-43 associated with neurodegeneration 191
Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity 186
Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase 184
Nanoscopic insights into the surface conformation of neurotoxic amyloid b oligomers 184
PROTEIN AGGREGATION STARTING FROM THE NATIVE GLOBULAR STATE 183
Amyloid Fibril Formation can Proceed from Different Conformations of a Partially Unfolded Protein 183
A Complex Equilibrium among Partially Unfolded Conformations in Monomeric Transthyretin 181
Sphingosine 1-phosphate attenuates neuronal dysfunction induced by amyloid-β oligomers through endocytic internalization of NMDA receptors 180
Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: insights into the effect of pH on protein fibrillogenesis 180
Probing conformational changes of monomeric transthyretin with second derivative fluorescence 177
Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity 175
Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases. 174
Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates 174
The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity 174
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers 174
Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N 173
Amyloid formation from HypF-N under conditions in which the protein is initially in its native state 172
Sequence and structural determinants of amyloid fibril formation 168
Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies 168
The polyphenol Oleuropein aglycone hinders the growth of toxic transthyretin amyloid assemblies 167
A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state. 167
A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells 166
Characterizing intermolecular interactions that initiate native-like protein aggregation. 163
Quantitative Measurement of the Affinity of Toxic and Nontoxic Misfolded Protein Oligomers for Lipid Bilayers and of its Modulation by Lipid Composition and Trodusquemine 162
Mutations of Profilin-1 Associated with Amyotrophic Lateral Sclerosis Promote Aggregation Due to Structural Changes of Its Native State 162
Glycosaminoglycans (GAGs) Suppress the Toxicity of HypF-N Prefibrillar Aggregates 162
Conversion of the Native N-Terminal Domain of TDP-43 into a Monomeric Alternative Fold with Lower Aggregation Propensity 161
Probing the origin of the toxicity of oligomeric aggregates of α-synuclein with antibodies 161
Studying the trafficking of labeled trodusquemine and its application as nerve marker for light-sheet and expansion microscopy 160
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 160
Biological function in a non-native partially folded state of a protein. 158
Biophysical characterization of full-length TAR DNA-binding protein (TDP-43) phase separation. 157
An in situ and in vitro investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature 157
C-terminal region contributes to muscle acylphosphatase three-dimensional structure stabilisation 157
Making biological membrane resistant to the toxicity of misfolded protein oligomers: a lesson from trodusquemine 156
Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases 156
Reorganization of the outer layer of a model of the plasma membrane induced by a neuroprotective aminosterol 155
A quantitative biology approach correlates neuronal toxicity with the largest inclusions of TDP-43 154
Nanoscale Discrimination between Toxic and Nontoxic Protein Misfolded Oligomers with Tip-Enhanced Raman Spectroscopy 154
Extracellular chaperones prevent Aβ42-induced toxicity in rat brains 153
Bis(indolyl)phenylmethane derivatives are effective small molecules for inhibition of amyloid fibril formation by hen lysozyme 153
Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers 152
Aggregation of the acylphosphatase from S. solfataricus. The folded and partially unfolded states can be both precursors for amyloid formation. 151
Structure-toxicity relationship in intermediate fibrils from lα-Synuclein condensates 150
Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro 150
Characterization of a novel Drosophila melanogaster acylphosphatase 149
Structural differences between toxic and nontoxic HypF-N oligomers 149
FRET studies of various conformational states adopted by transthyretin 148
Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus. 147
Quantitative assessment of the degradation of aggregated TDP-43 mediated by the ubiquitin proteasome system and macroautophagy 147
Full-length TDP-43 and its C-terminal domain form filaments in vitro having non-amyloid properties 146
Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding. 145
Protein misfolding, functional amyloid, and human disease 145
SERS Detection of Amyloid Oligomers on Metallorganic-Decorated Plasmonic Beads 145
Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes 143
Very rapid amyloid fibril formation by a bacterial lipase in the absence of a detectable lag phase 143
Differential interactome and innate immune response activation of two structurally distinct misfolded protein oligomers 143
Squalamine and trodusquemine: two natural products for neurodegenerative diseases, from physical chemistry to the clinic 141
EQUILIBRIUM COLLAPSE AND THE KINETIC 'FOLDABILITY' OF PROTEINS. 141
Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism 141
Acceleration of the folding of acylphosphatase by stabilization of local secondary structure. 140
Prevention of amyloid-like aggregation as a driving force of protein evolution 140
Totale 20.393
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Categoria #
all - tutte 88.089
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 88.089
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Totale Lug Ago Sett Ott Nov Dic Gen Feb Mar Apr Mag Giu
2020/20211.743 0 0 0 0 0 348 119 250 225 418 125 258
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
2024/20259.293 274 968 541 1.413 2.815 1.131 219 440 458 234 404 396
2025/20265.876 1.231 1.519 948 767 1.228 183 0 0 0 0 0 0
Totale 33.339