CHITI, FABRIZIO
 Distribuzione geografica
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Continente #
NA - Nord America 8013
EU - Europa 7398
AS - Asia 290
AF - Africa 25
Continente sconosciuto - Info sul continente non disponibili 1
SA - Sud America 1
Totale 15728
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Nazione #
US - Stati Uniti d'America 7994
PL - Polonia 4340
IE - Irlanda 862
IT - Italia 602
SE - Svezia 593
DE - Germania 349
UA - Ucraina 304
FI - Finlandia 150
VN - Vietnam 118
GB - Regno Unito 110
CN - Cina 97
TR - Turchia 39
FR - Francia 19
CA - Canada 17
ES - Italia 17
BE - Belgio 16
SC - Seychelles 16
KR - Corea 13
IN - India 12
NL - Olanda 9
AT - Austria 8
BG - Bulgaria 5
IR - Iran 5
RO - Romania 5
CH - Svizzera 4
CM - Camerun 4
MU - Mauritius 3
RU - Federazione Russa 3
JP - Giappone 2
SG - Singapore 2
BR - Brasile 1
CZ - Repubblica Ceca 1
DK - Danimarca 1
EG - Egitto 1
EU - Europa 1
GT - Guatemala 1
IL - Israele 1
MX - Messico 1
TW - Taiwan 1
ZA - Sudafrica 1
Totale 15728
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Città #
Warsaw 4340
Fairfield 1509
Dublin 862
Chandler 756
Woodbridge 707
Ashburn 643
Seattle 626
Cambridge 568
Houston 552
Wilmington 538
Jacksonville 491
Ann Arbor 252
Altamura 248
Lawrence 216
Princeton 206
Florence 144
Boston 143
Bremen 128
Boardman 110
Dong Ket 106
San Diego 85
Medford 67
Beijing 64
Buffalo 43
Norwalk 36
Izmir 33
Phoenix 30
Auburn Hills 27
Milan 20
Andover 19
Barcelona 17
Falls Church 17
Brussels 16
Dearborn 15
Redwood City 15
Toronto 13
Frankfurt Am Main 11
London 11
Seongnam 9
Castelliri 8
Salerno 8
Verona 8
Vienna 8
Guangzhou 7
Philadelphia 7
Chicago 5
Los Angeles 5
Naples 5
Sofia 5
Dallas 4
Munich 4
Serra 4
Timisoara 4
Fuzhou 3
Hefei 3
Laurel 3
Nanjing 3
Old Bridge 3
Ottawa 3
Padova 3
Pisa 3
Pittsburgh 3
Redmond 3
San Mateo 3
Venice 3
Wuhan 3
Xian 3
Brentford 2
Caravaggio 2
Genova 2
Groningen 2
Hebei 2
Helsinki 2
Kunming 2
Myrtle Beach 2
Napoli 2
Nürnberg 2
Parma 2
Prato 2
San Marcos 2
Siena 2
Tamm 2
Torrita di Siena 2
Alexandria 1
Anghiari 1
Ardebil 1
Augusta 1
Brixen 1
Bromma 1
Brooklyn 1
Castelfiorentino 1
Catonsville 1
Cedar Knolls 1
Cernobbio 1
Chianciano Terme 1
Cornigliano 1
Curitiba 1
Dung 1
Empoli 1
Falkenstein 1
Totale 13866
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Nome #
(1)H, (13)C and (15)N resonance assignments of human muscle acylphosphatase 276
Insight into the structure of amyloid fibrils from the analysis of globular proteins 253
A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation 229
The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosis 224
A causative link between the structure of aberrant protein oligomers and their toxicity 221
Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia 221
Aggregation propensity of the human proteome 215
Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases 214
Patterns of cell death triggered in two different cell lines by HypF-N prefibrillar aggregates. 212
Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils 209
Quantification of the Relative Contributions of Loss-of function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies 209
The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain. 208
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity 205
TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells 205
Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy 203
Soluble Oligomers Require a Ganglioside to Trigger Neuronal Calcium Overload 200
Chaperones in Neurodegeneration 198
TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells 198
The contribution of acidic residues to the conformational stability of common-type acylphosphatase 197
Effect of molecular chaperones on aberrant protein oligomers in vitro: super- versus sub-stoichiometric chaperone concentrations 195
Systematic in vivo analysis of the intrinsic determinants of amyloid Beta pathogenicity 193
TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells 189
Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions 188
Cloning, expression and characterization of a new human LMW-PTP isoform originating by alternative splicing 187
Thermodynamics and kinetics of folding of common type acylphosphatase 180
Toxic HypF-N oligomers selectively bind the plasma membrane to impair cell adhesion capability 178
Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Ther42 and Thr46 169
Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers 160
Single particle tracking to study the binding of protein misfolded oligomer to membrane ganglioside GM1 159
Molecular links between aberrant protein oligomers and neurodegeneration in Alzheimer’s disease 154
Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers 143
Capturing Aβ42 aggregation in the cell 140
Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes 139
Partial Failure of Proteostasis Systems Counteracting TDP-43 Aggregates in Neurodegenerative Diseases 131
Multistep Inhibition of α‑Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine 126
The toxicity of misfolded protein oligomers is independent of their secondary structure 125
The polyphenol Oleuropein aglycone hinders the growth of toxic transthyretin amyloid assemblies 117
Identification of Novel 1,3,5-Triphenylbenzene Derivative Compounds as Inhibitors of Hen Lysozyme Amyloid Fibril Formation 113
Probing the origin of the toxicity of oligomeric aggregates of α-synuclein with antibodies 109
Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: insights into the effect of pH on protein fibrillogenesis 103
Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity 101
Probing conformational changes of monomeric transthyretin with second derivative fluorescence 100
Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases. 99
Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates 97
Amyloid Fibril Formation can Proceed from Different Conformations of a Partially Unfolded Protein 94
Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. 93
Prevention of amyloid-like aggregation as a driving force of protein evolution 92
Isolation and characterization of soluble human full-length TDP-43 associated with neurodegeneration 89
Characterizing intermolecular interactions that initiate native-like protein aggregation. 88
Mutational Analysis of the Aggregation-Prone and Disaggregation-Prone Regions of Acylphosphatase. 87
The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity 87
A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state. 86
Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity 86
Amyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanism 85
Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase 85
Conformational properties of the aggregation precursor state of HypF-N 84
Protein misfolding, functional amyloid, and human disease 83
C-terminal region contributes to muscle acylphosphatase three-dimensional structure stabilisation 83
EQUILIBRIUM COLLAPSE AND THE KINETIC 'FOLDABILITY' OF PROTEINS. 82
PROTEIN AGGREGATION STARTING FROM THE NATIVE GLOBULAR STATE 82
The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. 82
Protein misfolding, amyloid formation, and human disease: A summary of progress over the last decade 82
Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. 81
Sequence and structural determinants of amyloid fibril formation 81
Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation. 81
A Complex Equilibrium among Partially Unfolded Conformations in Monomeric Transthyretin 81
Amyloid formation from HypF-N under conditions in which the protein is initially in its native state 80
Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation. 79
Searching for conditions to form stable protein oligomers with amyloid-like characteristics: The unexplored basic pH 79
Prefibrillar amyloid aggregates could be generic toxins in higher organisms 79
Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers 79
Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway 78
Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N 78
SERS Detection of Amyloid Oligomers on Metallorganic-Decorated Plasmonic Beads 78
Amyloid formation by globular proteins under native conditions 77
Detection of populations of amyloid-like protofibrils with different physical properties. 77
Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers 76
Biological function in a non-native partially folded state of a protein. 75
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 75
Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies 75
Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding. 74
Monitoring equilibria and kinetics of proteins folding/unfolding reactions by capillary zone electrophoresis 74
Investigating the effects of mutations on protein aggregation in the cell. 74
Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro 74
Glycosaminoglycans (GAGs) Suppress the Toxicity of HypF-N Prefibrillar Aggregates 74
Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis 73
Rationalization of the effects of mutations on peptide and protein aggregation rates 73
Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration and pH 73
A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells 73
Extracellular chaperones prevent Aβ42-induced toxicity in rat brains 73
The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution 72
Prefibrillar amyloid protein aggregates share common features of cytotoxicity 72
Reversal of protein aggregation provides evidence for multiple aggregated states 72
FRET studies of various conformational states adopted by transthyretin 72
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases 71
Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case. 70
Characterization of a novel Drosophila melanogaster acylphosphatase 70
Nanoscopic insights into the surface conformation of neurotoxic amyloid b oligomers 70
Mutations of Profilin-1 Associated with Amyotrophic Lateral Sclerosis Promote Aggregation Due to Structural Changes of Its Native State 69
Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. 69
Totale 12093
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Categoria #
all - tutte 23305
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 23305
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Totale Lug Ago Sett Ott Nov Dic Gen Feb Mar Apr Mag Giu
2017/2018654 0000 00 066 168175126119
2018/20192327 677312666 22368 9575 128294614498
2019/20204456 345436127382 524512 450574 42524135981
2020/20212871 226275155351 131347 118248 224416123257
2021/20221292 7815610233 4758 6382 5674231312
2022/20233112 321615192405 298684 5970 0000
Totale 15966