Fabrizio Chiti
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Computer Science
Fabrizio Chiti's Degrees
- PhD Computer Science University of Florence
- Masters Computer Engineering Consorzio ICoN
- Bachelors Computer Engineering Consorzio ICoN
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(Suggest an Edit or Addition)Fabrizio Chiti's Published Works
Number of citations in a given year to any of this author's works
Total number of citations to an author for the works they published in a given year. This highlights publication of the most important work(s) by the author
Published Works
- Protein misfolding, functional amyloid, and human disease. (2006) (5662)
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases (2002) (2412)
- Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017) (1540)
- Rationalization of the effects of mutations on peptide andprotein aggregation rates (2003) (1018)
- Designing conditions for in vitro formation of amyloid protofilaments and fibrils. (1999) (1011)
- Amyloid formation by globular proteins under native conditions. (2009) (768)
- Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. (2005) (576)
- A causative link between the structure of aberrant protein oligomers and their toxicity. (2010) (513)
- Prediction of aggregation-prone regions in structured proteins. (2008) (443)
- Kinetic partitioning of protein folding and aggregation (2002) (404)
- Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers (2017) (398)
- Prefibrillar Amyloid Protein Aggregates Share Common Features of Cytotoxicity* (2004) (381)
- Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. (2004) (309)
- Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases (2002) (274)
- Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding (1999) (272)
- Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships. (2012) (248)
- Prevention of amyloid‐like aggregation as a driving force of protein evolution (2007) (244)
- Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case. (2004) (244)
- Prefibrillar Amyloid Aggregates Could Be Generic Toxins in Higher Organisms (2006) (240)
- Mutational analysis of the propensity for amyloid formation by a globular protein (2000) (232)
- Protein folding: Defining a “standard” set of experimental conditions and a preliminary kinetic data set of two‐state proteins (2005) (205)
- A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity (2017) (199)
- Insight into the Structure of Amyloid Fibrils from the Analysis of Globular Proteins (2006) (198)
- Systematic In Vivo Analysis of the Intrinsic Determinants of Amyloid β Pathogenicity (2007) (188)
- Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers (2012) (153)
- Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity. (2014) (152)
- Amyloid fibril formation can proceed from different conformations of a partially unfolded protein. (2005) (145)
- A Partially Structured Species of β2-Microglobulin Is Significantly Populated under Physiological Conditions and Involved in Fibrillogenesis* (2001) (138)
- Nature and significance of the interactions between amyloid fibrils and biological polyelectrolytes. (2006) (127)
- Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates. (2005) (126)
- Relative influence of hydrophobicity and net charge in the aggregation of two homologous proteins. (2003) (124)
- Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N‐terminal domain (2001) (117)
- Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases. (2008) (110)
- Rational design of aggregation-resistant bioactive peptides: reengineering human calcitonin. (2005) (108)
- Sequence and structural determinants of amyloid fibril formation. (2006) (106)
- Prediction of amyloid aggregation in vivo (2011) (105)
- Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin. (2001) (105)
- Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis. (2003) (103)
- Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase (2006) (100)
- Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. (2004) (98)
- Reversal of protein aggregation provides evidence for multiple aggregated States. (2005) (94)
- Investigating the Effects of Mutations on Protein Aggregation in the Cell* (2005) (91)
- Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases (2016) (90)
- Slow folding of muscle acylphosphatase in the absence of intermediates. (1998) (89)
- Acceleration of the folding of acylphosphatase by stabilization of local secondary structure (1999) (87)
- Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes (2019) (86)
- Aggregation of the Acylphosphatase from Sulfolobus solfataricus (2004) (85)
- Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation. (2005) (83)
- Chaperones in Neurodegeneration (2015) (82)
- Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers (2012) (82)
- Aggregation Propensity of the Human Proteome (2008) (81)
- Structure, Folding Dynamics, and Amyloidogenesis of D76N β2-Microglobulin (2013) (77)
- Amyloid formation from HypF-N under conditions in which the protein is initially in its native state. (2005) (77)
- SERS Detection of Amyloid Oligomers on Metallorganic-Decorated Plasmonic Beads. (2015) (73)
- The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells (2021) (72)
- TDP-43 Inclusion Bodies Formed in Bacteria Are Structurally Amorphous, Non-Amyloid and Inherently Toxic to Neuroblastoma Cells (2014) (70)
- Transthyretin suppresses the toxicity of oligomers formed by misfolded proteins in vitro. (2013) (69)
- Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility (2011) (68)
- Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol (2000) (67)
- Multistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine. (2018) (65)
- Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: insights into the effect of pH on protein fibrillogenesis. (2007) (64)
- Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state. (2005) (63)
- Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation (2001) (61)
- Extracellular chaperones prevent Aβ42-induced toxicity in rat brains. (2013) (60)
- A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells (2011) (60)
- The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution. (2007) (58)
- Kinetic Analysis of Amyloid Formation in the Presence of Heparan Sulfate (2009) (57)
- Large Proteins Have a Great Tendency to Aggregate but a Low Propensity to Form Amyloid Fibrils (2011) (55)
- Quantification of the Relative Contributions of Loss-of-function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies * (2016) (52)
- Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding. (2000) (50)
- Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions (2015) (50)
- Intrinsic determinants of neurotoxic aggregate formation by the amyloid beta peptide. (2010) (50)
- Amyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanism. (2009) (49)
- Conformational properties of the aggregation precursor state of HypF-N. (2008) (47)
- Structural characterization of the transition state for folding of muscle acylphosphatase. (1998) (46)
- Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity (2017) (46)
- Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding. (2003) (46)
- Conformational stability of muscle acylphosphatase: the role of temperature, denaturant concentration, and pH. (1998) (46)
- Capillary electrophoresis investigation of a partially unfolded conformation of β2‐microglobulin (2002) (46)
- Patterns of cell death triggered in two different cell lines by HypF‐N prefibrillar aggregates (2005) (45)
- Folding and Aggregation Are Selectively Influenced by the Conformational Preferences of the α-Helices of Muscle Acylphosphatase* (2001) (44)
- Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus (2005) (43)
- Equilibrium collapse and the kinetic 'foldability' of proteins. (2002) (43)
- Detection of populations of amyloid-like protofibrils with different physical properties. (2010) (42)
- “Native‐like aggregation” of the acylphosphatase from Sulfolobus solfataricus and its biological implications (2009) (40)
- Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation. (2008) (40)
- Looking for residues involved in the muscle acylphosphatase catalytic mechanism and structural stabilization: role of Asn41, Thr42, and Thr46. (1996) (39)
- Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-β Peptide Aggregation and Reduces the Toxicity of Its Oligomers (2020) (38)
- Biological function in a non‐native partially folded state of a protein (2008) (37)
- Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia (2016) (37)
- The polyphenol Oleuropein aglycone hinders the growth of toxic transthyretin amyloid assemblies. (2016) (37)
- Agitation and high ionic strength induce amyloidogenesis of a folded PDZ domain in native conditions. (2009) (35)
- Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzyme. (1999) (35)
- Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus. (2006) (35)
- Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway. (2006) (33)
- Relative Importance of Hydrophobicity, Net Charge, and Secondary Structure Propensities in Protein Aggregation (2006) (33)
- Soluble Oligomers Require a Ganglioside to Trigger Neuronal Calcium Overload. (2017) (32)
- Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism (2020) (32)
- Nanoscale Discrimination between Toxic and Nontoxic Protein Misfolded Oligomers with Tip-Enhanced Raman Spectroscopy. (2018) (30)
- Investigation of the effects of copper ions on protein aggregation using a model system (2004) (30)
- The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. (2004) (30)
- Amyloid-β oligomer synaptotoxicity is mimicked by oligomers of the model protein HypF-N (2013) (29)
- Monitoring equilibria and kinetics of protein folding/unfolding reactions by capillary zone electrophoresis. (2000) (29)
- Searching for conditions to form stable protein oligomers with amyloid-like characteristics: The unexplored basic pH. (2010) (29)
- The toxicity of misfolded protein oligomers is independent of their secondary structure. (2019) (29)
- Rapid oligomer formation of human muscle acylphosphatase induced by heparan sulfate (2012) (28)
- Quantitative assessment of the degradation of aggregated TDP‐43 mediated by the ubiquitin proteasome system and macroautophagy (2017) (27)
- Probing the Origin of the Toxicity of Oligomeric Aggregates of α-Synuclein with Antibodies (2019) (26)
- Structural and Folding Dynamic Properties of the T70N Variant of Human Lysozyme* (2003) (26)
- Characterizing intermolecular interactions that initiate native-like protein aggregation. (2012) (26)
- The degree of structural protection at the edge beta-strands determines the pathway of amyloid formation in globular proteins. (2008) (26)
- Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers (2021) (25)
- Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state. (2012) (25)
- Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy (2016) (24)
- Mutations of Profilin-1 Associated with Amyotrophic Lateral Sclerosis Promote Aggregation Due to Structural Changes of Its Native State. (2015) (24)
- Low-level expression of a folding-incompetent protein in Escherichia coli: search for the molecular determinants of protein aggregation in vivo. (2010) (24)
- A model for the aggregation of the acylphosphatase from Sulfolobus solfataricus in its native-like state. (2008) (23)
- Structural and Dynamics Characteristics of Acylphosphatase from Sulfolobus solfataricus in the Monomeric State and in the Initial Native-like Aggregates* (2010) (23)
- Development of Enzymatic Activity during Protein Folding (1999) (21)
- Aβ Oligomers Dysregulate Calcium Homeostasis by Mechanosensitive Activation of AMPA and NMDA Receptors (2021) (20)
- 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 (2016) (19)
- Effect of molecular chaperones on aberrant protein oligomers in vitro: super-versus sub-stoichiometric chaperone concentrations (2016) (19)
- Structural differences between toxic and nontoxic HypF-N oligomers. (2018) (18)
- Cloning, expression and characterisation of a new human low M r phosphotyrosine protein phosphatase originating by alternative splicing (1998) (18)
- Glycosaminoglycans (GAGs) suppress the toxicity of HypF-N prefibrillar aggregates. (2012) (17)
- Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. A comparative analysis with other proteins from the same superfamily. (2004) (17)
- Correction for Perni et al., A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity (2017) (17)
- Bis(indolyl)phenylmethane derivatives are effective small molecules for inhibition of amyloid fibril formation by hen lysozyme. (2016) (17)
- Partial Failure of Proteostasis Systems Counteracting TDP-43 Aggregates in Neurodegenerative Diseases (2019) (17)
- The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosis (2015) (16)
- Isolation and characterization of soluble human full‐length TDP‐43 associated with neurodegeneration (2019) (16)
- The folding process of acylphosphatase from Escherichia coli is remarkably accelerated by the presence of a disulfide bond. (2008) (15)
- The N-terminal Helix Controls the Transition between the Soluble and Amyloid States of an FF Domain (2013) (15)
- Protein aggregation starting from the native globular state. (2006) (15)
- Very rapid amyloid fibril formation by a bacterial lipase in the absence of a detectable lag phase. (2017) (14)
- Sequence‐specific recognition of peptide substrates by the low M r phosphotyrosine protein phosphatase isoforms (1998) (14)
- Edge strand engineering prevents native‐like aggregation in Sulfolobus solfataricus acylphosphatase (2014) (14)
- 1H, 13C and 15N resonance assignments of human muscle acylphosphatase (2012) (14)
- Aggregation of the Acylphosphatase from Sulfolobus solfataricus THE FOLDED AND PARTIALLY UNFOLDED STATES CAN BOTH BE PRECURSORS FOR AMYLOID FORMATION* (2004) (13)
- Structural and kinetic investigations on the 15-21 and 42-45 loops of muscle acylphosphatase: evidence for their involvement in enzyme catalysis and conformational stabilization. (1997) (13)
- Mutational analysis of the aggregation-prone and disaggregation-prone regions of acylphosphatase. (2009) (12)
- C‐terminal region contributes to muscle acylphosphatase three‐dimensional structure stabilisation (1996) (12)
- A complex equilibrium among partially unfolded conformations in monomeric transthyretin. (2014) (12)
- Rationally Designed Antibodies as Research Tools to Study the Structure–Toxicity Relationship of Amyloid-β Oligomers (2020) (11)
- Characterization of a novel Drosophila melanogaster acylphosphatase (2003) (11)
- Insight into the Folding and Dimerization Mechanisms of the N-Terminal Domain from Human TDP-43 (2020) (10)
- Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies. (2017) (10)
- Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity (2018) (10)
- Making biological membrane resistant to the toxicity of misfolded protein oligomers: a lesson from trodusquemine. (2020) (9)
- Squalamine and trodusquemine: two natural products for neurodegenerative diseases, from physical chemistry to the clinic. (2021) (9)
- A Computational Approach for Identifying the Chemical Factors Involved in the Glycosaminoglycans-Mediated Acceleration of Amyloid Fibril Formation (2010) (9)
- Nanoscopic insights into the surface conformation of neurotoxic amyloid β oligomers (2020) (9)
- Amyloid fibril formation by a normally folded protein in the absence of denaturants and agitation (2013) (8)
- The induction of α-helical structure in partially unfolded HypF-N does not affect its aggregation propensity. (2011) (8)
- Toxic HypF-N Oligomers Selectively Bind the Plasma Membrane to Impair Cell Adhesion Capability. (2018) (8)
- Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes (2020) (8)
- Differential interactome and innate immune response activation of two structurally distinct misfolded protein oligomers. (2019) (7)
- Quantitative Measurement of the Affinity of Toxic and Nontoxic Misfolded Protein Oligomers for Lipid Bilayers and of its Modulation by Lipid Composition and Trodusquemine (2021) (7)
- Probing conformational changes of monomeric transthyretin with second derivative fluorescence (2019) (7)
- Insight into the aggregation of lipase from Pseudomonas sp. using mutagenesis: protection of aggregation prone region by adoption of α-helix structure. (2018) (6)
- FRET studies of various conformational states adopted by transthyretin (2017) (6)
- Full-length TDP-43 and its C-terminal domain form filaments in vitro having non-amyloid properties (2020) (6)
- Properties of Cys21-mutated muscle acylphosphatases (1996) (6)
- Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases (2022) (6)
- Distinct responses of human peripheral blood cells to different misfolded protein oligomers (2021) (6)
- Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans (2021) (5)
- The contribution of acidic residues to the conformational stability of common-type acylphosphatase. (1999) (5)
- Pathways of Amyloid Formation (2013) (4)
- Studies on enzymatic activity and conformational stability of muscle acylphosphatase mutated at conserved lysine residues. (1998) (4)
- Small molecule protein binding to correct cellular folding or stabilize the native state against misfolding and aggregation (2022) (4)
- A quantitative biology approach correlates neuronal toxicity with the largest inclusions of TDP-43 (2022) (4)
- Misfolded protein oligomers induce an increase of intracellular Ca2+ causing an escalation of reactive oxidative species (2022) (4)
- Selection of antibody fragments specific for an alpha-helix region of acylphosphatase. (2004) (4)
- Identification of Novel 1,3,5-Triphenylbenzene Derivative Compounds as Inhibitors of Hen Lysozyme Amyloid Fibril Formation (2019) (4)
- Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerization (2000) (3)
- Selection of antibody fragments specific for an α‐helix region of acylphosphatase (2004) (3)
- A Brain-Permeable Aminosterol Regulates Cell Membranes to Mitigate the Toxicity of Diverse Pore-Forming Agents (2022) (3)
- Urea titration of a lipase from Pseudomonas sp. reveals four different conformational states, with a stable partially folded state explaining its high aggregation propensity. (2021) (3)
- The role of structural dynamics in the thermal adaptation of hyperthermophilic enzymes (2022) (2)
- Biophysical characterization of full‐length TAR DNA‐binding protein (TDP‐43) phase separation (2022) (2)
- Why Proteins Misfold (2010) (2)
- Thermodynamics and kinetics of folding of common type acylphosphatase (1999) (2)
- Conversion of the Native N-Terminal Domain of TDP-43 into a Monomeric Alternative Fold with Lower Aggregation Propensity (2022) (2)
- 1H, 13C and 15N resonance assignments of human muscle acylphosphatase (2011) (2)
- Phase II study of oral vinorelbine plus hormone therapy in hormone-refractory prostate cancer (2006) (1)
- Modulating Amyloid-Beta Aggregation to Reduce the Toxicity of its Oligomeric Aggregates (2018) (1)
- Interaction between Biomimetic Lipid Membranes and Trodusquemine: An Atomic Force Microscopy Study (2021) (1)
- Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers (2018) (1)
- Information for : “ A causative link between the structure of aberrant protein oligomers and their ability to cause cellular dysfunction (2009) (1)
- 1 WHY PROTEINS MISFOLD (2010) (1)
- Reorganization of the outer layer of a model of the plasma membrane induced by a neuroprotective aminosterol. (2022) (1)
- Soluble Prion Peptide 107–120 Protects Neuroblastoma SH-SY5Y Cells against Oligomers Associated with Alzheimer’s Disease (2020) (1)
- An in situ and in vitro investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature (2022) (1)
- FRET studies of various conformational states adopted by transthyretin (2017) (1)
- Capturing Aβ42 aggregation in the cell (2019) (1)
- Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration, 2013; 14(Suppl. 2): 200–217 P253 BIOPHYSICAL AND BIOLOGICAL CHARACTERISATION OF INCLUSION BODIES CONTAINING TDP-43 (2013) (0)
- Identification and estimation of aflatoxins in different substances. (1990) (0)
- Characterization of the aggregation competent state of the acylphosphatase from Sulfolobus solfataricus (2010) (0)
- Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism (2020) (0)
- Enzymatic activity outside the folded states of proteins (2009) (0)
- Multistep Inhibition of a-synuclein aggregation and toxicity in vitro 1 and in vivo by trodusquemine 2 3 (2019) (0)
- Evidence on the ability of molecular chaperones to bind and neutralize toxic protein oligomers and molecular insight into their mechanism of action (2011) (0)
- Mechanosensitivity of N-methyl-D-aspartate receptors (NMDAR) is the key through which amyloid beta oligomers activate them (2021) (0)
- Chaperones suppress the toxicity of aberrant protein aggregates. Molecular insight into the mechanism of action (2012) (0)
- Single particle tracking to study the binding of protein misfolded oligomer to membrane ganglioside GM1 (2014) (0)
- Studying the trafficking of labeled trodusquemine and its application as nerve marker for light‐sheet and expansion microscopy (2022) (0)
- Disaggregation Experiments as a Tool to Detect Protofibrillar Intermediates (2004) (0)
- Identification of Novel 1,3,5-Triphenylbenzene Derivative Compounds as Inhibitors of Hen Lysozyme Amyloid Fibril Formation (2019) (0)
- Sequence and Structural Deteminants of Amyloid Fibril Formation (2006) (0)
- Trace metals in human milk (1983) (0)
- Homage to Chris Dobson (2019) (0)
- Editorial overview: Folding and binding. (2022) (0)
- Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases. (2023) (0)
- The sequence determinants of amyloid fibril formation (2007) (0)
- Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes (2019) (0)
- Title Structure , Folding Dynamics , and Amyloidogenesis of D 76 N β 2-Microglobulin : ROLES OF SHEAR FLOW , HYDROPHOBIC SURFACES (0)
- Self-assembly of a globular protein into native-like and enzymatically active aggregates that subsequently reorganize to form amyloid structures (2005) (0)
- Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers (2018) (0)
- Sphingosine 1‐phosphate attenuates neuronal dysfunction induced by amyloid‐β oligomers through endocytic internalization of NMDA receptors (2022) (0)
- EGCG inactivates a pore-forming toxin by promoting its oligomerization and decreasing its solvent-exposed hydrophobicity. (2022) (0)
- C‐terminal region contributes to muscle acylphosphate three‐dimensional structure stabilisation (0)
- Mini-Symposium Chaperones in Neurodegeneration (2015) (0)
- 1H NMR Structure of Acylphosphatase from the hyperthermophile Sulfolobus Solfataricus (2005) (0)
- Crystal structure of DACM F87M/L110M Transthyretin mutant (2017) (0)
- Investigating partially unfolded conformations populated by monomeric human transthyretin (2015) (0)
- Molecular links between aberrant protein oligomers and neurodegeneration in Alzheimer’s disease (2015) (0)
- Crystal structure of DACM wild type Transthyretin (2017) (0)
- Selective Interaction between Toxic Amyloid Oligomers and the Cell Membrane Revealed by Innovative AFM Applications (2016) (0)
- The mechanisms of conversion of proteins into amyloid fibrils (2005) (0)
- Selection of scFv against cytotoxic protein aggregates (2006) (0)
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What Schools Are Affiliated With Fabrizio Chiti?
Fabrizio Chiti is affiliated with the following schools:
