| scholarly article | Q13442814 |
| P356 | DOI | 10.1021/BI030135S |
| P8608 | Fatcat ID | release_gcyonmgsangwnojm3ulqy2k2hm |
| P698 | PubMed publication ID | 14690417 |
| P50 | author | Massimo Stefani | Q56635756 |
| Niccolo Taddei | Q57476604 | ||
| Giampietro Ramponi | Q114439219 | ||
| Martino Calamai | Q39190352 | ||
| P2093 | author name string | Fabrizio Chiti | |
| P433 | issue | 51 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | Acylphosphatase | Q24722433 |
| hydrophobicity | Q41854968 | ||
| P304 | page(s) | 15078-15083 | |
| P577 | publication date | 2003-12-01 | |
| P1433 | published in | Biochemistry | Q764876 |
| P1476 | title | Relative influence of hydrophobicity and net charge in the aggregation of two homologous proteins | |
| P478 | volume | 42 |
| Q30428011 | A polymetamorphic protein |
| Q43203312 | Amyloid fibril formation can proceed from different conformations of a partially unfolded protein |
| Q46250306 | Amyloid-beta peptide (Abeta) neurotoxicity is modulated by the rate of peptide aggregation: Abeta dimers and trimers correlate with neurotoxicity |
| Q38065104 | Analytical methods and formulation factors to enhance protein stability in solution |
| Q36458269 | Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase |
| Q46858641 | C-terminal truncation modulates both nucleation and extension phases of tau fibrillization |
| Q45118972 | Conformational stability of amyloid fibrils of beta2-microglobulin probed by guanidine-hydrochloride-induced unfolding |
| Q83070153 | Effect of ions on agitation- and temperature-induced aggregation reactions of antibodies |
| Q89459128 | Effective Therapeutic Drug Delivery by GALA3, an Endosomal Escape Peptide with Reduced Hydrophobicity |
| Q101038816 | Fast kinetics of environmentally induced α-synuclein aggregation mediated by structural alteration in NAC region and result in structure dependent cytotoxicity |
| Q41499639 | Human beta-synuclein rendered fibrillogenic by designed mutations |
| Q38779738 | Hypothesis: The unfolding power of protein dielectricity |
| Q55428758 | Identification of novel superoxide dismutase isoenzymes in the olive (Olea europaea L.) pollen. |
| Q57472390 | Increased sequence hydrophobicity reduces conformational specificity: a mutational case study of the Arc repressor protein |
| Q45195856 | Investigating the effects of mutations on protein aggregation in the cell. |
| Q42683737 | Kinetic analysis of amyloid formation in the presence of heparan sulfate: faster unfolding and change of pathway |
| Q57644896 | Lysine functionalised amyloid fibrils: the design and assembly of a TTR1-based peptide |
| Q38223686 | Misfolding of amyloidogenic proteins and their interactions with membranes |
| Q64992649 | Monitoring site-specific conformational changes in real-time reveals a misfolding mechanism of the prion protein. |
| Q43154901 | Nonspecific interaction of prefibrillar amyloid aggregates with glutamatergic receptors results in Ca2+ increase in primary neuronal cells. |
| Q33321436 | Protein abundance profiling of the Escherichia coli cytosol |
| Q54453538 | Protein aggregation starting from the native globular state. |
| Q30879431 | RNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivity |
| Q34694133 | Rational development of a strategy for modifying the aggregatibility of proteins |
| Q45284384 | Site-specific pseudophosphorylation modulates the rate of tau filament dissociation |
| Q90189862 | Structure and Aggregation Mechanisms in Amyloids |
| Q33716773 | Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disorders |
| Q51730305 | Toxic HypF-N Oligomers Selectively Bind the Plasma Membrane to Impair Cell Adhesion Capability. |
| Q36806901 | Understanding protein aggregation from the view of monomer dynamics |
| Q38288126 | Unraveling Prion Protein Interactions with Aptamers and Other PrP-Binding Nucleic Acids |
| Q37295060 | Variation in aggregation propensities among ALS-associated variants of SOD1: correlation to human disease. |
Search more.