scholarly article | Q13442814 |
P50 | author | Salvador Ventura | Q41047849 |
Carlo Santambrogio | Q64683010 | ||
Tiago Fleming Outeiro | Q79139390 | ||
P2093 | author name string | Jordi Pujols | |
Rita Grandori | |||
Anita Carija | |||
Francisca Pinheiro | |||
Susanna Navarro | |||
Diana Fernandes Lázaro | |||
Inês C Brás | |||
P2860 | cites work | Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease | Q24321355 |
The FoldX web server: an online force field | Q24530376 | ||
alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies | Q24653247 | ||
A simple method for displaying the hydropathic character of a protein | Q26778481 | ||
Alpha-synuclein in Lewy bodies | Q27860680 | ||
Seeking a mechanism for the toxicity of oligomeric α-synuclein | Q28080551 | ||
Role of Different Alpha-Synuclein Strains in Synucleinopathies, Similarities with other Neurodegenerative Diseases | Q28082714 | ||
Alpha-synuclein and neurodegenerative diseases | Q28204386 | ||
Distinct α-synuclein strains differentially promote tau inclusions in neurons | Q28293967 | ||
Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds | Q28308021 | ||
IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content | Q29615888 | ||
Contribution of disulfide bonds to stability, folding, and amyloid fibril formation: the PI3-SH3 domain case | Q30010266 | ||
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity | Q30838501 | ||
Small-volume extrusion apparatus for preparation of large, unilamellar vesicles | Q30965369 | ||
The rat brain synucleins; family of proteins transiently associated with neuronal membrane | Q33240068 | ||
AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides | Q33275645 | ||
Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing α-synuclein oligomeric species toxicity | Q33619357 | ||
Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein | Q33817987 | ||
alpha-Synuclein occurs in lipid-rich high molecular weight complexes, binds fatty acids, and shows homology to the fatty acid-binding proteins | Q33929879 | ||
beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor | Q34099593 | ||
Beta-synuclein modulates alpha-synuclein neurotoxicity by reducing alpha-synuclein protein expression | Q34564479 | ||
In vivo demonstration that alpha-synuclein oligomers are toxic | Q34652122 | ||
The many faces of α-synuclein: from structure and toxicity to therapeutic target | Q34972009 | ||
Disulfide by Design 2.0: a web-based tool for disulfide engineering in proteins | Q35056453 | ||
Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour | Q35175448 | ||
Association of alpha-, beta-, and gamma-Synuclein with diffuse lewy body disease | Q36504239 | ||
The Zyggregator method for predicting protein aggregation propensities | Q37196192 | ||
Structural basis of synaptic vesicle assembly promoted by α-synuclein | Q37273635 | ||
Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein. | Q37278078 | ||
Structural and functional characterization of two alpha-synuclein strains | Q37305236 | ||
Structure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathies | Q38550428 | ||
α-Synuclein strains cause distinct synucleinopathies after local and systemic administration | Q41681113 | ||
The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation. | Q42355152 | ||
Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synuclein | Q43256880 | ||
Identification of the region of non-Abeta component (NAC) of Alzheimer's disease amyloid responsible for its aggregation and toxicity | Q43681032 | ||
Dependence of alpha-synuclein aggregate morphology on solution conditions | Q44129175 | ||
Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? | Q45300712 | ||
The N-terminal region of non-A beta component of Alzheimer's disease amyloid is responsible for its tendency to assume beta-sheet and aggregate to form fibrils | Q46178347 | ||
Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers | Q46241023 | ||
Toxicity of protein oligomers is rationalized by a function combining size and surface hydrophobicity | Q46858479 | ||
Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid. | Q46866171 | ||
Minimal Nucleation State of α-Synuclein Is Stabilized by Dynamic Threonine-Water Networks | Q47958898 | ||
FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence | Q48239540 | ||
The contribution of cross-links to protein stability: a normal mode analysis of the configurational entropy of the native state. | Q52407607 | ||
A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly. | Q54031652 | ||
IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding. | Q55518742 | ||
Structural properties of pore-forming oligomers of alpha-synuclein | Q57185914 | ||
Compact conformations of α-synuclein induced by alcohols and copper | Q57267827 | ||
Global Protein Stabilization Does Not Suffice to Prevent Amyloid Fibril Formation | Q58434151 | ||
The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: is NAC a common trigger or target in neurodegenerative disease? | Q73909478 | ||
Modulation of α-synuclein aggregation by dopamine in the presence of MPTP and its metabolite | Q83630151 | ||
P4510 | describes a project that uses | ImageJ | Q1659584 |
P407 | language of work or name | English | Q1860 |
P921 | main subject | disulfide bond | Q423252 |
neurotoxicity | Q3338704 | ||
toxic encephalopathy | Q7830379 | ||
Synuclein | Q24767155 | ||
P304 | page(s) | 101135 | |
P577 | publication date | 2019-02-05 | |
P1433 | published in | Redox Biology | Q27724751 |
P859 | sponsor | Collaborative Research Centre (CRC) 1286: "Quantitative Synaptologie" | Q87186232 |
P1476 | title | Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity | |
P478 | volume | 22 |
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