scholarly article | Q13442814 |
P6179 | Dimensions Publication ID | 1026304126 |
P356 | DOI | 10.1038/SREP30473 |
P2888 | exact match | https://scigraph.springernature.com/pub.10.1038/srep30473 |
P932 | PMC publication ID | 4965831 |
P698 | PubMed publication ID | 27469540 |
P50 | author | Katsuya Araki | Q59700907 |
Hiroshi Sekiguchi | Q43110121 | ||
P2093 | author name string | Hisashi Yagi | |
Yuji Goto | |||
Hideki Mochizuki | |||
Masatomo So | |||
Naoto Yagi | |||
Noboru Ohta | |||
Yoshitaka Nagai | |||
Rie Nakatani | |||
P2860 | cites work | The structure of dopamine induced alpha-synuclein oligomers. | Q43121446 |
The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice: paraquat and alpha-synuclein | Q43798526 | ||
Evidence for a partially folded intermediate in alpha-synuclein fibril formation | Q46097239 | ||
Amyloid fibril formation of alpha-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases | Q46703068 | ||
Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease | Q48353748 | ||
Red blood cells are the major source of alpha-synuclein in blood. | Q50663283 | ||
PRIMUS: a Windows PC-based system for small-angle scattering data analysis | Q57091059 | ||
Alpha-synuclein oligomers and fibrils originate in two distinct conformer pools: a small angle X-ray scattering and ensemble optimisation modelling study | Q57982348 | ||
Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro | Q64865343 | ||
Probing conformational change of intrinsically disordered α-synuclein to helical structures by distinctive regional interactions with lipid membranes | Q87023706 | ||
α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation | Q24605589 | ||
alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies | Q24653247 | ||
Properties of native brain α-synuclein | Q26269846 | ||
Characterization of fibrillation process of alpha-synuclein at the initial stage | Q33323132 | ||
Targeted amino-terminal acetylation of recombinant proteins in E. coli | Q33784412 | ||
A soluble α-synuclein construct forms a dynamic tetramer | Q34050129 | ||
α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer | Q34252869 | ||
The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system | Q34318718 | ||
Expression pattern and localization of alpha-synuclein in the human enteric nervous system | Q34360563 | ||
Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation | Q34602533 | ||
Wildtype and A30P mutant alpha-synuclein form different fibril structures | Q34825913 | ||
Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies. | Q35764504 | ||
O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's disease | Q36200921 | ||
Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein | Q36217340 | ||
Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson's disease patients. | Q36333500 | ||
Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal | Q36455215 | ||
Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein. | Q37278078 | ||
Structural disorder of monomeric α-synuclein persists in mammalian cells. | Q38799574 | ||
N-Terminal acetylation is critical for forming α-helical oligomer of α-synuclein | Q42247351 | ||
P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
P6216 | copyright status | copyrighted | Q50423863 |
P407 | language of work or name | English | Q1860 |
P921 | main subject | X-ray scattering techniques | Q12073245 |
Synuclein | Q24767155 | ||
P304 | page(s) | 30473 | |
P577 | publication date | 2016-07-29 | |
P1433 | published in | Scientific Reports | Q2261792 |
P1476 | title | A small-angle X-ray scattering study of alpha-synuclein from human red blood cells | |
P478 | volume | 6 |
Q91841683 | A behavior-based drug screening system using a Caenorhabditis elegans model of motor neuron disease |
Q91288432 | Endogenous alpha-synuclein monomers, oligomers and resulting pathology: let's talk about the lipids in the room |
Q52716959 | The localization of α-synuclein in the process of differentiation of human erythroid cells. |
Q64052834 | Ultrasonication-based rapid amplification of α-synuclein aggregates in cerebrospinal fluid |
Q47213644 | Using a FRET Library with Multiple Probe Pairs To Drive Monte Carlo Simulations of α-Synuclein. |
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