| scholarly article | Q13442814 |
| P356 | DOI | 10.1038/SREP40859 |
| P2888 | exact match | https://scigraph.springernature.com/pub.10.1038/srep40859 |
| P932 | PMC publication ID | 5244355 |
| P698 | PubMed publication ID | 28102321 |
| P50 | author | Begoña Sot | Q86624546 |
| Cintia Roodveldt | Q47151783 | ||
| José María Valpuesta | Q39715548 | ||
| Miguel Marcilla | Q40011330 | ||
| P2093 | author name string | Ahudrey Leal-Quintero | |
| Alejandra Rubio-Muñoz | |||
| Javier Martínez-Sabando | |||
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| Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state. | Q52573641 | ||
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| A Rationally Designed Six-Residue Swap Generates Comparability in the Aggregation Behavior of α-Synuclein and β-Synuclein | Q57227098 | ||
| Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein | Q33817987 | ||
| Nucleated conformational conversion and the replication of conformational information by a prion determinant | Q33915141 | ||
| Chaperonins: two rings for folding | Q34197022 | ||
| Direct observation of the interconversion of normal and toxic forms of α-synuclein | Q34277399 | ||
| The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system | Q34318718 | ||
| Structure and dynamics of micelle-bound human alpha-synuclein | Q34379131 | ||
| Heat-shock protein 70 modulates toxic extracellular α-synuclein oligomers and rescues trans-synaptic toxicity | Q34421765 | ||
| Common core structure of amyloid fibrils by synchrotron X-ray diffraction. | Q34444888 | ||
| Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation | Q34602533 | ||
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| Α-synuclein misfolding and Parkinson's disease | Q37949158 | ||
| Molecular chaperones, α-synuclein, and neurodegeneration | Q38038121 | ||
| Hsp90 inhibits α-synuclein aggregation by interacting with soluble oligomers. | Q39109956 | ||
| Explaining the structural plasticity of α-synuclein | Q39485110 | ||
| Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils | Q39632694 | ||
| CHIP targets toxic alpha-Synuclein oligomers for degradation | Q39988391 | ||
| The molecular chaperone Hsp90 modulates intermediate steps of amyloid assembly of the Parkinson-related protein alpha-synuclein. | Q41987647 | ||
| Structural insights into amyloid oligomers of the Parkinson disease-related protein α-synuclein. | Q42178188 | ||
| The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation | Q42699018 | ||
| Salt bridges at the inter-ring interface regulate the thermostat of GroEL. | Q44058488 | ||
| Dependence of alpha-synuclein aggregate morphology on solution conditions | Q44129175 | ||
| Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis | Q44430539 | ||
| A structural and functional role for 11-mer repeats in alpha-synuclein and other exchangeable lipid binding proteins | Q44466072 | ||
| Analysis of alpha-synuclein-associated proteins by quantitative proteomics | Q44964546 | ||
| P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
| P6216 | copyright status | copyrighted | Q50423863 |
| P4510 | describes a project that uses | ImageJ | Q1659584 |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | Synuclein | Q24767155 |
| P304 | page(s) | 40859 | |
| P577 | publication date | 2017-01-19 | |
| P1433 | published in | Scientific Reports | Q2261792 |
| P1476 | title | The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction | |
| P478 | volume | 7 |
| Q91904849 | Elevated levels of Secreted-Frizzled-Related-Protein 1 contribute to Alzheimer's disease pathogenesis |
| Q92155282 | Human Molecular Chaperone Hsp60 and Its Apical Domain Suppress Amyloid Fibril Formation of α-Synuclein |
| Q48023023 | Mechanisms of protein homeostasis (proteostasis) maintain stem cell identity in mammalian pluripotent stem cells |
| Q92651177 | TRiC/CCT Chaperonin: Structure and Function |
| Q93057873 | The ATP-powered gymnastics of TRiC/CCT: an asymmetric protein folding machine with a symmetric origin story |
| Q92905117 | The Chaperonin TRiC/CCT Associates with Prefoldin through a Conserved Electrostatic Interface Essential for Cellular Proteostasis |
| Q91712283 | The Molecular Chaperone CCT/TRiC: An Essential Component of Proteostasis and a Potential Modulator of Protein Aggregation |
| Q48139412 | The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity |
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