| scholarly article | Q13442814 |
| P819 | ADS bibcode | 2014PLoSO...986495N |
| P356 | DOI | 10.1371/JOURNAL.PONE.0086495 |
| P932 | PMC publication ID | 3901707 |
| P698 | PubMed publication ID | 24475132 |
| P5875 | ResearchGate publication ID | 259961211 |
| P2093 | author name string | Iveta Sosova | |
| Krishna Neupane | |||
| Michael T Woodside | |||
| Allison Solanki | |||
| Miro Belov | |||
| P2860 | cites work | Conformational equilibria in monomeric alpha-synuclein at the single-molecule level | Q21563559 |
| α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation | Q24605589 | ||
| Optical trapping | Q24669585 | ||
| Atomic View of a Toxic Amyloid Small Oligomer | Q27677948 | ||
| Protein misfolding, functional amyloid, and human disease | Q28131732 | ||
| Stretching DNA with optical tweezers | Q28237199 | ||
| Protein aggregation and neurodegenerative disease | Q28273600 | ||
| Common features at the start of the neurodegeneration cascade | Q28483979 | ||
| The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide | Q28854601 | ||
| Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes | Q29617606 | ||
| Direct observation of a force-induced switch in the anisotropic mechanical unfolding pathway of a protein | Q30010019 | ||
| Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation | Q30160009 | ||
| High-resolution, single-molecule measurements of biomolecular motion | Q30501806 | ||
| Optical trapping with high forces reveals unexpected behaviors of prion fibrils | Q30504869 | ||
| In vitro and in vivo neurotoxicity of prion protein oligomers. | Q33296885 | ||
| alpha-Synuclein misfolding: single molecule AFM force spectroscopy study | Q33379030 | ||
| Coupling between properties of the protein shape and the rate of protein folding. | Q33489605 | ||
| Early aggregation steps in alpha-synuclein as measured by FCS and FRET: evidence for a contagious conformational change. | Q33550002 | ||
| The pleated sheet, a new layer configuration of polypeptide chains | Q33711390 | ||
| Full distance-resolved folding energy landscape of one single protein molecule | Q33719574 | ||
| Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein | Q33817987 | ||
| The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques | Q33904638 | ||
| Dynamic strength of molecular adhesion bonds | Q33915225 | ||
| A soluble α-synuclein construct forms a dynamic tetramer | Q34050129 | ||
| The complex folding network of single calmodulin molecules | Q34228218 | ||
| Evidence for a partially folded intermediate in alpha-synuclein fibril formation | Q46097239 | ||
| Single-molecule assays for investigating protein misfolding and aggregation | Q46164744 | ||
| Direct observation of chaperone-induced changes in a protein folding pathway | Q46874460 | ||
| Mechanics and structure of titin oligomers explored with atomic force microscopy. | Q47889684 | ||
| Pathogenic mutations shift the equilibria of alpha-synuclein single molecules towards structured conformers. | Q48806783 | ||
| Signal-pair correlation analysis of single-molecule trajectories. | Q51764057 | ||
| Mapping Long-Range Interactions in α-Synuclein using Spin-Label NMR and Ensemble Molecular Dynamics Simulations | Q57976902 | ||
| Detection and Analysis of Protein Aggregation with Confocal Single Molecule Fluorescence Spectroscopy | Q59332567 | ||
| Reversible unfolding of individual titin immunoglobulin domains by AFM | Q73334897 | ||
| Single molecule characterization of α-synuclein in aggregation-prone states | Q34250768 | ||
| α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer | Q34252869 | ||
| Direct observation of multiple misfolding pathways in a single prion protein molecule | Q34261701 | ||
| Direct observation of the interconversion of normal and toxic forms of α-synuclein | Q34277399 | ||
| Effect of spermidine on misfolding and interactions of alpha-synuclein | Q34291522 | ||
| The protein folding 'speed limit'. | Q34315486 | ||
| Structure and dynamics of micelle-bound human alpha-synuclein | Q34379131 | ||
| Direct observation of the three-state folding of a single protein molecule | Q34453219 | ||
| Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins | Q35177787 | ||
| Single-molecule force spectroscopy of the add adenine riboswitch relates folding to regulatory mechanism | Q35224302 | ||
| Aggregation of α-synuclein is kinetically controlled by intramolecular diffusion | Q35786977 | ||
| Supramolecular non-amyloid intermediates in the early stages of α-synuclein aggregation | Q35810050 | ||
| The molten globule state is unusually deformable under mechanical force. | Q35844982 | ||
| Expression in drosophila of tandem amyloid β peptides provides insights into links between aggregation and neurotoxicity | Q36017019 | ||
| Energy landscape analysis of native folding of the prion protein yields the diffusion constant, transition path time, and rates | Q36221715 | ||
| Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? | Q36595270 | ||
| The aggregation and fibrillation of alpha-synuclein | Q36596606 | ||
| Single-molecule approaches to prion protein misfolding | Q36719202 | ||
| The fold of alpha-synuclein fibrils | Q36735295 | ||
| NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded | Q36830682 | ||
| Direct characterization of amyloidogenic oligomers by single-molecule fluorescence | Q36936286 | ||
| Single-molecule studies of protein folding. | Q37138477 | ||
| Interplay of alpha-synuclein binding and conformational switching probed by single-molecule fluorescence. | Q37153744 | ||
| Alpha-synuclein misfolding and neurodegenerative diseases | Q37294354 | ||
| α-Synuclein misfolding assessed with single molecule AFM force spectroscopy: effect of pathogenic mutations | Q37351690 | ||
| Theoretical perspectives on protein folding | Q37700641 | ||
| Unravelling the design principles for single protein mechanical strength | Q37764589 | ||
| A diversity of assembly mechanisms of a generic amyloid fold | Q37897372 | ||
| A mechanically stabilized receptor-ligand flex-bond important in the vasculature. | Q39665373 | ||
| Protein-DNA chimeras for single molecule mechanical folding studies with the optical tweezers | Q40311799 | ||
| alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease | Q41676981 | ||
| Alteration of the alpha-synuclein folding landscape by a mutation related to Parkinson's disease | Q41905102 | ||
| Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions | Q42008466 | ||
| Mechanical resistance in unstructured proteins. | Q42077482 | ||
| Contact order revisited: influence of protein size on the folding rate | Q42115099 | ||
| The mechanical stability of ubiquitin is linkage dependent | Q44552415 | ||
| Detection of polyglutamine protein oligomers in cells by fluorescence correlation spectroscopy | Q45305431 | ||
| P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
| P6216 | copyright status | copyrighted | Q50423863 |
| P433 | issue | 1 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | spectroscopy | Q483666 |
| Synuclein | Q24767155 | ||
| P304 | page(s) | e86495 | |
| P577 | publication date | 2014-01-01 | |
| P1433 | published in | PLOS One | Q564954 |
| P1476 | title | Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopy | |
| P478 | volume | 9 |
| Q47555193 | A scalable approach to the computation of invariant measures for high-dimensional Markovian systems |
| Q37167847 | Comparing the energy landscapes for native folding and aggregation of PrP. |
| Q41256282 | Conformational dynamics of α-synuclein: insights from mass spectrometry |
| Q35529960 | Direct Detection of α-Synuclein Dimerization Dynamics: Single-Molecule Fluorescence Analysis |
| Q61797045 | Early stages of aggregation of engineered α-synuclein monomers and oligomers in solution |
| Q38944980 | How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe |
| Q39149504 | Nanomolar oligomerization and selective co-aggregation of α-synuclein pathogenic mutants revealed by single-molecule fluorescence |
| Q47127143 | Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories |
| Q86957603 | Phase transitions and structure analysis in wild-type, A30P, E46K, and A53T mutants of α-synuclein |
| Q33776138 | Post translational changes to α-synuclein control iron and dopamine trafficking; a concept for neuron vulnerability in Parkinson's disease |
| Q46236939 | Pre-aggregation kinetics and intermediates of α-synuclein monitored by the ESIPT probe 7MFE. |
| Q35118034 | Probing protein disorder and complexity at single-molecule resolution |
| Q38550066 | Probing the structural dynamics of proteins and nucleic acids with optical tweezers |
| Q35845795 | Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape |
| Q39977051 | Single-molecule chemo-mechanical unfolding reveals multiple transition state barriers in a small single-domain protein |
| Q56890280 | Single-molecule force spectroscopy of rapidly fluctuating, marginally stable structures in the intrinsically disordered protein α-synuclein |
| Q101224590 | Single-molecule studies of amyloid proteins: from biophysical properties to diagnostic perspectives |
| Q55114623 | Structural characteristics and membrane interactions of tandem α-synuclein oligomers. |
| Q38549882 | Structural, morphological, and functional diversity of amyloid oligomers |
| Q100512294 | Synthesis runs counter to directional folding of a nascent protein domain |
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