| scholarly article | Q13442814 |
| P6179 | Dimensions Publication ID | 1038522527 |
| P356 | DOI | 10.1016/J.JASMS.2004.08.003 |
| P2888 | exact match | https://scigraph.springernature.com/pub.10.1016/j.jasms.2004.08.003 |
| P698 | PubMed publication ID | 15465356 |
| P5875 | ResearchGate publication ID | 8250973 |
| P50 | author | Harry B. Gray | Q369975 |
| P2093 | author name string | Jay R Winkler | |
| Michael T Bowers | |||
| Thomas Wyttenbach | |||
| Jennifer C Lee | |||
| Dengfeng Liu | |||
| Summer L Bernstein | |||
| P2860 | cites work | Duplex formation and the onset of helicity in poly d(CG)n oligonucleotides in a solvent-free environment | Q45153107 |
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| Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. | Q48353748 | ||
| Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. | Q48830095 | ||
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| Protein Structurein Vacuo: Gas-Phase Conformations of BPTI and Cytochromec | Q56519905 | ||
| Experimental evidence for the formation of fullerenes by collisional heating of carbon rings in the gas phase | Q59086524 | ||
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| Alpha-synuclein in Lewy bodies | Q27860680 | ||
| Prospects for new restorative and neuroprotective treatments in Parkinson's disease | Q28138668 | ||
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| Peptides and proteins in the vapor phase | Q30941184 | ||
| Translating cell biology into therapeutic advances in Alzheimer's disease | Q33678168 | ||
| Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry | Q34173720 | ||
| Identification of two distinct synucleins from human brain | Q34341909 | ||
| Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways | Q34468169 | ||
| Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation | Q35700288 | ||
| Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies. | Q35764504 | ||
| Mass spectrometry of ribosomes and ribosomal subunits | Q36488442 | ||
| Detection and selective dissociation of intact ribosomes in a mass spectrometer | Q36966659 | ||
| Gas-phase conformations of deprotonated trinucleotides (dGTT-, dTGT-, and dTTG-): the question of zwitterion formation | Q42694770 | ||
| Conformational properties of alpha-synuclein in its free and lipid-associated states | Q43564642 | ||
| Gas-phase conformations and folding energetics of oligonucleotides: dTG- and dGT-. | Q43628238 | ||
| Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure | Q43735123 | ||
| Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling | Q45112183 | ||
| P433 | issue | 10 | |
| P921 | main subject | Synuclein | Q24767155 |
| P304 | page(s) | 1435-1443 | |
| P577 | publication date | 2004-10-01 | |
| P1433 | published in | Journal of the American Society for Mass Spectrometry | Q3020250 |
| P1476 | title | Alpha-synuclein: stable compact and extended monomeric structures and pH dependence of dimer formation | |
| P478 | volume | 15 |
| Q34447530 | A relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synuclein |
| Q47662080 | Adding a new separation dimension to MS and LC-MS: What is the utility of ion mobility spectrometry? |
| Q38051908 | Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly |
| Q35139572 | Alpha-synuclein in peripheral tissues and body fluids as a biomarker for Parkinson's disease - a systematic review |
| Q46703068 | Amyloid fibril formation of alpha-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases |
| Q39584678 | Analyzing slowly exchanging protein conformations by ion mobility mass spectrometry: study of the dynamic equilibrium of prolyl oligopeptidase. |
| Q37083478 | Binding of Dopamine to Alpha-Synuclein is Mediated by Specific Conformational States |
| Q39871699 | Biophysical Characterization of α-Synuclein and Rotenone Interaction |
| Q37872627 | Capturing protein structural kinetics by mass spectrometry |
| Q43550120 | Characterisation of an intrinsically disordered protein complex of Swi5-Sfr1 by ion mobility mass spectrometry and small-angle X-ray scattering |
| Q43256880 | Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synuclein |
| Q58028826 | Characterizing Early Aggregates Formed by an Amyloidogenic Peptide by Mass Spectrometry |
| Q58028836 | Characterizing Early Aggregates Formed by an Amyloidogenic Peptide by Mass Spectrometry |
| Q33413124 | Characterizing ion mobility-mass spectrometry conformation space for the analysis of complex biological samples |
| Q30402284 | Compaction properties of an intrinsically disordered protein: Sic1 and its kinase-inhibitor domain |
| Q92952593 | Computational Insights into Compaction of Gas-Phase Protein and Protein Complex Ions in Native Ion Mobility-Mass Spectrometry |
| Q41256282 | Conformational dynamics of α-synuclein: insights from mass spectrometry |
| Q24298122 | Dequalinium-induced protofibril formation of alpha-synuclein |
| Q57948233 | Different Structural Conformers of Monomeric α-Synuclein Identified after Lyophilizing and Freezing |
| Q34655170 | Distance geometry protocol to generate conformations of natural products to structurally interpret ion mobility-mass spectrometry collision cross sections |
| Q41634522 | Effect of acidic pH on the stability of α-synuclein dimers |
| Q33859337 | Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry |
| Q34010129 | Elucidating the tertiary structure of protein ions in vacuo with site specific photoinitiated radical reactions |
| Q55312267 | Exploring the Structural Diversity in Inhibitors of α-Synuclein Amyloidogenic Folding, Aggregation, and Neurotoxicity. |
| Q26852660 | Exploring the accessible conformations of N-terminal acetylated α-synuclein |
| Q96135531 | Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity |
| Q85478769 | How Closely Related Are Conformations of Protein Ions Sampled by IM-MS to Native Solution Structures? |
| Q37785763 | How useful is ion mobility mass spectrometry for structural biology? The relationship between protein crystal structures and their collision cross sections in the gas phase |
| Q30492870 | Human islet amyloid polypeptide monomers form ordered beta-hairpins: a possible direct amyloidogenic precursor |
| Q38044422 | Intrinsic disorder in proteins: a challenge for (un)structural biology met by ion mobility-mass spectrometry |
| Q43099036 | Ion Mobility Spectrometry-Mass Spectrometry of Intrinsically Unfolded Proteins: Trying to Put Order into Disorder |
| Q37888870 | Ion mobility mass spectrometry for peptide analysis |
| Q37737098 | Ion mobility mass spectrometry of proteins and protein assemblies. |
| Q33450048 | Ion mobility measurements of nondenatured 12-150 kDa proteins and protein multimers by tandem differential mobility analysis-mass spectrometry (DMA-MS). |
| Q35076599 | Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitors |
| Q34602533 | Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation |
| Q38056343 | Mass spectrometry methods for intrinsically disordered proteins. |
| Q92583152 | Multiple solution structures of the disordered peptide indolicidin from IMS-MS analysis |
| Q42247305 | N-terminal acetylation of α-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer |
| Q89304623 | Native Top-Down Mass Spectrometry and Ion Mobility MS for Characterizing the Cobalt and Manganese Metal Binding of α-Synuclein Protein |
| Q30426229 | Novel insights into protein misfolding diseases revealed by ion mobility-mass spectrometry |
| Q37369361 | Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1 |
| Q51730571 | Pulsed HDX Illuminates the Aggregation Kinetics of Alpha-Synuclein, the Causative Agent for Parkinson's Disease. |
| Q30409364 | Reflections on charge state distributions, protein structure, and the mystical mechanism of electrospray ionization |
| Q43122934 | Separation of isomers L-alanine and sarcosine in urine by electrospray ionization and tandem differential mobility analysis-mass spectrometry |
| Q52721887 | Small Molecules Attenuate the Interplay between Conformational Fluctuations, Early Oligomerization and Amyloidosis of Alpha Synuclein. |
| Q37091555 | Spermine binding to Parkinson's protein alpha-synuclein and its disease-related A30P and A53T mutants |
| Q33934394 | Structural characterization of copper(II) binding to alpha-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease |
| Q45284957 | Structural characterization of sialic acid synthase by electrospray mass spectrometry--a tetrameric enzyme composed of dimeric dimers |
| Q48044175 | The attachment of α-synuclein to a fiber: A coarse-grain approach. |
| Q36379177 | The conformational ensembles of α-synuclein and tau: combining single-molecule FRET and simulations |
| Q40688335 | The use of ion mobility mass spectrometry to probe modulation of the structure of p53 and of MDM2 by small molecule inhibitors |
| Q36828634 | Transfer of structural elements from compact to extended states in unsolvated ubiquitin |
| Q37982686 | Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry. |
| Q50064138 | Two possible improvements for mass spectrometry analysis of intact biomolecules. |
| Q41564716 | pH-induced structural change of a multi-tryptophan protein MPT63 with immunoglobulin-like fold: identification of perturbed tryptophan residue/residues. |
| Q24316089 | α-Synuclein as an intrinsically disordered monomer--fact or artefact? |
| Q37351690 | α-Synuclein misfolding assessed with single molecule AFM force spectroscopy: effect of pathogenic mutations |
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