Literature DB >> 20872101

Backbone assignment and dynamics of human α-synuclein in viscous 2 M glucose solution.

Kuen-Phon Wu1, Jean Baum.   

Abstract

We present (1)H(N), (15)N, (13)C(α), (13)C(β) and (13)C' assignments and (15)N transverse relaxation rates (R(2)) of a Parkinson's disease-related intrinsically disordered protein, α-synuclein, in the presence of 2 M (360 g/l) glucose solution.

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Year:  2010        PMID： 20872101      PMCID： PMC3064444          DOI： 10.1007/s12104-010-9263-4

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN： 1874-270X            Impact factor:   0.746


  14 in total

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6.  Molecular crowding accelerates fibrillization of alpha-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease?

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9.  Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation.

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3.  A maximum entropy approach to the study of residue-specific backbone angle distributions in α-synuclein, an intrinsically disordered protein.

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4.  Prion-like C-Terminal Domain of TDP-43 and α-Synuclein Interact Synergistically to Generate Neurotoxic Hybrid Fibrils.

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Journal:  J Mol Biol       Date:  2021-03-24       Impact factor: 5.469

5.  Bacterial Chaperones CsgE and CsgC Differentially Modulate Human α-Synuclein Amyloid Formation via Transient Contacts.

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6.  α-Synuclein interacts directly but reversibly with psychosine: implications for α-synucleinopathies.

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7.  Monomeric a-synuclein (aS) inhibits amyloidogenesis of human prion protein (hPrP) by forming a stable aS-hPrP hetero-dimer.

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Review 8.  Mechanisms of amyloid formation revealed by solution NMR.

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  8 in total

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