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    SNCB synuclein beta [ Homo sapiens (human) ]

    Gene ID: 6620, updated on 3-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Understanding Genetic Risks: Computational Exploration of Human beta-Synuclein nsSNPs and their Potential Impact on Structural Alteration.

    Understanding Genetic Risks: Computational Exploration of Human β-Synuclein nsSNPs and their Potential Impact on Structural Alteration.
    Mahur P, Sharma A, Jahan G, S G A, Kumar Singh A, Muthukumaran J, Jain M.

    06/11/2024
    Serum beta-synuclein, neurofilament light chain and glial fibrillary acidic protein as prognostic biomarkers in moderate-to-severe acute ischemic stroke.

    Serum β-synuclein, neurofilament light chain and glial fibrillary acidic protein as prognostic biomarkers in moderate-to-severe acute ischemic stroke.
    Barba L, Vollmuth C, Abu-Rumeileh S, Halbgebauer S, Oeckl P, Steinacker P, Kollikowski AM, Schultz C, Wolf J, Pham M, Schuhmann MK, Heuschmann PU, Haeusler KG, Stoll G, Neugebauer H, Otto M., Free PMC Article

    12/1/2023
    Plasma beta-synuclein, GFAP, and neurofilaments in patients with malignant gliomas undergoing surgical and adjuvant therapy.

    Plasma β-synuclein, GFAP, and neurofilaments in patients with malignant gliomas undergoing surgical and adjuvant therapy.
    Abu-Rumeileh S, Barba L, Bache M, Halbgebauer S, Oeckl P, Steinacker P, Güttler A, Keßler J, Illert J, Strauss C, Vordermark D, Otto M., Free PMC Article

    10/30/2023
    Blood beta-Synuclein and Neurofilament Light Chain During the Course of Prion Disease.

    Blood β-Synuclein and Neurofilament Light Chain During the Course of Prion Disease.
    Halbgebauer S, Abu-Rumeileh S, Oeckl P, Steinacker P, Roselli F, Wiesner D, Mammana A, Beekes M, Kortazar-Zubizarreta I, Perez de Nanclares G, Capellari S, Giese A, Castilla J, Ludolph AC, Žáková D, Parchi P, Otto M.

    04/16/2022
    Dementia with Lewy bodies-associated ss-synuclein mutations V70M and P123H cause mutation-specific neuropathological lesions.

    Dementia with Lewy bodies-associated ß-synuclein mutations V70M and P123H cause mutation-specific neuropathological lesions.
    Psol M, Darvas SG, Leite K, Mahajani SU, Bähr M, Kügler S.

    11/13/2021
    Effect of Disease-Associated P123H and V70M Mutations on beta-Synuclein Fibrillation.

    Effect of Disease-Associated P123H and V70M Mutations on β-Synuclein Fibrillation.
    Sharma K, Mehra S, Sawner AS, Markam PS, Panigrahi R, Navalkar A, Chatterjee D, Kumar R, Kadu P, Patel K, Ray S, Kumar A, Maji SK.

    07/10/2021
    beta-synuclein-specific T cells were enriched in patients with chronic-progressive multiple sclerosis; findings reveal a previously unrecognized role of beta-synuclein in provoking T-cell-mediated pathology of the central nervous system

    β-Synuclein-reactive T cells induce autoimmune CNS grey matter degeneration.
    Lodygin D, Hermann M, Schweingruber N, Flügel-Koch C, Watanabe T, Schlosser C, Merlini A, Körner H, Chang HF, Fischer HJ, Reichardt HM, Zagrebelsky M, Mollenhauer B, Kügler S, Fitzner D, Frahm J, Stadelmann C, Haberl M, Odoardi F, Flügel A.

    08/17/2019
    This analyzed identify functional insertion and deletion (INDEL) variations upstream of SNCB, determined SNCB expression levels, and correlated INDEL lengths with expression levels.

    INDEL Length and Haplotypes in the β-Synuclein Gene: A Key to Differentiate Dementia with Lewy Bodies?
    Gámez-Valero A, Canet-Pons J, Urbizu A, Anillo A, Santos C, Ariza A, Beyer K.

    08/3/2019
    Vibrational Circular Dichroism Sheds New Light on the Competitive Effects of Crowding and beta-Synuclein on the Fibrillation Process of alpha-Synuclein.

    Vibrational Circular Dichroism Sheds New Light on the Competitive Effects of Crowding and β-Synuclein on the Fibrillation Process of α-Synuclein.
    Van de Vondel E, Baatsen P, Van Elzen R, Lambeir AM, Keiderling TA, Herrebout WA, Johannessen C.

    07/20/2019
    Results show that the non-amyloid-beta component domain of SNCB is the primary determinant of self-association leading to fibril formation, while the N- and C-terminal domains play critical roles in the fibril inhibition process. These data provide evidence that all three domains together contribute to providing effective inhibition.

    Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein.
    Williams JK, Yang X, Atieh TB, Olson MP, Khare SD, Baum J., Free PMC Article

    07/6/2019
    These studies could be helpful in understanding collective human synuclein behavior in various protein environments and in the modulation of the homeostasis between beta-syn and healthy versus corrupt alpha- and gamma-syn that can potentially affect PD pathology.

    Comparative Analysis of the Conformation, Aggregation, Interaction, and Fibril Morphologies of Human α-, β-, and γ-Synuclein Proteins.
    Jain MK, Singh P, Roy S, Bhat R.

    02/9/2019
    Cells that overexpress alpha-syn showed increased susceptibility to the toxicity of the oligomers, while those that overexpressed beta-syn showed increased resistance to the toxic oligomers.

    Levels of α- and β-synuclein regulate cellular susceptibility to toxicity from α-synuclein oligomers.
    Angelova DM, Jones HBL, Brown DR.

    10/27/2018
    alterations in the plasma alpha-synuclein and beta-synuclein levels might be implicated in the association between synaptic abnormalities and autism spectrum disorder pathogenesis.

    Significant Changes in Plasma Alpha-Synuclein and Beta-Synuclein Levels in Male Children with Autism Spectrum Disorder.
    Sriwimol W, Limprasert P., Free PMC Article

    10/6/2018
    Study suggests that beta-synuclein changes in Dementia with Lewy bodies may exacerbate neuronal dysfunction caused by accumulation of alpha-synuclein by influencing protein degradation.

    Accumulation of beta-synuclein in cortical neurons is associated with autophagy attenuation in the brains of dementia with Lewy body patients.
    Evans T, Kok WL, Cowan K, Hefford M, Anichtchik O.

    08/18/2018
    Data suggest that pH serves as an on/off switch for beta- synuclein to form aggregates/fibrils (as seem in Parkinson disease); hydrogen bonding between glutamate residues appears to be involved in fibril formation.

    A pH-dependent switch promotes β-synuclein fibril formation via glutamate residues.
    Moriarty GM, Olson MP, Atieh TB, Janowska MK, Khare SD, Baum J., Free PMC Article

    10/21/2017
    Cellular pathways affected by bSyn are similar to those affected by aSyn, including impairment of vesicular trafficking and induction of oxidative stress.

    Yeast reveals similar molecular mechanisms underlying alpha- and beta-synuclein toxicity.
    Tenreiro S, Rosado-Ramos R, Gerhardt E, Favretto F, Magalhães F, Popova B, Becker S, Zweckstetter M, Braus GH, Outeiro TF.

    10/22/2016
    loss of inhibitory C-terminal conformations in disease associated P123H beta-synuclein

    The loss of inhibitory C-terminal conformations in disease associated P123H β-synuclein.
    Janowska MK, Baum J., Free PMC Article

    10/1/2016
    beta-Synuclein expression was locally concentrated and rather modest, but nevertheless changed its effect on amyloid precursor protein expression and plaque load in a time- and concentration-dependent manner.

    Influence of Lentiviral β-Synuclein Overexpression in the Hippocampus of a Transgenic Mouse Model of Alzheimer's Disease on Amyloid Precursor Protein Metabolism and Pathology.
    Krassnig S, Schweinzer C, Taub N, Havas D, Auer E, Flunkert S, Schreibmayer W, Hutter-Paier B, Windisch M.

    04/23/2016
    The differing aggregation propensities of alpha-synuclein and beta-synuclein are associated with differences in the degree of residual structure in the C-terminus coupled to the shorter separation between the N- and C-termini in beta-synuclein.

    A relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synuclein.
    Allison JR, Rivers RC, Christodoulou JC, Vendruscolo M, Dobson CM., Free PMC Article

    01/24/2015
    Beta-synuclein protects against isoaspartate accumulation in alpha-synuclein.

    Molecular ageing of alpha- and Beta-synucleins: protein damage and repair mechanisms.
    Vigneswara V, Cass S, Wayne D, Bolt EL, Ray DE, Carter WG., Free PMC Article

    11/16/2013
    both alphaS- and P123H betaS-globules were formed through similar but distinct pathogenic mechanisms.

    Distinct mechanisms of axonal globule formation in mice expressing human wild type α-synuclein or dementia with Lewy bodies-linked P123H β-synuclein.
    Sekigawa A, Fujita M, Sekiyama K, Takamatsu Y, Hatano T, Rockenstein E, La Spada AR, Masliah E, Hashimoto M., Free PMC Article

    05/18/2013
    In vivo cross-linking reveals principally oligomeric forms of alpha-synuclein and beta-synuclein in neurons and non-neural cells

    In vivo cross-linking reveals principally oligomeric forms of α-synuclein and β-synuclein in neurons and non-neural cells.
    Dettmer U, Newman AJ, Luth ES, Bartels T, Selkoe D., Free PMC Article

    05/11/2013
    Thermodynamic studies in conjunction with EPR confirm that alpha-synuclein, beta-synuclein, and gamma-synuclein bind copper(II) in a high affinity 1:1 stoichiometry.

    The synucleins are a family of redox-active copper binding proteins.
    Davies P, Wang X, Sarell CJ, Drewett A, Marken F, Viles JH, Brown DR.

    12/8/2012
    Data provide evidence for the role of beta-synuclein minor transcript variants in the development of complex diseases and provide new insights into the pathogenesis of Lewy body diseases.

    New brain-specific beta-synuclein isoforms show expression ratio changes in Lewy body diseases.
    Beyer K, Munoz-Marmol AM, Sanz C, Marginet-Flinch R, Ferrer I, Ariza A.

    05/26/2012
    This study suggested that the pathogenesis of dementia in Parkinson disease, indicating that differential sncb expression in the caudate nucleus may represent one of the molecular mechanisms involved in these complex diseases.

    Alpha- and beta-synuclein expression in Parkinson disease with and without dementia.
    Beyer K, Ispierto L, Latorre P, Tolosa E, Ariza A.

    02/18/2012
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