Journal of Neurochemistry

Cover image for Vol. 136 Issue 4

Edited By: Jörg Schulz

Impact Factor: 4.281

ISI Journal Citation Reports © Ranking: 2014: 56/252 (Neurosciences); 72/290 (Biochemistry & Molecular Biology)

Online ISSN: 1471-4159

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Recently Published Articles

  1. You have free access to this content
  2. Multisite tyrosine phosphorylation of the N-terminus of Mint1/X11α by Src kinase regulates the trafficking of amyloid precursor protein

    Christopher J.R. Dunning, Hannah L. Black, Katie L. Andrews, Elizabeth C. Davenport, Michael Conboy, Sangeeta Chawla, Adam A. Dowle, David Ashford, Jerry R. Thomas and Gareth J.O. Evans

    Accepted manuscript online: 10 FEB 2016 07:39AM EST | DOI: 10.1111/jnc.13571

  3. You have free access to this content
    Sorting out release, uptake and processing of alpha-synuclein during prion-like spread of pathology

    Trevor Tyson, Jennifer A. Steiner and Patrik Brundin

    Article first published online: 10 FEB 2016 | DOI: 10.1111/jnc.13449

    Thumbnail image of graphical abstract

    The prion-like hypothesis of α-synuclein pathology suggests a method for the transmission of misfolded α-synuclein from one neuron to another. This hypothesis postulates that misfolded α-synuclein becomes aggregation prone and when released and taken up by neighboring cells, seeds further misfolding and aggregation. In this review we examine the cellular mechanisms that are involved in the processing of α-synuclein and how these may contribute to the prion-like propagation of α-synuclein pathology.

    This article is part of a special issue on Parkinson disease.

  4. You have free access to this content
    Parkinson's disease: acid-glucocerebrosidase activity and alpha-synuclein clearance

    Judith Blanz and Paul Saftig

    Article first published online: 10 FEB 2016 | DOI: 10.1111/jnc.13517

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    Lysosomes are critical for protein and lipid homeostasis. Recent research revealed that dysfunction of this organelle contributes to the development of neurodegenerative diseases such as Parkinson's disease (PD). Mutations in the lysosomal hydrolase β-glucocerebrosidase (GBA1) are a major risk factor for the development of PD and the molecular events linked to the reduced activity of GBA1 and the pathological accumulation of lipids and α-synuclein are just at the beginning to be understood. New therapeutic concepts in regards to how to increase the expression, stability, or delivery of β-glucocerebrosidase to lysosomes are currently developed.

    This article is part of aspecial issue on Parkinson disease.

  5. You have free access to this content
    Therapeutic approaches in Parkinson's disease and related disorders

    Elvira Valera and Eliezer Masliah

    Article first published online: 10 FEB 2016 | DOI: 10.1111/jnc.13529

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    Synucleinopathies, neurodegenerative disorders characterized by the abnormal accumulation of the protein alpha-synuclein, constitute the second leading cause of parkinsonism and dementia in the elderly population, however, no disease-modifying options are available yet. In this review, we summarize the therapeutic approaches currently being explored for synucleinopathies, suggest possible explanations to the clinical outcomes, and propose areas of further therapeutic improvement.

    This article is part of aspecial issue on Parkinson disease.

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