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. Acylated but not des-acyl ghrelin is neuroprotective in an MPTP mouse model of Parkinson's Disease

    Jacqueline A Bayliss, Moyra Lemus, Vanessa V Santos, Minh Deo, John Elsworth and Zane B. Andrews

    Accepted manuscript online: 12 FEB 2016 09:04AM EST | DOI: 10.1111/jnc.13576

  2. You have free access to this content
    Walking the tightrope: Proteostasis and neurodegenerative disease

    Justin J. Yerbury, Lezanne Ooi, Andy Dillin, Darren N. Saunders, Danny M. Hatters, Philip M. Beart, Neil R. Cashman, Mark R. Wilson and Heath Ecroyd

    Accepted manuscript online: 12 FEB 2016 09:04AM EST | DOI: 10.1111/jnc.13575

  3. Enhanced Ubiquitination and Proteasomal-degradation of Catalytically-deficient Human Choline Acetyltransferase Mutants

    Trevor M. Morey, Shawn Albers, Brian H. Shilton and R Jane Rylett

    Accepted manuscript online: 12 FEB 2016 08:52AM EST | DOI: 10.1111/jnc.13574

  4. Conventional protein kinase Cβ-mediated phosphorylation inhibits collapsin response-mediated protein 2 proteolysis and alleviates ischemic injury in cultured cortical neurons and ischemic stroke-induced mice

    Xuan Yang, Xinxin Zhang, Yun Li, Song Han, David W. Howells, Shujuan Li and Junfa Li

    Article first published online: 11 FEB 2016 | DOI: 10.1111/jnc.13538

    Thumbnail image of graphical abstract

    Focal cerebral ischemia induces a large flux of Ca2+ to activate calpain which cleaves collapsin response mediator (CRMP) 2 into breakdown product (BDP). Inhibition of CRMP2 cleavage by calpeptin and TAT-CRMP2 alleviates ischemic injury. Conventional protein kinase C (cPKC)β-mediated phosphorylation could inhibit CRMP2 proteolysis and alleviate ischemic injury in cultured cortical neurons and ischemic stroke-induced mice.

  5. Loss of stability and hydrophobicity of presenilin 1 mutations causing Alzheimer's disease

    Arun Kumar Somavarapu and Kasper P. Kepp

    Article first published online: 11 FEB 2016 | DOI: 10.1111/jnc.13535

    Thumbnail image of graphical abstract

    Close to 200 mutations in presenilin 1 (PSEN1) cause Alzheimer's disease, but the biochemical relating these to disease remains debated. The chemical properties of PSEN1 variants were computed and correlated against clinical age of symptom onset. Loss of stability and hydrophobicity and gain of polarity relate to disease onset, suggesting that mutants impair the membrane structure of PSEN1 and that therapies should increase PSEN1 structural integrity.

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