Journal of Neurochemistry (J NEUROCHEM)

Publisher: International Society for Neurochemistry, Wiley

Journal description

The Journal of Neurochemistry is the leading source for current research worldwide on the molecular chemical and cellular biology of the nervous system. Each issue contains dozens of full-length presentations of significant original findings written by investigators at leading medical and research institutions around the world. The Journal of Neurochemistry is devoted to the prompt publication of high-quality original findings in areas relevant to molecular chemical and cell biological aspects of the nervous system. Papers that are wholly pharmalogical histochemical or immunological and methods papers or the cloning of confirmatory sequences that do not advance knowledge in neurochemistry are not normally considered. The Journal particularly encourages submissions in the areas of molecular and cellular biology. A highlight of each issue is the Journal's critically acclaimed Rapid Communications section presenting new ideas and data of particular importance and timeliness. The Journal's Mini-Reviews present concise self-contained summaries of current research in particularly important areas.

Current impact factor: 4.28

Impact Factor Rankings

2015 Impact Factor Available summer 2016
2014 Impact Factor 4.281
2013 Impact Factor 4.244
2012 Impact Factor 3.973
2011 Impact Factor 4.061
2010 Impact Factor 4.337
2009 Impact Factor 3.999
2008 Impact Factor 4.5
2007 Impact Factor 4.451
2006 Impact Factor 4.26
2005 Impact Factor 4.604
2004 Impact Factor 4.824
2003 Impact Factor 4.825
2002 Impact Factor 4.969
2001 Impact Factor 4.834
2000 Impact Factor 4.9
1999 Impact Factor 4.906
1998 Impact Factor 4.651
1997 Impact Factor 4.234
1996 Impact Factor 4.219
1995 Impact Factor 4.852
1994 Impact Factor 4.525
1993 Impact Factor 4.223
1992 Impact Factor 4.215

Impact factor over time

Impact factor

Additional details

5-year impact 3.97
Cited half-life 9.60
Immediacy index 1.00
Eigenfactor 0.05
Article influence 1.20
Website Journal of Neurochemistry website
Other titles Journal of neurochemistry, JNC
ISSN 0022-3042
OCLC 1782775
Material type Periodical, Internet resource
Document type Journal / Magazine / Newspaper, Internet Resource

Publisher details


  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author cannot archive a post-print version
  • Restrictions
    • 12 months embargo
  • Conditions
    • Some journals have separate policies, please check with each journal directly
    • On author's personal website, institutional repositories, arXiv, AgEcon, PhilPapers, PubMed Central, RePEc or Social Science Research Network
    • Author's pre-print may not be updated with Publisher's Version/PDF
    • Author's pre-print must acknowledge acceptance for publication
    • Non-Commercial
    • Publisher's version/PDF cannot be used
    • Publisher source must be acknowledged with citation
    • Must link to publisher version with set statement (see policy)
    • If OnlineOpen is available, BBSRC, EPSRC, MRC, NERC and STFC authors, may self-archive after 12 months
    • If OnlineOpen is available, AHRC and ESRC authors, may self-archive after 24 months
    • Publisher last contacted on 07/08/2014
    • This policy is an exception to the default policies of 'Wiley'
  • Classification

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: This Editorial highlights a study by Hermey and colleagues in the current issue of Journal of Neurochemistry. In their study, the authors provide novel insights into single-nucleotide polymorphisms associated with Alzheimer's disease and linked to the SorCS1 gene, toward a better understanding of the interaction of sorting receptor proteins which physically interact with the amyloid-beta protein precursor (APP). SorCS1, sortilin-related VPS10 domain-containing receptor 1; SorLA, sortilin-related Receptor with A-type Repeats. Read the full article ‘SorCS1 variants and amyloid precursor protein (APP) are co-transported in neurons but only SorCS1c modulates anterograde APP transport’ on page 60.
    Journal of Neurochemistry 10/2015; 135(1):1-3. DOI:10.1111/jnc.13231
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    ABSTRACT: Chronic activity perturbation in neurons can trigger homeostatic mechanisms to restore the baseline function. Although the importance and dysregulation of neuronal activity homeostasis has been implicated in neurological disorders such as epilepsy, the complete signaling by which chronic changes in neuronal activity initiate the homeostatic mechanisms is unclear. We report here that the tumor suppressor p53 and its signaling are involved in neuronal activity homeostasis. Upon chronic elevation of neuronal activity in primary cortical neuron cultures, the ubiquitin E3 ligase Mdm2 is phosphorylated by the kinase Akt. Phosphorylated Mdm2 triggers the degradation of p53 and subsequent induction of a p53 target gene, Nedd4-2. Nedd4-2 encodes another ubiquitin E3 ligase. We identified GluA1 subunit of AMPA receptors as a novel substrate of Nedd4-2. The regulation of GluA1 level is known to be crucial for neuronal activity homeostasis. We confirmed that, by pharmacologically inhibiting Mdm2-mediated p53 degradation or genetically reducing Nedd4-2 in a mouse model, the GluA1 ubiquitination and down-regulation induced by chronically elevated neuronal activity are both attenuated. Our findings demonstrate the first direct function of p53 in neuronal homeostasis and elucidate a new mechanism by which cortical neurons respond to chronic activity perturbation. This article is protected by copyright. All rights reserved. This article is protected by copyright. All rights reserved.
    Journal of Neurochemistry 08/2015; 135(2). DOI:10.1111/jnc.13271

  • Journal of Neurochemistry 07/2015;

  • Journal of Neurochemistry 05/2015; in press.
  • [Show abstract] [Hide abstract]
    ABSTRACT: A major hallmark feature of Alzheimer's disease (AD) is the accumulation of amyloid β (Aβ), whose formation is regulated by the γ-secretase complex and its activating protein (also known as γ-secretase activating protein, or GSAP). Because GSAP interacts with the γ-secretase without affecting the cleavage of Notch, it is an ideal target for a viable anti-Aβ therapy. GSAP derives from a C-terminal fragment of a larger precursor protein of 98kDa via a caspase-3-mediated cleavage. However, the mechanism(s) involved in its degradation are unknown. In the current paper, we show that GSAP has a short half-life of approximately 5 hours. Neuronal cells treated with proteasome inhibitors markedly prevented GSAP protein degradation, which was associated with a significant increment in Aβ levels and γ-secretase cleavage products. By contrast, treatment with calpain blocker and lysosome inhibitors had no effect. In addition, we provide experimental evidence that GSAP is ubiquitinated. Taken together, our findings reveal that GSAP is degraded through the ubiquitin-proteasome system. Modulation of the GSAP degradation pathway may be implemented as a viable target for a safer anti-Aβ therapeutic approach in AD. This article is protected by copyright. All rights reserved. This article is protected by copyright. All rights reserved.
    Journal of Neurochemistry 12/2014; 133(3). DOI:10.1111/jnc.13011
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    ABSTRACT: Tumor necrosis factor alpha (TNF-α) is known to exacerbate ischemic brain injury; however, the mechanism is unknown. Previous studies have evaluated the effects of TNF-α on neurons with long exposures to high doses of TNF-α, which is not pathophysiologically relevant. We characterized the rapid effects of TNF-α on basal respiration, ATP production, and maximal respiration using pathophysiologically relevant, post-stroke concentrations of TNF-α. We observed a reduction in mitochondrial function as early as 1.5 hours after exposure to low doses of TNF-α, followed by a decrease in cell viability in HT-22 cells and primary neurons. Subsequently, we used the HT-22 cell line to determine the mechanism by which TNF-α causes a rapid and profound reduction in mitochondrial function. Pre-treating with TNF-R1 antibody, but not TNF-R2 antibody, ameliorated the neurotoxic effects of TNF-α, indicating that TNF-α exerts its neurotoxic effects through TNF-R1. We observed an increase in caspase 8 activity and a decrease in mitochondrial membrane potential after exposure to TNF-α which resulted in a release of cytochrome c from the mitochondria into the cytosol. These novel findings indicate for the first time that an acute exposure to pathophysiologically relevant concentrations of TNF-α has neurotoxic effects mediated by a rapid impairment of mitochondrial function. This article is protected by copyright. All rights reserved. This article is protected by copyright. All rights reserved.
    Journal of Neurochemistry 12/2014; 132(4). DOI:10.1111/jnc.13008
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    ABSTRACT: For over the last 50 years, the molecular mechanism of antipsychotic drugs' action has been far from clear. While risperidone is very often used in clinical practice, the most efficient known antipsychotic drug is clozapine. However, the biochemical background of clozapine's action still remains elusive. In the present study, we performed comparative proteomic analysis of rat cerebral cortex following chronic administration of these two drugs. We observed significant changes in the expression of cytoskeletal, synaptic and regulatory proteins caused by both antipsychotics. Among other proteins, alterations in collapsin response mediator proteins, CRMP2 and CRMP4, were the most spectacular consequences of treatment with both drugs. Moreover, risperidone increased the level of proteins involved in cell proliferation such as fatty acid binding protein-7 and translin-associated factor X. Clozapine significantly upregulated the expression of visinin-like protein 1, neurocalcin δ and mitochondrial, stomatin-like protein 2, the calcium-binding proteins regulating calcium homeostasis and the functioning of ion channels and receptors. This article is protected by copyright. All rights reserved. This article is protected by copyright. All rights reserved.
    Journal of Neurochemistry 12/2014; 132(6). DOI:10.1111/jnc.13007
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    ABSTRACT: A hallmark of ischemic/reperfusion injury is a change in subunit composition of synaptic AMPARs. This change in AMPAR subunit composition leads to an increase in surface expression of GluA2-lacking Ca(2+) /Zn(2+) permeable AMPARs. These GluA2-lacking AMPARs play a key role in promoting delayed neuronal death following ischemic injury. At present, the mechanism(s) responsible for the ischemia/reperfusion-induced subunit composition switch and degradation of the GluA2 subunit remain unclear. In this study, we investigated the role of NADPH oxidase, and its importance in mediating endocytosis and subsequent degradation of the GluA2 AMPAR subunit in adult rat hippocampal slices subjected to oxygen-glucose deprivation/reperfusion (OGD/R) injury. In hippocampal slices pretreated with the NADPH oxidase inhibitor apocynin attenuated OGD/R-mediated sequestration of GluA2 and GluA1 as well as prevent the degradation of GluA2. We provide compelling evidence that NADPH oxidase mediated sequestration of GluA1- and GluA2- involved activation of p38 MAPK. Furthermore, we demonstrate that inhibition of NADPH oxidase blunts the OGD/R-induced association of GluA2 with protein interacting with C kinase-1 (PICK1). In summary, this study identifies a novel mechanism that may underlie the ischemia/reperfusion-induced AMPAR subunit composition switch and a potential therapeutic target. This article is protected by copyright. All rights reserved. This article is protected by copyright. All rights reserved.
    Journal of Neurochemistry 12/2014; 132(5). DOI:10.1111/jnc.13005
  • [Show abstract] [Hide abstract]
    ABSTRACT: An important pathological hallmark of Alzheimer's disease (AD) is the deposition of amyloid-beta (Aβ) peptides in the brain parenchyma, leading to neuronal death and impaired learning and memory. The protease γ-secretase is responsible for the intramembrane proteolysis of the amyloid-β precursor protein (APP), which leads to the production of the toxic Aβ peptides. Thus, an attractive therapeutic strategy to treat AD is the modulation of the γ-secretase activity, to reduce Aβ42 production. Because phosphorylation of proteins is a post-translational modification known to modulate the activity of many different enzymes, we used electrospray (LC-MS/MS) mass spectrometry to identify new phosphosites on highly purified human γ-secretase. We identified eleven new single or double phosphosites in two well-defined domains of Presenilin-1 (PS1), the catalytic subunit of the γ-secretase complex. Next, mutagenesis and biochemical approaches were used to investigate the role of each phosphosite in the maturation and activity of γ-secretase. Together, our results suggest that the newly identified phosphorylation sites in PS1 do not modulate γ-secretase activity and the production of the Alzheimer's Aβ peptides. Individual PS1 phosphosites shall probably not be considered therapeutic targets for reducing cerebral Aβ plaque formation in Alzheimer's disease. This article is protected by copyright. All rights reserved. This article is protected by copyright. All rights reserved.
    Journal of Neurochemistry 12/2014; 133(3). DOI:10.1111/jnc.12996

  • Journal of Neurochemistry 12/2014; 131(6):878-878. DOI:10.1111/jnc.12952
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    ABSTRACT: While motivated behavior involves multiple neurochemical systems, few studies have focused on the role of glutamate, the brain's excitatory neurotransmitter, and glucose, the energetic substrate of neural activity in reward-related neural processes. Here, we used high-speed amperometry with enzyme-based substrate-sensitive and control, enzyme-free biosensors to examine second-scale fluctuations in the extracellular levels of these substances in the nucleus accumbens shell during glucose-drinking behavior in trained rats. Glutamate rose rapidly after the presentation of a glucose-containing cup and before the initiation of drinking (reward seeking), decreased more slowly to levels below baseline during consumption (sensory reward), and returned to baseline when the ingested glucose reached the brain (metabolic reward). When water was substituted for glucose, glutamate rapidly increased with cup presentation and in contrast to glucose drinking, increased above baseline after rats tasted the water and refused to drink further. Therefore, extracellular glutamate show distinct changes associated with key events of motivated drinking behavior and opposite dynamics during sensory and metabolic components of reward. In contrast to glutamate, glucose increased at each stimulus and behavioral event, showing a sustained elevation during the entire behavior and a robust post-ingestion rise that correlated with the gradual return of glutamate levels to their baseline. By comparing active drinking with passive intra-gastric glucose delivery, we revealed that fluctuations in extracellular glucose are highly dynamic, reflecting a balance between rapid delivery due to neural activity, intense metabolism, and the influence of ingested glucose reaching the brain This article is protected by copyright. All rights reserved.
    Journal of Neurochemistry 11/2014; 132(3). DOI:10.1111/jnc.12993