Biochemical Journal Impact Factor & Information

Publisher: Biochemical Society (Great Britain), Portland Press

Journal description

The Biochemical Journal publishes over 7000 pages of high-quality scientific information every year. The papers are carefully selected by an international editorial board to cover all aspects of biochemistry, and cell and molecular biology. The journal features regular papers, authoritative reviews, research communications (short articles reporting novel and significant findings) and correspondence.

Current impact factor: 4.40

Impact Factor Rankings

2015 Impact Factor Available summer 2016
2014 Impact Factor 4.396
2013 Impact Factor 4.779
2012 Impact Factor 4.654
2011 Impact Factor 4.897
2010 Impact Factor 5.016
2009 Impact Factor 5.155
2008 Impact Factor 4.371
2007 Impact Factor 4.009
2006 Impact Factor 4.1
2005 Impact Factor 4.224
2004 Impact Factor 4.278
2003 Impact Factor 4.101
2002 Impact Factor 4.589
2001 Impact Factor 4.326
2000 Impact Factor 4.28
1999 Impact Factor 4.349
1998 Impact Factor 3.855
1997 Impact Factor 3.579
1996 Impact Factor 3.687
1995 Impact Factor 4.159
1994 Impact Factor 4.262
1993 Impact Factor 3.659
1992 Impact Factor 3.716

Impact factor over time

Impact factor

Additional details

5-year impact 4.66
Cited half-life >10.0
Immediacy index 0.89
Eigenfactor 0.06
Article influence 1.75
Website Biochemical Journal website
Other titles Biochemical journal (London, England: 1984), Biochemical journal
ISSN 0264-6021
OCLC 10379627
Material type Periodical, Internet resource
Document type Journal / Magazine / Newspaper, Internet Resource

Publisher details

Portland Press

  • Pre-print
    • Author cannot archive a pre-print version
  • Post-print
    • Author cannot archive a post-print version
  • Restrictions
    • 6 months embargo
  • Conditions
    • On author's personal website or institutional repository
    • Accepted version may be placed on PubMed Central and Europe PMC after 12 months from publication
    • Must link to journal website
    • Published source must be acknowledged ('The final version of record is available at [insert Journals URL]')
    • Publisher's version/PDF cannot be used
    • Must link to journal website, e.g. with a DOI
  • Classification

Publications in this journal

  • Biochemical Journal 12/2015; 472(3):249-259. DOI:10.1042/BJ20150832

  • Biochemical Journal 12/2015; 472(3):e27-e30. DOI:10.1042/BJ20151016

  • Biochemical Journal 12/2015; 472(2):e25-e26. DOI:10.1042/BJ20150970

  • Biochemical Journal 12/2015; 472(2):135-146. DOI:10.1042/BJ20150837
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    ABSTRACT: The fatty acid-binding proteins (FABPs) are a family of low-molecular weight, intracellular lipid-binding proteins consisting of ten isoforms. FABPs are involved in binding and storing hydrophobic ligands such as long-chain fatty acids, as well as transporting these ligands to the appropriate compartments in the cell. FABP5 is overexpressed in multiple types of tumors. Furthermore, upregulation of FABP5 is strongly associated with poor survival in triple-negative breast cancer. However, the mechanisms underlying the specific upregulation of the FABP5 gene in these cancers remain poorly characterized. In this study, we determined that FABP5 has a typical CpG island around its promoter region. The DNA methylation status of the CpG island in the FABP5 promoter of benign prostate cells (PNT2), prostate cancer cells (PC-3, DU-145, 22Rv1 and LNCaP) and human normal or tumor tissue was assessed by bisulfite sequencing analysis, and then confirmed by combined bisulfite restriction analysis (COBRA) and quantitative analysis of DNA methylation using real-time PCR (qAMP). These results demonstrated that overexpression of FABP5 in prostate cancer cells can be attributed to hypomethylation of the CpG island in its promoter region, along with upregulation of the direct trans-acting factors SP1 and c-MYC. Together, these mechanisms result in the transcriptional activation of FABP5 expression during human prostate carcinogenesis. Importantly, silencing of SP1, c-MYC, or FABP5 expression led to a significant decrease in cell proliferation, indicating that upregulation of FABP5 expression by SP1 and c-MYC is critical for the proliferation of prostate cancer cells.
    Biochemical Journal 11/2015; DOI:10.1042/BJ20150926
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    ABSTRACT: Mammalian 2-Cys peroxiredoxins are susceptible to hyperoxidation by excess H2O2. The cytoplasmic family member Prx2 hyperoxidizes more readily than mitochondrial Prx3 due to slower dimerization of the sulfenic acid intermediate. Four variant amino acids near the C-terminus have been shown to contribute to this difference. We have performed kinetic analysis of the relationship between hyperoxidation and disulfide formation, using whole protein mass spectrometry and comparing wild type Prx2 and Prx3 with tail-swap mutants in which the four amino acids were reversed. These changes make Prx3 more sensitive and Prx2 less sensitive to hyperoxidation, and accounted for ~70% of the difference between the two proteins. The tail swap mutant of Prx3 was also more susceptible when expressed in the mitochondria of HeLa cells. The hyperoxidized product at lower excesses of H2O2 was a semi-hyperoxidized dimer with one active site disulfide and the other a sulfinic acid. For Prx2, increasing the H2O2 concentration resulted in complete hyperoxidation. In contrast, only about half the Prx3 active sites underwent hyperoxidation and even with high H2O2 the predominant product was the hyperoxidized dimer. Size exclusion chromatography showed that the oligomeric forms of all redox states of Prx3 dissociated more readily into dimeric units than their Prx2 counterparts. Notably the species with one disulfide and one hyperoxidized active site was decameric for Prx2 and dimeric for Prx3. Reduction and re-oxidation of the hyperoxidized dimer of Prx3 produced hyperoxidized monomers, implying dissociation and rearrangement of the subunits of the functional homodimer.
    Biochemical Journal 11/2015; DOI:10.1042/BJ20150572
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    ABSTRACT: The eukaryotic translation initiation factor eIF2B is a multi-subunit complex with a crucial role in the regulation of global protein synthesis in the cell. The complex is comprised of five subunits, termed α through ε in order of increasing size, arranged as a heterodecamer with two copies of each subunit. Regulation of the co-stoichiometric expression of the eIF2B subunits is crucial for the proper function and regulation of the eIF2B complex in cells. We have investigated the control of stoichiometric eIF2B complexes through mutual stabilisation of eIF2B subunits. Our data show that the stable expression of the catalytic eIF2Bε subunit in human cells requires co-expression of eIF2Bγ. Similarly, stable expression of eIF2Bδ requires both eIF2Bβ and eIF2Bγ+ε. The expression of these subunits decreases despite there being no change in either the levels or the translation of their mRNAs. Instead, these subunits are targeted for degradation by the ubiquitin-proteasome system. The data allow us to propose a model for the formation of stoichiometric eIF2B complexes which can ensure their stoichiometric incorporation into the holocomplex.
    Biochemical Journal 11/2015; DOI:10.1042/BJ20150828
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    ABSTRACT: Ca(2+) release is tightly sequestered in eukaryotic cells to enable fine spatio-temporal control of signaling but how Ca(2+) release from the endoplasmic reticulum (ER) is linked to cell adhesions is not defined. We examined the spatial restriction of Ca(2+) release through the inositol triphosphate receptor (IP3R1) in response to IL-1 and the functions of the adhesion-associated proteins, focal adhesion kinase (FAK) and protein tyrosine phosphatase-a (PTPa). In cultured fibroblasts IL-1 treatment promoted co-localization of PTPa and FAK with the ER and increased association of IP3R1 with PTPa and FAK at focal adhesions. GST pull-down assays of purified proteins demonstrated that PTP-a and FAK directly interacted with IP3R1. These interactions depended on the FAT and FERM domains of FAK. PTPa was required for the association of IP3R1 with Src, which mediated IP3R1 phosphorylation and consequently ER Ca(2+) release. Collectively, these data indicate that PTPa and FAK, which are enriched in focal adhesions, interact with IP3R1 at adjacent ER sites to spatially sequester IL-1-induced Ca(2+) signaling.
    Biochemical Journal 11/2015; DOI:10.1042/BJ20150907
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    ABSTRACT: Overactivation of the Wnt signaling pathway underlies oncogenic transformation and proliferation in many cancers, including the triple-negative breast cancer (TNBC) - the deadliest form of tumor in the breast, taking about a quarter of a million lives annually world-wide. No clinically approved targeted therapies attacking Wnt signaling currently exist. Repositioning of approved drugs is a promising approach in drug discovery. Here we show that a multi-purpose drug suramin inhibits Wnt signaling and proliferation of TNBC cells in vitro and in mouse models, inhibiting a component in the upper levels of the pathway. Through a set of investigations we identify heterotrimeric G proteins and regulation of Wnt endocytosis as the likely target of suramin in this pathway. G protein-dependent endocytosis of plasma membrane-located components of the Wnt pathway was previously shown to be important for amplification of the signal in this cascade. Our data identify endocytic regulation within Wnt signaling as a promising target for anti-Wnt and anti-cancer drug discovery. Suramin, as the first example of such drug, or its analogs might pave the way for appearance of first-in-class targeted therapies against TNBC and other Wnt-dependent cancers.
    Biochemical Journal 11/2015; DOI:10.1042/BJ20150913
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    ABSTRACT: The BRICHOS domain is associated with proliferative, degenerative and amyloid diseases, and it has been shown to inhibit fibril formation and toxicity of the Alzheimer disease associated amyloid-β peptide. Prosurfactant protein C (proSP-C) BRICHOS binds to stretches of hydrophobic amino acid residues, which are unfolded or in β-strand conformation, suggesting that it may have broad anti-amyloid activity. We have studied the effect of the proSP-C BRICHOS domain on the designed amyloidogenic β-sheet proteins β17 and β23. β17 expressed in the secretory pathway of HEK293 cells forms intracellular inclusions, while β23 is rapidly degraded. Co-expression of BRICHOS leads to a reduction in β17 inclusion size and increased levels of soluble β17 and β23. Furthermore, BRICHOS interacts with the β-proteins intracellularly, reduces their ubiquitination, and decreases aggresome formation and proteasomal inhibition. Collectively, these data suggest that BRICHOS is capable of delaying the aggregation process and toxicity of amyloidogenic proteins in a generic manner.
    Biochemical Journal 11/2015; DOI:10.1042/BJ20150920

  • Biochemical Journal 11/2015; 472(1):17-32. DOI:10.1042/BJ20150710

  • Biochemical Journal 11/2015; 472(1):1-15. DOI:10.1042/BJ20150787
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    ABSTRACT: Homocysteine S -methyltransferases (HMTs, EC catalyze the conversion of homocysteine to methionine using S -methylmethionine or S -adenosylmethionine as the methyl donor. HMTs play an important role in methionine biosynthesis and are widely distributed among microorganisms, plants, and animals. Additionally, HMTs play a role in metabolite repair of S -adenosylmethionine by removing an inactive diastereomer from the pool. The mmuM gene product from Escherichia coli is an archetypal HMT family protein and contains a predicted Zn-binding motif in the enzyme active site. Here we present X-ray structures for MmuM in oxidized, apo, and metallated forms, representing the first such structures for any member of the HMT family. The structures reveal a metal/substrate binding pocket distinct from those in related enzymes. The presented structure analysis and modelling of co-substrate interactions provide valuable insight into the function of MmuM in both methionine biosynthesis and cofactor repair.
    Biochemical Journal 11/2015; DOI:10.1042/BJ20150980
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    ABSTRACT: Thioredoxin interacting protein (TXNIP) negatively regulates the antioxidative activity of thioredoxin, and participates in pleiotropic cellular processes. Its deregulation is linked to various human diseases including diabetes, acute myeloid leukemia and cardiovascular diseases. The E3 ubiquitin ligase Itch polyubiquitinates TXNIP to promote its degradation via the ubiquitin proteasome pathway, and this Itch-mediated poly-ubiquitination of TXNIP is dependent on the interaction of the four WW domains of Itch with the two PPxY motifs of TXNIP. However, the molecular mechanism of this interaction of TXNIP with Itch remains elusive. In this study, we found that each of the four WW domains of Itch exhibited different binding affinities to TXNIP, while multivalent engagement between the four WW domains of Itch and the two PPxY motifs of TXNIP resulted in their strong binding avidity. Our structural analyses demonstrated that the third and fourth WW domains of Itch were able to recognize both PPxY motifs of TXNIP simultaneously, supporting a multivalent binding mode between Itch and TXNIP. Interestingly, phosphorylation status on the tyrosine residue of the PPxY motifs of TXNIP serves as a molecular switch in its choice of binding partners and thereby downstream biological signaling outcomes. Phosphorylation of this tyrosine residue of TXNIP diminished the binding capability of PPxY motifs of TXNIP to Itch, whereas this phosphorylation is a prerequisite to the binding activity of TXNIP to SH2 domain containing protein SHP2 and their roles in stabilizing the phosphorylation and activation of CSK.
    Biochemical Journal 11/2015; DOI:10.1042/BJ20150830
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    ABSTRACT: Although it is well established that the release of HCV occurs through the secretory pathway, many aspects concerning the control of this process are not yet fully understood. α-taxilin was identified as a novel binding partner of syntaxin-4 and of other members of the syntaxin family, which are part of SNARE complexes and so are involved in intracellular vesicle traffic. Since α-taxilin prevents t-SNARE formation by binding exclusively to free syntaxin-4 it exerts an inhibitory effect on the vesicular transport. HCV replicating Huh7.5 cells and HCV-infected primary human hepatocytes and liver samples of patients suffering from chronic HCV contain significant less α-taxilin as compared to the controls. HCV impairs the expression of α-taxilin via NS5A-dependent interruption of the Raf-MEK-signal transduction cascade. Moreover, the half-life time of α-taxilin is significantly reduced in HCV-replicating cells. While modulation of α-taxilin expression does not significantly affect genome replication, the overexpression of α-taxilin prevents the release of HCV. In contrast to this, silencing of α-taxilin expression leads to increased release of infectious viral particles. This is due to the negative effect of α-taxilin on t-SNARE formation that leads to impaired vesicular trafficking. In accordance to this, overexpression of the t-SNARE component syntaxin-4 increases release of HCV, while silencing leads to an impaired release. These data identify α-taxilin as a novel factor that controls the release of HCV and reveal the mechanism by which HCV controls the activity of α-taxilin.
    Biochemical Journal 11/2015; DOI:10.1042/BJ20150717

  • Biochemical Journal 11/2015; 471(3):347-356. DOI:10.1042/BJ20150676