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: 4.78

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 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 5.02
Cited half-life 0.00
Immediacy index 1.19
Eigenfactor 0.08
Article influence 1.94
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
    ​ white

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: In blood platelets, stimulation of G protein-coupled receptors by thrombin triggers the activation of Src family kinases (SFKs), resulting in the tyrosine-phosphorylation of multiple substrates, but the mechanism underlying this process is still poorly understood. Here we show that the time-dependent protein-tyrosine phosphorylation triggered by thrombin in human or murine platelets was totally suppressed only upon concomitant chelation of intracellular Ca2+ and inhibition of SFKs. Thrombin-induced activation of SFKs was regulated by intracellular Ca2+, and accordingly, the Ca2+ ionophore A23187 was sufficient to stimulate SFKs. A23187 also triggered the phosphorylation and activation of the Ca2+-dependent focal adhesion kinase Pyk2, and Pyk2 activation by thrombin was Ca2+-dependent. Stimulation of SFKs by thrombin or A23187 was strongly reduced in platelets from Pyk2 knockout mice, as it was the overall pattern of protein-tyrosine phosphorylation. By immunoprecipitation experiments, we demonstrate that Lyn and Fyn, but not Src, were activated by Pyk2. Inhibition of SFKs by PP2 also reduced the phosphorylation of Pyk2 in thrombin- or A23187-stimulated platelets. Analysis of knockout mice demonstrated that Fyn, but not Lyn, was required for complete Pyk2 phosphorylation by thrombin. Finally, PP2 reduced aggregation of murine platelets to a level comparable to that of Pyk2-deficient platelets, but did not have further effects in the absence of Pyk2. These results indicate that in thrombin-stimulated platelets, stimulation of Pyk2 by intracellular Ca2+ initiates SFKs activation, establishing a positive loop that reinforces the Pyk2/SFK axis and allows the subsequent massive tyrosine phosphorylation of multiple substrates required for platelet aggregation.
    Biochemical Journal 05/2015;
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    ABSTRACT: RecQ helicases are a family of highly conserved proteins that maintain genomic stability through their important roles in replication restart mechanisms. Cellular phenotypes of RECQ1 deficiency are indicative of aberrant repair of stalled replication forks, but the molecular functions of RECQ1, the most abundant of the five known human RecQ homologs, have remained poorly understood. We show that RECQ1 associates with FEN-1 in nuclear extracts and exhibits direct protein interaction in vitro. Recombinant RECQ1 significantly stimulated FEN-1 endonucleolytic cleavage of 5'-flap DNA substrates containing nontelomeric or telomeric repeat sequence. RECQ1 and FEN-1 were constitutively present at telomeres and their binding to the telomeric chromatin was enhanced following DNA damage. Telomere residence of FEN-1 was dependent on RECQ1 since depletion of RECQ1 reduced FEN-1 binding to telomeres in unperturbed cycling cells. Our results confirm a conserved collaboration of human RecQ helicases with FEN-1, and suggest both overlapping and specialized roles of RECQ1 in the processing of DNA structure intermediates proposed to arise during replication, repair and recombination.
    Biochemical Journal 03/2015; DOI:10.1042/BJ20141021
  • [Show abstract] [Hide abstract]
    ABSTRACT: The serotonin (5-HT) transporter (SERT) controls serotonergic neurotransmission in the brain by rapid clearance of 5-HT from the synaptic cleft into presynaptic neurons. SERTs are primary target for antidepressants for therapeutic intervention of mood disorders. Our previous studies have identified the involvement of several signaling pathways and protein kinases in regulating SERT function, trafficking and phosphorylation. However, whether the protein kinase B/Akt regulates SERT function is not known. Here, we made novel observation that inhibition of Akt resulted in the down regulation of SERT function through the regulation of SERT trafficking and phosphorylation. Akt inhibitor Akt X reduced the endogenously phosphorylated Akt and significantly decreased 5-HT uptake and 5-HT uptake capacity. Furthermore, SERT activity is also reduced by small interfering RNA downregulation of total and phospho-Akt levels. The reduction in SERT activity is paralleled by lower level of surface SERT protein, reduced SERT exocytosis with no effect on SERT endocytosis and accumulation of SERT in intracellular endocytic compartments with the most prominent localization to late endosomes and lysosomes. Akt2 inhibitor was more effective than Akt1 inhibitor in inhibiting SERT activity. Inhibition of downstream Akt kinase GSK3a/ß stimulates SERT function. Akt inhibition leads to decrease in SERT basal phosphorylation. Our results provide evidence that Akt regulates SERT function and cell surface expression by regulating the intracellular SERT distribution and plasma membrane availability, which perhaps may be linked to SERT phosphorylation state. Thus, any changes in the activation of Akt and/or GSK3a/ß could alter SERT mediated 5-HT clearance and subsequently serotonergic neurotransmission.
    Biochemical Journal 03/2015; DOI:10.1042/BJ20140826
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    ABSTRACT: Peroxiredoxin-6 (PRDX6) is an unusual member of the peroxiredoxin family of antioxidant enzymes that has only one evolutionarily conserved cysteine. It reduces oxidized lipids and ROS by oxidation of the active site cysteine (Cys-47) to a sulfenic acid, but the mechanism for conversion back to a sulfhydryl is not completely understood. Moreover, it has a phospholipase A2 activity in addition to its peroxidase activity. Interestingly, some biochemical data are inconsistent with a known high-resolution crystal structure of the catalytic intermediate of the protein, and biophysical data indicate the protein undergoes conformational changes that affect enzyme activity. In order to further elucidate the solution structure of this important enzyme, we used chemical cross-linking coupled with high-resolution mass spectrometry (CX-MS), with an emphasis on zero-length cross-links. Distance constraints from high confidence cross-links were used in homology modeling experiments to determine a solution structure of the reduced form of the protein. This structure was further evaluated using chemical cross-links produced by several homo-bifunctional amine-reactive cross-linking reagents, which helped confirm the solution structure. The results show that several regions of the reduced version of human PRDX6 are in a substantially different conformation from that shown for the crystal structure of the peroxidase catalytic intermediate. The differences between these two structures are likely to reflect catalysis-related conformational changes. These studies also demonstrate that CX-MS using zero-length cross-linking is a powerful strategy for probing protein conformational changes that is complementary to alternative methods such as crystallographic, NMR, and biophysical studies.
    Biochemical Journal 03/2015; DOI:10.1042/BJ20141463
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    ABSTRACT: Proteins of the echinoderm microtubule associated protein-like (EML) family contribute to formation of the mitotic spindle and interphase microtubule (MT) network. EML1-4 consist of WD40 repeats and an N-terminal region containing a putative coiled-coil. Recurrent gene rearrangements in non-small cell lung cancer (NSCLC) fuse EML4 to anaplastic lymphoma kinase (ALK) causing expression of several oncogenic fusion variants. The fusions have constitutive ALK activity due to self-association through the EML4 coiled-coil. We have determined crystal structures of the coiled-coils from EML2 and EML4, which describe the structural basis of both EML self-association and oncogenic EML4-ALK activation. The structures reveal a trimeric oligomerization state directed by a conserved pattern of hydrophobic residues and salt bridges. We show that the trimerization domain (TD) of EML1 is necessary and sufficient for self-association. The TD is also essential for MT binding, however this property requires an adjacent basic region. These observations prompted us to investigate MT association of EML4-ALK and EML1-ABL1 fusions in which variable portions of the EML component are present. Uniquely, EML4-ALK variant 3, which includes the TD and basic region of EML4 but none of the WD40 repeats, was localized to MTs, both when expressed recombinantly and in a patient-derived NSCLC cell line (H2228). This raises the question of whether the mislocalization of ALK activity to MTs might influence downstream signalling and malignant properties of cells. Furthermore, the structure of EML4 TD may enable the development of protein-protein interaction inhibitors targeting the trimerization interface, providing a possible avenue towards therapeutic intervention in EML4-ALK NSCLC.
    Biochemical Journal 03/2015; DOI:10.1042/BJ20150039
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    ABSTRACT: Tandem-arranged PDZ domains often form structural and functional supramodules with distinct target-binding properties. Here, we found that the two PDZ domains within the PDZ34 tandem of Scribble, a cell polarity regulator, tightly pack in a "front-to-back" mode to form a compact supramodule. Although PDZ4 contains a distorted αB/βB pocket, the attachment of PDZ4 to PDZ3 generates an unexpected interdomain pocket that is adjacent to and integrates with the canonical αB/βB pocket of PDZ3 to form an expanded target-binding groove. The structure of the PDZ34/target peptide complex further demonstrated that the peptide binds to this expanded target-binding groove with its upstream residues anchoring into the interdomain pocket directly. Mutations of the interdomain pocket or disruptions of the PDZ34 supramodule both interfere with its target-binding capacity. Therefore, the interdomain interface between the PDZ34 supramodule is intrinsically required for its target recognition and determines its target-binding specificity. This interdomain interface-mediated specific recognition may represent a novel mode of target recognition and would broaden the target-binding versatility for PDZ supramodules. The supramodular nature and target recognition mode of the PDZ34 tandem found in this study would also help to identify the new binding partners of Scribble and thus may direct the further research on the PDZ domain-mediated assembly of Scribble polarity complexes.
    Biochemical Journal 03/2015; 468(1). DOI:10.1042/BJ20141473