Journal of Biological Chemistry Impact Factor & Information

Publisher: American Society of Biological Chemists; Rockefeller Institute for Medical Research; American Society for Biochemistry and Molecular Biology, American Society for Biochemistry and Molecular Biology

Journal description

Complete content of the Journal of Biological Chemistry as of April 1995.

Current impact factor: 4.60

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 Impact Factor 4.6
2012 Impact Factor 4.651
2011 Impact Factor 4.773
2010 Impact Factor 5.328
2009 Impact Factor 5.328
2008 Impact Factor 5.52
2007 Impact Factor 5.581
2006 Impact Factor 5.808
2005 Impact Factor 5.854
2004 Impact Factor 6.355
2003 Impact Factor 6.482
2002 Impact Factor 6.696
2001 Impact Factor 7.258
2000 Impact Factor 7.368
1999 Impact Factor 7.666
1998 Impact Factor 7.199
1997 Impact Factor 6.963
1996 Impact Factor 7.452
1995 Impact Factor 7.385
1994 Impact Factor 7.716
1993 Impact Factor 6.793
1992 Impact Factor 6.733

Impact factor over time

Impact factor

Additional details

5-year impact 5.02
Cited half-life 10.00
Immediacy index 0.94
Eigenfactor 0.68
Article influence 1.95
Website Journal of Biological Chemistry website
Other titles The Journal of biological chemistry, JBC
ISSN 0021-9258
OCLC 1782222
Material type Periodical, Internet resource
Document type Journal / Magazine / Newspaper, Internet Resource

Publisher details

American Society for Biochemistry and Molecular Biology

  • Pre-print
    • Author cannot archive a pre-print version
  • Post-print
    • Author cannot archive a post-print version
  • Restrictions
    • 12 months embargo
  • Conditions
    • Authors accepted peer-reviewed manuscript may be posted on an institutional repository
    • Publisher copyright and source must be acknowledged with set phrase: "This research was originally published in Journal Name. Author(s). Title. Journal Name. Year. Vol:pp-pp. © the American Society for Biochemistry and Molecular Biology"
    • On a non-profit server
    • Publisher's version/PDF cannot be used
  • Classification
    ​ white

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: A rise in tissue-embedded macrophages displaying "M1-like" pro-inflammatory polarization is a hallmark of metabolic inflammation during high fat diet or obesity. Here we show that bone marrow-derived macrophages (BMDM) from high fat-fed mice retain memory of their dietary environment in vivo (displaying elevated pro-inflammatory genes Cxcl1, Il6, Tnf, Nos2), in spite of 7-days differentiation and proliferation ex vivo. Notably, 6 h incubation with palmitoleate (PO) reversed the pro-inflammatory gene expression and cytokine secretion seen in BMDM from high fat-fed mice. BMDM from low fat-fed mice exposed to palmitate (PA) for 18 h ex vivo also showed elevated expression of pro-inflammatory genes (Cxcl1, Il6, Tnf, Nos2, Il12b) associated with M1 polarization. Conversely, PO treatment increased anti-inflammatory genes (Mrc1, Tgfb1, Il10, Mgl2), and oxidative metabolism, characteristic of M2 macrophages. Thus, saturated and unsaturated fatty acids bring about opposite macrophage polarization states. Co-incubation of BMDM with both fatty acids counteracted the PA-induced Nos2 expression in a PO dose-dependent fashion. PO also prevented the PA-induced IκBα degradation, RelA nuclear translocation, NO production and cytokine secretion. Mechanistically, PO exerted its anti-inflammatory function through AMPK, as AMPK inhibition by Compound C offset the PO-dependent prevention of PA-induced IκBα degradation, Nos2 expression and NO production. These results demonstrate a nutritional memory of BMDM ex vivo, highlight the plasticity of BMDM polarization in response to saturated and unsaturated fatty acids, and identify the potential to reverse diet- and saturated fat-induced M1-like polarization by administering palmitoleate. These findings could have applicability to reverse obesity-linked inflammation in metabolically-relevant tissues. Copyright © 2015, The American Society for Biochemistry and Molecular Biology.
    Journal of Biological Chemistry 05/2015; DOI:10.1074/jbc.M115.646992
  • [Show abstract] [Hide abstract]
    ABSTRACT: The identity of calcium channels in the thyroid is unclear. In human follicular thyroid ML-1 cancer cells, sphingolipid sphingosine 1-phosphate (S1P), through S1P receptor 1 and -3 (S1P1/S1P3), and VEGF receptor 2 (VEGFR2) stimulate migration. We show that human thyroid cells express several forms of TRPC channels, including TRPC1. In TRPC1 knock-down (TRPC1-KD) ML-1 cells, the basal and S1P-evoked invasion and migration was attenuated. Furthermore, the expression of S1P3, and VEGFR2 was significantly downregulated. Transfecting wild-type ML-1 cells with a non-conducting TRPC1 mutant decreased S1P3 and VEGFR2 expression. In TRPC1-KD cells, receptor-operated calcium entry was decreased. To investigate whether the decreased receptor expression was due to attenuated calcium entry, cells were incubated with the calcium chelator BAPTA-AM. In these cells, and in cells where calmodulin and calmodulin-dependent kinase were blocked pharmacologically, S1P3 and VEGFR2 expression was decreased. In TRPC1-KD cells, both HIF-1α expression, and the secretion and activity of MMP2 and -9, was attenuated, and proliferation was decreased in TRPC1-KD cells. This was due to a prolonged G1 phase of the cell cycle, a significant increase in the expression of the cyclin-dependent kinase inhibitors p-21 and p-27, and a decrease in the expression of cyclin D2, cyclin D3, and CDK6. Transfecting TRPC1 to TRPC1-KD cells rescued receptor expression, migration, and proliferation. Thus, the expression of S1P3 and VEGFR2 is mediated by a calcium-dependent mechanism. TRPC1 has a crucial role in this process. This regulation is important for the invasion, migration and proliferation of thyroid cancer cells. Copyright © 2015, The American Society for Biochemistry and Molecular Biology.
    Journal of Biological Chemistry 05/2015; DOI:10.1074/jbc.M115.643668
  • [Show abstract] [Hide abstract]
    ABSTRACT: RNF4 is a SUMO-targeted ubiquitin E3 ligase with a pivotal function in the DNA damage response (DDR). SUMO Interaction Motifs (SIMs) in the N-terminal part of RNF4 tightly bind to SUMO polymers, and RNF4 can ubiquitinate these polymers in vitro. Using a proteomic approach, we identified the deubiquitinating enzyme USP11, a known DDR-component, as a functional interactor of RNF4. USP11 can deubiquitinate hybrid SUMO-ubiquitin chains to counteract RNF4. SUMO-enriched nuclear bodies are stabilized by USP11, which functions downstream of RNF4 as a counterbalancing factor. In response to DNA damage induced by methyl methanesulfonate, USP11 could counteract RNF4 to inhibit the dissolution of nuclear bodies. Thus, we provide novel insight into crosstalk between ubiquitin and SUMO, and uncover USP11 and RNF4 as a balanced SUMO-targeted ubiquitin ligase/protease pair with a role in the DDR. Copyright © 2015, The American Society for Biochemistry and Molecular Biology.
    Journal of Biological Chemistry 05/2015; DOI:10.1074/jbc.M114.618132
  • [Show abstract] [Hide abstract]
    ABSTRACT: The liver stages (LS) of malaria parasite are clinically silent and constitute ideal targets for causal prophylactic drugs and vaccines. Cellular and molecular events responsible for LS development are poorly characterized. Here, we show that SLTRiP forms large multimers. Mice immunized with a purified recombinant SLTRiP protein gave high antibody titers in both inbred and outbred mice. Immunized mice showed highly significant levels of protection upon challenge with sporozoites and exhibited 10,000-fold fewer parasite 18SrRNA copy numbers in their livers. The protection offered by immunization with SLTRiP came mainly from T cells, and antibodies had little role to play despite their high titers. Immunoflourescence assays showed that SLTRiP is expressed in the sporozoite and early to late liver stages of malaria parasites. SLTRiP protein is exported to the cytosol of infected host cells during the early hrs of parasite infection. Parasites deficient in SLTRiP were moderately defective in liver stage parasite development. A transcriptome profile of SLTRiP-deficient parasite infected hepatocytes highlighted that SLTRiP interferes with multiple pathways in the host cell. We have demonstrated a role for SLTRiP in sporozoites and the liver stage of malaria parasites
    Journal of Biological Chemistry 05/2015; DOI:10.1074/jbc.M114.588129
  • [Show abstract] [Hide abstract]
    ABSTRACT: TNFRSF10A and TNFRSF10B are cell surface receptors that bind to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) and mediate the extrinsic pathway of apoptosis. However, the mechanisms of transcriptional regulation of TNFRSF10A and TNFRSF10B remain largely uncharacterized. In this study, two putative DDIT3 binding sites (-1636/-1625; -374/-364) and a putative AP-1 binding site (-304/-298) were identified in the TNFRSF10A promoter region. We found that DDIT3 interacts with phospho-JUN, and the DDIT3/phospho-JUN complex binds to the AP-1 binding site (-304/-298) within the TNFRSF10A promoter region. In addition, we confirmed that KAT2A physically interacts with the N-terminal region (aa 1-26) of DDIT3. Importantly, knockdown of KAT2A downregulated TNFRSF10A and TNFRSF10B and dramatically decreased promoter activity of cells transfected with luciferase reporter plasmid containing AP-1 binding site (-304/-298) of the TNFRSF10A promoter, and cells transfected with luciferase reporter plasmid containing DDIT3 binding site (-276/-264) of the TNFRSF10B promoter. Chromatin immunoprecipitation (ChIP) results suggest that KAT2A may participate in a KAT2A/DDIT3/phospho-JUN complex, or a KAT2A/DDIT3 complex and acetylate H3K9/K14, respectively. Moreover, we verified that TNFRSF10A mediates apoptosis triggered by ER stress in human lung cancer cells. Collectively, we demonstrate that DDIT3 and KAT2A cooperatively upregulate TNFRSF10A and TNFRSF10B. Our findings highlight two distinct mechanisms underlying ER stress-induced TNFRSF10A and TNFRSF10B expressions and apoptosis. These findings will be helpful for elucidating mechanisms related to anticancer drugs in mediating apoptosis. Copyright © 2015, The American Society for Biochemistry and Molecular Biology.
    Journal of Biological Chemistry 04/2015; 290(17):11108-11118. DOI:10.1074/jbc.M115.645333
  • Journal of Biological Chemistry 04/2015; 290(16). DOI:10.1074/jbc.L115.648089
  • Journal of Biological Chemistry 04/2015; 290(16):10571-10571. DOI:10.1074/jbc.L115.648600
  • [Show abstract] [Hide abstract]
    ABSTRACT: Gene-wide-association and candidate gene studies indicate that the greatest effect on multiple sclerosis (MS) risk is driven by the HLA-DRB1*15:01 allele within the HLA-DR15-haplotype (HLA-DRB1*15:01-DQA1*01:02-DQB1*0602-DRB5*01:01). Nevertheless, linkage-disequilibrium makes it difficult to define, without functional studies, whether the functionally relevant effect derives from DRB1*15:01 only, its neighboring DQA1*01:02-DQB1*06:02 or DRB5*01:01 genes of HLA-DR15-haplotype, or from their combinations or epistatic interactions. Here, we analyzed the impact of the different HLA-DR15-haplotype alleles on disease-susceptibility in a new humanized model of MS induced in HLA-transgenic (Tg) mice by human oligodendrocyte-specific protein (OSP)/claudin-11 (hOSP), one of the bone fide potential primary target antigens in MS. We show that the hOSP-associated MS-like disease is dominated by DRB1*15:01 allele not only as the DRA1*01:01;DRB1*15:01 isotypic-heterodimer, but also, unexpectedly, as a functional DQA1*01:02;DRB1*15:01 mixed-isotype heterodimer. The contribution of HLA-DQA1/DRB1 mixed-isotype heterodimer to OSP-pathogenesis was revealed in (DRB1*1501xDQB1*0602)F1-double-Tg mice immunized with hOSP142-161 peptide, where the encephalitogenic potential of prevalent DRB1*1501/hOSP142-161-reactive Th1/Th17-cells is hindered due to a single amino acid difference in the OSP142-161 region between human and mouse; this impedes binding of DRB1*1501 to mouse-OSP142-161 epitope in mouse CNS while exposing functional binding of mouse-OSP142-161 to DQA1*01:02;DRB1*15:01-mixed-isotype heterodimer. This study, which shows for the first time a functional HLA-DQA1/DRB1 mixed-isotype-heterodimer and its potential association with disease-susceptibility, provides a rationale for potential effect on MS-risk from DQA1*01:02 through functional DQA1*01:02;DRB1*15:01-antigen presentation. Furthermore, it highlights a potential contribution to MS-risk also from interisotypic combination between products of neighboring HLA-DR15-haplotype alleles, in this case the DQA1/DRB1 combination. Copyright © 2015, The American Society for Biochemistry and Molecular Biology.
    Journal of Biological Chemistry 04/2015; DOI:10.1074/jbc.M115.641209