Journal of Proteome Research Impact Factor & Information

Publisher: American Chemical Society

Journal description

The Journal of Proteome Research (JPR) provides content encompassing all aspects of systems-oriented, global protein analysis and function, emphasizing the synergy between physical and life sciences resulting in a multi-disciplinary approach to the understanding of biological processes. JPR integrates the fields of chemistry, mathematics, applied physics, biology, and medicine in order to better understand the function of proteins in biological systems. In addition to publishing original peer-reviewed research papers, JPR also publishes research highlights, current events, book and software reviews, and a calendar of upcoming short courses and symposia of interest to proteomic scientists.

Current impact factor: 5.00

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 Impact Factor 5.001
2012 Impact Factor 5.056
2011 Impact Factor 5.113
2010 Impact Factor 5.46
2009 Impact Factor 5.132
2008 Impact Factor 5.684
2007 Impact Factor 5.675
2006 Impact Factor 5.151
2005 Impact Factor 6.901
2004 Impact Factor 6.917
2003 Impact Factor 5.611
2002 Impact Factor

Impact factor over time

Impact factor
Year

Additional details

5-year impact 5.22
Cited half-life 3.90
Immediacy index 0.88
Eigenfactor 0.07
Article influence 1.46
Website Journal of Proteome Research website
Other titles Journal of proteome research (Online), Journal of proteome research, Proteome research, JPR
ISSN 1535-3893
OCLC 47082841
Material type Document, Periodical, Internet resource
Document type Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details

American Chemical Society

  • Pre-print
    • Author cannot archive a pre-print version
  • Restrictions
    • Must obtain written permission from Editor
    • Must not violate ACS ethical Guidelines
  • Post-print
    • Author cannot archive a post-print version
  • Restrictions
    • If mandated by funding agency or employer/ institution
    • If mandated to deposit before 12 months, must obtain waiver from Institution/Funding agency or use AuthorChoice
    • 12 months embargo
  • Conditions
    • On author's personal website, pre-print servers, institutional website, institutional repositories or subject repositories
    • Non-Commercial
    • Must be accompanied by set statement (see policy)
    • Must link to publisher version
    • Publisher's version/PDF cannot be used
    • If mandated sooner than 12 months, must obtain waiver from Editors or use AuthorChoice
    • Reviewed on 07/08/2014
  • Classification
    ​ white

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: To improve the quality of life of animals, understanding of stress-induced changes is necessary. Previously, we established a subchronic and mild social defeat stress (sCSDS) model in mice, which showed significantly higher body weight gain, food intake, and water intake compared to control mice. In this study, we elucidated metabolic profiles of plasma, liver, and urine in sCSDS mice by using metabolome and biochemical analyses. There was no significant difference between defeated and control mice in the plasma metabolites. In the liver of sCSDS mice, levels of taurocyamine (GES), phosphorylcholine, D-alanyl-D-alanine (D-ala-D-ala), and 1-methylnicotinamide (MNA) were elevated compared to controls. Taurine plays a role in osmotic regulation, and GES is a potential inhibitor of the taurine transporter. The polydipsia and increased body water content in sCSDS mice may disrupt body fluid balance following GES elevation. Furthermore, sCSDS increased heart and spleen weight significantly. Because MNA and D-ala-D-ala have anti-inflammatory and hepatoprotective effects, they may reduce inflammation in the liver of sCSDS mice. Finally, suppressed excretion of urine sodium was observed in sCSDS mice. Therefore, sCSDS induces various changes in metabolite concentrations, especially related to osmoregulation and inflammation, that may be used as biomarkers for stress-induced changes in animals.
    Journal of Proteome Research 02/2015; 14(2). DOI:10.1021/pr501044k
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    ABSTRACT: Protein carbonylation is a common nonenzymatic oxidative post-translational modification, which is often considered as biomarker of oxidative stress. Recent evidence links protein carbonylation also to obesity and type 2 diabetes mellitus (T2DM), though the protein targets of carbonylation in human plasma have not been identified. In this study, we profiled carbonylated proteins in plasma samples obtained from lean individuals and obese patients with or without T2DM. The plasma samples were digested with trypsin, carbonyl groups were derivatized with O-(biotinylcarbazoylmethyl)hydroxylamine, enriched by avidin affinity chromatography, and analyzed by RPC-MS/MS. Signals of potentially modified peptides were targeted in a second LC-MS/MS analysis to retrieve the peptide sequence and the modified residues. A total of 158 unique carbonylated proteins were identified, of which 52 were detected in plasma samples of all three groups. Interestingly, 36 carbonylated proteins were detected only in obese patients with T2DM, whereas 18 were detected in both nondiabetic groups. The carbonylated proteins originated mostly from liver, plasma, platelet, and endothelium. Functionally, they were mainly involved in cell adhesion, signaling, angiogenesis, and cytoskeletal remodeling. Among the identified carbonylated proteins were several candidates, such as VEGFR-2, MMP-1, argin, MKK4, and compliment C5, already connected before to diabetes, obesity and metabolic diseases.
    Journal of Proteome Research 07/2014; 13(11). DOI:10.1021/pr500324y
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    ABSTRACT: Ewing sarcoma is a cancer of bone and soft tissue in children that is characterized by a chromosomal translocation involving EWS and an Ets family transcription factor, most commonly Fli-1. EWS-Fli-1 fusion accounts for 85% of cases. The growth and survival of Ewing sarcoma cells are critically dependent on EWS-Fli-1. A large body of evidence has established that EWS-Fli-1 functions as a DNA-binding transcription factor that regulates the expression of a number of genes important for cell proliferation and transformation. However, little is known about the biochemical properties of the EWS-Fli-1 protein. We undertook a series of proteomic analyses to dissect the EWS-Fli-1 interactome. Employing a proximity-dependent biotinylation technique, BioID, we identified cation-independent mannose 6-phosphate receptor (CIMPR) as a protein located in the vicinity of EWS-Fli-1 within a cell. CIMPR is a cargo that mediates the delivery of lysosomal hydrolases from trans-Golgi network to endosome, which are subsequently transferred to the lysosomes. Further molecular cell biological analyses uncovered a role for lysosomes in the turnover of the EWS-Fli-1 protein. We demonstrate that an mTORC1 active-site inhibitor torin 1, which stimulates the TFEB-lysosome pathway, can induce the degradation of EWS-Fli-1, suggesting a potential therapeutic approach to target EWS-Fli-1 for degradation.
    Journal of Proteome Research 07/2014; 13(8). DOI:10.1021/pr500387m
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    ABSTRACT: Stationary-phase, carbon-starved shake-flask cultures of Saccharomyces cerevisiae are popular models for studying eukaryotic chronological ageing. However, their nutrient-starved physiological status differs substantially from that of post-mitotic metazoan cells. Retentostat cultures offer an attractive alternative model system in which yeast cells, maintained under continuous calorie restriction, hardly divide but retain high metabolic activity and viability for prolonged periods of time. Using TMT labeling and UHPLC-MS/MS, the present study explores the proteome of yeast cultures during transition from exponential growth to near-zero growth in severely calorie-restricted retentostats. This transition elicited protein level changes in 20% of the yeast proteome. Increased abundance of heat-shock-related proteins correlated with increased transcript levels of the corresponding genes and was consistent with a strongly increased heat-shock tolerance of retentostat-grown cells. A sizeable fraction (43%) of the proteins with increased abundance under calorie restriction was involved in oxidative phosphorylation and in various mitochondrial functions that, under the anaerobic, non-growing conditions used, have a very limited role. While it may seem surprising that yeast cells confronted with severe calorie restriction invest in the synthesis of proteins that, under those conditions, do not contribute to fitness, these responses may confer metabolic flexibility and thereby a selective advantage in fluctuating natural habitats.
    Journal of Proteome Research 07/2014; 13(8). DOI:10.1021/pr5003388
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    ABSTRACT: Epidermal homeostasis is a balancing act governed by a multitude of underlying regulatory events, and several growth factors and signaling pathways have been implicated in regulation of the balance between proliferation and differentiation in keratinocytes. We show here that the signal transducer/transcription factor FIZ1 (Flt3 interacting zinc finger protein-1) is a previously unknown player in this regulatory axis, promoting an increase in proliferation of HaCaT human immortalized keratinocytes that is driven by more rapid G1/S progression and mediated by activation of the MAP/ERK kinase pathway. Utilizing quantitative SILAC-based secretome analysis, we identified the insulin growth factor binding protein IGFBP3 as the key mediating factor, demonstrating that elevated FIZ1 levels promote increased IGFBP3 expression and secretion and a concurrent increased sensitivity to IGF1 signaling, while antibody-based neutralization of IGFBP3 abrogates the FIZ1-induced growth advantage. To identify underlying protein-protein interactions likely to govern these events, we mapped the interactome of FIZ1 and found eight novel binding partners that form complexes with the protein in the cytoplasm and nucleus. These include signal transduction and transcription factors and the cell cycle regulatory NDR (Nuclear Dbf2-related) kinases. Our results provide further insight into the complex balance of epidermal homeostasis and identify FIZ1 as a novel therapeutic target.
    Journal of Proteome Research 06/2014; 13(7). DOI:10.1021/pr500392m
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    ABSTRACT: Myostatin, a highly conserved secretory protein negatively regulates muscle development affecting both proliferation and differentiation of muscle cells. Proteolytic processing of the myostatin precursor protein generates a myostatin pro-peptide and mature protein. Dimerization of the mature myostatin protein creates the active myostatin form. Myostatin dimer activity can be inhibited by non-covalent binding of two monomeric myostatin pro-peptides. This ability for myostatin to self-regulate and altered expression of myostatin in states of abnormal health (e.g. muscle wasting) support the need for specific detection of myostatin forms. Current protein detection methods (e.g. Western blot) rely greatly on antibodies and are semi-quantitative at best. Tandem mass spectometry (as in this study) provides a highly specific method of detection, enabling the characterisation of myostatin protein forms through the analysis of discrete peptides fragments. Utilizing the scheduled high-resolution multiple reaction monitoring paradigm (sMRMHR; AB SCIEX 5600 TripleTOF) we identified the lower limit of quantitation (LLOQ) of both mature (DFGLDCDEHSTESR) and pro-peptide regions (ELIDQYDVQR) as 0.19nmol/L. Furthermore, scheduled multiple reaction monitoring (sMRM; AB SCIEX QTRAP® 5500) identified a LLOQ for apeptide of the pro-peptide region (LETAPNISK) as 0.16nmol/L and a peptide of the mature region (EQIIYGK) as 0.25nmol/L.
    Journal of Proteome Research 06/2014; 13(8). DOI:10.1021/pr5004642