Science Journal Impact Factor & Information

Publisher: American Association for the Advancement of Science, American Association for the Advancement of Science

Current impact factor: 33.61

Impact Factor Rankings

2015 Impact Factor Available summer 2016
2014 Impact Factor 33.611
2013 Impact Factor 31.477
2012 Impact Factor 31.027
2011 Impact Factor 31.201
2010 Impact Factor 31.364
2009 Impact Factor 29.747
2008 Impact Factor 28.103
2007 Impact Factor 26.372
2006 Impact Factor 30.028
2005 Impact Factor 30.927
2004 Impact Factor 31.853
2003 Impact Factor 29.162
2002 Impact Factor 26.682
2001 Impact Factor 23.329
2000 Impact Factor 23.872
1999 Impact Factor 24.595
1998 Impact Factor 24.386
1997 Impact Factor 24.676
1996 Impact Factor 23.605
1995 Impact Factor 21.911
1994 Impact Factor 22.067
1993 Impact Factor 21.074
1992 Impact Factor 20.967

Impact factor over time

Impact factor

Additional details

5-year impact 35.26
Cited half-life >10.0
Immediacy index 7.22
Eigenfactor 1.22
Article influence 17.87
Website Science website
Other titles Science (New York, N.Y.: Online), Science, Science magazine on-line, Science online, Science on-line, Science magazine online
ISSN 1095-9203
OCLC 34298537
Material type Document, Periodical, Internet resource
Document type Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details

American Association for the Advancement of Science

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • Pre-print may be considered prior publication
    • Pre-print on not-for-profit preprint servers where allowed, please contact editors for clarification
    • Cannot archive until publication
    • Authors retain copyright
    • On author's personal website or institutional repository
    • Publisher's version/PDF cannot be used
    • Must link to publisher version
    • Set statement must accompany post-print (see policy)
    • Published source must be acknowledged with DOI
    • Authors covered by funding agency rules, may post author's post-print in PubMed Central or funder's designated repository after a 6 month embargo
    • Authors covered by funding agency rules, must state on submission, for article to be released in PubMed Central or funder's designated repository after 6 months after publication.
  • Classification

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: Leucine is a proteogenic amino acid that also regulates many aspects of mammalian physiology, in large part by activating the mTOR complex 1 (mTORC1) protein kinase, a master growth controller. Amino acids signal to mTORC1 through the Rag guanosine triphosphatases (GTPases). Several factors regulate the Rags, including GATOR1, a GTPase-activating protein (GAP); GATOR2, a positive regulator of unknown function; and Sestrin2, a GATOR2-interacting protein that inhibits mTORC1 signaling. We find that leucine, but not arginine, disrupts the Sestrin2-GATOR2 interaction by binding to Sestrin2 with a dissociation constant of 20 μM, which is the leucine concentration that half-maximally activates mTORC1. The leucine-binding capacity of Sestrin2 is required for leucine to activate mTORC1 in cells. These results indicate that Sestrin2 is a leucine sensor for the mTORC1 pathway.
    Science 10/2015; DOI:10.1126/science.aab2674
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    ABSTRACT: Responding to stimuli, nucleotide-binding domain and leucine-rich repeat-containing proteins (NLRs) oligomerize into multi-protein complexes termed inflammasomes mediating innate immunity. Recognition of bacterial pathogens by NLR apoptosis inhibitory proteins (NAIPs) induces NLR family CARD domain-containing protein 4 (NLRC4) activation and formation of NAIP-NLRC4 inflammasomes. The wheel-like structure of a PrgJ-NAIP2-NLRC4 complex determined by cryo-EM at 6.6 angstrom reveals that NLRC4 activation involves substantial structural reorganization that creates one oligomerization surface (catalytic surface). Once activated, NLRC4 utilizes this surface to catalyze the activation of an inactive NLRC4, self-propagating its active conformation to form the wheel-like architecture. NAIP proteins possess a catalytic surface matching the other oligomerization surface (receptor surface) of NLRC4 but not those of their own, ensuring that one NAIP is sufficient to initiate NLRC4 oligomerization.
    Science 10/2015; 350(6259). DOI:10.1126/science.aac5489
  • [Show abstract] [Hide abstract]
    ABSTRACT: Mirarab et al. (Research Article, 12 December 2014, p. 1250463) introduced statistical binning to improve the signal in phylogenetic methods using the multispecies coalescent model. We show that all forms of binning-naïve, statistical, and weighted statistical- display poor performance and are statistically inconsistent in large regions of parameter space, unlike unbinned sequence data used with species tree methods.
    Science 10/2015; 350(6257):171. DOI:10.1126/science.aaa7343
  • [Show abstract] [Hide abstract]
    ABSTRACT: There is growing promise in using engineered cells as therapeutic agents. For example, synthetic Chimeric Antigen Receptors (CARs) can redirect T cells to recognize and eliminate tumor cells expressing specific antigens. Despite promising clinical results, excessive activity and poor control over such engineered T cells can cause severe toxicities. We present the design of "ON-switch" CARs that enable small molecule-control over T cell therapeutic functions, while still retaining antigen specificity. In these split receptors, antigen binding and intracellular signaling components only assemble in the presence of a heterodimerizing small molecule. This titratable pharmacologic regulation could allow physicians to precisely control the timing, location, and dosage of T cell activity, thereby mitigating toxicity. This work illustrates the potential of combining cellular engineering with orthogonal chemical tools to yield safer therapeutic cells that tightly integrate both cell autonomous recognition and user control.
    Science 09/2015; 350(6258). DOI:10.1126/science.aab4077

  • Science 09/2015; 349(6255):1459. DOI:10.1126/science.349.6255.1459-a
  • [Show abstract] [Hide abstract]
    ABSTRACT: Cyclic GMP-AMP synthase (cGAS) detects intracellular DNA and signals through the adapter protein STING to initiate the antiviral response to DNA viruses. Whether DNA viruses can prevent activation of the cGAS-STING pathway remains largely unknown. Here, we identify the viral oncogenes of the DNA tumor viruses, including E7 from human papillomavirus (HPV) and E1A from adenovirus, as potent and specific inhibitors of the cGAS-STING pathway. We show that the LXCXE motif of these oncoproteins, which is essential for blockade of the Retinoblastoma tumor suppressor, is also important for antagonizing DNA sensing. E1A and E7 bind to STING, and silencing of these oncogenes in human tumor cells restores the cGAS-STING pathway. Our findings reveal a host-virus conflict that may have shaped the evolution of viral oncogenes.
    Science 09/2015; 350(6260). DOI:10.1126/science.aab3291