Human GAPDH Is a Target of Aspirin’s Primary Metabolite Salicylic Acid and Its Derivatives
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{"title"=>"Human GAPDH is a target of aspirin's primary metabolite salicylic acid and its derivatives", "type"=>"journal", "authors"=>[{"first_name"=>"Hyong Woo", "last_name"=>"Choi", "scopus_author_id"=>"14627068300"}, {"first_name"=>"Miaoying", "last_name"=>"Tian", "scopus_author_id"=>"7202800238"}, {"first_name"=>"Murli", "last_name"=>"Manohar", "scopus_author_id"=>"36468823700"}, {"first_name"=>"Maged M.", "last_name"=>"Harraz", "scopus_author_id"=>"12792471900"}, {"first_name"=>"Sang Wook", "last_name"=>"Park", "scopus_author_id"=>"57157561800"}, {"first_name"=>"Frank C.", "last_name"=>"Schroeder", "scopus_author_id"=>"8342418700"}, {"first_name"=>"Solomon H.", "last_name"=>"Snyder", "scopus_author_id"=>"35406091300"}, {"first_name"=>"Daniel F.", "last_name"=>"Klessig", "scopus_author_id"=>"7006250375"}], "year"=>2015, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "doi"=>"10.1371/journal.pone.0143447", "sgr"=>"84960153197", "scopus"=>"2-s2.0-84960153197", "isbn"=>"10.1371/journal.pone.0143447", "pmid"=>"26606248", "pui"=>"608758572"}, "id"=>"070174bb-7364-36ba-bf49-10e635153950", "abstract"=>"The plant hormone salicylic acid (SA) controls several physiological processes and is a key regulator of multiple levels of plant immunity. To decipher the mechanisms through which SA's multiple physiological effects are mediated, particularly in immunity, two high-throughput screens were developed to identify SA-binding proteins (SABPs). Glyceraldehyde 3-Phosphate Dehydrogenase (GAPDH) from plants (Arabidopsis thaliana) was identified in these screens. Similar screens and subsequent analyses using SA analogs, in conjunction with either a photoaffinity labeling technique or surface plasmon resonance-based technology, established that human GAPDH (HsGAPDH) also binds SA. In addition to its central role in glycolysis, HsGAPDH participates in several pathological processes, including viral replication and neuronal cell death. The anti-Parkinson's drug deprenyl has been shown to suppress nuclear translocation of HsGAPDH, an early step in cell death and the resulting cell death induced by the DNA alkylating agent N-methyl-N'-nitro-N-nitrosoguanidine. Here, we demonstrate that SA, which is the primary metabolite of aspirin (acetyl SA) and is likely responsible for many of its pharmacological effects, also suppresses nuclear translocation of HsGAPDH and cell death. Analysis of two synthetic SA derivatives and two classes of compounds from the Chinese medicinal herb Glycyrrhiza foetida (licorice), glycyrrhizin and the SA-derivatives amorfrutins, revealed that they not only appear to bind HsGAPDH more tightly than SA, but also exhibit a greater ability to suppress translocation of HsGAPDH to the nucleus and cell death.", "link"=>"http://www.mendeley.com/research/human-gapdh-target-aspirins-primary-metabolite-salicylic-acid-derivatives", "reader_count"=>38, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>2, "Librarian"=>1, "Student > Doctoral Student"=>2, "Researcher"=>10, "Student > Ph. D. Student"=>8, "Student > Postgraduate"=>2, "Other"=>3, "Student > Master"=>4, "Student > Bachelor"=>2, "Professor"=>2}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>2, "Librarian"=>1, "Student > Doctoral Student"=>2, "Researcher"=>10, "Student > Ph. D. Student"=>8, "Student > Postgraduate"=>2, "Other"=>3, "Student > Master"=>4, "Student > Bachelor"=>2, "Professor"=>2}, "reader_count_by_subject_area"=>{"Unspecified"=>7, "Engineering"=>2, "Biochemistry, Genetics and Molecular Biology"=>2, "Materials Science"=>1, "Agricultural and Biological Sciences"=>13, "Medicine and Dentistry"=>6, "Neuroscience"=>1, "Pharmacology, Toxicology and Pharmaceutical Science"=>2, "Chemistry"=>2, "Psychology"=>2}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>2}, "Materials Science"=>{"Materials Science"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>6}, "Neuroscience"=>{"Neuroscience"=>1}, "Chemistry"=>{"Chemistry"=>2}, "Psychology"=>{"Psychology"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>13}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>2}, "Unspecified"=>{"Unspecified"=>7}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>2}}, "reader_count_by_country"=>{"United States"=>2}, "group_count"=>1}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/2576234"], "description"=>"<p>Crosslinking of 4AzSA to HsGAPDH is suppressed by SA. HsGAPDH was incubated without (-) or with (+) 4AzSA (0.05 mM) in the absence or presence of the indicated concentrations of SA for 1 h, and then exposed to UV light (50 mJ). Proteins crosslinked with 4AzSA were detected by immunoblot analysis using α-SA antibody. Proteins stained with Coomassie brilliant blue (CBB) served as a loading control. The experiment was repeated three times with similar results. Results are expressed as a percentage of inhibition (in lower panel) in the presence of the indicated concentrations of SA as compared to the signal observed in the absence of SA, which was assigned 0% inhibition.</p>", "links"=>[], "tags"=>["gapdh", "herb Glycyrrhiza foetida", "SABP", "dna", "translocation", "sa", "HsGAPDH", "Cell death"], "article_id"=>1612309, "categories"=>["Biological Sciences"], "users"=>["Hyong Woo Choi", "Miaoying Tian", "Murli Manohar", "Maged M. Harraz", "Sang-Wook Park", "Frank C. Schroeder", "Solomon H. Snyder", "Daniel F. Klessig"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0143447.g001", "stats"=>{"downloads"=>4, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SA_binding_activity_of_HsGAPDH_monitored_by_photoaffinity_labeling_with_4AzSA_/1612309", "title"=>"SA-binding activity of HsGAPDH monitored by photoaffinity labeling with 4AzSA.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-11-25 02:47:17"}
  • {"files"=>["https://ndownloader.figshare.com/files/2576240"], "description"=>"<p>(A-D) Sensorgrams of HsGAPDH flowing over 3AESA-immobilized CM5 sensor chip surface. (A) Concentration-dependent response to increasing amounts of HsGAPDH. (B) Concentration-dependent inhibition by SA of HsGAPDH (0.5 μM) binding to a 3AESA-immobilized sensor chip. (C) Suppression by amorfrutin derivatives B1, FN1, and FN2 of HsGAPDH (0.5 μM) binding to a 3AESA-immobilized sensor chip. (D) Suppression by 4-HBA, SA and 5-ASA of HsGAPDH (0.27 μM) binding to a 3AESA-immobilized sensor chip. The signal from the mock-immobilized surface was subtracted.</p>", "links"=>[], "tags"=>["gapdh", "herb Glycyrrhiza foetida", "SABP", "dna", "translocation", "sa", "HsGAPDH", "Cell death"], "article_id"=>1612311, "categories"=>["Biological Sciences"], "users"=>["Hyong Woo Choi", "Miaoying Tian", "Murli Manohar", "Maged M. Harraz", "Sang-Wook Park", "Frank C. Schroeder", "Solomon H. Snyder", "Daniel F. Klessig"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0143447.g002", "stats"=>{"downloads"=>4, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SA_binding_activity_of_HsGAPDH_monitored_by_SPR_analyses_/1612311", "title"=>"SA-binding activity of HsGAPDH monitored by SPR analyses.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-11-25 02:47:17"}
  • {"files"=>["https://ndownloader.figshare.com/files/2576244"], "description"=>"<p>Conserved hydroxyl (-OH) and a carboxyl (-COOH) groups of salicylates are denoted by dashed circles.</p>", "links"=>[], "tags"=>["gapdh", "herb Glycyrrhiza foetida", "SABP", "dna", "translocation", "sa", "HsGAPDH", "Cell death"], "article_id"=>1612312, "categories"=>["Biological Sciences"], "users"=>["Hyong Woo Choi", "Miaoying Tian", "Murli Manohar", "Maged M. Harraz", "Sang-Wook Park", "Frank C. Schroeder", "Solomon H. Snyder", "Daniel F. Klessig"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0143447.g003", "stats"=>{"downloads"=>11, "page_views"=>67, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Chemical_structures_of_salicylic_acid_and_its_synthetic_and_natural_derivatives_/1612312", "title"=>"Chemical structures of salicylic acid and its synthetic and natural derivatives.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-11-25 02:47:17"}
  • {"files"=>["https://ndownloader.figshare.com/files/2576247"], "description"=>"<p>(A-D) Suppression of MNNG-induced nuclear translocation of HsGAPDH by SA (A), by amorfrutin B1 and its derivatives FN1 and FN2 (B), by ac3AESA (C), and by 5-ASA (D). HEK-293 cells were treated with DNA alkylating agent MNNG and nuclear translocation of HsGAPDH in the absence and presence of SA and its derivatives was determined by immunoblotting the nuclear fraction with α-GAPDH antibody. The anti-Parkinson’s drug deprenyl (Dep) served as a positive control suppression of HsGAPDH nuclear translocation.</p>", "links"=>[], "tags"=>["gapdh", "herb Glycyrrhiza foetida", "SABP", "dna", "translocation", "sa", "HsGAPDH", "Cell death"], "article_id"=>1612314, "categories"=>["Biological Sciences"], "users"=>["Hyong Woo Choi", "Miaoying Tian", "Murli Manohar", "Maged M. Harraz", "Sang-Wook Park", "Frank C. Schroeder", "Solomon H. Snyder", "Daniel F. Klessig"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0143447.g004", "stats"=>{"downloads"=>2, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effect_of_SA_and_its_derivatives_on_MNNG_induced_nuclear_translocation_of_HsGAPDH_in_HEK_293_cells_/1612314", "title"=>"Effect of SA and its derivatives on MNNG-induced nuclear translocation of HsGAPDH in HEK 293 cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-11-25 02:47:17"}
  • {"files"=>["https://ndownloader.figshare.com/files/2576253"], "description"=>"<p>(A) Concentration-dependent inhibition of MNNG-induced cell death by SA, B1 and FN2. (B) Concentration-dependent inhibition of MNNG-induced cell death by ac3AESA, 5-ASA and Gly. The anti-Parkinson’s drug deprenyl (Dep) served as a positive control. Cell death was evaluated 6 h after MNNG treatment by trypan blue staining. Data are mean ± SD (n = 6). Asterisks indicate the statistical significance difference compared to the MNNG-treated control (one-way analyses of variance (ANOVA) with post-hoc t test; * P<0.05).</p>", "links"=>[], "tags"=>["gapdh", "herb Glycyrrhiza foetida", "SABP", "dna", "translocation", "sa", "HsGAPDH", "Cell death"], "article_id"=>1612316, "categories"=>["Biological Sciences"], "users"=>["Hyong Woo Choi", "Miaoying Tian", "Murli Manohar", "Maged M. Harraz", "Sang-Wook Park", "Frank C. Schroeder", "Solomon H. Snyder", "Daniel F. Klessig"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0143447.g005", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effect_of_salicylates_and_glycyrrhizin_on_MNNG_induced_cell_death_in_HEK_293_cells_/1612316", "title"=>"Effect of salicylates and glycyrrhizin on MNNG-induced cell death in HEK 293 cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-11-25 02:47:17"}
  • {"files"=>["https://ndownloader.figshare.com/files/2576257"], "description"=>"<p>(A) Chemical structure of glycyrrhizin. (B) SPR sensorgram of HsGAPDH (0.5 μM) in the absence (control) or presence of SA and glycyrrhizin flowing over 3AESA-immobilized CM5 sensor chip surface. The signal from the mock-immobilized surface was subtracted. (C) Suppression of nuclear translocation of HsGAPDH by glycyrrhizin. HEK-293 cells were treated with DNA alkylating agent MNNG and nuclear translocation of HsGAPDH in the absence and presence of glycyrrhizin was determined by immunoblotting the nuclear fraction with α-GAPDH antibody.</p>", "links"=>[], "tags"=>["gapdh", "herb Glycyrrhiza foetida", "SABP", "dna", "translocation", "sa", "HsGAPDH", "Cell death"], "article_id"=>1612317, "categories"=>["Biological Sciences"], "users"=>["Hyong Woo Choi", "Miaoying Tian", "Murli Manohar", "Maged M. Harraz", "Sang-Wook Park", "Frank C. Schroeder", "Solomon H. Snyder", "Daniel F. Klessig"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0143447.g006", "stats"=>{"downloads"=>2, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effects_of_SA_and_glycyrrhizin_on_HsGAPDH_binding_to_3AESA_and_MNNG_induced_nuclear_translocation_/1612317", "title"=>"Effects of SA and glycyrrhizin on HsGAPDH binding to 3AESA and MNNG-induced nuclear translocation.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-11-25 02:47:17"}
  • {"files"=>["https://ndownloader.figshare.com/files/2576259"], "description"=>"<div><p>The plant hormone salicylic acid (SA) controls several physiological processes and is a key regulator of multiple levels of plant immunity. To decipher the mechanisms through which SA’s multiple physiological effects are mediated, particularly in immunity, two high-throughput screens were developed to identify SA-binding proteins (SABPs). Glyceraldehyde 3-Phosphate Dehydrogenase (GAPDH) from plants (<i>Arabidopsis thaliana</i>) was identified in these screens. Similar screens and subsequent analyses using SA analogs, in conjunction with either a photoaffinity labeling technique or surface plasmon resonance-based technology, established that human GAPDH (HsGAPDH) also binds SA. In addition to its central role in glycolysis, HsGAPDH participates in several pathological processes, including viral replication and neuronal cell death. The anti-Parkinson’s drug deprenyl has been shown to suppress nuclear translocation of HsGAPDH, an early step in cell death and the resulting cell death induced by the DNA alkylating agent N-methyl-N’-nitro-N-nitrosoguanidine. Here, we demonstrate that SA, which is the primary metabolite of aspirin (acetyl SA) and is likely responsible for many of its pharmacological effects, also suppresses nuclear translocation of HsGAPDH and cell death. Analysis of two synthetic SA derivatives and two classes of compounds from the Chinese medicinal herb <i>Glycyrrhiza foetida</i> (licorice), glycyrrhizin and the SA-derivatives amorfrutins, revealed that they not only appear to bind HsGAPDH more tightly than SA, but also exhibit a greater ability to suppress translocation of HsGAPDH to the nucleus and cell death.</p></div>", "links"=>[], "tags"=>["gapdh", "herb Glycyrrhiza foetida", "SABP", "dna", "translocation", "sa", "HsGAPDH", "Cell death"], "article_id"=>1612318, "categories"=>["Biological Sciences"], "users"=>["Hyong Woo Choi", "Miaoying Tian", "Murli Manohar", "Maged M. Harraz", "Sang-Wook Park", "Frank C. Schroeder", "Solomon H. Snyder", "Daniel F. Klessig"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0143447", "stats"=>{"downloads"=>3, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Human_GAPDH_Is_a_Target_of_Aspirin_8217_s_Primary_Metabolite_Salicylic_Acid_and_Its_Derivatives_/1612318", "title"=>"Human GAPDH Is a Target of Aspirin’s Primary Metabolite Salicylic Acid and Its Derivatives", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-11-25 02:47:17"}

PMC Usage Stats | Further Information

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  • {"unique-ip"=>"92", "full-text"=>"75", "pdf"=>"60", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"16", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"12"}
  • {"unique-ip"=>"42", "full-text"=>"44", "pdf"=>"23", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"13", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"1"}
  • {"unique-ip"=>"24", "full-text"=>"25", "pdf"=>"14", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"5", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"3"}
  • {"unique-ip"=>"20", "full-text"=>"16", "pdf"=>"9", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"4"}
  • {"unique-ip"=>"16", "full-text"=>"19", "pdf"=>"5", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"5"}
  • {"unique-ip"=>"14", "full-text"=>"13", "pdf"=>"5", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"3", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"6"}
  • {"unique-ip"=>"12", "full-text"=>"13", "pdf"=>"5", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"7"}
  • {"unique-ip"=>"15", "full-text"=>"16", "pdf"=>"5", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"5", "supp-data"=>"0", "cited-by"=>"1", "year"=>"2016", "month"=>"8"}
  • {"unique-ip"=>"13", "full-text"=>"13", "pdf"=>"7", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"5", "supp-data"=>"0", "cited-by"=>"1", "year"=>"2016", "month"=>"9"}
  • {"unique-ip"=>"15", "full-text"=>"17", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"10", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"10"}
  • {"unique-ip"=>"24", "full-text"=>"29", "pdf"=>"5", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2016", "month"=>"11"}
  • {"unique-ip"=>"14", "full-text"=>"14", "pdf"=>"5", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"12"}
  • {"unique-ip"=>"15", "full-text"=>"13", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"1", "year"=>"2017", "month"=>"1"}
  • {"unique-ip"=>"17", "full-text"=>"32", "pdf"=>"7", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"8", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"2"}
  • {"unique-ip"=>"16", "full-text"=>"23", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"10", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"3"}
  • {"unique-ip"=>"17", "full-text"=>"21", "pdf"=>"7", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"3", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"4"}
  • {"unique-ip"=>"17", "full-text"=>"20", "pdf"=>"5", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2017", "month"=>"5"}
  • {"unique-ip"=>"11", "full-text"=>"13", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"6"}
  • {"unique-ip"=>"7", "full-text"=>"7", "pdf"=>"4", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"8", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"7"}
  • {"unique-ip"=>"6", "full-text"=>"6", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"8"}
  • {"unique-ip"=>"18", "full-text"=>"28", "pdf"=>"7", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"9"}
  • {"unique-ip"=>"7", "full-text"=>"18", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"10"}
  • {"unique-ip"=>"11", "full-text"=>"13", "pdf"=>"4", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"11"}
  • {"unique-ip"=>"20", "full-text"=>"21", "pdf"=>"4", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"5", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"12"}
  • {"unique-ip"=>"5", "full-text"=>"5", "pdf"=>"4", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"1"}
  • {"unique-ip"=>"17", "full-text"=>"14", "pdf"=>"4", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"3"}
  • {"unique-ip"=>"11", "full-text"=>"12", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"3", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"1"}
  • {"unique-ip"=>"13", "full-text"=>"14", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"12"}
  • {"unique-ip"=>"7", "full-text"=>"10", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"9"}
  • {"unique-ip"=>"8", "full-text"=>"7", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"4"}
  • {"unique-ip"=>"11", "full-text"=>"16", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"5"}
  • {"unique-ip"=>"11", "full-text"=>"12", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2018", "month"=>"6"}
  • {"unique-ip"=>"8", "full-text"=>"7", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"1", "cited-by"=>"1", "year"=>"2018", "month"=>"7"}
  • {"unique-ip"=>"7", "full-text"=>"6", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"8"}
  • {"unique-ip"=>"7", "full-text"=>"6", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"10"}
  • {"unique-ip"=>"9", "full-text"=>"8", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"11"}
  • {"unique-ip"=>"10", "full-text"=>"8", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"5", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"2"}
  • {"unique-ip"=>"9", "full-text"=>"7", "pdf"=>"5", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
  • {"unique-ip"=>"12", "full-text"=>"12", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"4"}
  • {"unique-ip"=>"10", "full-text"=>"10", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"3", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"5"}
  • {"unique-ip"=>"10", "full-text"=>"9", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"8"}
  • {"unique-ip"=>"14", "full-text"=>"13", "pdf"=>"7", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"9"}
  • {"unique-ip"=>"13", "full-text"=>"15", "pdf"=>"11", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"10"}
  • {"unique-ip"=>"9", "full-text"=>"8", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2019", "month"=>"12"}

Relative Metric

{"start_date"=>"2015-01-01T00:00:00Z", "end_date"=>"2015-12-31T00:00:00Z", "subject_areas"=>[]}
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