Design of a Selective Substrate and Activity Based Probe for Human Neutrophil Serine Protease 4
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{"title"=>"Design of a selective substrate and activity based probe for human neutrophil serine protease 4", "type"=>"journal", "authors"=>[{"first_name"=>"Paulina", "last_name"=>"Kasperkiewicz", "scopus_author_id"=>"36935951600"}, {"first_name"=>"Marcin", "last_name"=>"Poreba", "scopus_author_id"=>"36988756400"}, {"first_name"=>"Scott J.", "last_name"=>"Snipas", "scopus_author_id"=>"6603348851"}, {"first_name"=>"S. Jack", "last_name"=>"Lin", "scopus_author_id"=>"52464107000"}, {"first_name"=>"Daniel", "last_name"=>"Kirchhofer", "scopus_author_id"=>"7004336610"}, {"first_name"=>"Guy S.", "last_name"=>"Salvesen", "scopus_author_id"=>"35493461100"}, {"first_name"=>"Marcin", "last_name"=>"Drag", "scopus_author_id"=>"55975502600"}], "year"=>2015, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"605803283", "pmid"=>"26172376", "doi"=>"10.1371/journal.pone.0132818", "issn"=>"19326203", "scopus"=>"2-s2.0-84940530222", "sgr"=>"84940530222", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)"}, "id"=>"d33bb3e4-7d87-3b6e-af60-4478c67e3762", "abstract"=>"Human neutrophil serine protease 4 (NSP4), also known as PRSS57, is a recently discovered fourth member of the neutrophil serine proteases family. Although its biological function is not precisely defined, it is suggested to regulate neutrophil response and innate immune reactions. To create optimal substrates and visualization probes for NSP4 that distinguish it from other NSPs we have employed a Hybrid Combinatorial Substrate Library approach that utilizes natural and unnatural amino acids to explore protease subsite preferences. Library results were validated by synthesizing individual substrates, leading to the identification of an optimal substrate peptide. This substrate was converted to a covalent diphenyl phosphonate probe with an embedded biotin tag. This probe demonstrated high inhibitory activity and stringent specificity and may be suitable for visualizing NSP4 in the background of other NSPs.", "link"=>"http://www.mendeley.com/research/design-selective-substrate-activity-based-probe-human-neutrophil-serine-protease-4", "reader_count"=>11, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Researcher"=>2, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>2, "Student > Master"=>1, "Student > Bachelor"=>2}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Researcher"=>2, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>2, "Student > Master"=>1, "Student > Bachelor"=>2}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>4, "Agricultural and Biological Sciences"=>2, "Pharmacology, Toxicology and Pharmaceutical Science"=>1, "Chemistry"=>3}, "reader_count_by_subdiscipline"=>{"Chemistry"=>{"Chemistry"=>3}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>2}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>4}, "Unspecified"=>{"Unspecified"=>1}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>1}}, "group_count"=>1}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/2175599"], "description"=>"<div><p>Human neutrophil serine protease 4 (NSP4), also known as PRSS57, is a recently discovered fourth member of the neutrophil serine proteases family. Although its biological function is not precisely defined, it is suggested to regulate neutrophil response and innate immune reactions. To create optimal substrates and visualization probes for NSP4 that distinguish it from other NSPs we have employed a Hybrid Combinatorial Substrate Library approach that utilizes natural and unnatural amino acids to explore protease subsite preferences. Library results were validated by synthesizing individual substrates, leading to the identification of an optimal substrate peptide. This substrate was converted to a covalent diphenyl phosphonate probe with an embedded biotin tag. This probe demonstrated high inhibitory activity and stringent specificity and may be suitable for visualizing NSP4 in the background of other NSPs.</p></div>", "links"=>[], "tags"=>["visualizing NSP 4", "NSP 4", "substrate peptide", "protease subsite preferences", "prss", "visualization probes", "library results", "Selective Substrate", "Human Neutrophil Serine Protease 4 Human neutrophil serine protease 4", "Hybrid Combinatorial Substrate Library approach", "neutrophil serine proteases family", "neutrophil response", "covalent diphenyl phosphonate probe", "biotin tag"], "article_id"=>1483131, "categories"=>["Biological Sciences"], "users"=>["Paulina Kasperkiewicz", "Marcin Poreba", "Scott J. Snipas", "S. Jack Lin", "Daniel Kirchhofer", "Guy S. Salvesen", "Marcin Drag"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0132818", "stats"=>{"downloads"=>1, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Design_of_a_Selective_Substrate_and_Activity_Based_Probe_for_Human_Neutrophil_Serine_Protease_4_/1483131", "title"=>"Design of a Selective Substrate and Activity Based Probe for Human Neutrophil Serine Protease 4", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2015-07-14 04:02:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/2175588"], "description"=>"<p>NA–no activity detected.</p><p>Kinetic parameters/constants for the hydrolysis of Ac-hCha-Phe(guan)-Oic-Arg-ACC substrate by neutrophil serine proteases to three significant digits.</p>", "links"=>[], "tags"=>["visualizing NSP 4", "NSP 4", "substrate peptide", "protease subsite preferences", "prss", "visualization probes", "library results", "Selective Substrate", "Human Neutrophil Serine Protease 4 Human neutrophil serine protease 4", "Hybrid Combinatorial Substrate Library approach", "neutrophil serine proteases family", "neutrophil response", "covalent diphenyl phosphonate probe", "biotin tag"], "article_id"=>1483125, "categories"=>["Biological Sciences"], "users"=>["Paulina Kasperkiewicz", "Marcin Poreba", "Scott J. Snipas", "S. Jack Lin", "Daniel Kirchhofer", "Guy S. Salvesen", "Marcin Drag"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0132818.t002", "stats"=>{"downloads"=>2, "page_views"=>20, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Kinetic_parameters_constants_for_the_hydrolysis_of_Ac_hCha_Phe_guan_Oic_Arg_ACC_substrate_by_neutrophil_serine_proteases_to_three_significant_digits_/1483125", "title"=>"Kinetic parameters/constants for the hydrolysis of Ac-hCha-Phe(guan)-Oic-Arg-ACC substrate by neutrophil serine proteases to three significant digits.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2015-07-14 04:02:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/2175587"], "description"=>"<p>Results are shown as an average of a minimum of 2 separate experiments with S.D.</p>", "links"=>[], "tags"=>["visualizing NSP 4", "NSP 4", "substrate peptide", "protease subsite preferences", "prss", "visualization probes", "library results", "Selective Substrate", "Human Neutrophil Serine Protease 4 Human neutrophil serine protease 4", "Hybrid Combinatorial Substrate Library approach", "neutrophil serine proteases family", "neutrophil response", "covalent diphenyl phosphonate probe", "biotin tag"], "article_id"=>1483124, "categories"=>["Biological Sciences"], "users"=>["Paulina Kasperkiewicz", "Marcin Poreba", "Scott J. Snipas", "S. Jack Lin", "Daniel Kirchhofer", "Guy S. Salvesen", "Marcin Drag"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0132818.t001", "stats"=>{"downloads"=>7, "page_views"=>15, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Kinetic_analysis_of_tetrapeptide_substrates_for_NSP4_/1483124", "title"=>"Kinetic analysis of tetrapeptide substrates for NSP4.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2015-07-14 04:02:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/2175582"], "description"=>"<p>The general library structure contains tetrapeptide derivatives with the sequence Ac-P4-X-X-Arg-ACC, Ac-X-P3-X-Arg-ACC, Ac-X-X-P2-Arg-ACC, where P4, P3 and P2 represents one of 120 fixed natural or unnatural amino acids and X represents an equimolar mixture of natural amino acids (omitting Cys and substituting Nle for Met) with ACC (7-amino-4-carbamoylmethylcoumarin) as a reporter group.</p>", "links"=>[], "tags"=>["visualizing NSP 4", "NSP 4", "substrate peptide", "protease subsite preferences", "prss", "visualization probes", "library results", "Selective Substrate", "Human Neutrophil Serine Protease 4 Human neutrophil serine protease 4", "Hybrid Combinatorial Substrate Library approach", "neutrophil serine proteases family", "neutrophil response", "covalent diphenyl phosphonate probe", "biotin tag"], "article_id"=>1483119, "categories"=>["Biological Sciences"], "users"=>["Paulina Kasperkiewicz", "Marcin Poreba", "Scott J. Snipas", "S. Jack Lin", "Daniel Kirchhofer", "Guy S. Salvesen", "Marcin Drag"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0132818.g001", "stats"=>{"downloads"=>0, "page_views"=>19, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Scheme_of_the_HyCoSuL_P1_Arg_library_/1483119", "title"=>"Scheme of the HyCoSuL P1 Arg library.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-07-14 04:02:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/2175583"], "description"=>"<p>Preferences in the P4-P2 positions were determined by screening HyCoSuL, which contains tetramer peptides with the general structures Ac-P4-X-X-Arg-ACC, Ac-X-P3-X-Arg-ACC, Ac-X-X-P2-Arg-ACC, where P4, P3 and P2 represents fixed natural or unnatural amino acid and X represents an equimolar mixture of natural amino acids (omitting Cys and substituting Nle for Met). Screening was performed on a SpectraMax Gemini plate reader. Substrate hydrolysis rates were normalized to the most active component (100%) y axis. Natural amino acids are colored grey, unnatural black. Results are shown as an average of 3 experiments with S.D.</p>", "links"=>[], "tags"=>["visualizing NSP 4", "NSP 4", "substrate peptide", "protease subsite preferences", "prss", "visualization probes", "library results", "Selective Substrate", "Human Neutrophil Serine Protease 4 Human neutrophil serine protease 4", "Hybrid Combinatorial Substrate Library approach", "neutrophil serine proteases family", "neutrophil response", "covalent diphenyl phosphonate probe", "biotin tag"], "article_id"=>1483120, "categories"=>["Biological Sciences"], "users"=>["Paulina Kasperkiewicz", "Marcin Poreba", "Scott J. Snipas", "S. Jack Lin", "Daniel Kirchhofer", "Guy S. Salvesen", "Marcin Drag"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0132818.g002", "stats"=>{"downloads"=>0, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Determination_of_NSP4_substrate_specificity_/1483120", "title"=>"Determination of NSP4 substrate specificity.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-07-14 04:02:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/2175589"], "description"=>"<p>NI–no inhibition observed; K<sub>m</sub> values relate to the substrate used for analysis,</p><p>* K<sub>m</sub> for this substrate was above 100μM, the concentration used in the assay. AMC – 7-amino-4-methylcoumarin.</p><p>Inhibition rate constants of NSPs by Biot-Ahx-hCha-Phe(guan)-Oic-Arg<sup>P</sup>(OPh)<sub>2</sub> (PK401).</p>", "links"=>[], "tags"=>["visualizing NSP 4", "NSP 4", "substrate peptide", "protease subsite preferences", "prss", "visualization probes", "library results", "Selective Substrate", "Human Neutrophil Serine Protease 4 Human neutrophil serine protease 4", "Hybrid Combinatorial Substrate Library approach", "neutrophil serine proteases family", "neutrophil response", "covalent diphenyl phosphonate probe", "biotin tag"], "article_id"=>1483126, "categories"=>["Biological Sciences"], "users"=>["Paulina Kasperkiewicz", "Marcin Poreba", "Scott J. Snipas", "S. Jack Lin", "Daniel Kirchhofer", "Guy S. Salvesen", "Marcin Drag"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0132818.t003", "stats"=>{"downloads"=>2, "page_views"=>17, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Inhibition_rate_constants_of_NSPs_by_Biot_Ahx_hCha_Phe_guan_Oic_Arg_P_OPh_2_PK401_/1483126", "title"=>"Inhibition rate constants of NSPs by Biot-Ahx-hCha-Phe(guan)-Oic-Arg<sup>P</sup>(OPh)<sub>2</sub> (PK401).", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2015-07-14 04:02:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/2175586"], "description"=>"<p>(A) NSP4 was treated with PK401 in a range from 1 to 2000nM. (B) 100nM of NE, PR3, CatG and NSP4 with or without 100nM of PK401. (A, B) Samples were denatured in SDS sample buffer, run in SDS/PAGE followed by membrane transfer. The blot was developed with fluorescently-tagged streptavidin and imaged by fluorescence scanning (See <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0132818#pone.0132818.s001\" target=\"_blank\">S1 Text</a>).</p>", "links"=>[], "tags"=>["visualizing NSP 4", "NSP 4", "substrate peptide", "protease subsite preferences", "prss", "visualization probes", "library results", "Selective Substrate", "Human Neutrophil Serine Protease 4 Human neutrophil serine protease 4", "Hybrid Combinatorial Substrate Library approach", "neutrophil serine proteases family", "neutrophil response", "covalent diphenyl phosphonate probe", "biotin tag"], "article_id"=>1483123, "categories"=>["Biological Sciences"], "users"=>["Paulina Kasperkiewicz", "Marcin Poreba", "Scott J. Snipas", "S. Jack Lin", "Daniel Kirchhofer", "Guy S. Salvesen", "Marcin Drag"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0132818.g004", "stats"=>{"downloads"=>1, "page_views"=>31, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Visualization_of_PK401_with_purified_NSP4_and_all_NSP_8217_s_/1483123", "title"=>"Visualization of PK401 with purified NSP4 and all NSP’s.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-07-14 04:02:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/2175585"], "description"=>"<p>The activity-based probe (PK401), a diphenyl phosphonate derived from the optimal substrate sequence—PK421—is shown as the last structure.</p>", "links"=>[], "tags"=>["visualizing NSP 4", "NSP 4", "substrate peptide", "protease subsite preferences", "prss", "visualization probes", "library results", "Selective Substrate", "Human Neutrophil Serine Protease 4 Human neutrophil serine protease 4", "Hybrid Combinatorial Substrate Library approach", "neutrophil serine proteases family", "neutrophil response", "covalent diphenyl phosphonate probe", "biotin tag"], "article_id"=>1483122, "categories"=>["Biological Sciences"], "users"=>["Paulina Kasperkiewicz", "Marcin Poreba", "Scott J. Snipas", "S. Jack Lin", "Daniel Kirchhofer", "Guy S. Salvesen", "Marcin Drag"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0132818.g003", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structures_of_the_optimized_NSP4_substrates_based_on_natural_PK417_and_PK418_and_natural_unnatural_amino_acids_PK421_and_PK431_/1483122", "title"=>"Structures of the optimized NSP4 substrates based on natural (PK417 and PK418) and natural/unnatural amino acids (PK421 and PK431).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-07-14 04:02:05"}

PMC Usage Stats | Further Information

  • {"unique-ip"=>"17", "full-text"=>"21", "pdf"=>"8", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"7"}
  • {"unique-ip"=>"16", "full-text"=>"17", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"8"}
  • {"unique-ip"=>"21", "full-text"=>"18", "pdf"=>"9", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"2", "cited-by"=>"0", "year"=>"2015", "month"=>"9"}
  • {"unique-ip"=>"15", "full-text"=>"14", "pdf"=>"5", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"6", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2015", "month"=>"10"}
  • {"unique-ip"=>"9", "full-text"=>"8", "pdf"=>"6", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"2"}
  • {"unique-ip"=>"20", "full-text"=>"21", "pdf"=>"6", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"9", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"11"}
  • {"unique-ip"=>"12", "full-text"=>"7", "pdf"=>"8", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"8", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"12"}
  • {"unique-ip"=>"16", "full-text"=>"13", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"9", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"1"}
  • {"unique-ip"=>"16", "full-text"=>"17", "pdf"=>"10", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"5", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"3"}
  • {"unique-ip"=>"12", "full-text"=>"10", "pdf"=>"5", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"11", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"4"}
  • {"unique-ip"=>"8", "full-text"=>"8", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"5"}
  • {"unique-ip"=>"9", "full-text"=>"6", "pdf"=>"7", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"6"}
  • {"unique-ip"=>"6", "full-text"=>"9", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2016", "month"=>"7"}
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  • {"unique-ip"=>"12", "full-text"=>"6", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"9", "supp-data"=>"1", "cited-by"=>"1", "year"=>"2017", "month"=>"1"}
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  • {"unique-ip"=>"10", "full-text"=>"11", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"11"}
  • {"unique-ip"=>"6", "full-text"=>"6", "pdf"=>"4", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"12"}
  • {"unique-ip"=>"6", "full-text"=>"9", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"1"}
  • {"unique-ip"=>"9", "full-text"=>"7", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"5", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"3"}
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  • {"unique-ip"=>"5", "full-text"=>"5", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"12"}
  • {"unique-ip"=>"14", "full-text"=>"17", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2018", "month"=>"11"}
  • {"unique-ip"=>"6", "full-text"=>"7", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"2", "cited-by"=>"0", "year"=>"2018", "month"=>"4"}
  • {"unique-ip"=>"9", "full-text"=>"9", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"5"}
  • {"unique-ip"=>"9", "full-text"=>"10", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2018", "month"=>"6"}
  • {"unique-ip"=>"7", "full-text"=>"7", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"9"}
  • {"unique-ip"=>"6", "full-text"=>"4", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2018", "month"=>"7"}
  • {"unique-ip"=>"8", "full-text"=>"9", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2018", "month"=>"10"}
  • {"unique-ip"=>"4", "full-text"=>"2", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"2", "cited-by"=>"0", "year"=>"2018", "month"=>"8"}
  • {"unique-ip"=>"1", "full-text"=>"1", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"2"}
  • {"unique-ip"=>"7", "full-text"=>"6", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"5", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
  • {"unique-ip"=>"4", "full-text"=>"4", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"4"}
  • {"unique-ip"=>"11", "full-text"=>"10", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"5"}
  • {"unique-ip"=>"10", "full-text"=>"7", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"8"}
  • {"unique-ip"=>"21", "full-text"=>"23", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2019", "month"=>"9"}
  • {"unique-ip"=>"11", "full-text"=>"12", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"10"}
  • {"unique-ip"=>"14", "full-text"=>"8", "pdf"=>"6", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"12"}
  • {"unique-ip"=>"7", "full-text"=>"6", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"2"}
  • {"unique-ip"=>"9", "full-text"=>"10", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"3"}
  • {"unique-ip"=>"9", "full-text"=>"9", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"4"}

Relative Metric

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

Source
Counter
Time
2019-04-06 02:38:25 UTC
Target URL
http://counter-101.soma.plos.org/api/v1.0/stats/doi/10.1371%2Fjournal.pone.0132818
Trace

/app/models/concerns/networkable.rb:21:in `get_result'
/app/models/source.rb:165:in `get_data'
/app/models/retrieval_status.rb:47:in `perform_get_data'
/app/jobs/source_job.rb:52:in `block (2 levels) in perform'
/app/jobs/source_job.rb:51:in `block in perform'
/app/jobs/source_job.rb:35:in `each'
/app/jobs/source_job.rb:35:in `perform'