Improving Kinetic or Thermodynamic Stability of an Azoreductase by Directed Evolution
Events
Loading … Spinner

Mendeley | Further Information

{"title"=>"Improving kinetic or thermodynamic stability of an azoreductase by directed evolution", "type"=>"journal", "authors"=>[{"first_name"=>"Vânia", "last_name"=>"Brissos", "scopus_author_id"=>"24079497500"}, {"first_name"=>"Nádia", "last_name"=>"Gonçalves", "scopus_author_id"=>"56155107300"}, {"first_name"=>"Eduardo P.", "last_name"=>"Melo", "scopus_author_id"=>"35566177900"}, {"first_name"=>"Lígia O.", "last_name"=>"Martins", "scopus_author_id"=>"7102109314"}], "year"=>2014, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"373059124", "sgr"=>"84900338484", "issn"=>"19326203", "pmid"=>"24475252", "scopus"=>"2-s2.0-84900338484", "doi"=>"10.1371/journal.pone.0087209", "isbn"=>"1932-6203"}, "id"=>"8af7dea8-7947-33ab-87cd-2c05c0fc5df9", "abstract"=>"Protein stability arises from a combination of factors which are often difficult to rationalise. Therefore its improvement is better addressed through directed evolution than by rational design approaches. In this study, five rounds of mutagenesis/recombination followed by high-throughput screening (≈10,000 clones) yielded the hit 1B6 showing a 300-fold higher half life at 50°C than that exhibited by the homodimeric wild type PpAzoR azoreductase from Pseudomonas putida MET94. The characterization using fluorescence, calorimetry and light scattering shows that 1B6 has a folded state slightly less stable than the wild type (with lower melting and optimal temperatures) but in contrast is more resistant to irreversible denaturation. The superior kinetic stability of 1B6 variant was therefore related to an increased resistance of the unfolded monomers to aggregation through the introduction of mutations that disturbed hydrophobic patches and increased the surface net charge of the protein. Variants 2A1 and 2A1-Y179H with increased thermodynamic stability (10 to 20°C higher melting temperature than wild type) were also examined showing the distinctive nature of mutations that lead to improved structural robustness: these occur in residues that are mostly involved in strengthening the solvent-exposed loops or the inter-dimer interactions of the folded state.", "link"=>"http://www.mendeley.com/research/improving-kinetic-thermodynamic-stability-azoreductase-directed-evolution", "reader_count"=>36, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Professor > Associate Professor"=>1, "Student > Doctoral Student"=>2, "Researcher"=>4, "Student > Ph. D. Student"=>10, "Student > Master"=>10, "Other"=>1, "Student > Bachelor"=>6}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Professor > Associate Professor"=>1, "Student > Doctoral Student"=>2, "Researcher"=>4, "Student > Ph. D. Student"=>10, "Student > Master"=>10, "Other"=>1, "Student > Bachelor"=>6}, "reader_count_by_subject_area"=>{"Engineering"=>2, "Unspecified"=>3, "Biochemistry, Genetics and Molecular Biology"=>4, "Agricultural and Biological Sciences"=>20, "Physics and Astronomy"=>1, "Chemistry"=>4, "Computer Science"=>2}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>2}, "Chemistry"=>{"Chemistry"=>4}, "Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>20}, "Computer Science"=>{"Computer Science"=>2}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>4}, "Unspecified"=>{"Unspecified"=>3}}, "reader_count_by_country"=>{"United States"=>1, "Malaysia"=>1}, "group_count"=>0}

Scopus | Further Information

{"@_fa"=>"true", "link"=>[{"@_fa"=>"true", "@ref"=>"self", "@href"=>"https://api.elsevier.com/content/abstract/scopus_id/84900338484"}, {"@_fa"=>"true", "@ref"=>"author-affiliation", "@href"=>"https://api.elsevier.com/content/abstract/scopus_id/84900338484?field=author,affiliation"}, {"@_fa"=>"true", "@ref"=>"scopus", "@href"=>"https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84900338484&origin=inward"}, {"@_fa"=>"true", "@ref"=>"scopus-citedby", "@href"=>"https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=84900338484&origin=inward"}], "prism:url"=>"https://api.elsevier.com/content/abstract/scopus_id/84900338484", "dc:identifier"=>"SCOPUS_ID:84900338484", "eid"=>"2-s2.0-84900338484", "dc:title"=>"Improving kinetic or thermodynamic stability of an azoreductase by directed evolution", "dc:creator"=>"Brissos V.", "prism:publicationName"=>"PLoS ONE", "prism:eIssn"=>"19326203", "prism:volume"=>"9", "prism:issueIdentifier"=>"1", "prism:pageRange"=>nil, "prism:coverDate"=>"2014-01-27", "prism:coverDisplayDate"=>"27 January 2014", "prism:doi"=>"10.1371/journal.pone.0087209", "citedby-count"=>"20", "affiliation"=>[{"@_fa"=>"true", "affilname"=>"Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa", "affiliation-city"=>"Oeiras", "affiliation-country"=>"Portugal"}], "pubmed-id"=>"24475252", "prism:aggregationType"=>"Journal", "subtype"=>"ar", "subtypeDescription"=>"Article", "article-number"=>"e87209", "source-id"=>"10600153309", "openaccess"=>"1", "openaccessFlag"=>true}

Facebook

  • {"url"=>"http%3A%2F%2Fjournals.plos.org%2Fplosone%2Farticle%3Fid%3D10.1371%252Fjournal.pone.0087209", "share_count"=>0, "like_count"=>0, "comment_count"=>0, "click_count"=>0, "total_count"=>0}

Twitter

Counter

  • {"month"=>"1", "year"=>"2014", "pdf_views"=>"15", "xml_views"=>"6", "html_views"=>"59"}
  • {"month"=>"2", "year"=>"2014", "pdf_views"=>"32", "xml_views"=>"0", "html_views"=>"116"}
  • {"month"=>"3", "year"=>"2014", "pdf_views"=>"29", "xml_views"=>"2", "html_views"=>"90"}
  • {"month"=>"4", "year"=>"2014", "pdf_views"=>"13", "xml_views"=>"4", "html_views"=>"93"}
  • {"month"=>"5", "year"=>"2014", "pdf_views"=>"19", "xml_views"=>"1", "html_views"=>"144"}
  • {"month"=>"6", "year"=>"2014", "pdf_views"=>"13", "xml_views"=>"0", "html_views"=>"57"}
  • {"month"=>"7", "year"=>"2014", "pdf_views"=>"11", "xml_views"=>"0", "html_views"=>"69"}
  • {"month"=>"8", "year"=>"2014", "pdf_views"=>"4", "xml_views"=>"2", "html_views"=>"29"}
  • {"month"=>"9", "year"=>"2014", "pdf_views"=>"5", "xml_views"=>"1", "html_views"=>"39"}
  • {"month"=>"10", "year"=>"2014", "pdf_views"=>"14", "xml_views"=>"1", "html_views"=>"69"}
  • {"month"=>"11", "year"=>"2014", "pdf_views"=>"10", "xml_views"=>"1", "html_views"=>"61"}
  • {"month"=>"12", "year"=>"2014", "pdf_views"=>"5", "xml_views"=>"2", "html_views"=>"27"}
  • {"month"=>"1", "year"=>"2015", "pdf_views"=>"13", "xml_views"=>"0", "html_views"=>"61"}
  • {"month"=>"2", "year"=>"2015", "pdf_views"=>"4", "xml_views"=>"0", "html_views"=>"47"}
  • {"month"=>"3", "year"=>"2015", "pdf_views"=>"16", "xml_views"=>"0", "html_views"=>"52"}
  • {"month"=>"4", "year"=>"2015", "pdf_views"=>"24", "xml_views"=>"1", "html_views"=>"50"}
  • {"month"=>"5", "year"=>"2015", "pdf_views"=>"9", "xml_views"=>"0", "html_views"=>"35"}
  • {"month"=>"6", "year"=>"2015", "pdf_views"=>"14", "xml_views"=>"0", "html_views"=>"30"}
  • {"month"=>"7", "year"=>"2015", "pdf_views"=>"6", "xml_views"=>"0", "html_views"=>"17"}
  • {"month"=>"8", "year"=>"2015", "pdf_views"=>"4", "xml_views"=>"0", "html_views"=>"20"}
  • {"month"=>"9", "year"=>"2015", "pdf_views"=>"8", "xml_views"=>"1", "html_views"=>"43"}
  • {"month"=>"10", "year"=>"2015", "pdf_views"=>"12", "xml_views"=>"0", "html_views"=>"47"}
  • {"month"=>"11", "year"=>"2015", "pdf_views"=>"7", "xml_views"=>"0", "html_views"=>"39"}
  • {"month"=>"12", "year"=>"2015", "pdf_views"=>"5", "xml_views"=>"0", "html_views"=>"31"}
  • {"month"=>"1", "year"=>"2016", "pdf_views"=>"7", "xml_views"=>"0", "html_views"=>"26"}
  • {"month"=>"2", "year"=>"2016", "pdf_views"=>"2", "xml_views"=>"0", "html_views"=>"31"}
  • {"month"=>"3", "year"=>"2016", "pdf_views"=>"8", "xml_views"=>"0", "html_views"=>"58"}
  • {"month"=>"4", "year"=>"2016", "pdf_views"=>"14", "xml_views"=>"0", "html_views"=>"40"}
  • {"month"=>"5", "year"=>"2016", "pdf_views"=>"15", "xml_views"=>"0", "html_views"=>"28"}
  • {"month"=>"6", "year"=>"2016", "pdf_views"=>"3", "xml_views"=>"0", "html_views"=>"20"}
  • {"month"=>"7", "year"=>"2016", "pdf_views"=>"1", "xml_views"=>"0", "html_views"=>"33"}
  • {"month"=>"8", "year"=>"2016", "pdf_views"=>"6", "xml_views"=>"0", "html_views"=>"25"}
  • {"month"=>"9", "year"=>"2016", "pdf_views"=>"12", "xml_views"=>"0", "html_views"=>"36"}
  • {"month"=>"10", "year"=>"2016", "pdf_views"=>"5", "xml_views"=>"0", "html_views"=>"33"}
  • {"month"=>"11", "year"=>"2016", "pdf_views"=>"7", "xml_views"=>"0", "html_views"=>"39"}
  • {"month"=>"12", "year"=>"2016", "pdf_views"=>"10", "xml_views"=>"1", "html_views"=>"26"}
  • {"month"=>"1", "year"=>"2017", "pdf_views"=>"6", "xml_views"=>"0", "html_views"=>"43"}
  • {"month"=>"2", "year"=>"2017", "pdf_views"=>"7", "xml_views"=>"1", "html_views"=>"50"}
  • {"month"=>"3", "year"=>"2017", "pdf_views"=>"8", "xml_views"=>"0", "html_views"=>"34"}
  • {"month"=>"4", "year"=>"2017", "pdf_views"=>"6", "xml_views"=>"0", "html_views"=>"32"}
  • {"month"=>"5", "year"=>"2017", "pdf_views"=>"5", "xml_views"=>"0", "html_views"=>"28"}
  • {"month"=>"6", "year"=>"2017", "pdf_views"=>"4", "xml_views"=>"0", "html_views"=>"41"}
  • {"month"=>"7", "year"=>"2017", "pdf_views"=>"9", "xml_views"=>"2", "html_views"=>"28"}
  • {"month"=>"8", "year"=>"2017", "pdf_views"=>"13", "xml_views"=>"1", "html_views"=>"25"}
  • {"month"=>"9", "year"=>"2017", "pdf_views"=>"12", "xml_views"=>"1", "html_views"=>"21"}
  • {"month"=>"10", "year"=>"2017", "pdf_views"=>"3", "xml_views"=>"1", "html_views"=>"36"}
  • {"month"=>"11", "year"=>"2017", "pdf_views"=>"7", "xml_views"=>"0", "html_views"=>"59"}
  • {"month"=>"12", "year"=>"2017", "pdf_views"=>"2", "xml_views"=>"2", "html_views"=>"31"}
  • {"month"=>"1", "year"=>"2018", "pdf_views"=>"2", "xml_views"=>"1", "html_views"=>"24"}
  • {"month"=>"2", "year"=>"2018", "pdf_views"=>"8", "xml_views"=>"0", "html_views"=>"10"}
  • {"month"=>"3", "year"=>"2018", "pdf_views"=>"12", "xml_views"=>"1", "html_views"=>"33"}
  • {"month"=>"4", "year"=>"2018", "pdf_views"=>"3", "xml_views"=>"0", "html_views"=>"9"}
  • {"month"=>"5", "year"=>"2018", "pdf_views"=>"4", "xml_views"=>"2", "html_views"=>"21"}
  • {"month"=>"6", "year"=>"2018", "pdf_views"=>"2", "xml_views"=>"2", "html_views"=>"10"}
  • {"month"=>"7", "year"=>"2018", "pdf_views"=>"2", "xml_views"=>"3", "html_views"=>"9"}
  • {"month"=>"8", "year"=>"2018", "pdf_views"=>"3", "xml_views"=>"1", "html_views"=>"14"}
  • {"month"=>"9", "year"=>"2018", "pdf_views"=>"10", "xml_views"=>"0", "html_views"=>"22"}
  • {"month"=>"10", "year"=>"2018", "pdf_views"=>"25", "xml_views"=>"1", "html_views"=>"52"}
  • {"month"=>"11", "year"=>"2018", "pdf_views"=>"9", "xml_views"=>"0", "html_views"=>"26"}
  • {"month"=>"12", "year"=>"2018", "pdf_views"=>"9", "xml_views"=>"0", "html_views"=>"17"}
  • {"month"=>"1", "year"=>"2019", "pdf_views"=>"3", "xml_views"=>"1", "html_views"=>"24"}
  • {"month"=>"2", "year"=>"2019", "pdf_views"=>"14", "xml_views"=>"0", "html_views"=>"9"}
  • {"month"=>"3", "year"=>"2019", "pdf_views"=>"8", "xml_views"=>"0", "html_views"=>"18"}
  • {"month"=>"4", "year"=>"2019", "pdf_views"=>"11", "xml_views"=>"0", "html_views"=>"22"}
  • {"month"=>"5", "year"=>"2019", "pdf_views"=>"12", "xml_views"=>"0", "html_views"=>"29"}
  • {"month"=>"6", "year"=>"2019", "pdf_views"=>"9", "xml_views"=>"0", "html_views"=>"24"}
  • {"month"=>"7", "year"=>"2019", "pdf_views"=>"8", "xml_views"=>"0", "html_views"=>"18"}
  • {"month"=>"8", "year"=>"2019", "pdf_views"=>"9", "xml_views"=>"1", "html_views"=>"23"}
  • {"month"=>"9", "year"=>"2019", "pdf_views"=>"3", "xml_views"=>"0", "html_views"=>"19"}
  • {"month"=>"10", "year"=>"2019", "pdf_views"=>"19", "xml_views"=>"0", "html_views"=>"45"}
  • {"month"=>"11", "year"=>"2019", "pdf_views"=>"22", "xml_views"=>"0", "html_views"=>"36"}
  • {"month"=>"12", "year"=>"2019", "pdf_views"=>"17", "xml_views"=>"0", "html_views"=>"32"}
  • {"month"=>"1", "year"=>"2020", "pdf_views"=>"10", "xml_views"=>"0", "html_views"=>"30"}
  • {"month"=>"2", "year"=>"2020", "pdf_views"=>"8", "xml_views"=>"0", "html_views"=>"13"}

Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1361841"], "description"=>"<p>(A) Initial activity <i>vs</i> thermostability of 2214 clones screened relative to the wild type. (B) Re-screening of the best mutants identified. Stability was measured by the ratio of residual activity following incubation at 55°C for 60 min to initial activity.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymes", "Enzyme kinetics", "Enzyme structure", "biocatalysis", "proteins", "biophysics", "Protein folding", "biotechnology", "Environmental biotechnology", "biodegradation", "Evolutionary biology", "Forms of evolution", "Directed evolution", "mutant"], "article_id"=>914285, "categories"=>["Biological Sciences"], "users"=>["Vânia Brissos", "Nádia Gonçalves", "Eduardo P. Melo", "Lígia O. Martins"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0087209.g001", "stats"=>{"downloads"=>1, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Directed_evolution_landscape_for_the_first_generation_mutant_library_/914285", "title"=>"Directed evolution landscape for the first generation mutant library.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-01-27 03:30:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/1361854"], "description"=>"1)<p>Ratio of the initial activity of the variant to the parent type (Ai<sub>v</sub>/Ai<sub>p</sub>),</p>2)<p>Ratio of the residual activity to the initial activity of the variant (v), normalized to the parent type (p) – (A<sub>r</sub>/A<sub>i</sub>)<sub>v</sub>/(A<sub>r</sub>/A<sub>i</sub>)<sub>p</sub></p><p>The parents for the next generations are in bold.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymes", "Enzyme kinetics", "Enzyme structure", "biocatalysis", "proteins", "biophysics", "Protein folding", "biotechnology", "Environmental biotechnology", "biodegradation", "Evolutionary biology", "Forms of evolution", "Directed evolution", "amino", "substitutions", "accumulated", "ppazor", "variants", "thermostability"], "article_id"=>914298, "categories"=>["Biological Sciences"], "users"=>["Vânia Brissos", "Nádia Gonçalves", "Eduardo P. Melo", "Lígia O. Martins"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0087209.t001", "stats"=>{"downloads"=>3, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Summary_of_library_screening_conditions_amino_acid_substitutions_accumulated_in_PpAzoR_variants_and_initial_activity_and_thermostability_relative_to_their_parents_/914298", "title"=>"Summary of library screening conditions, amino acid substitutions accumulated in PpAzoR variants and initial activity and thermostability relative to their parents.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-01-27 03:30:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/1361849"], "description"=>"<p>(A) Temperature dependence of purified wild type PpAzoR (circles), 2A1 (diamonds) and 2A1-Y179H (triangles) variants. Reactions were performed in 100 mM sodium phosphate buffer, pH 7, in the presence of 100 µM AQS and 250 µM NADPH. (B) Light scattering of wild type PpAzoR (circles), 1B6 (squares) and 2A1-Y179H (triangles) variants. (C) Thermal inactivation of wild type PpAzoR (circles) and 2A1-Y179H (triangles) variant; enzyme samples were incubated at 50°C and activity measured at 30°C in aliquots taken at different time intervals.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymes", "Enzyme kinetics", "Enzyme structure", "biocatalysis", "proteins", "biophysics", "Protein folding", "biotechnology", "Environmental biotechnology", "biodegradation", "Evolutionary biology", "Forms of evolution", "Directed evolution", "2a1-y179h", "variants"], "article_id"=>914293, "categories"=>["Biological Sciences"], "users"=>["Vânia Brissos", "Nádia Gonçalves", "Eduardo P. Melo", "Lígia O. Martins"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0087209.g007", "stats"=>{"downloads"=>0, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_2A1_and_2A1_Y179H_variants_characterization_/914293", "title"=>"2A1 and 2A1-Y179H variants characterization.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-01-27 03:30:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/1361848"], "description"=>"<p>Wild type PpAzoR (circles), B1G6 from 1<sup>st</sup> generation (squares), 16B7 from 2<sup>nd</sup> generation (triangles), 2A1 from 3<sup>rd</sup> generation (diamonds) and 23C10 from 3<sup>rd</sup> generation (stars). Reactions were performed using crude extracts in 100 mM sodium phosphate buffer, pH 7, in the presence of 100 µM AQS and 250 µM NADPH.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymes", "Enzyme kinetics", "Enzyme structure", "biocatalysis", "proteins", "biophysics", "Protein folding", "biotechnology", "Environmental biotechnology", "biodegradation", "Evolutionary biology", "Forms of evolution", "Directed evolution", "dependence", "ppazor", "variants", "crude"], "article_id"=>914292, "categories"=>["Biological Sciences"], "users"=>["Vânia Brissos", "Nádia Gonçalves", "Eduardo P. Melo", "Lígia O. Martins"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0087209.g006", "stats"=>{"downloads"=>1, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Temperature_dependence_of_PpAzoR_wild_type_and_variants_measured_in_crude_cell_extracts_/914292", "title"=>"Temperature dependence of PpAzoR wild type and variants measured in crude cell extracts.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-01-27 03:30:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/1361845"], "description"=>"<p>(A) Activity remaining at 30°C following heating to the indicated temperature for 1 h of wild type PpAzoR (circles) and 1B6 variant (squares). Reactions were performed in 100 mM sodium phosphate buffer pH 7, 100 µM AQS and 250 µM NADPH. (B) Thermal inactivation of wild type PpAzoR (circles) and 1B6 variant (squares). Enzyme samples were incubated at 50°C and activity measured at 30°C in aliquots taken at different time intervals. (C) Temperature dependence of wild type PpAzoR (circles) and 1B6 variant (squares).</p>", "links"=>[], "tags"=>["Biochemistry", "enzymes", "Enzyme kinetics", "Enzyme structure", "biocatalysis", "proteins", "biophysics", "Protein folding", "biotechnology", "Environmental biotechnology", "biodegradation", "Evolutionary biology", "Forms of evolution", "Directed evolution", "variant"], "article_id"=>914289, "categories"=>["Biological Sciences"], "users"=>["Vânia Brissos", "Nádia Gonçalves", "Eduardo P. Melo", "Lígia O. Martins"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0087209.g004", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_1B6_variant_characterization_/914289", "title"=>"1B6 variant characterization.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-01-27 03:30:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/1361844"], "description"=>"<p>Activity was measured after incubation at different temperatures (55–70°C) for 30 min: 1B6 (black), 2E4 (grey), 2F11 (diagonal), 6F11 (dot), 3B9 (white). Reactions were performed in 100 mM sodium phosphate buffer pH 7, 100 µM AQS and 250 µM NADPH.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymes", "Enzyme kinetics", "Enzyme structure", "biocatalysis", "proteins", "biophysics", "Protein folding", "biotechnology", "Environmental biotechnology", "biodegradation", "Evolutionary biology", "Forms of evolution", "Directed evolution", "variants"], "article_id"=>914288, "categories"=>["Biological Sciences"], "users"=>["Vânia Brissos", "Nádia Gonçalves", "Eduardo P. Melo", "Lígia O. Martins"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0087209.g003", "stats"=>{"downloads"=>1, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Residual_activity_of_variants_from_the_5_th_generation_/914288", "title"=>"Residual activity of variants from the 5<sup>th</sup> generation.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-01-27 03:30:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/1361842"], "description"=>"<p>Only non-synonymous mutations are shown. The mutants with higher stability are in white and the mutants with higher activity are in grey.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymes", "Enzyme kinetics", "Enzyme structure", "biocatalysis", "proteins", "biophysics", "Protein folding", "biotechnology", "Environmental biotechnology", "biodegradation", "Evolutionary biology", "Forms of evolution", "Directed evolution", "ppazor", "variants", "generated"], "article_id"=>914286, "categories"=>["Biological Sciences"], "users"=>["Vânia Brissos", "Nádia Gonçalves", "Eduardo P. Melo", "Lígia O. Martins"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0087209.g002", "stats"=>{"downloads"=>3, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Lineage_of_PpAzoR_variants_generated_in_this_study_/914286", "title"=>"Lineage of PpAzoR variants generated in this study.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-01-27 03:30:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/1361853"], "description"=>"_", "links"=>[], "tags"=>["Biochemistry", "enzymes", "Enzyme kinetics", "Enzyme structure", "biocatalysis", "proteins", "biophysics", "Protein folding", "biotechnology", "Environmental biotechnology", "biodegradation", "Evolutionary biology", "Forms of evolution", "Directed evolution", "thermostabilization", "ppazor", "variants", "created", "directed"], "article_id"=>914297, "categories"=>["Biological Sciences"], "users"=>["Vânia Brissos", "Nádia Gonçalves", "Eduardo P. Melo", "Lígia O. Martins"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0087209.t003", "stats"=>{"downloads"=>0, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Mechanisms_of_protein_thermostabilization_present_in_PpAzoR_variants_created_by_directed_evolution_4_46_48_54_57_/914297", "title"=>"Mechanisms of protein thermostabilization present in PpAzoR variants created by directed evolution [4], [46]–[48], [54]–[57].", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-01-27 03:30:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/1361851"], "description"=>"<p>(A) 2A1 and (B) 1B6 variants. Mutations responsible for the thermodynamic stability are in red; mutations responsible for aggregation-resistance are in blue; the FMN is in orange.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymes", "Enzyme kinetics", "Enzyme structure", "biocatalysis", "proteins", "biophysics", "Protein folding", "biotechnology", "Environmental biotechnology", "biodegradation", "Evolutionary biology", "Forms of evolution", "Directed evolution", "amino", "acids", "thermostabilization", "ppazor"], "article_id"=>914295, "categories"=>["Biological Sciences"], "users"=>["Vânia Brissos", "Nádia Gonçalves", "Eduardo P. Melo", "Lígia O. Martins"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0087209.g009", "stats"=>{"downloads"=>0, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Mapping_of_key_amino_acids_for_protein_thermostabilization_in_PpAzoR_crystal_structure_PDB_code_4C0W_/914295", "title"=>"Mapping of key amino acids for protein thermostabilization in PpAzoR crystal structure (PDB code 4C0W).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-01-27 03:30:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/1361852"], "description"=>"_", "links"=>[], "tags"=>["Biochemistry", "enzymes", "Enzyme kinetics", "Enzyme structure", "biocatalysis", "proteins", "biophysics", "Protein folding", "biotechnology", "Environmental biotechnology", "biodegradation", "Evolutionary biology", "Forms of evolution", "Directed evolution", "tertiary", "ppazor", "2a1-y179h", "1b6", "variants", "fluorescence"], "article_id"=>914296, "categories"=>["Biological Sciences"], "users"=>["Vânia Brissos", "Nádia Gonçalves", "Eduardo P. Melo", "Lígia O. Martins"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0087209.t002", "stats"=>{"downloads"=>2, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Thermodynamic_stability_of_the_tertiary_structure_of_PpAzoR_wild_type_2A1_2A1_Y179H_and_1B6_variants_as_assessed_by_fluorescence_spectroscopy_/914296", "title"=>"Thermodynamic stability of the tertiary structure of PpAzoR wild type, 2A1, 2A1-Y179H and 1B6 variants as assessed by fluorescence spectroscopy.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-01-27 03:30:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/1361850"], "description"=>"<p>Unfolded fraction (f<sub>Unf</sub>) of wild type PpAzoR (circles) and 1B6 (squares), 2A1 (diamond) and 2A1-Y179H (triangles) variants by GdnHCl at pH 7.6 as measured by fluorescence emission. The solid line is the fit according to the equation f<sub>U</sub> = e<sup>(−ΔG°/RT)/(1+e (−ΔG°<b>/</b>RT))</sup>.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymes", "Enzyme kinetics", "Enzyme structure", "biocatalysis", "proteins", "biophysics", "Protein folding", "biotechnology", "Environmental biotechnology", "biodegradation", "Evolutionary biology", "Forms of evolution", "Directed evolution"], "article_id"=>914294, "categories"=>["Biological Sciences"], "users"=>["Vânia Brissos", "Nádia Gonçalves", "Eduardo P. Melo", "Lígia O. Martins"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0087209.g008", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Chemical_stability_/914294", "title"=>"Chemical stability.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-01-27 03:30:58"}
  • {"files"=>["https://ndownloader.figshare.com/files/1361847"], "description"=>"<p>(A) Wild type PpAzoR (thin line), 2A1 variant (dash line) and 1B6 variant (thick line). Arrows indicate the optimal temperature for activity which occurs in the initial part of the endothermic peak. (B) 1B6 variant fitted by non-two-state transitions (red line); Inset - Fraction of 1B6 variant unfolded (f<sub>Unf</sub>) by temperature at pH 7.6 as measured by fluorescence emission. The solid line is the fit according to the equation f<sub>U</sub> = e<sup>(−ΔG°/RT)/(1+e (−ΔG°<b>/</b>RT))</sup>.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymes", "Enzyme kinetics", "Enzyme structure", "biocatalysis", "proteins", "biophysics", "Protein folding", "biotechnology", "Environmental biotechnology", "biodegradation", "Evolutionary biology", "Forms of evolution", "Directed evolution", "scanning"], "article_id"=>914291, "categories"=>["Biological Sciences"], "users"=>["Vânia Brissos", "Nádia Gonçalves", "Eduardo P. Melo", "Lígia O. Martins"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0087209.g005", "stats"=>{"downloads"=>3, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Differential_scanning_thermograms_/914291", "title"=>"Differential scanning thermograms.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-01-27 03:30:58"}

PMC Usage Stats | Further Information

  • {"unique-ip"=>"18", "full-text"=>"18", "pdf"=>"13", "abstract"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"2"}
  • {"unique-ip"=>"17", "full-text"=>"15", "pdf"=>"3", "abstract"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"3"}
  • {"unique-ip"=>"11", "full-text"=>"9", "pdf"=>"6", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"5"}
  • {"unique-ip"=>"11", "full-text"=>"16", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"6"}
  • {"unique-ip"=>"14", "full-text"=>"13", "pdf"=>"8", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"6", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"4"}
  • {"unique-ip"=>"11", "full-text"=>"16", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"4"}
  • {"unique-ip"=>"5", "full-text"=>"5", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"5"}
  • {"unique-ip"=>"2", "full-text"=>"3", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"6"}
  • {"unique-ip"=>"8", "full-text"=>"23", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"7"}
  • {"unique-ip"=>"11", "full-text"=>"11", "pdf"=>"5", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"3"}
  • {"unique-ip"=>"15", "full-text"=>"15", "pdf"=>"5", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"3", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"2"}
  • {"unique-ip"=>"11", "full-text"=>"9", "pdf"=>"5", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"8"}
  • {"unique-ip"=>"9", "full-text"=>"8", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"9"}
  • {"unique-ip"=>"8", "full-text"=>"9", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"10"}
  • {"unique-ip"=>"16", "full-text"=>"16", "pdf"=>"4", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"7"}
  • {"unique-ip"=>"6", "full-text"=>"6", "pdf"=>"1", "abstract"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"8"}
  • {"unique-ip"=>"7", "full-text"=>"5", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"9"}
  • {"unique-ip"=>"11", "full-text"=>"9", "pdf"=>"4", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"10"}
  • {"unique-ip"=>"15", "full-text"=>"15", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"2"}
  • {"unique-ip"=>"10", "full-text"=>"6", "pdf"=>"5", "abstract"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"11"}
  • {"unique-ip"=>"3", "full-text"=>"2", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"12"}
  • {"unique-ip"=>"12", "full-text"=>"11", "pdf"=>"6", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"1"}
  • {"unique-ip"=>"10", "full-text"=>"6", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"1", "year"=>"2015", "month"=>"11"}
  • {"unique-ip"=>"10", "full-text"=>"7", "pdf"=>"6", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"12"}
  • {"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"=>"2016", "month"=>"1"}
  • {"unique-ip"=>"6", "full-text"=>"10", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"3"}
  • {"unique-ip"=>"4", "full-text"=>"5", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"4"}
  • {"unique-ip"=>"6", "full-text"=>"6", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"5"}
  • {"unique-ip"=>"4", "full-text"=>"3", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"6"}
  • {"unique-ip"=>"7", "full-text"=>"9", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"16", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"7"}
  • {"unique-ip"=>"11", "full-text"=>"8", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"8"}
  • {"unique-ip"=>"3", "full-text"=>"3", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"14", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"9"}
  • {"unique-ip"=>"6", "full-text"=>"4", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"10"}
  • {"unique-ip"=>"5", "full-text"=>"7", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"11"}
  • {"unique-ip"=>"4", "full-text"=>"4", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"12"}
  • {"unique-ip"=>"9", "full-text"=>"6", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"1"}
  • {"unique-ip"=>"5", "full-text"=>"5", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"2"}
  • {"unique-ip"=>"9", "full-text"=>"9", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"3"}
  • {"unique-ip"=>"9", "full-text"=>"9", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"4"}
  • {"unique-ip"=>"12", "full-text"=>"13", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"5"}
  • {"unique-ip"=>"5", "full-text"=>"5", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"6", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"6"}
  • {"unique-ip"=>"4", "full-text"=>"12", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"7"}
  • {"unique-ip"=>"3", "full-text"=>"3", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"8"}
  • {"unique-ip"=>"6", "full-text"=>"6", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"9"}
  • {"unique-ip"=>"12", "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"=>"10"}
  • {"unique-ip"=>"8", "full-text"=>"9", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"10", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"11"}
  • {"unique-ip"=>"3", "full-text"=>"3", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"12"}
  • {"unique-ip"=>"5", "full-text"=>"7", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"1"}
  • {"unique-ip"=>"8", "full-text"=>"8", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"3"}
  • {"unique-ip"=>"10", "full-text"=>"10", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"1"}
  • {"unique-ip"=>"9", "full-text"=>"12", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"4"}
  • {"unique-ip"=>"14", "full-text"=>"12", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"5"}
  • {"unique-ip"=>"9", "full-text"=>"9", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"6"}
  • {"unique-ip"=>"5", "full-text"=>"5", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"7"}
  • {"unique-ip"=>"12", "full-text"=>"11", "pdf"=>"7", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"10"}
  • {"unique-ip"=>"7", "full-text"=>"7", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"8"}
  • {"unique-ip"=>"5", "full-text"=>"6", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"11"}
  • {"unique-ip"=>"3", "full-text"=>"4", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"9"}
  • {"unique-ip"=>"10", "full-text"=>"10", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"12"}
  • {"unique-ip"=>"2", "full-text"=>"5", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"2"}
  • {"unique-ip"=>"6", "full-text"=>"6", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
  • {"unique-ip"=>"9", "full-text"=>"11", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"4"}
  • {"unique-ip"=>"7", "full-text"=>"7", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"5"}
  • {"unique-ip"=>"8", "full-text"=>"6", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"8"}
  • {"unique-ip"=>"14", "full-text"=>"14", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"9"}
  • {"unique-ip"=>"19", "full-text"=>"21", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"10"}
  • {"unique-ip"=>"8", "full-text"=>"6", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"12"}

Relative Metric

{"start_date"=>"2014-01-01T00:00:00Z", "end_date"=>"2014-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences/Evolutionary biology", "average_usage"=>[333]}, {"subject_area"=>"/Biology and life sciences/Molecular biology", "average_usage"=>[292, 461]}, {"subject_area"=>"/Engineering and technology", "average_usage"=>[282]}, {"subject_area"=>"/Engineering and technology/Synthetic biology", "average_usage"=>[386, 689]}, {"subject_area"=>"/Physical sciences/Physics", "average_usage"=>[266]}]}
Loading … Spinner
There are currently no alerts