Evaluating Molecular Mechanical Potentials for Helical Peptides and Proteins
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Mendeley | Further Information

{"title"=>"Evaluating molecular mechanical potentials for helical peptides and proteins", "type"=>"journal", "authors"=>[{"first_name"=>"Erik J.", "last_name"=>"Thompson", "scopus_author_id"=>"36460366500"}, {"first_name"=>"Allison J.", "last_name"=>"Depaul", "scopus_author_id"=>"36459806800"}, {"first_name"=>"Sarav S.", "last_name"=>"Patel", "scopus_author_id"=>"36459855800"}, {"first_name"=>"Eric J.", "last_name"=>"Sorin", "scopus_author_id"=>"6508040981"}], "year"=>2010, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "scopus"=>"2-s2.0-77956302920", "pui"=>"359482146", "doi"=>"10.1371/journal.pone.0010056", "isbn"=>"1932-6203", "sgr"=>"77956302920", "pmid"=>"20418937"}, "id"=>"50f56f8a-24b3-3733-ac9a-fae0f74fc607", "abstract"=>"Multiple variants of the AMBER all-atom force field were quantitatively evaluated with respect to their ability to accurately characterize helix-coil equilibria in explicit solvent simulations. Using a global distributed computing network, absolute conformational convergence was achieved for large ensembles of the capped A(21) and F(s) helical peptides. Further assessment of these AMBER variants was conducted via simulations of a flexible 164-residue five-helix-bundle protein, apolipophorin-III, on the 100 ns timescale. Of the contemporary potentials that had not been assessed previously, the AMBER-99SB force field showed significant helix-destabilizing tendencies, with beta bridge formation occurring in helical peptides, and unfolding of apolipophorin-III occurring on the tens of nanoseconds timescale. The AMBER-03 force field, while showing adequate helical propensities for both peptides and stabilizing apolipophorin-III, (i) predicts an unexpected decrease in helicity with ALA-->ARG(+) substitution, (ii) lacks experimentally observed 3(10) helical content, and (iii) deviates strongly from average apolipophorin-III NMR structural properties. As is observed for AMBER-99SB, AMBER-03 significantly overweighs the contribution of extended and polyproline backbone configurations to the conformational equilibrium. In contrast, the AMBER-99phi force field, which was previously shown to best reproduce experimental measurements of the helix-coil transition in model helical peptides, adequately stabilizes apolipophorin-III and yields both an average gyration radius and polar solvent exposed surface area that are in excellent agreement with the NMR ensemble.", "link"=>"http://www.mendeley.com/research/evaluating-molecular-mechanical-potentials-helical-peptides-proteins", "reader_count"=>44, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>4, "Student > Doctoral Student"=>3, "Researcher"=>15, "Student > Ph. D. Student"=>11, "Student > Postgraduate"=>2, "Student > Master"=>3, "Other"=>2, "Student > Bachelor"=>1, "Professor"=>3}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>4, "Student > Doctoral Student"=>3, "Researcher"=>15, "Student > Ph. D. Student"=>11, "Student > Postgraduate"=>2, "Student > Master"=>3, "Other"=>2, "Student > Bachelor"=>1, "Professor"=>3}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Engineering"=>2, "Biochemistry, Genetics and Molecular Biology"=>4, "Mathematics"=>1, "Agricultural and Biological Sciences"=>12, "Physics and Astronomy"=>6, "Chemical Engineering"=>1, "Chemistry"=>14, "Computer Science"=>3}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>2}, "Chemistry"=>{"Chemistry"=>14}, "Physics and Astronomy"=>{"Physics and Astronomy"=>6}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>12}, "Computer Science"=>{"Computer Science"=>3}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>4}, "Mathematics"=>{"Mathematics"=>1}, "Unspecified"=>{"Unspecified"=>1}, "Chemical Engineering"=>{"Chemical Engineering"=>1}}, "reader_count_by_country"=>{"Canada"=>2, "Argentina"=>1, "United States"=>2, "United Kingdom"=>2, "Portugal"=>1, "Germany"=>1}, "group_count"=>2}

Scopus | Further Information

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  • {"files"=>["https://ndownloader.figshare.com/files/855675"], "description"=>"<p>These maps represent equilibrium sampling of the F<sub>s</sub> peptide in the AMBER force fields evaluated, which have been ordered to match <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0010056#pone-0010056-g001\" target=\"_blank\">Figure 1</a> in (a) through (d). Each map consists of backbone torsional values binned in 3° intervals for all residues, and contours represent <i>k</i>T units at 305 K, the midpoint temperature of the helical peptide.</p>", "links"=>[], "tags"=>["landscapes", "projected", "ramachandran"], "article_id"=>526117, "categories"=>["Immunology", "Medicine", "Biophysics", "Physics", "Biochemistry", "Chemistry", "Cancer", "Computational Biology"], "users"=>["Erik J. Thompson", "Allison J. DePaul", "Sarav S. Patel", "Eric J. Sorin"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010056.g003", "stats"=>{"downloads"=>1, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Free_energy_landscapes_projected_onto_the_Ramachandran_map_/526117", "title"=>"Free energy landscapes projected onto the Ramachandran map.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 01:58:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/855484"], "description"=>"<p>Landscapes are shown to highlight relative magnitude differences between the potentials (top), while contours more clearly display the positions of local and global minima and maxima for each force field. The regions corresponding to alpha helix (purple), beta strand (yellow), and polyproline type II (red) conformations are indicated based on the definitions used by Garcia for Ala peptides <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0010056#pone.0010056-Garcia2\" target=\"_blank\">[11]</a>.</p>", "links"=>[], "tags"=>["potentials", "amber", "fields", "compared"], "article_id"=>525928, "categories"=>["Immunology", "Medicine", "Biophysics", "Physics", "Biochemistry", "Chemistry", "Cancer", "Computational Biology"], "users"=>["Erik J. Thompson", "Allison J. DePaul", "Sarav S. Patel", "Eric J. Sorin"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010056.g001", "stats"=>{"downloads"=>1, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_966_968_potentials_for_the_four_AMBER_force_fields_compared_in_this_work_/525928", "title"=>"The φ/ψ potentials for the four AMBER force fields compared in this work.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 01:56:59"}
  • {"files"=>["https://ndownloader.figshare.com/files/855867"], "description"=>"<p>These profiles represent averages over eight 100 ns simulations using the AMBER-94 (black), AMBER-03 (red), AMBER-99φ (blue), and AMBER-99SB (green) force fields. From top to bottom are the average number of helical residues, average all-atom root-mean-square deviation, and average radius of gyration.</p>", "links"=>[], "tags"=>["properties", "simulated", "apolipophorin-iii"], "article_id"=>526314, "categories"=>["Immunology", "Medicine", "Biophysics", "Physics", "Biochemistry", "Chemistry", "Cancer", "Computational Biology"], "users"=>["Erik J. Thompson", "Allison J. DePaul", "Sarav S. Patel", "Eric J. Sorin"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010056.g005", "stats"=>{"downloads"=>0, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Mean_structural_properties_of_simulated_apolipophorin_III_ensembles_/526314", "title"=>"Mean structural properties of simulated apolipophorin-III ensembles.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 01:59:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/856086"], "description"=>"<p>*Each force field was sampled using 1,000 trajectories starting in the fully helical state (H) and 1,000 trajectories starting in the random coil state (C) with no structured residues.</p><p>Max (longest individual trajectory), Total time (total ensemble simulation time), and >EQ (total equilibrium simulation time) are shown for each data set.</p>", "links"=>[], "tags"=>["ensemble"], "article_id"=>526539, "categories"=>["Immunology", "Medicine", "Biophysics", "Physics", "Biochemistry", "Chemistry", "Cancer", "Computational Biology"], "users"=>["Erik J. Thompson", "Allison J. DePaul", "Sarav S. Patel", "Eric J. Sorin"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010056.t001", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Simulated_ensemble_statistics_for_the_F_s_and_A_21_peptides_/526539", "title"=>"Simulated ensemble statistics for the F<sub>s</sub> and A<sub>21</sub> peptides.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-21 02:00:14"}
  • {"files"=>["https://ndownloader.figshare.com/files/855996"], "description"=>"<p>Probabilities of sampling helix (H), turn (T), random coil (C), and polyproline type II (P) states when simulated using the AMBER-94, AMBER-99φ, AMBER-03, and AMBER-99SB force fields are shown. The schematic at the top represents the NMR model that was used to initiate all simulations, with turns shown in green and coil regions shown in pink to match the color coded state sampling plots below, which show probability ranges from 0.0 (black) to 1.0 (color).</p>", "links"=>[], "tags"=>["sampling", "apolipophorin-iii"], "article_id"=>526447, "categories"=>["Immunology", "Medicine", "Biophysics", "Physics", "Biochemistry", "Chemistry", "Cancer", "Computational Biology"], "users"=>["Erik J. Thompson", "Allison J. DePaul", "Sarav S. Patel", "Eric J. Sorin"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010056.g006", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structural_sampling_of_apolipophorin_III_per_residue_/526447", "title"=>"Structural sampling of apolipophorin-III per residue.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 01:59:46"}
  • {"files"=>["https://ndownloader.figshare.com/files/856179"], "description"=>"<p>*SASA (solvent-accessible surface area) is in Å<sup>2</sup> and was calculated using VEGA (<a href=\"http://nova.colombo58.unimi.it\" target=\"_blank\">http://nova.colombo58.unimi.it</a>).</p>‡<p>All 21 NMR models were used to generate these means and standard deviations.</p>", "links"=>[], "tags"=>["apolipophorin-iii"], "article_id"=>526632, "categories"=>["Immunology", "Medicine", "Biophysics", "Physics", "Biochemistry", "Chemistry", "Cancer", "Computational Biology"], "users"=>["Erik J. Thompson", "Allison J. DePaul", "Sarav S. Patel", "Eric J. Sorin"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010056.t003", "stats"=>{"downloads"=>7, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Mean_SASA_for_apolipophorin_III_simulations_/526632", "title"=>"Mean SASA<sup>*</sup> for apolipophorin-III simulations.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-21 02:00:43"}
  • {"files"=>["https://ndownloader.figshare.com/files/855777"], "description"=>"<p>NMR model 1 of this 164-residue, five-helix-bundle protein (PDB 1LS4) was used to start our simulations in the noted AMBER force fields. Bright green and black unstructured regions represent turn and random coil regions, respectively. Helices are colored from blue (helix 1) to green (helix 5). The bottom view is rotated toward the reader to provide an axial view down the helical bundle central core region.</p>", "links"=>[], "tags"=>["views", "nmr"], "article_id"=>526229, "categories"=>["Immunology", "Medicine", "Biophysics", "Physics", "Biochemistry", "Chemistry", "Cancer", "Computational Biology"], "users"=>["Erik J. Thompson", "Allison J. DePaul", "Sarav S. Patel", "Eric J. Sorin"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010056.g004", "stats"=>{"downloads"=>1, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Ribbon_views_of_the_NMR_model_of_apolipophorin_III_/526229", "title"=>"Ribbon views of the NMR model of apolipophorin-III.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 01:58:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/856140"], "description"=>"<p>RMSD (all-atom root-mean-square deviation), R<sub>g</sub> (radius of gyration), N<sub>helix</sub> (number of α-helical residues), N<sub>310</sub> (number of 3<sub>10</sub>-helical residues), N<sub>seg</sub> (number of helical segments), and N<sub>cont</sub> (length of helical segments).</p>", "links"=>[], "tags"=>["averaged", "equilibrium", "properties"], "article_id"=>526587, "categories"=>["Immunology", "Medicine", "Biophysics", "Physics", "Biochemistry", "Chemistry", "Cancer", "Computational Biology"], "users"=>["Erik J. Thompson", "Allison J. DePaul", "Sarav S. Patel", "Eric J. Sorin"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010056.t002", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Ensemble_averaged_equilibrium_structural_properties_for_the_F_s_and_A_21_peptides_/526587", "title"=>"Ensemble averaged equilibrium structural properties for the F<sub>s</sub> and A<sub>21</sub> peptides.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-21 02:00:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/855589"], "description"=>"<p>The AMBER-03 (red), AMBER-99SB (green), and AMBER-99φ (blue) potentials are shown, where helix> represents the number of helical residues averaged across all runs in a given ensemble of 1,000 simulations. Dotted and solid lines represent simulation ensembles initiated from the fully random coil and fully helical states, respectively. Other structural properties listed in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0010056#pone-0010056-t002\" target=\"_blank\">Table 2</a> show similar convergence. Noise near the 100 ns regime is the result of a limited number of simulations reaching those times following the ensemble convergence that occurs prior to the 40 ns timepoint.</p>", "links"=>[], "tags"=>["helical"], "article_id"=>526046, "categories"=>["Immunology", "Medicine", "Biophysics", "Physics", "Biochemistry", "Chemistry", "Cancer", "Computational Biology"], "users"=>["Erik J. Thompson", "Allison J. DePaul", "Sarav S. Patel", "Eric J. Sorin"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0010056.g002", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Convergence_of_mean_helical_content_for_the_a_F_s_and_b_A_21_ensembles_/526046", "title"=>"Convergence of mean helical content for the (a) F<sub>s</sub> and (b) A<sub>21</sub> ensembles.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 01:57:39"}

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  • {"unique-ip"=>"13", "full-text"=>"15", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"8", "supp-data"=>"0", "cited-by"=>"1", "year"=>"2014", "month"=>"10"}
  • {"unique-ip"=>"5", "full-text"=>"4", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"2"}
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  • {"unique-ip"=>"5", "full-text"=>"3", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"1", "year"=>"2015", "month"=>"11"}
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  • {"unique-ip"=>"1", "full-text"=>"1", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"8"}
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  • {"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"=>"2016", "month"=>"10"}
  • {"unique-ip"=>"3", "full-text"=>"3", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"11"}
  • {"unique-ip"=>"2", "full-text"=>"2", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"12"}
  • {"unique-ip"=>"7", "full-text"=>"4", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"1"}
  • {"unique-ip"=>"1", "full-text"=>"1", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"2"}
  • {"unique-ip"=>"5", "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"=>"3"}
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  • {"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"=>"2017", "month"=>"7"}
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  • {"unique-ip"=>"7", "full-text"=>"5", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"4", "supp-data"=>"0", "cited-by"=>"1", "year"=>"2017", "month"=>"11"}
  • {"unique-ip"=>"1", "full-text"=>"1", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"1"}
  • {"unique-ip"=>"6", "full-text"=>"7", "pdf"=>"0", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"1", "year"=>"2018", "month"=>"3"}
  • {"unique-ip"=>"7", "full-text"=>"6", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"1"}
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  • {"unique-ip"=>"3", "full-text"=>"3", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"4"}
  • {"unique-ip"=>"9", "full-text"=>"22", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"6"}
  • {"unique-ip"=>"7", "full-text"=>"4", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"7"}
  • {"unique-ip"=>"6", "full-text"=>"3", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"8"}
  • {"unique-ip"=>"4", "full-text"=>"4", "pdf"=>"0", "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"=>"11"}
  • {"unique-ip"=>"5", "full-text"=>"6", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"9"}
  • {"unique-ip"=>"11", "full-text"=>"14", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"12"}
  • {"unique-ip"=>"10", "full-text"=>"13", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"2"}
  • {"unique-ip"=>"4", "full-text"=>"4", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
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  • {"unique-ip"=>"9", "full-text"=>"8", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"5"}
  • {"unique-ip"=>"7", "full-text"=>"6", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"8"}
  • {"unique-ip"=>"6", "full-text"=>"8", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"9"}
  • {"unique-ip"=>"14", "full-text"=>"12", "pdf"=>"6", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"10"}
  • {"unique-ip"=>"5", "full-text"=>"2", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"12"}
  • {"unique-ip"=>"8", "full-text"=>"8", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"2"}
  • {"unique-ip"=>"10", "full-text"=>"14", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"3"}
  • {"unique-ip"=>"10", "full-text"=>"10", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"4"}
  • {"unique-ip"=>"4", "full-text"=>"4", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"5"}
  • {"unique-ip"=>"2", "full-text"=>"1", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"6"}
  • {"unique-ip"=>"6", "full-text"=>"5", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"7"}
  • {"unique-ip"=>"6", "full-text"=>"3", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"8"}
  • {"unique-ip"=>"9", "full-text"=>"9", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "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"=>"2020", "month"=>"10"}
  • {"unique-ip"=>"4", "full-text"=>"5", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"11"}
  • {"unique-ip"=>"4", "full-text"=>"4", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"12"}
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Relative Metric

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