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{"title"=>"Laminin peptide-immobilized hydrogels modulate valve endothelial cell hemostatic regulation", "type"=>"journal", "authors"=>[{"first_name"=>"Liezl Rae", "last_name"=>"Balaoing", "scopus_author_id"=>"55361961900"}, {"first_name"=>"Allison Davis", "last_name"=>"Post", "scopus_author_id"=>"36994111800"}, {"first_name"=>"Adam Yuh", "last_name"=>"Lin", "scopus_author_id"=>"54907157700"}, {"first_name"=>"Hubert", "last_name"=>"Tseng", "scopus_author_id"=>"57109819900"}, {"first_name"=>"Joel L.", "last_name"=>"Moake", "scopus_author_id"=>"7006085656"}, {"first_name"=>"K. Jane", "last_name"=>"Grande-Allen", "scopus_author_id"=>"6602569298"}], "year"=>2015, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "scopus"=>"2-s2.0-84939127878", "pui"=>"605586275", "doi"=>"10.1371/journal.pone.0130749", "isbn"=>"1932-6203", "sgr"=>"84939127878", "pmid"=>"26090873"}, "id"=>"11fdf5bf-b101-3766-b1d1-727611b819e3", "abstract"=>"Valve endothelial cells (VEC) have unique phenotypic responses relative to other types of vascular endothelial cells and have highly sensitive hemostatic functions affected by changes in valve tissues. Furthermore, effects of environmental factors on VEC hemostatic function has not been characterized. This work used a poly(ethylene glycol) diacrylate (PEGDA) hydrogel platform to evaluate the effects of substrate stiffness and cell adhesive ligands on VEC phenotype and expression of hemostatic genes. Hydrogels of molecular weights (MWs) 3.4, 8, and 20 kDa were polymerized into platforms of different rigidities and thiol-modified cell adhesive peptides were covalently bound to acrylate groups on the hydrogel surfaces. The peptide RKRLQVQLSIRT (RKR) is a syndecan-1 binding ligand derived from laminin, a trimeric protein and a basement membrane matrix component. Conversely, RGDS is an integrin binding peptide found in many extracellular matrix (ECM) proteins including fibronectin, fibrinogen, and von Willebrand factor (VWF). VECs adhered to and formed a stable monolayer on all RKR-coated hydrogel-MW combinations. RGDS-coated platforms supported VEC adhesion and growth on RGDS-3.4 kDa and RGDS-8 kDa hydrogels. VECs cultured on the softer RKR-8 kDa and RKR-20 kDa hydrogel platforms had significantly higher gene expression for all anti-thrombotic (ADAMTS-13, tissue factor pathway inhibitor, and tissue plasminogen activator) and thrombotic (VWF, tissue factor, and P-selectin) proteins than VECs cultured on RGDS-coated hydrogels and tissue culture polystyrene controls. Stimulated VECs promoted greater platelet adhesion than non-stimulated VECs on their respective culture condition; yet stimulated VECs on RGDS-3.4 kDa gels were not as responsive to stimulation relative to the RKR-gel groups. Thus, the syndecan binding, laminin-derived peptide promoted stable VEC adhesion on the softer hydrogels and maintained VEC phenotype and natural hemostatic function. In conclusion, utilization of non-integrin adhesive peptide sequences derived from basement membrane ECM may recapitulate balanced VEC function and may benefit endothelialization of valve implants.", "link"=>"http://www.mendeley.com/research/laminin-peptideimmobilized-hydrogels-modulate-valve-endothelial-cell-hemostatic-regulation", "reader_count"=>26, "reader_count_by_academic_status"=>{"Student > Doctoral Student"=>6, "Researcher"=>5, "Student > Ph. D. Student"=>9, "Student > Postgraduate"=>3, "Student > Master"=>1, "Student > Bachelor"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Student > Doctoral Student"=>6, "Researcher"=>5, "Student > Ph. D. Student"=>9, "Student > Postgraduate"=>3, "Student > Master"=>1, "Student > Bachelor"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Engineering"=>9, "Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>3, "Materials Science"=>1, "Medicine and Dentistry"=>5, "Agricultural and Biological Sciences"=>3, "Pharmacology, Toxicology and Pharmaceutical Science"=>2, "Chemistry"=>2}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>9}, "Materials Science"=>{"Materials Science"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>5}, "Chemistry"=>{"Chemistry"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>3}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}, "Unspecified"=>{"Unspecified"=>1}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>2}}, "reader_count_by_country"=>{"United States"=>1}, "group_count"=>2}

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• http://doi.org/10.1016/j.actbio.2019.05.055
• http://doi.org/10.1007/s10965-019-1728-2
• http://doi.org/10.1016/j.actbio.2015.08.021
• http://doi.org/10.15406/atroa.2017.02.00033
• http://doi.org/10.1002/ar.23916
• http://doi.org/10.1007/s10439-018-02171-3
• http://doi.org/10.1039/C5CS00586H
• http://doi.org/10.1002/adhm.201700918
• http://doi.org/10.1007/s10439-018-02194-w
• http://doi.org/10.1016/j.tibtech.2018.01.003
• http://doi.org/10.1039/C9OB00270G
• http://doi.org/10.1016/j.biomaterials.2015.07.039

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Figshare

• {"files"=>["https://ndownloader.figshare.com/files/2126810"], "description"=>"<p>VEC gene expression of anti-thrombotic related proteins [A disintegrin and metalloproteinase with a thrombopondin type I motif, member 13 (ADAMTS-13), tissue factor pathway inhibitor (TFPI), and tissue plasminogen activation (tPA)] and thrombotic related proteins [von Willebrand factor (VWF), tissue factor (TF), and P-selectin)] when cultured on combinations of different molecular weight formulations (3.4, 8, and 20 kDa) of hydrogels and adhesive ligands (RKR or RGDS) relative to VECs cultures on TCPS (indicated by dashed line). Groups not connected by same symbols are significantly different. p < 0.05.</p>", "links"=>[], "tags"=>["tissue plasminogen activator", "pegda", "VEC adhesion", "von Willebrand factor", "basement membrane ECM", "VEC phenotype", "RKRLQVQLSIRT", "mw", "vwf", "adamts", "basement membrane matrix component", "kda", "hydrogel", "tissue culture polystyrene controls", "rkr", "integrin binding peptide", "VEC hemostatic function", "rgds"], "article_id"=>1454896, "categories"=>["Biological Sciences"], "users"=>["Liezl Rae Balaoing", "Allison Davis Post", "Adam Yuh Lin", "Hubert Tseng", "Joel L. Moake", "K. Jane Grande-Allen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0130749.g003", "stats"=>{"downloads"=>0, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_VEC_hemostatic_related_protein_gene_expression_/1454896", "title"=>"VEC hemostatic-related protein gene expression.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-06-19 03:08:12"}
• {"files"=>["https://ndownloader.figshare.com/files/2126811"], "description"=>"<p>(A) Non-stimulated VECs seeded on hydrogels (3.4 kDa) functionalized with RKR (left) or RGDS (right) stained for CD31 (red) and VWF (green). Nucleus was stained with DAPI (blue). Scale bar = 50 μm. (B) Quantification of rapidly released VWF and (C) the fraction of cleaved VWF-140 fragments from histamine-stimulated VECs cultured on different molecular weight hydrogels functionalized with RKR or RGDS, or TCPS. Groups not connected by same symbols are significantly different. p < 0.05.</p>", "links"=>[], "tags"=>["tissue plasminogen activator", "pegda", "VEC adhesion", "von Willebrand factor", "basement membrane ECM", "VEC phenotype", "RKRLQVQLSIRT", "mw", "vwf", "adamts", "basement membrane matrix component", "kda", "hydrogel", "tissue culture polystyrene controls", "rkr", "integrin binding peptide", "VEC hemostatic function", "rgds"], "article_id"=>1454897, "categories"=>["Biological Sciences"], "users"=>["Liezl Rae Balaoing", "Allison Davis Post", "Adam Yuh Lin", "Hubert Tseng", "Joel L. Moake", "K. Jane Grande-Allen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0130749.g004", "stats"=>{"downloads"=>6, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_VECs_produce_release_and_actively_cleave_von_Willebrand_factor_/1454897", "title"=>"VECs produce, release, and actively cleave von Willebrand factor.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-06-19 03:08:12"}
• {"files"=>["https://ndownloader.figshare.com/files/2126812"], "description"=>"<p>(A) Endothelialized peptide-immobilized hydrogel platforms significantly reduce platelet adhesion. Platelet adhesion on hydrogel scaffolds increases with increasing molecular weight PEGDA hydrogel. Platelet adhesion is significantly reduced on VEC-seeded peptide-coated hydrogels (gray bars) when compared to acellular peptide-coated constructs (white bars). * p <0.05. (B) Total adhered platelets onto stable and stimulated VECs cultured on TCPS and hydrogels with immobilized RKR or RGDS. Histamine stimulated VECs (black bars) of all culture condition promoted significantly more platelet adhesion when compared to the non-simulated VECs cultured on the same condition (gray bars). * p < 0.05. Platelet adhesions were significantly lower for the stimulated VECs on RGDS gels than for all other stimulated conditions. # p < 0.05. (B) Dyed platelets adhered onto anchored ultra-large VWF strings (yellow arrows) on the surface of histamine stimulated VECs cultured on a RKR-3.4 kDa hydrogel. Scale bar = 50 μm.</p>", "links"=>[], "tags"=>["tissue plasminogen activator", "pegda", "VEC adhesion", "von Willebrand factor", "basement membrane ECM", "VEC phenotype", "RKRLQVQLSIRT", "mw", "vwf", "adamts", "basement membrane matrix component", "kda", "hydrogel", "tissue culture polystyrene controls", "rkr", "integrin binding peptide", "VEC hemostatic function", "rgds"], "article_id"=>1454898, "categories"=>["Biological Sciences"], "users"=>["Liezl Rae Balaoing", "Allison Davis Post", "Adam Yuh Lin", "Hubert Tseng", "Joel L. Moake", "K. Jane Grande-Allen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0130749.g005", "stats"=>{"downloads"=>2, "page_views"=>18, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Histamine_stimulated_VECs_on_hydrogel_based_platforms_are_capable_of_promoting_platelet_adhesion_/1454898", "title"=>"Histamine stimulated VECs on hydrogel based platforms are capable of promoting platelet adhesion.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-06-19 03:08:12"}
• {"files"=>["https://ndownloader.figshare.com/files/2126813", "https://ndownloader.figshare.com/files/2126814"], "description"=>"<div><p>Valve endothelial cells (VEC) have unique phenotypic responses relative to other types of vascular endothelial cells and have highly sensitive hemostatic functions affected by changes in valve tissues. Furthermore, effects of environmental factors on VEC hemostatic function has not been characterized. This work used a poly(ethylene glycol) diacrylate (PEGDA) hydrogel platform to evaluate the effects of substrate stiffness and cell adhesive ligands on VEC phenotype and expression of hemostatic genes. Hydrogels of molecular weights (MWs) 3.4, 8, and 20 kDa were polymerized into platforms of different rigidities and thiol-modified cell adhesive peptides were covalently bound to acrylate groups on the hydrogel surfaces. The peptide RKRLQVQLSIRT (RKR) is a syndecan-1 binding ligand derived from laminin, a trimeric protein and a basement membrane matrix component. Conversely, RGDS is an integrin binding peptide found in many extracellular matrix (ECM) proteins including fibronectin, fibrinogen, and von Willebrand factor (VWF). VECs adhered to and formed a stable monolayer on all RKR-coated hydrogel-MW combinations. RGDS-coated platforms supported VEC adhesion and growth on RGDS-3.4 kDa and RGDS-8 kDa hydrogels. VECs cultured on the softer RKR-8 kDa and RKR-20 kDa hydrogel platforms had significantly higher gene expression for all anti-thrombotic (ADAMTS-13, tissue factor pathway inhibitor, and tissue plasminogen activator) and thrombotic (VWF, tissue factor, and P-selectin) proteins than VECs cultured on RGDS-coated hydrogels and tissue culture polystyrene controls. Stimulated VECs promoted greater platelet adhesion than non-stimulated VECs on their respective culture condition; yet stimulated VECs on RGDS-3.4 kDa gels were not as responsive to stimulation relative to the RKR-gel groups. Thus, the syndecan binding, laminin-derived peptide promoted stable VEC adhesion on the softer hydrogels and maintained VEC phenotype and natural hemostatic function. In conclusion, utilization of non-integrin adhesive peptide sequences derived from basement membrane ECM may recapitulate balanced VEC function and may benefit endothelialization of valve implants.</p></div>", "links"=>[], "tags"=>["tissue plasminogen activator", "pegda", "VEC adhesion", "von Willebrand factor", "basement membrane ECM", "VEC phenotype", "RKRLQVQLSIRT", "mw", "vwf", "adamts", "basement membrane matrix component", "kda", "hydrogel", "tissue culture polystyrene controls", "rkr", "integrin binding peptide", "VEC hemostatic function", "rgds"], "article_id"=>1454899, "categories"=>["Biological Sciences"], "users"=>["Liezl Rae Balaoing", "Allison Davis Post", "Adam Yuh Lin", "Hubert Tseng", "Joel L. Moake", "K. Jane Grande-Allen"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0130749.s001", "https://dx.doi.org/10.1371/journal.pone.0130749.s002"], "stats"=>{"downloads"=>6, "page_views"=>15, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Laminin_Peptide_Immobilized_Hydrogels_Modulate_Valve_Endothelial_Cell_Hemostatic_Regulation_/1454899", "title"=>"Laminin Peptide-Immobilized Hydrogels Modulate Valve Endothelial Cell Hemostatic Regulation", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2015-06-19 03:08:12"}
• {"files"=>["https://ndownloader.figshare.com/files/2126807"], "description"=>"<p>Representative images of valve endothelial cell (VEC) adhesion and growth when seeded on combinations of 3.4, 8, or 20 kDa molecular weight PEGDA hydrogels with immobilized CRKRLQVQLSIRT (RKR) (first panel) or CRGDS (RGDS) (second panel) and on tissue culture treated polystyrene (TCPS) on days 1 and 7. Scale bar = 100 μm.</p>", "links"=>[], "tags"=>["tissue plasminogen activator", "pegda", "VEC adhesion", "von Willebrand factor", "basement membrane ECM", "VEC phenotype", "RKRLQVQLSIRT", "mw", "vwf", "adamts", "basement membrane matrix component", "kda", "hydrogel", "tissue culture polystyrene controls", "rkr", "integrin binding peptide", "VEC hemostatic function", "rgds"], "article_id"=>1454893, "categories"=>["Biological Sciences"], "users"=>["Liezl Rae Balaoing", "Allison Davis Post", "Adam Yuh Lin", "Hubert Tseng", "Joel L. Moake", "K. Jane Grande-Allen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0130749.g001", "stats"=>{"downloads"=>2, "page_views"=>15, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_VECs_adhere_onto_hydrogel_scaffolds_immobilized_with_extracellular_matrix_derived_peptides_/1454893", "title"=>"VECs adhere onto hydrogel scaffolds immobilized with extracellular matrix-derived peptides.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-06-19 03:08:12"}
• {"files"=>["https://ndownloader.figshare.com/files/2126809"], "description"=>"<p>Extracellular matrix proteins fibronectin (FN, red) and laminin (Lam, green) present throughout the cell layer of VECs cultured on RKR-8 kDa scaffolds after 7 days. Scale bar = 50 μm.</p>", "links"=>[], "tags"=>["tissue plasminogen activator", "pegda", "VEC adhesion", "von Willebrand factor", "basement membrane ECM", "VEC phenotype", "RKRLQVQLSIRT", "mw", "vwf", "adamts", "basement membrane matrix component", "kda", "hydrogel", "tissue culture polystyrene controls", "rkr", "integrin binding peptide", "VEC hemostatic function", "rgds"], "article_id"=>1454895, "categories"=>["Biological Sciences"], "users"=>["Liezl Rae Balaoing", "Allison Davis Post", "Adam Yuh Lin", "Hubert Tseng", "Joel L. Moake", "K. Jane Grande-Allen"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0130749.g002", "stats"=>{"downloads"=>0, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_VECs_on_peptide_coated_hydrogels_produce_extracellular_matrix_proteins_/1454895", "title"=>"VECs on peptide-coated hydrogels produce extracellular matrix proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-06-19 03:08:12"}

PMC Usage Stats | Further Information

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

Relative Metric

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

F1000Prime