PROTEIN TARGETING TO STARCH Is Required for Localising GRANULE-BOUND STARCH SYNTHASE to Starch Granules and for Normal Amylose Synthesis in Arabidopsis
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{"title"=>"PROTEIN TARGETING TO STARCH Is Required for Localising GRANULE-BOUND STARCH SYNTHASE to Starch Granules and for Normal Amylose Synthesis in Arabidopsis", "type"=>"journal", "authors"=>[{"first_name"=>"David", "last_name"=>"Seung", "scopus_author_id"=>"36128948900"}, {"first_name"=>"Sebastian", "last_name"=>"Soyk", "scopus_author_id"=>"26023817800"}, {"first_name"=>"Mario", "last_name"=>"Coiro", "scopus_author_id"=>"55750488000"}, {"first_name"=>"Benjamin A.", "last_name"=>"Maier", "scopus_author_id"=>"56536204300"}, {"first_name"=>"Simona", "last_name"=>"Eicke", "scopus_author_id"=>"14008897200"}, {"first_name"=>"Samuel C.", "last_name"=>"Zeeman", "scopus_author_id"=>"6603783870"}], "year"=>2015, "source"=>"PLoS Biology", "identifiers"=>{"doi"=>"10.1371/journal.pbio.1002080", "sgr"=>"84924081191", "issn"=>"15457885", "pui"=>"602601523", "isbn"=>"1544-9173", "pmid"=>"25710501", "scopus"=>"2-s2.0-84924081191"}, "id"=>"74033319-99bf-3ce4-928e-768d3bec9b75", "abstract"=>"<p>The biosynthesis of starch in plant chloroplasts depends on a novel protein that targets starch synthase to the growing starch granules; this represents a potential target for the biotechnological modification of starch. Read the Synopsis.</p>", "link"=>"http://www.mendeley.com/research/protein-targeting-starch-required-localising-granulebound-starch-synthase-starch-granules-normal-amy", "reader_count"=>90, "reader_count_by_academic_status"=>{"Unspecified"=>4, "Professor > Associate Professor"=>1, "Researcher"=>20, "Student > Doctoral Student"=>8, "Student > Ph. D. Student"=>21, "Student > Postgraduate"=>6, "Student > Master"=>12, "Other"=>3, "Student > Bachelor"=>11, "Lecturer"=>1, "Professor"=>3}, "reader_count_by_user_role"=>{"Unspecified"=>4, "Professor > Associate Professor"=>1, "Researcher"=>20, "Student > Doctoral Student"=>8, "Student > Ph. D. Student"=>21, "Student > Postgraduate"=>6, "Student > Master"=>12, "Other"=>3, "Student > Bachelor"=>11, "Lecturer"=>1, "Professor"=>3}, "reader_count_by_subject_area"=>{"Unspecified"=>6, "Engineering"=>3, "Environmental Science"=>3, "Biochemistry, Genetics and Molecular Biology"=>14, "Materials Science"=>1, "Agricultural and Biological Sciences"=>57, "Medicine and Dentistry"=>1, "Physics and Astronomy"=>1, "Chemistry"=>2, "Social Sciences"=>2}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>3}, "Materials Science"=>{"Materials Science"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Chemistry"=>{"Chemistry"=>2}, "Social Sciences"=>{"Social Sciences"=>2}, "Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>57}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>14}, "Unspecified"=>{"Unspecified"=>6}, "Environmental Science"=>{"Environmental Science"=>3}}, "reader_count_by_country"=>{"Argentina"=>1, "Netherlands"=>1, "Philippines"=>1, "France"=>1, "Chile"=>1, "Switzerland"=>1, "Germany"=>1, "Spain"=>1}, "group_count"=>6}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1922740"], "description"=>"<p>Soluble (S) and insoluble (I) protein fractions of leaf extracts were subject to immunoblot analysis with GFP antibodies. Three independent lines generated in both wild-type and <i>ptst-1</i> backgrounds are shown, each with varying expression levels. Starch-bound proteins are contained in the insoluble fraction. The small difference in migration between soluble and insoluble fractions was reproducibly observed and may be due to differences in sample preparation and composition.</p>", "links"=>[], "tags"=>["amylose synthesis", "starch granules", "cbm", "PROTEIN TARGETING", "gbss", "Normal Amylose Synthesis", "synthase", "elongating amylose polymers", "protein", "starch", "PTST", "Arabidopsi"], "article_id"=>1316894, "categories"=>["Biological Sciences"], "users"=>["David Seung", "Sebastian Soyk", "Mario Coiro", "Benjamin A. Maier", "Simona Eicke", "Samuel C. Zeeman"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1002080.g009", "stats"=>{"downloads"=>2, "page_views"=>24, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Expression_of_GBSS_GFP_in_Arabidopsis_ptst_mutants_/1316894", "title"=>"Expression of GBSS-GFP in Arabidopsis <i>ptst</i> mutants.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-02-24 03:02:55"}
  • {"files"=>["https://ndownloader.figshare.com/files/1922731"], "description"=>"<p>(A) Silver-stained SDS-PAGE gels of granule-bound proteins from <i>ptst sex4</i> and <i>dpe1 ptst</i> double mutants. Lanes were loaded according to equivalent mass of starch (1.3 mg starch). (B) Iodine stained rosettes of <i>ptst sex4</i> mutants. Note that the younger leaves stain like the amylose-free <i>gbss sex4</i> mutant, while older leaves stain darker.</p>", "links"=>[], "tags"=>["amylose synthesis", "starch granules", "cbm", "PROTEIN TARGETING", "gbss", "Normal Amylose Synthesis", "synthase", "elongating amylose polymers", "protein", "starch", "PTST", "Arabidopsi"], "article_id"=>1316885, "categories"=>["Biological Sciences"], "users"=>["David Seung", "Sebastian Soyk", "Mario Coiro", "Benjamin A. Maier", "Simona Eicke", "Samuel C. Zeeman"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1002080.g004", "stats"=>{"downloads"=>1, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Introduction_of_the_ptst_allele_into_high_amylose_mutants_/1316885", "title"=>"Introduction of the <i>ptst</i> allele into high amylose mutants.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-02-24 03:02:55"}
  • {"files"=>["https://ndownloader.figshare.com/files/1922702"], "description"=>"<p>Angiosperm sequences are shown in red, mosses in blue, while chlorophyte sequences are shown in green. Bootstrap values that are >50 are shown over the branches. The alignment used to generate this tree is available as <a href=\"http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1002080#pbio.1002080.s001\" target=\"_blank\">S1 Data</a>.</p>", "links"=>[], "tags"=>["amylose synthesis", "starch granules", "cbm", "PROTEIN TARGETING", "gbss", "Normal Amylose Synthesis", "synthase", "elongating amylose polymers", "protein", "starch", "PTST", "Arabidopsi"], "article_id"=>1316880, "categories"=>["Biological Sciences"], "users"=>["David Seung", "Sebastian Soyk", "Mario Coiro", "Benjamin A. Maier", "Simona Eicke", "Samuel C. Zeeman"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1002080.g001", "stats"=>{"downloads"=>3, "page_views"=>75, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Maximum_likelihood_phylogenetic_tree_of_PTST_proteins_from_the_MAFFT_alignment_/1316880", "title"=>"Maximum likelihood phylogenetic tree of PTST proteins from the MAFFT alignment.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-02-24 03:02:55"}
  • {"files"=>["https://ndownloader.figshare.com/files/1930107", "https://ndownloader.figshare.com/files/1930108", "https://ndownloader.figshare.com/files/1930109", "https://ndownloader.figshare.com/files/1930110", "https://ndownloader.figshare.com/files/1930111", "https://ndownloader.figshare.com/files/1930112", "https://ndownloader.figshare.com/files/1930113", "https://ndownloader.figshare.com/files/1930114", "https://ndownloader.figshare.com/files/1930115", "https://ndownloader.figshare.com/files/1930116", "https://ndownloader.figshare.com/files/1930117", "https://ndownloader.figshare.com/files/1930118", "https://ndownloader.figshare.com/files/1930119", "https://ndownloader.figshare.com/files/1930120", "https://ndownloader.figshare.com/files/1930121"], "description"=>"<div><p>The domestication of starch crops underpinned the development of human civilisation, yet we still do not fully understand how plants make starch. Starch is composed of glucose polymers that are branched (amylopectin) or linear (amylose). The amount of amylose strongly influences the physico-chemical behaviour of starchy foods during cooking and of starch mixtures in non-food manufacturing processes. The GRANULE-BOUND STARCH SYNTHASE (GBSS) is the glucosyltransferase specifically responsible for elongating amylose polymers and was the only protein known to be required for its biosynthesis. Here, we demonstrate that PROTEIN TARGETING TO STARCH (PTST) is also specifically required for amylose synthesis in Arabidopsis. PTST is a plastidial protein possessing an N-terminal coiled coil domain and a C-terminal carbohydrate binding module (CBM). We discovered that Arabidopsis <i>ptst</i> mutants synthesise amylose-free starch and are phenotypically similar to mutants lacking GBSS. Analysis of granule-bound proteins showed a dramatic reduction of GBSS protein in <i>ptst</i> mutant starch granules. Pull-down assays with recombinant proteins <i>in vitro</i>, as well as immunoprecipitation assays <i>in planta</i>, revealed that GBSS physically interacts with PTST via a coiled coil. Furthermore, we show that the CBM domain of PTST, which mediates its interaction with starch granules, is also required for correct GBSS localisation. Fluorescently tagged Arabidopsis GBSS, expressed either in tobacco or Arabidopsis leaves, required the presence of Arabidopsis PTST to localise to starch granules. Mutation of the CBM of PTST caused GBSS to remain in the plastid stroma. PTST fulfils a previously unknown function in targeting GBSS to starch. This sheds new light on the importance of targeting biosynthetic enzymes to sub-cellular sites where their action is required. Importantly, PTST represents a promising new gene target for the biotechnological modification of starch composition, as it is exclusively involved in amylose synthesis.</p></div>", "links"=>[], "tags"=>["amylose synthesis", "starch granules", "cbm", "PROTEIN TARGETING", "gbss", "Normal Amylose Synthesis", "synthase", "elongating amylose polymers", "protein", "starch", "PTST", "Arabidopsi"], "article_id"=>1322350, "categories"=>["Biological Sciences"], "users"=>["David Seung", "Sebastian Soyk", "Mario Coiro", "Benjamin A. Maier", "Simona Eicke", "Samuel C. Zeeman"], "doi"=>["https://dx.doi.org/10.1371/journal.pbio.1002080.s001", "https://dx.doi.org/10.1371/journal.pbio.1002080.s002", "https://dx.doi.org/10.1371/journal.pbio.1002080.s003", "https://dx.doi.org/10.1371/journal.pbio.1002080.s004", "https://dx.doi.org/10.1371/journal.pbio.1002080.s005", "https://dx.doi.org/10.1371/journal.pbio.1002080.s006", "https://dx.doi.org/10.1371/journal.pbio.1002080.s007", "https://dx.doi.org/10.1371/journal.pbio.1002080.s008", "https://dx.doi.org/10.1371/journal.pbio.1002080.s009", "https://dx.doi.org/10.1371/journal.pbio.1002080.s010", "https://dx.doi.org/10.1371/journal.pbio.1002080.s011", "https://dx.doi.org/10.1371/journal.pbio.1002080.s012", "https://dx.doi.org/10.1371/journal.pbio.1002080.s013", "https://dx.doi.org/10.1371/journal.pbio.1002080.s014", "https://dx.doi.org/10.1371/journal.pbio.1002080.s015"], "stats"=>{"downloads"=>37, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_PROTEIN_TARGETING_TO_STARCH_Is_Required_for_Localising_GRANULE_BOUND_STARCH_SYNTHASE_to_Starch_Granules_and_for_Normal_Amylose_Synthesis_in_Arabidopsis_/1322350", "title"=>"PROTEIN TARGETING TO STARCH Is Required for Localising GRANULE-BOUND STARCH SYNTHASE to Starch Granules and for Normal Amylose Synthesis in Arabidopsis", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2015-02-24 16:24:53"}
  • {"files"=>["https://ndownloader.figshare.com/files/1922738"], "description"=>"<p>(A) PTST-YFP and GBSS-CFP were individually or co-expressed in tobacco epidermal cells and imaged using confocal microscopy. Note that the localisation of GBSS-CFP on starch granules depends on PTST-YFP co-expression. Bar = 10 μm. (B) Same as (A), but additionally using the W217A/W255A non-starch-binding variant of PTST. Bar = 4 μm.</p>", "links"=>[], "tags"=>["amylose synthesis", "starch granules", "cbm", "PROTEIN TARGETING", "gbss", "Normal Amylose Synthesis", "synthase", "elongating amylose polymers", "protein", "starch", "PTST", "Arabidopsi"], "article_id"=>1316892, "categories"=>["Biological Sciences"], "users"=>["David Seung", "Sebastian Soyk", "Mario Coiro", "Benjamin A. Maier", "Simona Eicke", "Samuel C. Zeeman"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1002080.g008", "stats"=>{"downloads"=>2, "page_views"=>17, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Localisation_of_fluorescently_tagged_PTST_and_GBSS_in_tobacco_leaves_/1316892", "title"=>"Localisation of fluorescently tagged PTST and GBSS in tobacco leaves.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-02-24 03:02:55"}
  • {"files"=>["https://ndownloader.figshare.com/files/1922735"], "description"=>"<p>Binding of GST-PTST recombinant protein to intact wild-type (WT) and waxy (<i>wx</i>) maize starch granules was assessed <i>in vitro</i>. Unbound proteins are in the soluble fraction (S), while bound proteins are in the pellet (P). No protein was detected in the final wash (W<sub>f</sub>). Mutating both Trp217 and Trp255 in the CBM48 domain abolished the interaction with starch.</p>", "links"=>[], "tags"=>["amylose synthesis", "starch granules", "cbm", "PROTEIN TARGETING", "gbss", "Normal Amylose Synthesis", "synthase", "elongating amylose polymers", "protein", "starch", "PTST", "Arabidopsi"], "article_id"=>1316889, "categories"=>["Biological Sciences"], "users"=>["David Seung", "Sebastian Soyk", "Mario Coiro", "Benjamin A. Maier", "Simona Eicke", "Samuel C. Zeeman"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1002080.g007", "stats"=>{"downloads"=>2, "page_views"=>33, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_CBM48_domain_is_required_for_glucan_binding_in_PTST_/1316889", "title"=>"The CBM48 domain is required for glucan-binding in PTST.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-02-24 03:02:55"}
  • {"files"=>["https://ndownloader.figshare.com/files/1922734"], "description"=>"<p>(A) <i>In vitro</i> pulldown assay using Ni<sup>2+</sup>-NTA resin against purified recombinant proteins. GBSS-His<sub>6</sub> and GST-PTST were detected by immunoblotting with anti-His and anti-GST antibodies respectively. Wild-type GBSS specifically pulls down PTST. Charge-shift mutations at the coiled coil reduce the interaction. (B) Visualisation of GBSS activity in-gel. Recombinant proteins were separated on SDS-PAGE gel containing 0.05% (<i>w/v</i>) amylopectin and renatured in-gel. Following incubation with ADP-glucose, activity was visualised by staining with iodine. (C) <i>In vivo</i> pulldown experiment by immunoprecipitation of tandem affinity purification (TAP) (c-Myc)-tagged PTST protein transiently co-expressed with variant forms of HA-tagged GBSS in tobacco leaves. Anti-Myc and anti-HA antibodies were used to detect the precipitated PTST and GBSS proteins respectively.</p>", "links"=>[], "tags"=>["amylose synthesis", "starch granules", "cbm", "PROTEIN TARGETING", "gbss", "Normal Amylose Synthesis", "synthase", "elongating amylose polymers", "protein", "starch", "PTST", "Arabidopsi"], "article_id"=>1316888, "categories"=>["Biological Sciences"], "users"=>["David Seung", "Sebastian Soyk", "Mario Coiro", "Benjamin A. Maier", "Simona Eicke", "Samuel C. Zeeman"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1002080.g006", "stats"=>{"downloads"=>1, "page_views"=>21, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_GBSS_interacts_with_PTST_through_its_coiled_coil_/1316888", "title"=>"GBSS interacts with PTST through its coiled coil.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-02-24 03:02:55"}
  • {"files"=>["https://ndownloader.figshare.com/files/1922732"], "description"=>"<p>(A) COILS analysis to predict coiled coils in Arabidopsis GBSS and PTST sequences. The location of predicted coiled coils are shown with an indication of the probability score (ranging from 0 to 1, where 1 is the highest probability). (B) Homology model of the Arabidopsis GBSS based on the rice GBSS1 crystal structure. The location of the predicted coiled coil from (A) is depicted on the structure in orange. (C) Presence of surface-exposed charged side chains on the coiled coil containing helix.</p>", "links"=>[], "tags"=>["amylose synthesis", "starch granules", "cbm", "PROTEIN TARGETING", "gbss", "Normal Amylose Synthesis", "synthase", "elongating amylose polymers", "protein", "starch", "PTST", "Arabidopsi"], "article_id"=>1316886, "categories"=>["Biological Sciences"], "users"=>["David Seung", "Sebastian Soyk", "Mario Coiro", "Benjamin A. Maier", "Simona Eicke", "Samuel C. Zeeman"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1002080.g005", "stats"=>{"downloads"=>1, "page_views"=>25, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Analysis_of_PTST_and_GBSS_using_bioinformatic_tools_/1316886", "title"=>"Analysis of PTST and GBSS using bioinformatic tools.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-02-24 03:02:55"}
  • {"files"=>["https://ndownloader.figshare.com/files/1922729"], "description"=>"<p>(A) Silver-stained SDS-PAGE gels of granule-bound proteins extracted from purified starch granules. Lanes were loaded according to equivalent mass of starch (1.3 mg starch). The band corresponding to GBSS is indicated. (B) Immunoblot detection of GBSS in granule-bound protein extracts. Loading was according to equivalent mass of starch (0.7 mg). (C) Same as (B), but more extract was loaded (equivalent to1.3 mg starch) and exposure time was greatly extended. (D) Immunoblot detection of PTST in granule-bound protein extracts. (E) Soluble (S) and insoluble (I) protein fractions of leaves were subject to immunoblot analysis with GBSS and PTST antibodies. Starch-bound proteins are contained in the insoluble fraction.</p>", "links"=>[], "tags"=>["amylose synthesis", "starch granules", "cbm", "PROTEIN TARGETING", "gbss", "Normal Amylose Synthesis", "synthase", "elongating amylose polymers", "protein", "starch", "PTST", "Arabidopsi"], "article_id"=>1316883, "categories"=>["Biological Sciences"], "users"=>["David Seung", "Sebastian Soyk", "Mario Coiro", "Benjamin A. Maier", "Simona Eicke", "Samuel C. Zeeman"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1002080.g003", "stats"=>{"downloads"=>1, "page_views"=>26, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_abundance_of_granule_bound_GBSS_protein_is_greatly_reduced_in_ptst_/1316883", "title"=>"The abundance of granule-bound GBSS protein is greatly reduced in <i>ptst</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-02-24 03:02:55"}
  • {"files"=>["https://ndownloader.figshare.com/files/1922720"], "description"=>"<p>(A) Schematic illustration of the exon-intron structure of the <i>PTST</i> gene. Exons are represented by blue boxes. Pale blue boxes represent the 5′ and 3′ UTRs. Translation start (ATG) and stop (TAG) codons are indicated with arrows. Red arrows indicate T-DNA insertion sites. (B) Immunoblot detection of PTST in soluble protein extracts from leaves. The corresponding wild types to <i>ptst-1</i> and <i>ptst-2</i> are Columbia (Col) and Wassilewskija (Ws), respectively. (C) Representative images of 4-week-old rosettes. Plants harvested at the end of the photoperiod were cleared of chlorophyll and iodine-stained to visualise starch. Amylose-free mutants (<i>gbss</i>, <i>ptst-1</i>, and <i>ptst-2</i>) produce a brown staining that is distinct from the wild types.</p>", "links"=>[], "tags"=>["amylose synthesis", "starch granules", "cbm", "PROTEIN TARGETING", "gbss", "Normal Amylose Synthesis", "synthase", "elongating amylose polymers", "protein", "starch", "PTST", "Arabidopsi"], "article_id"=>1316882, "categories"=>["Biological Sciences"], "users"=>["David Seung", "Sebastian Soyk", "Mario Coiro", "Benjamin A. Maier", "Simona Eicke", "Samuel C. Zeeman"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1002080.g002", "stats"=>{"downloads"=>1, "page_views"=>21, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_ptst_knockout_mutants_produce_amylose_free_starch_/1316882", "title"=>"<i>ptst</i> knockout mutants produce amylose-free starch.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-02-24 03:02:55"}
  • {"files"=>["https://ndownloader.figshare.com/files/1922741"], "description"=>"<p>(A) GBSS docks onto PTST in the stroma, and the complex binds to starch. (B) PTST dissociates from both GBSS and the starch granule, leaving GBSS on starch to mediate amylose synthesis. (C) PTST returns to the stroma to recruit another GBSS molecule.</p>", "links"=>[], "tags"=>["amylose synthesis", "starch granules", "cbm", "PROTEIN TARGETING", "gbss", "Normal Amylose Synthesis", "synthase", "elongating amylose polymers", "protein", "starch", "PTST", "Arabidopsi"], "article_id"=>1316895, "categories"=>["Biological Sciences"], "users"=>["David Seung", "Sebastian Soyk", "Mario Coiro", "Benjamin A. Maier", "Simona Eicke", "Samuel C. Zeeman"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1002080.g010", "stats"=>{"downloads"=>2, "page_views"=>39, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Proposed_model_of_PTST_mediated_GBSS_localisation_to_starch_/1316895", "title"=>"Proposed model of PTST-mediated GBSS localisation to starch.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-02-24 03:02:55"}

PMC Usage Stats | Further Information

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Relative Metric

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

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