A Global Census of Fission Yeast Deubiquitinating Enzyme Localization and Interaction Networks Reveals Distinct Compartmentalization Profiles and Overlapping Functions in Endocytosis and Polarity
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{"title"=>"A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity", "type"=>"journal", "authors"=>[{"first_name"=>"Ilektra", "last_name"=>"Kouranti", "scopus_author_id"=>"6505967975"}, {"first_name"=>"Janel R.", "last_name"=>"Mclean", "scopus_author_id"=>"16643299900"}, {"first_name"=>"Anna", "last_name"=>"Feoktistova", "scopus_author_id"=>"6701608240"}, {"first_name"=>"Ping", "last_name"=>"Liang", "scopus_author_id"=>"37031471400"}, {"first_name"=>"Alyssa E.", "last_name"=>"Johnson", "scopus_author_id"=>"35080606300"}, {"first_name"=>"Rachel H.", "last_name"=>"Roberts-Galbraith", "scopus_author_id"=>"24068868600"}, {"first_name"=>"Kathleen L.", "last_name"=>"Gould", "scopus_author_id"=>"35310146300"}], "year"=>2010, "source"=>"PLoS Biology", "identifiers"=>{"issn"=>"15449173", "scopus"=>"2-s2.0-77957893483", "sgr"=>"77957893483", "pui"=>"359761824", "isbn"=>"1544-9173", "pmid"=>"20838651", "doi"=>"10.1371/journal.pbio.1000471"}, "id"=>"539f7a71-6af5-3edf-b5c1-fb346093fd7c", "abstract"=>"Proteomic, localization, and enzymatic activity screens in fission yeast reveal how deubiquitinating enzyme localization and function are tuned.", "link"=>"http://www.mendeley.com/research/global-census-fission-yeast-deubiquitinating-enzyme-localization-interaction-networks-reveals-distin", "reader_count"=>75, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>4, "Librarian"=>1, "Student > Doctoral Student"=>2, "Researcher"=>25, "Student > Ph. D. Student"=>27, "Student > Postgraduate"=>2, "Student > Master"=>6, "Student > Bachelor"=>4, "Lecturer"=>1, "Professor"=>3}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>4, "Librarian"=>1, "Student > Doctoral Student"=>2, "Researcher"=>25, "Student > Ph. D. Student"=>27, "Student > Postgraduate"=>2, "Student > Master"=>6, "Student > Bachelor"=>4, "Lecturer"=>1, "Professor"=>3}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>17, "Agricultural and Biological Sciences"=>54, "Arts and Humanities"=>1, "Chemistry"=>1, "Social Sciences"=>2}, "reader_count_by_subdiscipline"=>{"Chemistry"=>{"Chemistry"=>1}, "Social Sciences"=>{"Social Sciences"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>54}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>17}, "Arts and Humanities"=>{"Arts and Humanities"=>1}}, "reader_count_by_country"=>{"Belgium"=>1, "United States"=>1, "United Kingdom"=>2, "Australia"=>1}, "group_count"=>2}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/831696"], "description"=>"<p>(A) Equivalent amounts of cells expressing C-terminally TAP-tagged DUBs were lysed under native conditions, the TAP-tagged proteins were immunoprecipitated, and detected by immunoblotting. Asterisks indicate the fainter bands corresponding to Ubp9 and Ubp11. The expected molecular weight (MW, in kilodaltons) of the TAP-tagged DUB is provided below each lane. (B) DUB activities of the DUB-TAP immunoprecipitates were analyzed using Ub-AMC as a substrate. Data are mean ± SEM of two independent experiments. (C) DUB activities of Sst2-TAP and Ubp14-TAP immunoprecipitates were analyzed using K63- and/or K48-linked ubiquitin chains as substrates. (D and E) Equivalent amounts of cells expressing low levels of N-terminally TAP-tagged DUBs from the <i>nmt81</i> promoter were lysed under native conditions, and the TAP-tagged proteins were detected by (D) IP and immunoblotting or (E) silver staining. Ubp7 is indicated by an asterisk. (F) DUB activities of N-terminally tagged proteins were assayed using Ub-AMC as a substrate. Data are mean ± SEM of two independent experiments.</p>", "links"=>[], "tags"=>["biochemistry/cell signaling and trafficking structures", "cell biology"], "article_id"=>502061, "categories"=>["Cell Biology", "Biochemistry"], "users"=>["Ilektra Kouranti", "Janel R. McLean", "Anna Feoktistova", "Ping Liang", "Alyssa E. Johnson", "Rachel H. Roberts-Galbraith", "Kathleen L. Gould"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1000471.g004", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Enzymatic_activity_of_S_pombe_DUBs_/502061", "title"=>"Enzymatic activity of <i>S. pombe</i> DUBs.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-09-07 00:34:21"}
  • {"files"=>["https://ndownloader.figshare.com/files/832356"], "description"=>"<p>(A) Ten-fold dilution series of cells grown to mid-log phase were spotted on YE agar and grown at the indicated temperatures for 3 d. (B) Cells of the indicated genotypes grown to early log phase at 32°C and then shifted to 36°C for 3 h were labeled with FM4-64 for 6 min and imaged by confocal microscopy. The arrow indicates polarity defects of <i>ubp4Δ1 ubp5Δ ubp9Δ ubp15Δ sst2Δ</i> cells. Bar: 5 µm. (C) Anti-ubiquitin immunoblot and Coomassie staining of wild-type or <i>ubp4Δ1 ubp5Δ ubp9Δ ubp15Δ sst2Δ</i> cell lysates produced under fully denaturing conditions. WB: Western Blot. (D) Anti-ubiquitin and streptavidin immunoblots of Can1-HBH and Pub1-HBH purified from wild-type or <i>ubp4Δ1 ubp5Δ ubp9Δ ubp15Δ sst2Δ</i> cells under fully denaturing conditions.</p>", "links"=>[], "tags"=>["functions", "sst2", "polarity"], "article_id"=>502715, "categories"=>["Cell Biology", "Biochemistry"], "users"=>["Ilektra Kouranti", "Janel R. McLean", "Anna Feoktistova", "Ping Liang", "Alyssa E. Johnson", "Rachel H. Roberts-Galbraith", "Kathleen L. Gould"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1000471.g009", "stats"=>{"downloads"=>1, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Redundant_functions_of_Ubp4_Ubp5_Ubp9_Ubp15_and_Sst2_in_cell_polarity_and_endocytosis_/502715", "title"=>"Redundant functions of Ubp4, Ubp5, Ubp9, Ubp15, and Sst2 in cell polarity and endocytosis.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-09-07 00:45:15"}
  • {"files"=>["https://ndownloader.figshare.com/files/831566"], "description"=>"<p>(A–G) Strains expressing the indicated tagged proteins or stained with MitoTracker Red were grown to mid-log phase at 25°C and imaged by confocal microscopy. Images from the left and center panels are merged in the right panels. Co-localizing and adjacent endosomal structures are indicated with arrows and arrowheads, respectively. All proteins were endogenously tagged at their C-termini with GFP or mCherry except GFP-Ubp1 and GFP-Ubp11, which were expressed at low levels under the control of the <i>nmt81</i> promoter. Bar: 5 µm.</p>", "links"=>[], "tags"=>["dubs", "cellular"], "article_id"=>501932, "categories"=>["Cell Biology", "Biochemistry"], "users"=>["Ilektra Kouranti", "Janel R. McLean", "Anna Feoktistova", "Ping Liang", "Alyssa E. Johnson", "Rachel H. Roberts-Galbraith", "Kathleen L. Gould"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1000471.g003", "stats"=>{"downloads"=>1, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Localization_of_DUBs_to_different_cellular_compartments_/501932", "title"=>"Localization of DUBs to different cellular compartments.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-09-07 00:32:12"}
  • {"files"=>["https://ndownloader.figshare.com/files/832240"], "description"=>"<p>(A) Ubp4-TAP, (B) Ubp5-TAP, and (C) Ubp9-TAP were immunoprecipitated from either wild-type or the indicated <i>sfp47, ftp105, bun107,</i> and/or <i>bun62</i> deletion strains. Immunoprecipitates were assayed for deubiquitinating activity using Ub-AMC as a substrate. Alanine substitutions of the catalytic cysteine residues were also created in the <i>ubp4, ubp5,</i> and <i>ubp9</i> genes, and each was tagged at its endogenous locus with TAP so that these were the only versions of these DUBs produced by the genome. AMC fluorescence from control immunoprecipitates (enzymatically inactive DUBs) was subtracted, and the data were normalized according to protein quantities. (D) Working model for Ubp9 regulation by Bun107 and Bun62.</p>", "links"=>[], "tags"=>["activities", "ubp9", "regulated"], "article_id"=>502601, "categories"=>["Cell Biology", "Biochemistry"], "users"=>["Ilektra Kouranti", "Janel R. McLean", "Anna Feoktistova", "Ping Liang", "Alyssa E. Johnson", "Rachel H. Roberts-Galbraith", "Kathleen L. Gould"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1000471.g008", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_activities_of_Ubp4_Ubp5_and_Ubp9_are_regulated_by_their_partners_/502601", "title"=>"The activities of Ubp4, Ubp5, and Ubp9 are regulated by their partners.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-09-07 00:43:21"}
  • {"files"=>["https://ndownloader.figshare.com/files/832457"], "description"=>"<p><b><sup>a</sup></b>Domains are as defined in <a href=\"http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1000471#pbio-1000471-g001\" target=\"_blank\">Figure 1</a> legend.</p><p><b><sup>b</sup></b>C, cytoplasmic; CS, cytoplasmic structure; N, nuclear; NE, nuclear envelope; No, nucleolus; M, mitochondria.</p><p>NA, not applicable.</p>", "links"=>[], "tags"=>["biochemistry/cell signaling and trafficking structures", "cell biology"], "article_id"=>502823, "categories"=>["Cell Biology", "Biochemistry"], "users"=>["Ilektra Kouranti", "Janel R. McLean", "Anna Feoktistova", "Ping Liang", "Alyssa E. Johnson", "Rachel H. Roberts-Galbraith", "Kathleen L. Gould"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1000471.t001", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Summary_of_the_domain_architecture_localization_and_interaction_profile_of_the_S_pombe_DUBs_/502823", "title"=>"Summary of the domain architecture, localization, and interaction profile of the <i>S. pombe</i> DUBs.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2010-09-07 00:47:03"}
  • {"files"=>["https://ndownloader.figshare.com/files/414279", "https://ndownloader.figshare.com/files/414282", "https://ndownloader.figshare.com/files/414286", "https://ndownloader.figshare.com/files/414290", "https://ndownloader.figshare.com/files/414293", "https://ndownloader.figshare.com/files/414297", "https://ndownloader.figshare.com/files/414300", "https://ndownloader.figshare.com/files/414303", "https://ndownloader.figshare.com/files/414305", "https://ndownloader.figshare.com/files/414312", "https://ndownloader.figshare.com/files/414318", "https://ndownloader.figshare.com/files/414320", "https://ndownloader.figshare.com/files/414326", "https://ndownloader.figshare.com/files/414332", "https://ndownloader.figshare.com/files/414335", "https://ndownloader.figshare.com/files/414339", "https://ndownloader.figshare.com/files/414347", "https://ndownloader.figshare.com/files/414352", "https://ndownloader.figshare.com/files/414358", "https://ndownloader.figshare.com/files/414368", "https://ndownloader.figshare.com/files/414373"], "description"=>"<div><p>Ubiquitination and deubiquitination are reciprocal processes that tune protein stability, function, and/or localization. The removal of ubiquitin and remodeling of ubiquitin chains is catalyzed by deubiquitinating enzymes (DUBs), which are cysteine proteases or metalloproteases. Although ubiquitination has been extensively studied for decades, the complexity of cellular roles for deubiquitinating enzymes has only recently been explored, and there are still several gaps in our understanding of when, where, and how these enzymes function to modulate the fate of polypeptides. To address these questions we performed a systematic analysis of the 20 <em>Schizosaccharomyces pombe</em> DUBs using confocal microscopy, proteomics, and enzymatic activity assays. Our results reveal that <em>S. pombe</em> DUBs are present in almost all cell compartments, and the majority are part of stable protein complexes essential for their function. Interestingly, DUB partners identified by our study include the homolog of a putative tumor suppressor gene not previously linked to the ubiquitin pathway, and two conserved tryptophan-aspartate (WD) repeat proteins that regulate Ubp9, a DUB that we show participates in endocytosis, actin dynamics, and cell polarity. In order to understand how DUB activity affects these processes we constructed multiple DUB mutants and find that a quintuple deletion of <em>ubp4 ubp5 ubp9 ubp15 sst2/amsh</em> displays severe growth, polarity, and endocytosis defects. This mutant allowed the identification of two common substrates for five cytoplasmic DUBs. Through these studies, a common regulatory theme emerged in which DUB localization and/or activity is modulated by interacting partners. Despite apparently distinct cytoplasmic localization patterns, several DUBs cooperate in regulating endocytosis and cell polarity. These studies provide a framework for dissecting DUB signaling pathways in <em>S. pombe</em> and may shed light on DUB functions in metazoans.</p></div>", "links"=>[], "tags"=>["census", "fission", "yeast", "deubiquitinating", "enzyme", "localization", "networks", "reveals", "compartmentalization", "profiles", "overlapping", "functions", "endocytosis", "polarity"], "article_id"=>141807, "categories"=>["Cell Biology", "Biochemistry"], "users"=>["Ilektra Kouranti", "Janel R. McLean", "Anna Feoktistova", "Ping Liang", "Alyssa E. Johnson", "Rachel H. Roberts-Galbraith", "Kathleen L. Gould"], "doi"=>["https://dx.doi.org/10.1371/journal.pbio.1000471.s001", "https://dx.doi.org/10.1371/journal.pbio.1000471.s002", "https://dx.doi.org/10.1371/journal.pbio.1000471.s003", "https://dx.doi.org/10.1371/journal.pbio.1000471.s004", "https://dx.doi.org/10.1371/journal.pbio.1000471.s005", "https://dx.doi.org/10.1371/journal.pbio.1000471.s006", "https://dx.doi.org/10.1371/journal.pbio.1000471.s007", "https://dx.doi.org/10.1371/journal.pbio.1000471.s008", "https://dx.doi.org/10.1371/journal.pbio.1000471.s009", "https://dx.doi.org/10.1371/journal.pbio.1000471.s010", "https://dx.doi.org/10.1371/journal.pbio.1000471.s011", "https://dx.doi.org/10.1371/journal.pbio.1000471.s012", "https://dx.doi.org/10.1371/journal.pbio.1000471.s013", "https://dx.doi.org/10.1371/journal.pbio.1000471.s014", "https://dx.doi.org/10.1371/journal.pbio.1000471.s015", "https://dx.doi.org/10.1371/journal.pbio.1000471.s016", "https://dx.doi.org/10.1371/journal.pbio.1000471.s017", "https://dx.doi.org/10.1371/journal.pbio.1000471.s018", "https://dx.doi.org/10.1371/journal.pbio.1000471.s019", "https://dx.doi.org/10.1371/journal.pbio.1000471.s020", "https://dx.doi.org/10.1371/journal.pbio.1000471.s021"], "stats"=>{"downloads"=>10, "page_views"=>23, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/A_Global_Census_of_Fission_Yeast_Deubiquitinating_Enzyme_Localization_and_Interaction_Networks_Reveals_Distinct_Compartmentalization_Profiles_and_Overlapping_Functions_in_Endocytosis_and_Polarity/141807", "title"=>"A Global Census of Fission Yeast Deubiquitinating Enzyme Localization and Interaction Networks Reveals Distinct Compartmentalization Profiles and Overlapping Functions in Endocytosis and Polarity", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2010-09-07 00:30:07"}
  • {"files"=>["https://ndownloader.figshare.com/files/832115"], "description"=>"<p>(A–C) Live cell imaging of the indicated endogenously tagged proteins in the indicated genetic backgrounds. Bar: 5 µm for all panels.</p>", "links"=>[], "tags"=>["ubp9", "depends"], "article_id"=>502478, "categories"=>["Cell Biology", "Biochemistry"], "users"=>["Ilektra Kouranti", "Janel R. McLean", "Anna Feoktistova", "Ping Liang", "Alyssa E. Johnson", "Rachel H. Roberts-Galbraith", "Kathleen L. Gould"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1000471.g007", "stats"=>{"downloads"=>1, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Localization_of_Ubp4_Ubp5_and_Ubp9_depends_on_their_partners_/502478", "title"=>"Localization of Ubp4, Ubp5, and Ubp9 depends on their partners.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-09-07 00:41:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/831801"], "description"=>"<p>Diagram of proteins identified by TAP/LC-MS/MS of Rpn11, Uch2, and Ubp6 and their interactions as curated in BioGRID (see <a href=\"http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1000471#s4\" target=\"_blank\">Materials and Methods</a> for details). DUB nodes are red, proteasome subunits and associated proteins are yellow (top MS hits in terms of TSC and validated by reciprocal Rpn11 and Uch2 TAPs), and all other protein nodes are blue. BioGRID interaction edge lines are shown in light orange, and TAP/LC-MS/MS edges are in black. TAP/LC-MS/MS edge line widths are coded according to TSC (thicker lines denote more spectral counts). The border color of the proteasomal nodes is as denoted in the key.</p>", "links"=>[], "tags"=>["diagram", "interactions", "proteasomal"], "article_id"=>502169, "categories"=>["Cell Biology", "Biochemistry"], "users"=>["Ilektra Kouranti", "Janel R. McLean", "Anna Feoktistova", "Ping Liang", "Alyssa E. Johnson", "Rachel H. Roberts-Galbraith", "Kathleen L. Gould"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1000471.g005", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Network_diagram_of_physical_interactions_of_the_proteasomal_DUBs_/502169", "title"=>"Network diagram of physical interactions of the proteasomal DUBs.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-09-07 00:36:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/831951"], "description"=>"<p>Diagrams were generated as described in <a href=\"http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1000471#s4\" target=\"_blank\">Materials and Methods</a>. DUB nodes are red, validated interactors (top MS hits in terms of TSC and confirmed by co-IP and/or reciprocal TAP) are yellow, and all other nodes are blue. Edges are colored and coded as in <a href=\"http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1000471#pbio-1000471-g005\" target=\"_blank\">Figure 5</a>.</p>", "links"=>[], "tags"=>["diagrams", "interactions", "dub", "complexes"], "article_id"=>502309, "categories"=>["Cell Biology", "Biochemistry"], "users"=>["Ilektra Kouranti", "Janel R. McLean", "Anna Feoktistova", "Ping Liang", "Alyssa E. Johnson", "Rachel H. Roberts-Galbraith", "Kathleen L. Gould"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1000471.g006", "stats"=>{"downloads"=>1, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Network_diagrams_of_physical_interactions_of_new_DUB_protein_complexes_identified_by_TAP_LC_MS_MS_/502309", "title"=>"Network diagrams of physical interactions of new DUB protein complexes identified by TAP/LC-MS/MS.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-09-07 00:38:29"}
  • {"files"=>["https://ndownloader.figshare.com/files/831281"], "description"=>"<p><i>S. pombe</i> DUBs belong to four subfamilies (USP, UCH, OTU, and JAMM). USP, UCH, and OTU domain DUBs are cysteine proteases, JAMM domain DUBs are metalloproteases. We retrieved domain architectures for each DUB using the SMART and Pfam databases. The following domains were found: DUSP (domain in ubiquitin-specific proteases), MATH (meprin and TRAF homology), UBL (ubiquitin-like), ZnF (ubiquitin carboxyl-terminal hydrolase-like zinc finger), UBA (Ubiquitin-associated). RPT, internal repeats.</p>", "links"=>[], "tags"=>["biochemistry/cell signaling and trafficking structures", "cell biology"], "article_id"=>501644, "categories"=>["Cell Biology", "Biochemistry"], "users"=>["Ilektra Kouranti", "Janel R. McLean", "Anna Feoktistova", "Ping Liang", "Alyssa E. Johnson", "Rachel H. Roberts-Galbraith", "Kathleen L. Gould"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1000471.g001", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Inventory_and_domain_architecture_of_S_pombe_DUBs_/501644", "title"=>"Inventory and domain architecture of <i>S. pombe</i> DUBs.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-09-07 00:27:24"}
  • {"files"=>["https://ndownloader.figshare.com/files/831425"], "description"=>"<p>Cells producing DUBs endogenously tagged at their C-termini with GFP and/or mildly overexpressing N-terminal GFP fusions from the weak <i>nmt81</i> promoter (indicated by GFP before their name) were grown to mid-log phase at 25°C and imaged by confocal microscopy. <i>S. pombe</i> DUBs localize (A) exclusively to the nucleus, (B) to the nuclear envelope, (C) both to the nucleus and cytoplasm, (D) both to the nucleus and specific cytoplasmic structures, (E) exclusively to specific cytoplasmic structures (arrows denote localization to septa), or (F) diffusely in the cytoplasm. Bar: 5 µm for all panels.</p>", "links"=>[], "tags"=>["biochemistry/cell signaling and trafficking structures", "cell biology"], "article_id"=>501791, "categories"=>["Cell Biology", "Biochemistry"], "users"=>["Ilektra Kouranti", "Janel R. McLean", "Anna Feoktistova", "Ping Liang", "Alyssa E. Johnson", "Rachel H. Roberts-Galbraith", "Kathleen L. Gould"], "doi"=>"https://dx.doi.org/10.1371/journal.pbio.1000471.g002", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Localization_of_S_pombe_DUBs_/501791", "title"=>"Localization of <i>S. pombe</i> DUBs.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2010-09-07 00:29:51"}

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

Relative Metric

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