Interactions between the Nse3 and Nse4 Components of the SMC5-6 Complex Identify Evolutionarily Conserved Interactions between MAGE and EID Families
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{"title"=>"Interactions between the Nse3 and Nse4 components of the SMC5-6 complex identify evolutionarily conserved interactions between MAGE and EID families", "type"=>"journal", "authors"=>[{"first_name"=>"Jessica J R", "last_name"=>"Hudson", "scopus_author_id"=>"8968467800"}, {"first_name"=>"Katerina", "last_name"=>"Bednarova", "scopus_author_id"=>"41560989800"}, {"first_name"=>"Lucie", "last_name"=>"Kozakova", "scopus_author_id"=>"41561370700"}, {"first_name"=>"Chunyan", "last_name"=>"Liao", "scopus_author_id"=>"41561649600"}, {"first_name"=>"Marc", "last_name"=>"Guerineau", "scopus_author_id"=>"41561138000"}, {"first_name"=>"Rita", "last_name"=>"Colnaghi", "scopus_author_id"=>"6602314894"}, {"first_name"=>"Susanne", "last_name"=>"Vidot", "scopus_author_id"=>"23091948500"}, {"first_name"=>"Jaromir", "last_name"=>"Marek", "scopus_author_id"=>"7202777122"}, {"first_name"=>"Sreenivas R.", "last_name"=>"Bathula", "scopus_author_id"=>"41561073000"}, {"first_name"=>"Alan R.", "last_name"=>"Lehmann", "scopus_author_id"=>"24561642600"}, {"first_name"=>"Jan", "last_name"=>"Palecek", "scopus_author_id"=>"36875296500"}], "year"=>2011, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"361359031", "sgr"=>"79952232768", "issn"=>"19326203", "pmid"=>"21364888", "scopus"=>"2-s2.0-79952232768", "doi"=>"10.1371/journal.pone.0017270", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)"}, "id"=>"4c508dc5-dd81-3f94-87f3-85e366411f51", "abstract"=>"BACKGROUND: The SMC5-6 protein complex is involved in the cellular response to DNA damage. It is composed of 6-8 polypeptides, of which Nse1, Nse3 and Nse4 form a tight sub-complex. MAGEG1, the mammalian ortholog of Nse3, is the founding member of the MAGE (melanoma-associated antigen) protein family and Nse4 is related to the EID (E1A-like inhibitor of differentiation) family of transcriptional repressors.\\n\\nMETHODOLOGY/PRINCIPAL FINDINGS: Using site-directed mutagenesis, protein-protein interaction analyses and molecular modelling, we have identified a conserved hydrophobic surface on the C-terminal domain of Nse3 that interacts with Nse4 and identified residues in its N-terminal domain that are essential for interaction with Nse1. We show that these interactions are conserved in the human orthologs. Furthermore, interaction of MAGEG1, the mammalian ortholog of Nse3, with NSE4b, one of the mammalian orthologs of Nse4, results in transcriptional co-activation of the nuclear receptor, steroidogenic factor 1 (SF1). In an examination of the evolutionary conservation of the Nse3-Nse4 interactions, we find that several MAGE proteins can interact with at least one of the NSE4/EID proteins.\\n\\nCONCLUSIONS/SIGNIFICANCE: We have found that, despite the evolutionary diversification of the MAGE family, the characteristic hydrophobic surface shared by all MAGE proteins from yeast to humans mediates its binding to NSE4/EID proteins. Our work provides new insights into the interactions, evolution and functions of the enigmatic MAGE proteins.", "link"=>"http://www.mendeley.com/research/interactions-between-nse3-nse4-components-smc56-complex-identify-evolutionarily-conserved-interactio", "reader_count"=>45, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>7, "Researcher"=>14, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>7, "Student > Postgraduate"=>1, "Student > Master"=>5, "Other"=>1, "Student > Bachelor"=>6, "Lecturer > Senior Lecturer"=>1, "Professor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>7, "Researcher"=>14, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>7, "Student > Postgraduate"=>1, "Student > Master"=>5, "Other"=>1, "Student > Bachelor"=>6, "Lecturer > Senior Lecturer"=>1, "Professor"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>11, "Agricultural and Biological Sciences"=>30, "Medicine and Dentistry"=>2, "Neuroscience"=>1, "Chemistry"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Neuroscience"=>{"Neuroscience"=>1}, "Chemistry"=>{"Chemistry"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>30}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>11}}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/795044"], "description"=>"<p>Alignment of the N-terminal (A) (aa 89 to 199 of <i>S.p.</i> Nse3) and C-terminal (B) (aa 211 to 301 of <i>S.p.</i> Nse3) part of MHD domain of Nse3/MAGEG1 subfamily. The Nse3/MAGEG1 orthologs are from <i>S. pombe</i> (<i>S.p.</i>), <i>Aspergillus nidulans</i> (<i>A.n.</i>), <i>Neosartorya fischeri</i> (<i>N.f.</i>), <i>Aspergillus terreus</i> (<i>A.t.</i>), <i>Aspergillus clavatus</i> (<i>A.c.</i>), <i>Neurospora crassa (N.c.)</i>, <i>Magnaporthe grisea</i> (<i>M.g.</i>), <i>Aspergillus oryzae</i> (<i>A.o.</i>), <i>S. cerevisiae</i> (<i>S.c.</i>), <i>Danio rerio</i> (<i>D.r.</i>), <i>Xenopus tropicalis</i> (<i>X.t.</i>), <i>Galus galus</i> (<i>G.g.</i>), <i>Ornithorhynchus anatinus</i> (<i>O.a.</i>), <i>Monodelphis domestica</i> (<i>M.d.</i>), <i>Dasypus novemcinctus</i> (<i>D.n.</i>), <i>Canis lupus familiaris</i> (<i>C.f.</i>), <i>Mus musculus</i> (<i>M.m.</i>), <i>Homo sapiens</i> (<i>H.s.</i>). Secondary structure derived from the 3D-structure model of Nse3 is indicated above the alignment: cyan rectangle, helix; orange arrow, beta-sheet. Most of the conserved residues were mutated (mut) in the <i>S. pombe</i> Nse3 sequence to alanine; m, mutated residue; red rectangles indicate Nse1- and/or Nse4-specific mutants, respectively; Y264 and L265 residues are labelled with asterisk (B). NSE4b-specific residues of MAGEG1 protein are also indicated in red below the MAGEG1 sequence (B). (C) Alignment of C-terminal part of MHD domain of human MAGE proteins. Shading represents amino acid groups conserved across the family: <i>dark green</i>, hydrophobic and aromatic; <i>light green</i>, polar; <i>blue</i>, acidic; <i>pink</i>, basic; all glycine and proline residues are highlighted in <i>yellow</i>.</p>", "links"=>[], "tags"=>["amino", "residues", "mage"], "article_id"=>465406, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Jessica J. R. Hudson", "Katerina Bednarova", "Lucie Kozakova", "Chunyan Liao", "Marc Guerineau", "Rita Colnaghi", "Susanne Vidot", "Jaromir Marek", "Sreenivas R. Bathula", "Alan R. Lehmann", "Jan Palecek"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017270.g002", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Conserved_amino_acid_residues_within_the_MAGE_protein_family_/465406", "title"=>"Conserved amino acid residues within the MAGE protein family.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-25 01:30:06"}
  • {"files"=>["https://ndownloader.figshare.com/files/795778"], "description"=>"<p>(A) Cell-free extracts of mouse testes were immunoprecipitated with either IgG or anti-NSE4b followed by Western blotting with the indicated antibodies. (B) S-tagged MAGEA1 or MAGEG1 were co-expressed with FLAG-tagged NSE4b in HEK293 cells. In lanes 1–6 and 13–18, extracts were precipitated with S-protein, whereas in lanes 7–12 they were immunoprecipitated with anti-FLAG antibody. (C–H) S-tagged Class I MAGE protein A1 (C), and class II MAGE proteins D4b (D), F1 (E), G1 (F), necdin (G) or vector alone (H) were co-transfected with FLAG-tagged NSE4a (N4a) (lanes 1–3) or NSE4b/EID3 (N4b) (lanes 4–6). Extracts were immunoprecipitated with S-protein and Western blotted with S-HRP and anti-FLAG antibody.</p>", "links"=>[], "tags"=>["mage", "proteins", "nse4a"], "article_id"=>466139, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Jessica J. R. Hudson", "Katerina Bednarova", "Lucie Kozakova", "Chunyan Liao", "Marc Guerineau", "Rita Colnaghi", "Susanne Vidot", "Jaromir Marek", "Sreenivas R. Bathula", "Alan R. Lehmann", "Jan Palecek"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017270.g007", "stats"=>{"downloads"=>1, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Binding_of_different_MAGE_proteins_to_NSE4a_and_NSE4b_EID3_proteins_/466139", "title"=>"Binding of different MAGE proteins to NSE4a and NSE4b/EID3 proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-25 01:42:19"}
  • {"files"=>["https://ndownloader.figshare.com/files/397741", "https://ndownloader.figshare.com/files/397835", "https://ndownloader.figshare.com/files/397884"], "description"=>"<div><h3>Background</h3><p>The SMC5-6 protein complex is involved in the cellular response to DNA damage. It is composed of 6–8 polypeptides, of which Nse1, Nse3 and Nse4 form a tight sub-complex. MAGEG1, the mammalian ortholog of Nse3, is the founding member of the MAGE (melanoma-associated antigen) protein family and Nse4 is related to the EID (E1A-like inhibitor of differentiation) family of transcriptional repressors.</p> <h3>Methodology/Principal Findings</h3><p>Using site-directed mutagenesis, protein-protein interaction analyses and molecular modelling, we have identified a conserved hydrophobic surface on the C-terminal domain of Nse3 that interacts with Nse4 and identified residues in its N-terminal domain that are essential for interaction with Nse1. We show that these interactions are conserved in the human orthologs. Furthermore, interaction of MAGEG1, the mammalian ortholog of Nse3, with NSE4b, one of the mammalian orthologs of Nse4, results in transcriptional co-activation of the nuclear receptor, steroidogenic factor 1 (SF1). In an examination of the evolutionary conservation of the Nse3-Nse4 interactions, we find that several MAGE proteins can interact with at least one of the NSE4/EID proteins.</p> <h3>Conclusions/Significance</h3><p>We have found that, despite the evolutionary diversification of the MAGE family, the characteristic hydrophobic surface shared by all MAGE proteins from yeast to humans mediates its binding to NSE4/EID proteins. Our work provides new insights into the interactions, evolution and functions of the enigmatic MAGE proteins.</p> </div>", "links"=>[], "tags"=>["interactions", "nse3", "nse4", "components", "smc5-6", "evolutionarily", "conserved", "mage", "eid"], "article_id"=>138569, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Jessica J. R. Hudson", "Katerina Bednarova", "Lucie Kozakova", "Chunyan Liao", "Marc Guerineau", "Rita Colnaghi", "Susanne Vidot", "Jaromir Marek", "Sreenivas R. Bathula", "Alan R. Lehmann", "Jan Palecek"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0017270.s001", "https://dx.doi.org/10.1371/journal.pone.0017270.s002", "https://dx.doi.org/10.1371/journal.pone.0017270.s003"], "stats"=>{"downloads"=>13, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Interactions_between_the_Nse3_and_Nse4_Components_of_the_SMC5_6_Complex_Identify_Evolutionarily_Conserved_Interactions_between_MAGE_and_EID_Families/138569", "title"=>"Interactions between the Nse3 and Nse4 Components of the SMC5-6 Complex Identify Evolutionarily Conserved Interactions between MAGE and EID Families", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2011-02-25 02:22:49"}
  • {"files"=>["https://ndownloader.figshare.com/files/794939"], "description"=>"<p>The indicated His-S-tagged fragments of Nse3 (A, B, C) or Nse1 (D, E) were bound to S-protein agarose-beads and then incubated with <i>in vitro</i> translated Nse1 (A) or Nse4 (B–E). The reaction mixtures were analysed by SDS–12% PAGE gel electrophoresis. The amount of His-S-tagged protein was analysed by immunoblotting with anti-His antibody and the <i>in vitro</i> translated proteins were measured by autoradiography. I, input (5% of total); U, unbound (5%); B, bound (40%). Control, no His-S-tagged protein present. (F) Cartoon of interactions based on panels A–E and our previous work <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017270#pone.0017270-Palecek1\" target=\"_blank\">[13]</a>.</p>", "links"=>[], "tags"=>["nse3"], "article_id"=>465306, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Jessica J. R. Hudson", "Katerina Bednarova", "Lucie Kozakova", "Chunyan Liao", "Marc Guerineau", "Rita Colnaghi", "Susanne Vidot", "Jaromir Marek", "Sreenivas R. Bathula", "Alan R. Lehmann", "Jan Palecek"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017270.g001", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Interactions_between_Nse1_Nse3_and_Nse4_/465306", "title"=>"Interactions between Nse1, Nse3 and Nse4.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-25 01:28:26"}
  • {"files"=>["https://ndownloader.figshare.com/files/796005"], "description"=>"<p>(A) Data from co-immunoprecipitation experiments were analysed visually; + and − signify whether or not an interaction was detected. (B) Cartoon of MAGE interactions showing evolutionary diversification of hypothetical MAGE complexes.</p>", "links"=>[], "tags"=>["mage"], "article_id"=>466370, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Jessica J. R. Hudson", "Katerina Bednarova", "Lucie Kozakova", "Chunyan Liao", "Marc Guerineau", "Rita Colnaghi", "Susanne Vidot", "Jaromir Marek", "Sreenivas R. Bathula", "Alan R. Lehmann", "Jan Palecek"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017270.g009", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Interactions_of_MAGE_proteins_/466370", "title"=>"Interactions of MAGE proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-25 01:46:10"}
  • {"files"=>["https://ndownloader.figshare.com/files/796141"], "description"=>"<p>MAGE and EID proteins used in this study.</p>", "links"=>[], "tags"=>["eid", "proteins"], "article_id"=>466507, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Jessica J. R. Hudson", "Katerina Bednarova", "Lucie Kozakova", "Chunyan Liao", "Marc Guerineau", "Rita Colnaghi", "Susanne Vidot", "Jaromir Marek", "Sreenivas R. Bathula", "Alan R. Lehmann", "Jan Palecek"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017270.t002", "stats"=>{"downloads"=>1, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MAGE_and_EID_proteins_used_in_this_study_/466507", "title"=>"MAGE and EID proteins used in this study.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2011-02-25 01:48:27"}
  • {"files"=>["https://ndownloader.figshare.com/files/795902"], "description"=>"<p>(A) Alignments of the five members of the human EID family. Hatched and grey boxes indicate kleisin motifs and regions of homology between EID1 and 2, respectively. (B–G) S-tagged Class I MAGE protein A1 (B), and class II MAGE proteins D4b (C), F1 (D), G1 (E), necdin (F) or vector alone (G) were co-transfected with FLAG-tagged EID1 (E1) (lanes 1–3), EID2 (E2) (lanes 4–6) or EID2b (E2b) (lanes 7–9) into HEK293. Extracts were immunoprecipitated with S-protein and Western blotted with S-HRP and anti-FLAG antibody.</p>", "links"=>[], "tags"=>["mage", "proteins"], "article_id"=>466269, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Jessica J. R. Hudson", "Katerina Bednarova", "Lucie Kozakova", "Chunyan Liao", "Marc Guerineau", "Rita Colnaghi", "Susanne Vidot", "Jaromir Marek", "Sreenivas R. Bathula", "Alan R. Lehmann", "Jan Palecek"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017270.g008", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Interactions_of_MAGE_proteins_with_EID1_2_and_2b_/466269", "title"=>"Interactions of MAGE proteins with EID1, 2 and 2b.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-25 01:44:29"}
  • {"files"=>["https://ndownloader.figshare.com/files/795623"], "description"=>"<p>(A) Effect of transfected FLAG-NSE4b and S-tagged MAGEG1 on transcriptional activation by SF-1 in HEK293 cells. “2×” indicates twice the concentration of MAGEG1 plasmid used in transfections. (B) Effects of FLAG-tagged EID1 or NSE4b on transcriptional activation by different MAGE proteins. The reporter activity in each column is normalised to the activity with nuclear receptor but with neither MAGE nor EID (column 2). Results show mean ± SEM of 3–5 independent transfections.</p>", "links"=>[], "tags"=>["mage", "eid", "proteins", "transcription", "activation"], "article_id"=>465979, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Jessica J. R. Hudson", "Katerina Bednarova", "Lucie Kozakova", "Chunyan Liao", "Marc Guerineau", "Rita Colnaghi", "Susanne Vidot", "Jaromir Marek", "Sreenivas R. Bathula", "Alan R. Lehmann", "Jan Palecek"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017270.g006", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Interplay_between_MAGE_and_EID_proteins_in_transcription_activation_system_/465979", "title"=>"Interplay between MAGE and EID proteins in transcription activation system.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-25 01:39:39"}
  • {"files"=>["https://ndownloader.figshare.com/files/795522"], "description"=>"<p>(A) Yeast-2-hybrid analysis of the interaction between the indicated mutants of MAGEG1 (aa 55 to 292) and NSE4b (aa 1 to 333) or NSE1 (aa 1 to 266). Interactions result in growth on -Leu,-Trp, -His plates +2 mM AT. Control, no MAGEG1. (B) Co-immunoprecipitation from HEK293 cells co-transfected with S-tagged wild-type and/or mutant MAGEG1 and with FLAG-tagged NSE4b. Lysates were immunoprecipitated with protein-S and immunoblotted with either S-HRP (top) or anti-FLAG (bottom). (C) Structure of the C-terminal domain of MAGEG1 (aa 175 to 270) <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017270#pone.0017270-Doyle1\" target=\"_blank\">[14]</a> with the NSE4b-interacting residues indicated in red.</p>", "links"=>[], "tags"=>["mageg1", "binds", "nse4b", "conserved", "hydrophobic"], "article_id"=>465884, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Jessica J. R. Hudson", "Katerina Bednarova", "Lucie Kozakova", "Chunyan Liao", "Marc Guerineau", "Rita Colnaghi", "Susanne Vidot", "Jaromir Marek", "Sreenivas R. Bathula", "Alan R. Lehmann", "Jan Palecek"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017270.g005", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Human_MAGEG1_binds_NSE4b_through_conserved_hydrophobic_surface_/465884", "title"=>"Human MAGEG1 binds NSE4b through conserved hydrophobic surface.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-25 01:38:04"}
  • {"files"=>["https://ndownloader.figshare.com/files/795253"], "description"=>"<p>Homology modelling was used to generate the predicted <i>S. pombe</i> Nse3 MHD structure. Ribbon representation (left panels) of the predicted Nse3 3D structure model with helices (cyan) and beta-sheets (orange) indicated as in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0017270#pone-0017270-g002\" target=\"_blank\">Figure 2</a>. Right panels represent surface views. (A) The residues that, when mutated, lost their ability to interact with both Nse1 and Nse4 interacting partners are buried inside (indicated in dark blue). (B) Sequence and structure of Nse3 (aa 211 to 300) showing which mutations inhibit interaction with Nse4 (red). Top view of the structure shown in panel (A). (C) Residues in the N-terminal domain (aa 92 to 187) that, when mutated, reduce the interaction with Nse1 are indicated in green. The small cartoons at the left of the panels are miniatures of the full-length structure. The parts indicated in red are expanded in the main panels.</p>", "links"=>[], "tags"=>["residues", "nse3", "modelled", "structures", "magea4", "mageg1"], "article_id"=>465610, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Jessica J. R. Hudson", "Katerina Bednarova", "Lucie Kozakova", "Chunyan Liao", "Marc Guerineau", "Rita Colnaghi", "Susanne Vidot", "Jaromir Marek", "Sreenivas R. Bathula", "Alan R. Lehmann", "Jan Palecek"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017270.g003", "stats"=>{"downloads"=>2, "page_views"=>17, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Interacting_residues_of_Nse3_modelled_on_the_crystal_structures_of_MAGEA4_PDB_2WA0_and_MAGEG1_PDB_3NW0_/465610", "title"=>"Interacting residues of Nse3 modelled on the crystal structures of MAGEA4 (PDB 2WA0) and MAGEG1 (PDB 3NW0).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-25 01:33:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/795390"], "description"=>"<p>(A) Yeast-2-hybrid plasmids expressing Nse3, either wild-type or mutated as indicated, fused to the Gal4 DNA-binding domain, and wild-type Nse4 fused to the Gal4 activation domain, were co-expressed with either empty vector (v) or Nse1 (1) in yeast cells, which were subsequently plated in the indicated media and grown at 30°C. AT, 3-aminotriazole. (B) Spot tests of Nse3 wild-type cells (wt:YL), Y264A/L265A (AA), L265A (YA) and Y264A (AL) plated under the indicated conditions.</p>", "links"=>[], "tags"=>["nse1", "nse3"], "article_id"=>465752, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Jessica J. R. Hudson", "Katerina Bednarova", "Lucie Kozakova", "Chunyan Liao", "Marc Guerineau", "Rita Colnaghi", "Susanne Vidot", "Jaromir Marek", "Sreenivas R. Bathula", "Alan R. Lehmann", "Jan Palecek"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017270.g004", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effect_of_Nse1_on_the_interaction_between_S_pombe_Nse3_and_Nse4_/465752", "title"=>"Effect of Nse1 on the interaction between <i>S.pombe</i> Nse3 and Nse4.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-02-25 01:35:52"}
  • {"files"=>["https://ndownloader.figshare.com/files/796101"], "description"=>"<p>Combinations of the indicated mutant Nse3 proteins with Nse1 or Nse4 were analysed in the Y2H system. + and − signify whether or not an interaction was detected. Some of the mutations were introduced into the <i>S. pombe</i> genome and sensitivity to MMS and HU was analysed. WT indicates no sensitivity.</p>", "links"=>[], "tags"=>["nse3", "mutants", "nse1"], "article_id"=>466463, "categories"=>["Molecular Biology", "Biochemistry", "Cell Biology"], "users"=>["Jessica J. R. Hudson", "Katerina Bednarova", "Lucie Kozakova", "Chunyan Liao", "Marc Guerineau", "Rita Colnaghi", "Susanne Vidot", "Jaromir Marek", "Sreenivas R. Bathula", "Alan R. Lehmann", "Jan Palecek"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0017270.t001", "stats"=>{"downloads"=>2, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Interaction_of_S_pombe_Nse3_mutants_with_Nse1_and_Nse4_/466463", "title"=>"Interaction of <i>S.pombe</i> Nse3 mutants with Nse1 and Nse4.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2011-02-25 01:47:43"}

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  • {"unique-ip"=>"7", "full-text"=>"8", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
  • {"unique-ip"=>"9", "full-text"=>"8", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"4"}
  • {"unique-ip"=>"9", "full-text"=>"10", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"5"}

Relative Metric

{"start_date"=>"2011-01-01T00:00:00Z", "end_date"=>"2011-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences/Evolutionary biology", "average_usage"=>[330, 550, 674, 772, 863, 958, 1034, 1108, 1180, 1252, 1324, 1393, 1460, 1526, 1597, 1664, 1725, 1783, 1848, 1901, 1974, 2049, 2125, 2185, 2260, 2326, 2383, 2440, 2511, 2581, 2647, 2711, 2760, 2815, 2874, 2928, 3008]}, {"subject_area"=>"/Biology and life sciences/Mycology", "average_usage"=>[330, 564, 723, 851, 962, 1064, 1145, 1232, 1331, 1386, 1446, 1540, 1589, 1706, 1779, 1864, 1945, 2015, 2066, 2138, 2184, 2251, 2303, 2352, 2438, 2485, 2576, 2685, 2798, 2848, 2905, 2960, 3040, 3125, 3181, 3258, 3319]}, {"subject_area"=>"/Biology and life sciences/Organisms", "average_usage"=>[316, 571, 699, 812, 915, 1008, 1095, 1180, 1255, 1319, 1393, 1461, 1528, 1595, 1662, 1729, 1802, 1868, 1937, 1997, 2062, 2130, 2192, 2254, 2324, 2386, 2450, 2510, 2579, 2642, 2716, 2778, 2842, 2908, 2979, 3042, 3095]}, {"subject_area"=>"/Physical sciences/Physics", "average_usage"=>[296, 505, 611, 719, 815, 886, 966, 1040, 1111, 1173, 1227, 1283, 1342, 1400, 1459, 1516, 1572, 1635, 1696, 1752, 1804, 1861, 1919, 1976, 2035, 2093, 2142, 2198, 2256, 2309, 2373, 2433, 2486, 2540, 2594, 2652, 2698]}]}
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