Novel Antimicrobial Peptides EeCentrocins 1, 2 and EeStrongylocin 2 from the Edible Sea Urchin Echinus esculentus Have 6-Br-Trp Post-Translational Modifications
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{"title"=>"Novel antimicrobial peptides EeCentrocins 1, 2 and EeStrongylocin 2 from the Edible sea urchin Echinus esculentus have 6-br-trp post-translational modifications", "type"=>"journal", "authors"=>[{"first_name"=>"Runar Gjerp", "last_name"=>"Solstad", "scopus_author_id"=>"57188651662"}, {"first_name"=>"Chun", "last_name"=>"Li", "scopus_author_id"=>"24512283100"}, {"first_name"=>"Johan", "last_name"=>"Isaksson", "scopus_author_id"=>"55897189900"}, {"first_name"=>"Jostein", "last_name"=>"Johansen", "scopus_author_id"=>"57193118291"}, {"first_name"=>"Johan", "last_name"=>"Svenson", "scopus_author_id"=>"7004264908"}, {"first_name"=>"Klara", "last_name"=>"Stensvåg", "scopus_author_id"=>"6506903254"}, {"first_name"=>"Tor", "last_name"=>"Haug", "scopus_author_id"=>"7006022876"}], "year"=>2016, "source"=>"PLoS ONE", "identifiers"=>{"scopus"=>"2-s2.0-84962109454", "sgr"=>"84962109454", "pui"=>"609303965", "issn"=>"19326203", "isbn"=>"1932-6203", "pmid"=>"27007817", "doi"=>"10.1371/journal.pone.0151820"}, "id"=>"daecaf9f-37d5-350c-bbc5-e6a71a6d9a02", "abstract"=>"The global problem of microbial resistance to antibiotics has resulted\\nin an urgent need to develop new antimicrobial agents. Natural\\nantimicrobial peptides are considered promising candidates for drug\\ndevelopment. Echinoderms, which rely on innate immunity factors in the\\ndefence against harmful microorganisms, are sources of novel\\nantimicrobial peptides. This study aimed to isolate and characterise\\nantimicrobial peptides from the Edible sea urchin Echinus esculentus.\\nUsing bioassay-guided purification and cDNA cloning, three antimicrobial\\npeptides were characterised from the haemocytes of the sea urchin; two\\nheterodimeric peptides and a cysteine-rich peptide. The peptides were\\nnamed EeCentrocin 1 and 2 and EeStrongylocin 2, respectively, due to\\ntheir apparent homology to the published centrocins and strongylocins\\nisolated from the green sea urchin Strongylocentrotus droebachiensis.\\nThe two centrocin-like peptides EeCentrocin 1 and 2 are intramolecularly\\nconnected via a disulphide bond to form a heterodimeric structure,\\ncontaining a cationic heavy chain of 30 and 32 amino acids and a light\\nchain of 13 amino acids. Additionally, the light chain of EeCentrocin 2\\nseems to be N-terminally blocked by a pyroglutamic acid residue. The\\nheavy chains of EeCentrocins 1 and 2 were synthesised and shown to be\\nresponsible for the antimicrobial activity of the natural peptides.\\nEeStrongylocin 2 contains 6 cysteines engaged in 3 disulphide bonds. A\\nfourth peptide (Ee4635) was also discovered but not fully characterised.\\nUsing mass spectrometric and NMR analyses, EeCentrocins 1 and 2,\\nEeStrongylocin 2 and Ee4635 were all shown to contain\\npost-translationally brominated Trp residues in the 6 position of the\\nindole ring.", "link"=>"http://www.mendeley.com/research/novel-antimicrobial-peptides-eecentrocins-1-2-eestrongylocin-2-edible-sea-urchin-echinus-esculentus", "reader_count"=>12, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Researcher"=>2, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>4, "Student > Master"=>1, "Other"=>1, "Student > Bachelor"=>2}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Researcher"=>2, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>4, "Student > Master"=>1, "Other"=>1, "Student > Bachelor"=>2}, "reader_count_by_subject_area"=>{"Unspecified"=>2, "Biochemistry, Genetics and Molecular Biology"=>2, "Agricultural and Biological Sciences"=>5, "Medicine and Dentistry"=>1, "Chemistry"=>1, "Immunology and Microbiology"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Chemistry"=>{"Chemistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>5}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>2}, "Unspecified"=>{"Unspecified"=>2}}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/4874716"], "description"=>"<p>LC = light chain, HC = heavy chain, HC-diBr = peptide with two brominated Trp residues.</p>", "links"=>[], "tags"=>["EeCentrocins 1", "3 disulphide bonds", "pyroglutamic acid residue", "EeStrongylocin 2", "Edible sea urchin Echinus esculentus", "novel antimicrobial peptides", "NMR", "sea urchin Strongylocentrotus droebachiensis", "Edible Sea Urchin Echinus esculentus", "characterise antimicrobial peptides", "light chain", "Natural antimicrobial peptides"], "article_id"=>3134113, "categories"=>["Biochemistry", "Molecular Biology", "Biotechnology", "Environmental Sciences not elsewhere classified", "Chemical Sciences not elsewhere classified", "Immunology", "Biological Sciences not elsewhere classified"], "users"=>["Runar Gjerp Solstad", "Chun Li", "Johan Isaksson", "Jostein Johansen", "Johan Svenson", "Klara Stensvåg", "Tor Haug"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0151820.t002", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Antimicrobial_activities_of_native_EeCentrocin_1_EeStrongylocin_2_and_synthesised_analogues_of_EeCentrocin_1_and_2_/3134113", "title"=>"Antimicrobial activities of native EeCentrocin 1, EeStrongylocin 2 and synthesised analogues of EeCentrocin 1 and 2.", "pos_in_sequence"=>12, "defined_type"=>3, "published_date"=>"2016-03-23 06:07:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/4874476"], "description"=>"<p>The peptides were separated using a preparative C<sub>18</sub> column using a flow rate of 8 ml/min, and an optimised HPLC gradient protocol of 0.05% TFA/ACN in 0.05% TFA/H<sub>2</sub>O for 60 min. One-minute fractions were collected and tested for antibacterial activity. Antibacterial fractions are marked with a black line under the chromatogram and peak fractions selected for further analysis are marked with arrows.</p>", "links"=>[], "tags"=>["EeCentrocins 1", "3 disulphide bonds", "pyroglutamic acid residue", "EeStrongylocin 2", "Edible sea urchin Echinus esculentus", "novel antimicrobial peptides", "NMR", "sea urchin Strongylocentrotus droebachiensis", "Edible Sea Urchin Echinus esculentus", "characterise antimicrobial peptides", "light chain", "Natural antimicrobial peptides"], "article_id"=>3133924, "categories"=>["Biochemistry", "Molecular Biology", "Biotechnology", "Environmental Sciences not elsewhere classified", "Chemical Sciences not elsewhere classified", "Immunology", "Biological Sciences not elsewhere classified"], "users"=>["Runar Gjerp Solstad", "Chun Li", "Johan Isaksson", "Jostein Johansen", "Johan Svenson", "Klara Stensvåg", "Tor Haug"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0151820.g002", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/RP_HPLC_chromatogram_showing_the_separation_of_AMPs_in_the_40_SPE_fraction_of_i_E_i_i_esculentus_i_coelomocytes_/3133924", "title"=>"RP-HPLC chromatogram showing the separation of AMPs in the 40% SPE fraction of <i>E</i>. <i>esculentus</i> coelomocytes.", "pos_in_sequence"=>3, "defined_type"=>1, "published_date"=>"2016-03-23 06:07:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/4874512"], "description"=>"<p>In the aligned sequences, grey indicates identical amino acids. The predicted signal peptides, propeptides and mature peptides are marked with curly brackets. Gaps are inserted to maximise similarity. In the top row accession numbers are given in parentheses, the mature peptide sequences are presented in the bottom rows.</p>", "links"=>[], "tags"=>["EeCentrocins 1", "3 disulphide bonds", "pyroglutamic acid residue", "EeStrongylocin 2", "Edible sea urchin Echinus esculentus", "novel antimicrobial peptides", "NMR", "sea urchin Strongylocentrotus droebachiensis", "Edible Sea Urchin Echinus esculentus", "characterise antimicrobial peptides", "light chain", "Natural antimicrobial peptides"], "article_id"=>3133957, "categories"=>["Biochemistry", "Molecular Biology", "Biotechnology", "Environmental Sciences not elsewhere classified", "Chemical Sciences not elsewhere classified", "Immunology", "Biological Sciences not elsewhere classified"], "users"=>["Runar Gjerp Solstad", "Chun Li", "Johan Isaksson", "Jostein Johansen", "Johan Svenson", "Klara Stensvåg", "Tor Haug"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0151820.g004", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Multiple_sequence_alignments_of_Ee5922_with_homologues_in_i_S_i_i_droebachiensis_i_and_i_S_i_i_purpuratus_i_/3133957", "title"=>"Multiple sequence alignments of Ee5922 with homologues in <i>S</i>. <i>droebachiensis</i> and <i>S</i>. <i>purpuratus</i>.", "pos_in_sequence"=>5, "defined_type"=>1, "published_date"=>"2016-03-23 06:07:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/4874458"], "description"=>"<p>Image credit: Runar Gjerp Solstad.</p>", "links"=>[], "tags"=>["EeCentrocins 1", "3 disulphide bonds", "pyroglutamic acid residue", "EeStrongylocin 2", "Edible sea urchin Echinus esculentus", "novel antimicrobial peptides", "NMR", "sea urchin Strongylocentrotus droebachiensis", "Edible Sea Urchin Echinus esculentus", "characterise antimicrobial peptides", "light chain", "Natural antimicrobial peptides"], "article_id"=>3133897, "categories"=>["Biochemistry", "Molecular Biology", "Biotechnology", "Environmental Sciences not elsewhere classified", "Chemical Sciences not elsewhere classified", "Immunology", "Biological Sciences not elsewhere classified"], "users"=>["Runar Gjerp Solstad", "Chun Li", "Johan Isaksson", "Jostein Johansen", "Johan Svenson", "Klara Stensvåg", "Tor Haug"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0151820.g001", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/The_Edible_sea_urchin_i_E_i_i_esculentus_i_/3133897", "title"=>"The Edible sea urchin, <i>E</i>. <i>esculentus</i>.", "pos_in_sequence"=>2, "defined_type"=>1, "published_date"=>"2016-03-23 06:07:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/4874692"], "description"=>"<p>X denotes unidentified amino acids.</p>", "links"=>[], "tags"=>["EeCentrocins 1", "3 disulphide bonds", "pyroglutamic acid residue", "EeStrongylocin 2", "Edible sea urchin Echinus esculentus", "novel antimicrobial peptides", "NMR", "sea urchin Strongylocentrotus droebachiensis", "Edible Sea Urchin Echinus esculentus", "characterise antimicrobial peptides", "light chain", "Natural antimicrobial peptides"], "article_id"=>3134092, "categories"=>["Biochemistry", "Molecular Biology", "Biotechnology", "Environmental Sciences not elsewhere classified", "Chemical Sciences not elsewhere classified", "Immunology", "Biological Sciences not elsewhere classified"], "users"=>["Runar Gjerp Solstad", "Chun Li", "Johan Isaksson", "Jostein Johansen", "Johan Svenson", "Klara Stensvåg", "Tor Haug"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0151820.t001", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Peptide_fractions_with_corresponding_retention_times_min_obtained_by_preparative_RP_HPLC_monoisotopic_masses_Da_of_the_native_peptides_obtained_by_HR_MS_and_the_partial_amino_acid_sequences_obtained_by_Edman_degradation_analysis_/3134092", "title"=>"Peptide fractions with corresponding retention times (min) obtained by preparative RP-HPLC, monoisotopic masses (Da) of the native peptides obtained by HR-MS, and the partial amino acid sequences obtained by Edman degradation analysis.", "pos_in_sequence"=>11, "defined_type"=>3, "published_date"=>"2016-03-23 06:07:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/4874311", "https://ndownloader.figshare.com/files/4874431", "https://ndownloader.figshare.com/files/4874422", "https://ndownloader.figshare.com/files/4874413", "https://ndownloader.figshare.com/files/4874404", "https://ndownloader.figshare.com/files/4874392", "https://ndownloader.figshare.com/files/4874386", "https://ndownloader.figshare.com/files/4874380", "https://ndownloader.figshare.com/files/4874377", "https://ndownloader.figshare.com/files/4874371", "https://ndownloader.figshare.com/files/4874356", "https://ndownloader.figshare.com/files/4874353", "https://ndownloader.figshare.com/files/4874347", "https://ndownloader.figshare.com/files/4874335", "https://ndownloader.figshare.com/files/4874329", "https://ndownloader.figshare.com/files/4874326", "https://ndownloader.figshare.com/files/4874437"], "description"=>"<div><p>The global problem of microbial resistance to antibiotics has resulted in an urgent need to develop new antimicrobial agents. Natural antimicrobial peptides are considered promising candidates for drug development. Echinoderms, which rely on innate immunity factors in the defence against harmful microorganisms, are sources of novel antimicrobial peptides. This study aimed to isolate and characterise antimicrobial peptides from the Edible sea urchin <i>Echinus esculentus</i>. Using bioassay-guided purification and cDNA cloning, three antimicrobial peptides were characterised from the haemocytes of the sea urchin; two heterodimeric peptides and a cysteine-rich peptide. The peptides were named EeCentrocin 1 and 2 and EeStrongylocin 2, respectively, due to their apparent homology to the published centrocins and strongylocins isolated from the green sea urchin <i>Strongylocentrotus droebachiensis</i>. The two centrocin-like peptides EeCentrocin 1 and 2 are intramolecularly connected via a disulphide bond to form a heterodimeric structure, containing a cationic heavy chain of 30 and 32 amino acids and a light chain of 13 amino acids. Additionally, the light chain of EeCentrocin 2 seems to be N-terminally blocked by a pyroglutamic acid residue. The heavy chains of EeCentrocins 1 and 2 were synthesised and shown to be responsible for the antimicrobial activity of the natural peptides. EeStrongylocin 2 contains 6 cysteines engaged in 3 disulphide bonds. A fourth peptide (Ee4635) was also discovered but not fully characterised. Using mass spectrometric and NMR analyses, EeCentrocins 1 and 2, EeStrongylocin 2 and Ee4635 were all shown to contain post-translationally brominated Trp residues in the 6 position of the indole ring.</p></div>", "links"=>[], "tags"=>["EeCentrocins 1", "3 disulphide bonds", "pyroglutamic acid residue", "EeStrongylocin 2", "Edible sea urchin Echinus esculentus", "novel antimicrobial peptides", "NMR", "sea urchin Strongylocentrotus droebachiensis", "Edible Sea Urchin Echinus esculentus", "characterise antimicrobial peptides", "light chain", "Natural antimicrobial peptides"], "article_id"=>3133807, "categories"=>["Biochemistry", "Molecular Biology", "Biotechnology", "Environmental Sciences not elsewhere classified", "Chemical Sciences not elsewhere classified", "Immunology", "Biological Sciences not elsewhere classified"], "users"=>["Runar Gjerp Solstad", "Chun Li", "Johan Isaksson", "Jostein Johansen", "Johan Svenson", "Klara Stensvåg", "Tor Haug"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0151820.s001", "https://dx.doi.org/10.1371/journal.pone.0151820.s016", "https://dx.doi.org/10.1371/journal.pone.0151820.s015", "https://dx.doi.org/10.1371/journal.pone.0151820.s014", "https://dx.doi.org/10.1371/journal.pone.0151820.s013", "https://dx.doi.org/10.1371/journal.pone.0151820.s012", "https://dx.doi.org/10.1371/journal.pone.0151820.s011", "https://dx.doi.org/10.1371/journal.pone.0151820.s010", "https://dx.doi.org/10.1371/journal.pone.0151820.s009", "https://dx.doi.org/10.1371/journal.pone.0151820.s008", "https://dx.doi.org/10.1371/journal.pone.0151820.s007", "https://dx.doi.org/10.1371/journal.pone.0151820.s006", "https://dx.doi.org/10.1371/journal.pone.0151820.s005", "https://dx.doi.org/10.1371/journal.pone.0151820.s004", "https://dx.doi.org/10.1371/journal.pone.0151820.s003", "https://dx.doi.org/10.1371/journal.pone.0151820.s002", "https://dx.doi.org/10.1371/journal.pone.0151820.s017"], "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Novel_Antimicrobial_Peptides_EeCentrocins_1_2_and_EeStrongylocin_2_from_the_Edible_Sea_Urchin_i_Echinus_esculentus_i_Have_6_Br_Trp_Post_Translational_Modifications/3133807", "title"=>"Novel Antimicrobial Peptides EeCentrocins 1, 2 and EeStrongylocin 2 from the Edible Sea Urchin <i>Echinus esculentus</i> Have 6-Br-Trp Post-Translational Modifications", "pos_in_sequence"=>1, "defined_type"=>4, "published_date"=>"2016-03-23 06:07:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/4874605"], "description"=>"<p>The chemical shifts are less well correlated for the 5-Br reference compound (left, 5.36 ppm average error) than those of the 6-Br reference compound (right, 1.55 ppm average error). Each data point in the figure represents a carbon of the indole of Trp.</p>", "links"=>[], "tags"=>["EeCentrocins 1", "3 disulphide bonds", "pyroglutamic acid residue", "EeStrongylocin 2", "Edible sea urchin Echinus esculentus", "novel antimicrobial peptides", "NMR", "sea urchin Strongylocentrotus droebachiensis", "Edible Sea Urchin Echinus esculentus", "characterise antimicrobial peptides", "light chain", "Natural antimicrobial peptides"], "article_id"=>3134032, "categories"=>["Biochemistry", "Molecular Biology", "Biotechnology", "Environmental Sciences not elsewhere classified", "Chemical Sciences not elsewhere classified", "Immunology", "Biological Sciences not elsewhere classified"], "users"=>["Runar Gjerp Solstad", "Chun Li", "Johan Isaksson", "Jostein Johansen", "Johan Svenson", "Klara Stensvåg", "Tor Haug"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0151820.g007", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Carbon_chemical_shifts_of_Br_Trp_in_native_peptides_correlated_with_synthetic_5_Br_Trp_and_6_Br_Trp_/3134032", "title"=>"Carbon chemical shifts of Br-Trp in native peptides correlated with synthetic 5-Br-Trp and 6-Br-Trp.", "pos_in_sequence"=>8, "defined_type"=>1, "published_date"=>"2016-03-23 06:07:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/4874497"], "description"=>"<p>In the aligned sequences, grey indicates identical amino acids. The predicted signal peptides, propeptides and mature peptides are marked with curly brackets. Gaps are inserted to maximise similarity. In the top row, accession numbers are given in parentheses, the mature peptide sequences are presented in the bottom rows.</p>", "links"=>[], "tags"=>["EeCentrocins 1", "3 disulphide bonds", "pyroglutamic acid residue", "EeStrongylocin 2", "Edible sea urchin Echinus esculentus", "novel antimicrobial peptides", "NMR", "sea urchin Strongylocentrotus droebachiensis", "Edible Sea Urchin Echinus esculentus", "characterise antimicrobial peptides", "light chain", "Natural antimicrobial peptides"], "article_id"=>3133939, "categories"=>["Biochemistry", "Molecular Biology", "Biotechnology", "Environmental Sciences not elsewhere classified", "Chemical Sciences not elsewhere classified", "Immunology", "Biological Sciences not elsewhere classified"], "users"=>["Runar Gjerp Solstad", "Chun Li", "Johan Isaksson", "Jostein Johansen", "Johan Svenson", "Klara Stensvåg", "Tor Haug"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0151820.g003", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Multiple_sequence_alignment_of_Ee4835_and_Ee5024_with_homologues_in_i_S_i_i_droebachiensis_i_and_i_S_i_i_purpuratus_i_/3133939", "title"=>"Multiple sequence alignment of Ee4835 and Ee5024 with homologues in <i>S</i>. <i>droebachiensis</i> and <i>S</i>. <i>purpuratus</i>.", "pos_in_sequence"=>4, "defined_type"=>1, "published_date"=>"2016-03-23 06:07:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/4874581"], "description"=>"<p>High-resolution mass spectra showing the <i>m/z</i> isotope cluster corresponding to the [M+H]<sup>+</sup> ions of A) Main peptide fragment from a tryptic digest of native EeCentrocin 1, B) Synthesised fragment GW<sub>Br</sub>W<sub>Br</sub>R, and C) Calculated isotope distribution of [GW<sub>Br</sub>W<sub>Br</sub>R+H]<sup>+</sup>. The identical and distinctive distributions (A, B and C) of the singly charged isotopes indicate the presence of two Br-Trp residues in EeCentrocin 1.</p>", "links"=>[], "tags"=>["EeCentrocins 1", "3 disulphide bonds", "pyroglutamic acid residue", "EeStrongylocin 2", "Edible sea urchin Echinus esculentus", "novel antimicrobial peptides", "NMR", "sea urchin Strongylocentrotus droebachiensis", "Edible Sea Urchin Echinus esculentus", "characterise antimicrobial peptides", "light chain", "Natural antimicrobial peptides"], "article_id"=>3134005, "categories"=>["Biochemistry", "Molecular Biology", "Biotechnology", "Environmental Sciences not elsewhere classified", "Chemical Sciences not elsewhere classified", "Immunology", "Biological Sciences not elsewhere classified"], "users"=>["Runar Gjerp Solstad", "Chun Li", "Johan Isaksson", "Jostein Johansen", "Johan Svenson", "Klara Stensvåg", "Tor Haug"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0151820.g006", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Characterisation_of_the_post_translational_modifications_of_EeCentrocin_1_HC_/3134005", "title"=>"Characterisation of the post-translational modifications of EeCentrocin 1 HC.", "pos_in_sequence"=>7, "defined_type"=>1, "published_date"=>"2016-03-23 06:07:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/4874668"], "description"=>"<p>The different synthetic peptide analogues of EeCentrocin 1 and 2 display minor haemolytic activity in concentrations up to 12.5 μM. EeCentrocin 2 HC displays the highest haemolytic activity (56.4% haemolysis at 100 μM).</p>", "links"=>[], "tags"=>["EeCentrocins 1", "3 disulphide bonds", "pyroglutamic acid residue", "EeStrongylocin 2", "Edible sea urchin Echinus esculentus", "novel antimicrobial peptides", "NMR", "sea urchin Strongylocentrotus droebachiensis", "Edible Sea Urchin Echinus esculentus", "characterise antimicrobial peptides", "light chain", "Natural antimicrobial peptides"], "article_id"=>3134074, "categories"=>["Biochemistry", "Molecular Biology", "Biotechnology", "Environmental Sciences not elsewhere classified", "Chemical Sciences not elsewhere classified", "Immunology", "Biological Sciences not elsewhere classified"], "users"=>["Runar Gjerp Solstad", "Chun Li", "Johan Isaksson", "Jostein Johansen", "Johan Svenson", "Klara Stensvåg", "Tor Haug"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0151820.g009", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Haemolytic_activity_of_synthetic_analogues_of_EeCentrocin_1_and_2_/3134074", "title"=>"Haemolytic activity of synthetic analogues of EeCentrocin 1 and 2.", "pos_in_sequence"=>10, "defined_type"=>1, "published_date"=>"2016-03-23 06:07:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/4874542"], "description"=>"<p><b>Evolutionary relationships of A) centrocins and B) strongylocins identified in <i>E</i>. <i>esculentus</i>, <i>S</i>. <i>droebachiensis</i> and <i>S</i>. <i>purpuratus</i>.</b> The evolutionary history was inferred using the Neighbour-joining method [<a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0151820#pone.0151820.ref039\" target=\"_blank\">39</a>] and the optimal trees are shown. The percentage of replicate trees in which the proteins clustered together during the bootstrap test (500 replicates) is given next to the nodes [<a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0151820#pone.0151820.ref055\" target=\"_blank\">55</a>]. The tree is drawn to scale, with branch lengths in the same units as those of the evolutionary distances used to infer the phylogenetic tree. The evolutionary distances were computed using the Poisson correction method [<a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0151820#pone.0151820.ref040\" target=\"_blank\">40</a>]. Accession numbers are given in parentheses.</p>", "links"=>[], "tags"=>["EeCentrocins 1", "3 disulphide bonds", "pyroglutamic acid residue", "EeStrongylocin 2", "Edible sea urchin Echinus esculentus", "novel antimicrobial peptides", "NMR", "sea urchin Strongylocentrotus droebachiensis", "Edible Sea Urchin Echinus esculentus", "characterise antimicrobial peptides", "light chain", "Natural antimicrobial peptides"], "article_id"=>3133981, "categories"=>["Biochemistry", "Molecular Biology", "Biotechnology", "Environmental Sciences not elsewhere classified", "Chemical Sciences not elsewhere classified", "Immunology", "Biological Sciences not elsewhere classified"], "users"=>["Runar Gjerp Solstad", "Chun Li", "Johan Isaksson", "Jostein Johansen", "Johan Svenson", "Klara Stensvåg", "Tor Haug"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0151820.g005", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Novel_Antimicrobial_Peptides_EeCentrocins_1_2_and_EeStrongylocin_2_from_the_Edible_Sea_Urchin_i_Echinus_esculentus_i_Have_6_Br_Trp_Post_Translational_Modifications_Fig_5/3133981", "title"=>"Novel Antimicrobial Peptides EeCentrocins 1, 2 and EeStrongylocin 2 from the Edible Sea Urchin <i>Echinus esculentus</i> Have 6-Br-Trp Post-Translational Modifications - Fig 5", "pos_in_sequence"=>6, "defined_type"=>1, "published_date"=>"2016-03-23 06:07:28"}
  • {"files"=>["https://ndownloader.figshare.com/files/4874635"], "description"=>"<p>The two top structures are the heterodimeric EeCentrocins 1 and 2. The disulphide bonds connecting the HC and LC are indicated with “|”. The lower sequence is the primary structure of EeStrongylocin 2. All Trp substitutions are assigned to the 6 position of the indole.</p>", "links"=>[], "tags"=>["EeCentrocins 1", "3 disulphide bonds", "pyroglutamic acid residue", "EeStrongylocin 2", "Edible sea urchin Echinus esculentus", "novel antimicrobial peptides", "NMR", "sea urchin Strongylocentrotus droebachiensis", "Edible Sea Urchin Echinus esculentus", "characterise antimicrobial peptides", "light chain", "Natural antimicrobial peptides"], "article_id"=>3134047, "categories"=>["Biochemistry", "Molecular Biology", "Biotechnology", "Environmental Sciences not elsewhere classified", "Chemical Sciences not elsewhere classified", "Immunology", "Biological Sciences not elsewhere classified"], "users"=>["Runar Gjerp Solstad", "Chun Li", "Johan Isaksson", "Jostein Johansen", "Johan Svenson", "Klara Stensvåg", "Tor Haug"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0151820.g008", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Structures_of_peptides_discovered_in_i_E_i_i_esculentus_i_/3134047", "title"=>"Structures of peptides discovered in <i>E</i>. <i>esculentus</i>.", "pos_in_sequence"=>9, "defined_type"=>1, "published_date"=>"2016-03-23 06:07:28"}

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  • {"unique-ip"=>"6", "full-text"=>"4", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"3"}
  • {"unique-ip"=>"13", "full-text"=>"25", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2019", "month"=>"1"}
  • {"unique-ip"=>"10", "full-text"=>"11", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"11"}
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  • {"unique-ip"=>"9", "full-text"=>"9", "pdf"=>"5", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"4"}
  • {"unique-ip"=>"7", "full-text"=>"6", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"5"}
  • {"unique-ip"=>"8", "full-text"=>"6", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"6"}
  • {"unique-ip"=>"11", "full-text"=>"5", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"14", "cited-by"=>"0", "year"=>"2018", "month"=>"7"}
  • {"unique-ip"=>"12", "full-text"=>"14", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"8"}
  • {"unique-ip"=>"15", "full-text"=>"19", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2018", "month"=>"10"}
  • {"unique-ip"=>"10", "full-text"=>"20", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"9", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"12"}
  • {"unique-ip"=>"13", "full-text"=>"14", "pdf"=>"7", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"2"}
  • {"unique-ip"=>"16", "full-text"=>"17", "pdf"=>"5", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"10", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
  • {"unique-ip"=>"13", "full-text"=>"26", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"4"}
  • {"unique-ip"=>"15", "full-text"=>"17", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"5"}
  • {"unique-ip"=>"15", "full-text"=>"16", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"10", "supp-data"=>"16", "cited-by"=>"0", "year"=>"2019", "month"=>"8"}
  • {"unique-ip"=>"6", "full-text"=>"6", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"9"}
  • {"unique-ip"=>"20", "full-text"=>"16", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"9", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"10"}
  • {"unique-ip"=>"9", "full-text"=>"6", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"3", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"12"}
  • {"unique-ip"=>"10", "full-text"=>"9", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"2"}

Relative Metric

{"start_date"=>"2016-01-01T00:00:00Z", "end_date"=>"2016-12-31T00:00:00Z", "subject_areas"=>[]}
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