Dimerization Interface of 3-Hydroxyacyl-CoA Dehydrogenase Tunes the Formation of Its Catalytic Intermediate
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{"title"=>"Dimerization interface of 3-hydroxyacyl-CoA dehydrogenase tunes the formation of its catalytic intermediate", "type"=>"journal", "authors"=>[{"first_name"=>"Yingzhi", "last_name"=>"Xu", "scopus_author_id"=>"55790829800"}, {"first_name"=>"He", "last_name"=>"Li", "scopus_author_id"=>"57195945026"}, {"first_name"=>"Ying Hua", "last_name"=>"Jin", "scopus_author_id"=>"8610761600"}, {"first_name"=>"Jun", "last_name"=>"Fan", "scopus_author_id"=>"16309720800"}, {"first_name"=>"Fei", "last_name"=>"Sun", "scopus_author_id"=>"55681446000"}], "year"=>2014, "source"=>"PLoS ONE", "identifiers"=>{"pui"=>"373008111", "sgr"=>"84899753548", "issn"=>"19326203", "pmid"=>"24763278", "scopus"=>"2-s2.0-84899753548", "doi"=>"10.1371/journal.pone.0095965"}, "id"=>"2b340726-ae10-3bde-87fd-6cb74772ffd6", "abstract"=>"3-Hydroxyacyl-CoA dehydrogenase (HAD, EC 1.1.1.35) is a homodimeric enzyme localized in the mitochondrial matrix, which catalyzes the third step in fatty acid β-oxidation. The crystal structures of human HAD and subsequent complexes with cofactor/substrate enabled better understanding of HAD catalytic mechanism. However, numerous human diseases were found related to mutations at HAD dimerization interface that is away from the catalytic pocket. The role of HAD dimerization in its catalytic activity needs to be elucidated. Here, we solved the crystal structure of Caenorhabditis elegans HAD (cHAD) that is highly conserved to human HAD. Even though the cHAD mutants (R204A, Y209A and R204A/Y209A) with attenuated interactions on the dimerization interface still maintain a dimerization form, their enzymatic activities significantly decrease compared to that of the wild type. Such reduced activities are in consistency with the reduced ratios of the catalytic intermediate formation. Further molecular dynamics simulations results reveal that the alteration of the dimerization interface will increase the fluctuation of a distal region (a.a. 60-80) that plays an important role in the substrate binding. The increased fluctuation decreases the stability of the catalytic intermediate formation, and therefore the enzymatic activity is attenuated. Our study reveals the molecular mechanism about the essential role of the HAD dimerization interface in its catalytic activity via allosteric effects.", "link"=>"http://www.mendeley.com/research/dimerization-interface-3hydroxyacylcoa-dehydrogenase-tunes-formation-catalytic-intermediate", "reader_count"=>8, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>2, "Student > Master"=>3, "Professor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Student > Doctoral Student"=>1, "Student > Ph. D. Student"=>2, "Student > Master"=>3, "Professor"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>2, "Medicine and Dentistry"=>2, "Agricultural and Biological Sciences"=>2, "Physics and Astronomy"=>1, "Chemistry"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Chemistry"=>{"Chemistry"=>1}, "Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>2}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>2}}, "reader_count_by_country"=>{"Colombia"=>1, "United States"=>1}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1474296"], "description"=>"a<p>Number of the mutant residue was revised with the exclusion of transit peptide as compared with original literature.</p>b<p>This deletion mutation affected RNA splicing and lead to a mRNA lacking exon 5.</p>c<p>This mutation locates in splice site and the resulting mRNA were shown to comprise abnormal exon 7 sequence.</p>d<p>The codon encoding Arg (CGA) was mutated to STOP codon (TGA) at position 224.</p>e<p>Hyperinsulinemic hypoglycemia.</p>f<p>Hyperinsulinism.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymology", "Enzyme chemistry", "Enzyme regulation", "Enzyme kinetics", "enzymes", "Enzyme structure", "proteins", "protein structure", "biophysics", "Biophysical simulations", "disease-causing", "mutations"], "article_id"=>1007104, "categories"=>["Biological Sciences"], "users"=>["Yingzhi Xu", "He Li", "Ying-Hua Jin", "Jun Fan", "Fei Sun"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0095965.t001", "stats"=>{"downloads"=>4, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Reported_disease_causing_mutations_of_human_HAD_gene_/1007104", "title"=>"Reported disease-causing mutations of human <i>HAD</i> gene.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-04-24 03:49:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1474291"], "description"=>"<p>(<b>A</b>) A combined surface and stick model presents the distances between the side chain of intrinsic W260 and bound NADHs of subunit A (cyan) and subunit B (yellow). The positions of NADHs are determined by superposition of the crystal structure of human HAD·NADH complex (PDB entry 1F17) with the present <i>c</i>HAD crystal structure. (<b>B</b>) Fluorescence resonance energy transfer (FRET) spectrum by titrating NADH with the wild type <i>c</i>HAD. The excitation wavelength is 270 nm and the emission wavelength is scanned from 290 to 500 nm. The FRET signal appears at the wavelength of 460 nm. (<b>C</b>) Hyperbolic curve of the FRET fluorescence signal at 460 nm against the titration of NADH concentration for the wild type <i>c</i>HAD. The insert represents the logarithmic Hill plot between 10 and 90% active site saturation.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymology", "Enzyme chemistry", "Enzyme regulation", "Enzyme kinetics", "enzymes", "Enzyme structure", "proteins", "protein structure", "biophysics", "Biophysical simulations", "nadh", "binding"], "article_id"=>1007099, "categories"=>["Biological Sciences"], "users"=>["Yingzhi Xu", "He Li", "Ying-Hua Jin", "Jun Fan", "Fei Sun"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0095965.g004", "stats"=>{"downloads"=>2, "page_views"=>18, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Negative_cooperation_effect_of_NADH_binding_within_the_c_HAD_dimer_/1007099", "title"=>"Negative cooperation effect of NADH binding within the <i>c</i>HAD dimer.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-24 03:49:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1474290"], "description"=>"<p>(<b>A</b>) Ribbon (left) and surface (right) diagram of the crystal structure of <i>c</i>HAD dimer in an asymmetric unit. The two molecules, subunit A and subunit B, colored in cyan and yellow respectively in the ribbon diagram, are arranged in a “tail-to-tail” manner through interactions between their C-terminal domains. The loop between helix α2 and α3 with weak electron density is indicated by dotted line. In the surface diagram, only secondary structures involving dimerization are depicted. (<b>B</b>) An “open-book” view of the dimerization interface between subunit A and B. The negatively charged, positively charged, polar, hydrophobic and glycine residues on the surface are represented in red, blue, green, yellow and white, respectively. The contact sites of the dimerization interface via α8/α8′, α9/β7′–β8′ and α9′/β7–β8 are indicated by the red dotted ellipse, green dotted rectangle and blue dotted rectangle. (<b>C</b>) Core dimerization interface. A combined ribbon and stick model illustrates both electrostatic (left) and hydrophobic (right) interactions between each α8 helix of two subunits. Salt bridges are indicated with the dashed lines. (<b>D</b>) Gel filtration profile of the wild type and mutated <i>c</i>HADs. Equal amount of protein (100 µg) was injected onto a pre-equilibrated Superdex 200 column (10/300 GL; GE healthcare) and eluted at a flow rate of 0.5 ml/min.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymology", "Enzyme chemistry", "Enzyme regulation", "Enzyme kinetics", "enzymes", "Enzyme structure", "proteins", "protein structure", "biophysics", "Biophysical simulations", "interface"], "article_id"=>1007098, "categories"=>["Biological Sciences"], "users"=>["Yingzhi Xu", "He Li", "Ying-Hua Jin", "Jun Fan", "Fei Sun"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0095965.g003", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Dimerization_interface_of_c_HAD_/1007098", "title"=>"Dimerization interface of <i>c</i>HAD.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-24 03:49:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1474285"], "description"=>"<p>Two monomers of HAD are colored in blue and grey, respectively. The carbon atoms of NAD<sup>+</sup>, acetoacetyl-CoA (AACoA), side chains of mutated residues and catalytic His-Glu pair of one monomer (blue) are colored in green, yellow, magentas and salmon, respectively. Regions colored in lemon refer to the in-frame deletion from 171–200 (c.547-3_549 deletion in <i>HAD</i> gene). If not mentioned, all the structure illustrations were generated with <i>PyMOL</i> (<a href=\"http://www.pymol.org\" target=\"_blank\">http://www.pymol.org</a>. Accessed 2014 March 26<sup>th</sup>.).</p>", "links"=>[], "tags"=>["Biochemistry", "enzymology", "Enzyme chemistry", "Enzyme regulation", "Enzyme kinetics", "enzymes", "Enzyme structure", "proteins", "protein structure", "biophysics", "Biophysical simulations", "mutations", "had"], "article_id"=>1007093, "categories"=>["Biological Sciences"], "users"=>["Yingzhi Xu", "He Li", "Ying-Hua Jin", "Jun Fan", "Fei Sun"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0095965.g001", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Mapping_disease_related_mutations_into_human_HAD_crystal_structure_PDB_entry_1F0Y_/1007093", "title"=>"Mapping disease related mutations into human HAD crystal structure (PDB entry 1F0Y).", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-24 03:49:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1474299"], "description"=>"a<p>The two values represent the averaged distances of C<sub>α</sub> atoms between corresponding residues and the standard deviation of distances.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymology", "Enzyme chemistry", "Enzyme regulation", "Enzyme kinetics", "enzymes", "Enzyme structure", "proteins", "protein structure", "biophysics", "Biophysical simulations", "distances", "corresponding", "residues", "molecular"], "article_id"=>1007107, "categories"=>["Biological Sciences"], "users"=>["Yingzhi Xu", "He Li", "Ying-Hua Jin", "Jun Fan", "Fei Sun"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0095965.t004", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Averaged_C_945_distances_of_corresponding_residues_from_molecular_dynamics_simulations_a_/1007107", "title"=>"Averaged C<sub>α</sub> distances of corresponding residues from molecular dynamics simulations<sup>a</sup>.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-04-24 03:49:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1474298"], "description"=>"a<p>Hill coefficent and the values are measured from fluorescence data.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymology", "Enzyme chemistry", "Enzyme regulation", "Enzyme kinetics", "enzymes", "Enzyme structure", "proteins", "protein structure", "biophysics", "Biophysical simulations", "mutant"], "article_id"=>1007106, "categories"=>["Biological Sciences"], "users"=>["Yingzhi Xu", "He Li", "Ying-Hua Jin", "Jun Fan", "Fei Sun"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0095965.t003", "stats"=>{"downloads"=>4, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Kinetic_parameters_of_wild_type_and_mutant_c_HAD_enzymes_/1007106", "title"=>"Kinetic parameters of wild type and mutant <i>c</i>HAD enzymes.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-04-24 03:49:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1474288"], "description"=>"<p>(<b>A</b>) Ribbon diagram of <i>c</i>HAD crystal structure (PDB entry 4J0F, this work) colored in purple. The loop between helix α2 and α3 with weak electron density is indicated by dotted line. (<b>B</b>) Tertiary structure alignment among 3-hydroxyacyl-CoA dehydrogenases from <i>C</i>. elegans (purple, PDB entry 4J0F), human (blue, 3HAD) and <i>E</i>. <i>coli</i> (yellow, 3MOG). The region from residue 286 to 475 in <i>E</i>. <i>coli</i> HAD is not shown. (<b>C</b>) Sequence alignment among 3-hydroxyacyl-CoA dehydrogenases from <i>Caenorhabditis elegans</i> (<i>C</i>. <i>elegans</i>, GenBank accession No. CAA80153.1), <i>Homo sapiens</i> (human, GenBank accession No. CAA65528.1), <i>Sus scrofa</i> (pig, GenBank accession No. AAD20939.1), <i>Mus musculus</i> (mouse, GenBank accession No. BAA06122) and <i>Escherichia coli</i> (<i>E</i>. <i>coli</i>, GenBank accession No.NP_415913.1, residues 1–286). The transit peptide sequence was excluded from human, pig and mouse HAD sequences. The secondary structures are corresponding to <i>c</i>HAD. The catalytic His-Glu pair is boxed in black. The disease related point mutations in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0095965#pone-0095965-t001\" target=\"_blank\"><b>Table 1</b></a> are boxed with dashed line. The conserved glycine residues flanking C-terminal domain helices are indicated by triangles. The conserved Arg and Glu forming salt-bridge on dimerization interface are indicated by asterisks; and the conserved hydrophobic residues on the dimerization interface are indicated by “#”. The labels of secondary structure are corresponding to those in (<b>A</b>).</p>", "links"=>[], "tags"=>["Biochemistry", "enzymology", "Enzyme chemistry", "Enzyme regulation", "Enzyme kinetics", "enzymes", "Enzyme structure", "proteins", "protein structure", "biophysics", "Biophysical simulations"], "article_id"=>1007096, "categories"=>["Biological Sciences"], "users"=>["Yingzhi Xu", "He Li", "Ying-Hua Jin", "Jun Fan", "Fei Sun"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0095965.g002", "stats"=>{"downloads"=>1, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Overall_structure_of_c_HAD_and_protein_primary_structure_comparison_between_c_HAD_and_its_homologues_/1007096", "title"=>"Overall structure of <i>c</i>HAD and protein primary structure comparison between <i>c</i>HAD and its homologues.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-24 03:49:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1474300", "https://ndownloader.figshare.com/files/1474301", "https://ndownloader.figshare.com/files/1474302", "https://ndownloader.figshare.com/files/1474303", "https://ndownloader.figshare.com/files/1474304"], "description"=>"<div><p>3-hydroxyacyl-CoA dehydrogenase (HAD, EC 1.1.1.35) is a homodimeric enzyme localized in the mitochondrial matrix, which catalyzes the third step in fatty acid <i>β</i>-oxidation. The crystal structures of human HAD and subsequent complexes with cofactor/substrate enabled better understanding of HAD catalytic mechanism. However, numerous human diseases were found related to mutations at HAD dimerization interface that is away from the catalytic pocket. The role of HAD dimerization in its catalytic activity needs to be elucidated. Here, we solved the crystal structure of <i>Caenorhabditis elegans</i> HAD (<i>c</i>HAD) that is highly conserved to human HAD. Even though the <i>c</i>HAD mutants (R204A, Y209A and R204A/Y209A) with attenuated interactions on the dimerization interface still maintain a dimerization form, their enzymatic activities significantly decrease compared to that of the wild type. Such reduced activities are in consistency with the reduced ratios of the catalytic intermediate formation. Further molecular dynamics simulations results reveal that the alteration of the dimerization interface will increase the fluctuation of a distal region (a.a. 60–80) that plays an important role in the substrate binding. The increased fluctuation decreases the stability of the catalytic intermediate formation, and therefore the enzymatic activity is attenuated. Our study reveals the molecular mechanism about the essential role of the HAD dimerization interface in its catalytic activity via allosteric effects.</p></div>", "links"=>[], "tags"=>["Biochemistry", "enzymology", "Enzyme chemistry", "Enzyme regulation", "Enzyme kinetics", "enzymes", "Enzyme structure", "proteins", "protein structure", "biophysics", "Biophysical simulations", "interface", "3-hydroxyacyl-coa", "dehydrogenase", "tunes", "catalytic"], "article_id"=>1007108, "categories"=>["Biological Sciences"], "users"=>["Yingzhi Xu", "He Li", "Ying-Hua Jin", "Jun Fan", "Fei Sun"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0095965.s001", "https://dx.doi.org/10.1371/journal.pone.0095965.s002", "https://dx.doi.org/10.1371/journal.pone.0095965.s003", "https://dx.doi.org/10.1371/journal.pone.0095965.s004", "https://dx.doi.org/10.1371/journal.pone.0095965.s005"], "stats"=>{"downloads"=>6, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Dimerization_Interface_of_3_Hydroxyacyl_CoA_Dehydrogenase_Tunes_the_Formation_of_Its_Catalytic_Intermediate_/1007108", "title"=>"Dimerization Interface of 3-Hydroxyacyl-CoA Dehydrogenase Tunes the Formation of Its Catalytic Intermediate", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2014-04-24 03:49:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1474297"], "description"=>"<p>*The data set was collected from one single crystal. Values in parentheses are for the highest resolution shell.</p>†<p>R<sub>merge</sub>  = ∑<sub>hkl</sub>∑<sub>I</sub> |<i>I</i><sub>i</sub>(<i>hkl</i>) − <i>(<i>hkl</i>)<i>></i>|/∑<sub>hkl</sub>∑<sub>i</sub><i>I</i><sub>i</sub>(<i>hkl</i>), where <i>I</i><sub>i</sub>(<i>hkl</i>) is the intensity of the <i>i</i>th observation of the reflection <i>hkl</i> and <i>(<i>hkl</i>)<i>></i> is the mean intensity of reflections <i>hkl</i>.</i></i></p><i><i>§<p>R<sub>work</sub>  = ∑(||<i>F</i>(<i>obs</i>)| − |<i>F</i>(<i>calc</i>)||)/∑|<i>F</i>(<i>obs</i>)|, where <i>F</i>(<i>obs</i>) and <i>F</i>(<i>calc</i>) are observed and calculated structure factors, respectively.</p>¶<p><i>R</i><sub>free</sub> was calculated using 5% of data excluded from refinement.</p></i></i>", "links"=>[], "tags"=>["Biochemistry", "enzymology", "Enzyme chemistry", "Enzyme regulation", "Enzyme kinetics", "enzymes", "Enzyme structure", "proteins", "protein structure", "biophysics", "Biophysical simulations", "refinement"], "article_id"=>1007105, "categories"=>["Biological Sciences"], "users"=>["Yingzhi Xu", "He Li", "Ying-Hua Jin", "Jun Fan", "Fei Sun"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0095965.t002", "stats"=>{"downloads"=>1, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Data_collection_and_refinement_statistics_/1007105", "title"=>"Data collection and refinement statistics<sup>*</sup>.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-04-24 03:49:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/1474295"], "description"=>"<p>(<b>A</b>) A combined surface and stick model presents a structural model of <i>c</i>HAD ternary complex with the NAD<sup>+</sup> and AACoA bound. The α8 helices of the dimer are depicted as ribbons. The positions of NAD<sup>+</sup> and AACoA are determined by superposition of the structure of human HAD·NAD·AACoA complex (PDB entry 1F0Y) with the present <i>c</i>HAD crystal structure. (<b>B</b>) Difference absorption spectra of the <i>c</i>HAD·NAD<sup>+</sup>·AACoA complexes for the wild type (purple), R204A mutant (green), Y209A mutant (blue) and R204A/Y209A mutant (red) at a ligand concentration of 2 m<i>M</i> as described in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0095965#s2\" target=\"_blank\"><b>MATERIALS AND METHODS</b></a>. (<b>C</b>) Effects of mutations on charge transfer complex formation. The columns filled in white represent the net absorbance of ternary complex formed by <i>c</i>HAD and its variants at 412 nm (scaled by left vertical axis), while the columns filled in black represent their V<sub>max</sub> values determined in kinetic experiments (scaled by right vertical axis). (<b>D</b>) Thermo shift assay of <i>c</i>HAD and its variants. (<b>E</b>) The critical melting temperature (<i>T</i><sub>m</sub>) of <i>c</i>HAD and its variants from the thermo shift assay in (D). (<b>F</b>) The root-mean-square fluctuations (RMSF) of <i>c</i>HAD (wild type at left, R204A at middle and R204A/Y209A at right) N-terminal domain residues (1–198) for each subunit (chain 1 and 2). The significant fluctuation regions (R1, a.a. 60–80) are label accordingly. (<b>G</b>) The RMSFs of <i>c</i>HAD (wild type at left, R204A at middle and R204A/Y209A at right) C-terminal domain residues (199–297) for each subunit (chain 1 and 2). The significant fluctuation regions (R2, a.a. 260–280) are label accordingly. (<b>H</b>) Cartoon representation of the crystal structure of <i>c</i>HAD with one subunit colored in cyan and another in gold. The significant fluctuation regions R1 (a.a. 60–80) and R2 (a.a. 260–280) observed in molecular dynamics simulation (F and G) are colored in red and blue, respectively.</p>", "links"=>[], "tags"=>["Biochemistry", "enzymology", "Enzyme chemistry", "Enzyme regulation", "Enzyme kinetics", "enzymes", "Enzyme structure", "proteins", "protein structure", "biophysics", "Biophysical simulations", "intermediate"], "article_id"=>1007103, "categories"=>["Biological Sciences"], "users"=>["Yingzhi Xu", "He Li", "Ying-Hua Jin", "Jun Fan", "Fei Sun"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0095965.g005", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Characterization_of_the_charge_transfer_complex_intermediate_formation_/1007103", "title"=>"Characterization of the charge transfer complex intermediate formation.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-04-24 03:49:47"}

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Relative Metric

{"start_date"=>"2014-01-01T00:00:00Z", "end_date"=>"2014-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences", "average_usage"=>[291]}, {"subject_area"=>"/Physical sciences", "average_usage"=>[271]}, {"subject_area"=>"/Physical sciences/Physics", "average_usage"=>[266]}]}
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