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{"title"=>"Contribution of Specific Residues of the β-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability", "type"=>"journal", "authors"=>[{"first_name"=>"Asen", "last_name"=>"Daskalov", "scopus_author_id"=>"6506033314"}, {"first_name"=>"Matthias", "last_name"=>"Gantner", "scopus_author_id"=>"56237467100"}, {"first_name"=>"Marielle Aulikki", "last_name"=>"Wälti", "scopus_author_id"=>"56084731500"}, {"first_name"=>"Thierry", "last_name"=>"Schmidlin", "scopus_author_id"=>"56237594000"}, {"first_name"=>"Celestine N.", "last_name"=>"Chi", "scopus_author_id"=>"15756726400"}, {"first_name"=>"Christian", "last_name"=>"Wasmer", "scopus_author_id"=>"23978869100"}, {"first_name"=>"Anne", "last_name"=>"Schütz", "scopus_author_id"=>"35196971100"}, {"first_name"=>"Johanna", "last_name"=>"Ceschin", "scopus_author_id"=>"50760969900"}, {"first_name"=>"Corinne", "last_name"=>"Clavé", "scopus_author_id"=>"6603052293"}, {"first_name"=>"Sandra", "last_name"=>"Cescau", "scopus_author_id"=>"16311901800"}, {"first_name"=>"Beat", "last_name"=>"Meier", "scopus_author_id"=>"7201655952"}, {"first_name"=>"Roland", "last_name"=>"Riek", "scopus_author_id"=>"7004321158"}, {"first_name"=>"Sven J.", "last_name"=>"Saupe", "scopus_author_id"=>"7004535582"}], "year"=>2014, "source"=>"PLoS Pathogens", "identifiers"=>{"scopus"=>"2-s2.0-84903464851", "doi"=>"10.1371/journal.ppat.1004158", "sgr"=>"84903464851", "isbn"=>"1553-7374 (Electronic)\\r1553-7366 (Linking)", "pmid"=>"24945274", "issn"=>"15537374", "pui"=>"373412656"}, "id"=>"83098fdd-7d9a-380b-a917-744d70775dfa", "abstract"=>"The [Het-s] prion of the fungus Podospora anserina represents a good model system for studying the structure-function relationship in amyloid proteins because a high resolution solid-state NMR structure of the amyloid prion form of the HET-s prion forming domain (PFD) is available. The HET-s PFD adopts a specific β-solenoid fold with two rungs of β-strands delimiting a triangular hydrophobic core. A C-terminal loop folds back onto the rigid core region and forms a more dynamic semi-hydrophobic pocket extending the hydrophobic core. Herein, an alanine scanning mutagenesis of the HET-s PFD was conducted. Different structural elements identified in the prion fold such as the triangular hydrophobic core, the salt bridges, the asparagines ladders and the C-terminal loop were altered and the effect of these mutations on prion function, fibril structure and stability was assayed. Prion activity and structure were found to be very robust; only a few key mutations were able to corrupt structure and function. While some mutations strongly destabilize the fold, many substitutions in fact increase stability of the fold. This increase in structural stability did not influence prion formation propensity in vivo. However, if an Ala replacement did alter the structure of the core or did influence the shape of the denaturation curve, the corresponding variant showed a decreased prion efficacy. It is also the finding that in addition to the structural elements of the rigid core region, the aromatic residues in the C-terminal semi-hydrophobic pocket are critical for prion propagation. Mutations in the latter region either positively or negatively affected prion formation. We thus identify a region that modulates prion formation although it is not part of the rigid cross-β core, an observation that might be relevant to other amyloid models. © 2014 Daskalov et al.", "link"=>"http://www.mendeley.com/research/contribution-specific-residues-%CE%B2solenoid-fold-hets-prion-function-amyloid-structure-stability", "reader_count"=>27, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Professor > Associate Professor"=>2, "Librarian"=>1, "Researcher"=>7, "Student > Ph. D. Student"=>7, "Other"=>1, "Student > Master"=>3, "Lecturer > Senior Lecturer"=>1, "Professor"=>4}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Professor > Associate Professor"=>2, "Librarian"=>1, "Researcher"=>7, "Student > Ph. D. Student"=>7, "Other"=>1, "Student > Master"=>3, "Lecturer > Senior Lecturer"=>1, "Professor"=>4}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>6, "Agricultural and Biological Sciences"=>12, "Medicine and Dentistry"=>2, "Neuroscience"=>1, "Chemistry"=>5}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Neuroscience"=>{"Neuroscience"=>1}, "Chemistry"=>{"Chemistry"=>5}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>12}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>6}, "Unspecified"=>{"Unspecified"=>1}}, "reader_count_by_country"=>{"Switzerland"=>1, "Russia"=>1}, "group_count"=>1}

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• http://doi.org/10.1080/19336896.2015.1038018
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• http://doi.org/10.1002/cbic.201800664
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• http://doi.org/10.1101/cshperspect.a023515

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Figshare

• {"files"=>["https://ndownloader.figshare.com/files/1532981"], "description"=>"<p>The GuHCl denaturation curve of amyloid fibrils of HET-s(218–289) and Ala variants (as indicated) were measured by the OD₅₀₀ (y-axis) at various GuHCl concentration (x-axis) after incubation in the corresponding GuHCl buffers for one day. The change of the OD₅₀₀ value is indicative of the loss of large aggregated protein species. Three samples each were incubated and the individual measurements are highlighted by asterisks, by small dots, or by open circles, respectively. Individual successful fits following the concept by Santoro and Bolen to study protein folding and unfolding <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004158#ppat.1004158-Santoro1\" target=\"_blank\">[61]</a> are shown by black lines and the calculated change in Gibbs energy (ΔG) with its standard deviation from the three measurements are listed in <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004158#ppat-1004158-t003\" target=\"_blank\">Table 3</a>.</p>", "links"=>[], "tags"=>["microbiology", "Microbial physiology", "Fungal physiology", "Biochemistry", "proteins", "Defense proteins", "prions", "protein structure", "Mycology", "unfolding", "amyloid", "fibrils", "ala", "variants"], "article_id"=>1055936, "categories"=>["Biological Sciences"], "users"=>["Asen Daskalov", "Matthias Gantner", "Marielle Aulikki Wälti", "Thierry Schmidlin", "Celestine N. Chi", "Christian Wasmer", "Anne Schütz", "Johanna Ceschin", "Corinne Clavé", "Sandra Cescau", "Beat Meier", "Roland Riek", "Sven J. Saupe"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1004158.g005", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_GuHCl_unfolding_measurements_of_HET_s_218_8211_289_amyloid_fibrils_and_Ala_variants_thereof_/1055936", "title"=>"GuHCl unfolding measurements of HET-s(218–289) amyloid fibrils and Ala variants thereof.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-06-12 03:23:16"}
• {"files"=>["https://ndownloader.figshare.com/files/1532930"], "description"=>"<p><b>A.</b> For wt and each mutant, the rate of [Het-s] propagation was measured in the experimental setting in which the length of the barrage line gives the distance of [Het-s] spreading in a period of 10 hours. <b>B.</b> Mean propagation distance in at least 4 experiments with standard deviation.</p>", "links"=>[], "tags"=>["microbiology", "Microbial physiology", "Fungal physiology", "Biochemistry", "proteins", "Defense proteins", "prions", "protein structure", "Mycology", "integrants", "alanine"], "article_id"=>1055899, "categories"=>["Biological Sciences"], "users"=>["Asen Daskalov", "Matthias Gantner", "Marielle Aulikki Wälti", "Thierry Schmidlin", "Celestine N. Chi", "Christian Wasmer", "Anne Schütz", "Johanna Ceschin", "Corinne Clavé", "Sandra Cescau", "Beat Meier", "Roland Riek", "Sven J. Saupe"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1004158.g003", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Propagation_rate_of_Het_s_in_single_copy_integrants_of_alanine_mutants_/1055899", "title"=>"Propagation rate of [Het-s] in single copy integrants of alanine mutants.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-06-12 03:23:16"}
• {"files"=>["https://ndownloader.figshare.com/files/1532996"], "description"=>"<p>*these mutants are unable to propagate [Het-s] even after infection by wt [Het-s].</p><p>**p-value is calculated in a two-tailed Fisher's test, n.s. non significant.</p>", "links"=>[], "tags"=>["microbiology", "Microbial physiology", "Fungal physiology", "Biochemistry", "proteins", "Defense proteins", "prions", "protein structure", "Mycology", "prion", "alanine", "mutants"], "article_id"=>1055945, "categories"=>["Biological Sciences"], "users"=>["Asen Daskalov", "Matthias Gantner", "Marielle Aulikki Wälti", "Thierry Schmidlin", "Celestine N. Chi", "Christian Wasmer", "Anne Schütz", "Johanna Ceschin", "Corinne Clavé", "Sandra Cescau", "Beat Meier", "Roland Riek", "Sven J. Saupe"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1004158.t001", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Spontaneous_Het_s_prion_formation_rate_for_alanine_mutants_of_HET_s_/1055945", "title"=>"Spontaneous [Het-s] prion formation rate for alanine mutants of HET-s.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-06-12 03:23:16"}
• {"files"=>["https://ndownloader.figshare.com/files/1532995"], "description"=>"<p>Infectivity of recombinant HET-s(218-289) F286A and W287 fibrils.</p>", "links"=>[], "tags"=>["microbiology", "Microbial physiology", "Fungal physiology", "Biochemistry", "proteins", "Defense proteins", "prions", "protein structure", "Mycology", "recombinant", "f286a", "w287"], "article_id"=>1055944, "categories"=>["Biological Sciences"], "users"=>["Asen Daskalov", "Matthias Gantner", "Marielle Aulikki Wälti", "Thierry Schmidlin", "Celestine N. Chi", "Christian Wasmer", "Anne Schütz", "Johanna Ceschin", "Corinne Clavé", "Sandra Cescau", "Beat Meier", "Roland Riek", "Sven J. Saupe"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1004158.t004", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Infectivity_of_recombinant_HET_s_218_289_F286A_and_W287_fibrils_/1055944", "title"=>"Infectivity of recombinant HET-s(218-289) F286A and W287 fibrils.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-06-12 03:23:16"}
• {"files"=>["https://ndownloader.figshare.com/files/1532993"], "description"=>"<p>HET-s-GFP F286A and W287A were expressed in <i>Δhet-s P. anserina</i> strain or the same strain over-expressing wild-type HET-s. Note that both mutants are unable to form dot-like aggregates in <i>Δhet-s</i> but can be incorporated in dot-like aggregates in the presence of wild-type HET-s.</p>", "links"=>[], "tags"=>["microbiology", "Microbial physiology", "Fungal physiology", "Biochemistry", "proteins", "Defense proteins", "prions", "protein structure", "Mycology", "het-s-gfp", "f286a", "w287a", "fusion"], "article_id"=>1055942, "categories"=>["Biological Sciences"], "users"=>["Asen Daskalov", "Matthias Gantner", "Marielle Aulikki Wälti", "Thierry Schmidlin", "Celestine N. Chi", "Christian Wasmer", "Anne Schütz", "Johanna Ceschin", "Corinne Clavé", "Sandra Cescau", "Beat Meier", "Roland Riek", "Sven J. Saupe"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1004158.g006", "stats"=>{"downloads"=>0, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Expression_of_a_HET_s_GFP_F286A_and_W287A_fusion_proteins_in_P_anserine_/1055942", "title"=>"Expression of a HET-s-GFP F286A and W287A fusion proteins in <i>P. anserine</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-06-12 03:23:16"}
• {"files"=>["https://ndownloader.figshare.com/files/1532917"], "description"=>"<p><b>A.</b> The structure of the first pseudo repeat (residue 226–246) as well as the second repeat and the C-terminal loop region (residue 262–289) are given (after PDB 2KJ3). The 32 residues that have been mutated are coloured. Colour coding is as follows, polar residues in green, hydrophobic in blue, aromatic in cyan, positively charge in red, negatively charged in magenta and glycine in yellow. <b>B.</b> Sequence alignment of the PFD region of various HET-S homologs from various fungal species. The 21 amino acid repeats are boxed. The position of the β-strands of the β-solenoid core is represented as blue arrows <b>C.</b> Consensus sequence of the first and second repeats of the HET-S homologs presented in the alignment in B. The consensus was generated using MEME. In this graphical representation, the size of the letter reflects the level of conservation of the corresponding residue, the scale is given in information content measured in bits.</p>", "links"=>[], "tags"=>["microbiology", "Microbial physiology", "Fungal physiology", "Biochemistry", "proteins", "Defense proteins", "prions", "protein structure", "Mycology", "het-s", "prion"], "article_id"=>1055889, "categories"=>["Biological Sciences"], "users"=>["Asen Daskalov", "Matthias Gantner", "Marielle Aulikki Wälti", "Thierry Schmidlin", "Celestine N. Chi", "Christian Wasmer", "Anne Schütz", "Johanna Ceschin", "Corinne Clavé", "Sandra Cescau", "Beat Meier", "Roland Riek", "Sven J. Saupe"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1004158.g001", "stats"=>{"downloads"=>2, "page_views"=>22, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structure_and_sequence_conservation_of_the_HET_s_prion_forming_domain_/1055889", "title"=>"Structure and sequence conservation of the HET-s prion forming domain.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-06-12 03:23:16"}
• {"files"=>["https://ndownloader.figshare.com/files/1533112", "https://ndownloader.figshare.com/files/1533113", "https://ndownloader.figshare.com/files/1533115", "https://ndownloader.figshare.com/files/1533117", "https://ndownloader.figshare.com/files/1533119", "https://ndownloader.figshare.com/files/1533120"], "description"=>"<div><p>The [Het-s] prion of the fungus <i>Podospora anserina</i> represents a good model system for studying the structure-function relationship in amyloid proteins because a high resolution solid-state NMR structure of the amyloid prion form of the HET-s prion forming domain (PFD) is available. The HET-s PFD adopts a specific β-solenoid fold with two rungs of β-strands delimiting a triangular hydrophobic core. A C-terminal loop folds back onto the rigid core region and forms a more dynamic semi-hydrophobic pocket extending the hydrophobic core. Herein, an alanine scanning mutagenesis of the HET-s PFD was conducted. Different structural elements identified in the prion fold such as the triangular hydrophobic core, the salt bridges, the asparagines ladders and the C-terminal loop were altered and the effect of these mutations on prion function, fibril structure and stability was assayed. Prion activity and structure were found to be very robust; only a few key mutations were able to corrupt structure and function. While some mutations strongly destabilize the fold, many substitutions in fact increase stability of the fold. This increase in structural stability did not influence prion formation propensity <i>in vivo</i>. However, if an Ala replacement did alter the structure of the core or did influence the shape of the denaturation curve, the corresponding variant showed a decreased prion efficacy. It is also the finding that in addition to the structural elements of the rigid core region, the aromatic residues in the C-terminal semi-hydrophobic pocket are critical for prion propagation. Mutations in the latter region either positively or negatively affected prion formation. We thus identify a region that modulates prion formation although it is not part of the rigid cross-β core, an observation that might be relevant to other amyloid models.</p></div>", "links"=>[], "tags"=>["microbiology", "Microbial physiology", "Fungal physiology", "Biochemistry", "proteins", "Defense proteins", "prions", "protein structure", "Mycology", "residues", "het-s", "prion", "amyloid"], "article_id"=>1056043, "categories"=>["Biological Sciences"], "users"=>["Asen Daskalov", "Matthias Gantner", "Marielle Aulikki Wälti", "Thierry Schmidlin", "Celestine N. Chi", "Christian Wasmer", "Anne Schütz", "Johanna Ceschin", "Corinne Clavé", "Sandra Cescau", "Beat Meier", "Roland Riek", "Sven J. Saupe"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1004158.s001", "https://dx.doi.org/10.1371/journal.ppat.1004158.s002", "https://dx.doi.org/10.1371/journal.ppat.1004158.s003", "https://dx.doi.org/10.1371/journal.ppat.1004158.s004", "https://dx.doi.org/10.1371/journal.ppat.1004158.s005", "https://dx.doi.org/10.1371/journal.ppat.1004158.s006"], "stats"=>{"downloads"=>2, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Contribution_of_Specific_Residues_of_the_946_Solenoid_Fold_to_HET_s_Prion_Function_Amyloid_Structure_and_Stability_/1056043", "title"=>"Contribution of Specific Residues of the β-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2014-06-12 03:23:16"}
• {"files"=>["https://ndownloader.figshare.com/files/1532978"], "description"=>"<p>The 2D DARR solid state NMR spectra of ¹⁵N,¹³C-labeled Ala variants of HET-S(218–289) amyloid fibrils are shown on top of the corresponding spectrum of wild-type HET-s(218–289) amyloid fibrils, the latter which contour lines are color-coded black. The spectra are labelled according to the amino acid replacement. The close resemblance between the variant and the wild-type spectra indicates the conservation of the β-solenoid fold in the variants with the exception for G278A and the double variant F286A/W287A. In <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004158#ppat.1004158.s003\" target=\"_blank\">Figure S3</a> the same spectra are shown including the assignment of wild-type HET-s(218–289) amyloid fibrils <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004158#ppat.1004158-Wasmer1\" target=\"_blank\">[29]</a>.</p>", "links"=>[], "tags"=>["microbiology", "Microbial physiology", "Fungal physiology", "Biochemistry", "proteins", "Defense proteins", "prions", "protein structure", "Mycology", "nmr", "spectra", "ala", "variants", "amyloid"], "article_id"=>1055933, "categories"=>["Biological Sciences"], "users"=>["Asen Daskalov", "Matthias Gantner", "Marielle Aulikki Wälti", "Thierry Schmidlin", "Celestine N. Chi", "Christian Wasmer", "Anne Schütz", "Johanna Ceschin", "Corinne Clavé", "Sandra Cescau", "Beat Meier", "Roland Riek", "Sven J. Saupe"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1004158.g004", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_2D_Solid_state_NMR_spectra_of_Ala_variants_of_HET_s_218_8211_289_amyloid_fibrils_/1055933", "title"=>"2D Solid state NMR spectra of Ala variants of HET-s(218–289) amyloid fibrils.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-06-12 03:23:16"}
• {"files"=>["https://ndownloader.figshare.com/files/1532998"], "description"=>"(a)<p>The ΔG value was obtained using the m-value of the wt unless stated in the fourth column that the curve fitting was improved with a free m-value different from the corresponding wt one.</p>(b)<p>The ΔG value was obtained using a free m-value. Two different denaturation curves were obtained and their individual ΔG values are listed.</p>", "links"=>[], "tags"=>["microbiology", "Microbial physiology", "Fungal physiology", "Biochemistry", "proteins", "Defense proteins", "prions", "protein structure", "Mycology", "unfolding", "amyloid"], "article_id"=>1055947, "categories"=>["Biological Sciences"], "users"=>["Asen Daskalov", "Matthias Gantner", "Marielle Aulikki Wälti", "Thierry Schmidlin", "Celestine N. Chi", "Christian Wasmer", "Anne Schütz", "Johanna Ceschin", "Corinne Clavé", "Sandra Cescau", "Beat Meier", "Roland Riek", "Sven J. Saupe"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1004158.t003", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Gibbs_free_unfolding_energy_of_HET_s_218_8211_289_amyloid_fibrils_/1055947", "title"=>"Gibbs free unfolding energy of HET-s(218–289) amyloid fibrils.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-06-12 03:23:16"}
• {"files"=>["https://ndownloader.figshare.com/files/1532997"], "description"=>"<p>*p-value is calculated in a two-tailed Fisher's test.</p>", "links"=>[], "tags"=>["microbiology", "Microbial physiology", "Fungal physiology", "Biochemistry", "proteins", "Defense proteins", "prions", "protein structure", "Mycology", "mutants"], "article_id"=>1055946, "categories"=>["Biological Sciences"], "users"=>["Asen Daskalov", "Matthias Gantner", "Marielle Aulikki Wälti", "Thierry Schmidlin", "Celestine N. Chi", "Christian Wasmer", "Anne Schütz", "Johanna Ceschin", "Corinne Clavé", "Sandra Cescau", "Beat Meier", "Roland Riek", "Sven J. Saupe"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1004158.t002", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Spore_killing_activity_of_selected_het_s_mutants_in_a_cross_a_with_het_S_male_parent_/1055946", "title"=>"Spore-killing activity of selected <i>het-s</i> mutants in a cross a with <i>het-S</i> male parent.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-06-12 03:23:16"}
• {"files"=>["https://ndownloader.figshare.com/files/1532924"], "description"=>"<p><i>Δhet-s</i> strain was transformed with the given mutants and the fraction of transformants producing a barrage reaction to [Het-S] (dark grey) and able to convert a [Het-s*] to the prion phenotype (light grey) is given in %. The mutants were grouped into three functional groups: mutants with wild-type or close to wild-type activity (>60%) were labeled by a green dot, slightly affected mutants (>30, <60%) were labeled by an orange dot, and strongly affected mutants (<30%) by a red dot, respectively. The “*” sign indicates that no transformant displayed the given activity.</p>", "links"=>[], "tags"=>["microbiology", "Microbial physiology", "Fungal physiology", "Biochemistry", "proteins", "Defense proteins", "prions", "protein structure", "Mycology", "alanine", "mutations"], "article_id"=>1055895, "categories"=>["Biological Sciences"], "users"=>["Asen Daskalov", "Matthias Gantner", "Marielle Aulikki Wälti", "Thierry Schmidlin", "Celestine N. Chi", "Christian Wasmer", "Anne Schütz", "Johanna Ceschin", "Corinne Clavé", "Sandra Cescau", "Beat Meier", "Roland Riek", "Sven J. Saupe"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1004158.g002", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Effect_of_alanine_mutations_on_Het_s_activity_in_vivo_/1055895", "title"=>"Effect of alanine mutations on [Het-s] activity <i>in vivo</i>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2014-06-12 03:23:16"}

PMC Usage Stats | Further Information

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Relative Metric

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F1000Prime