Catalytic Signature of a Heat-Stable, Chimeric Human Alkaline Phosphatase with Therapeutic Potential
Publication Date
February 24, 2014
Journal
PLOS ONE
Authors
Tina Kiffer Moreira, Campbell R. Sheen, Kellen Cristina Da Silva Gasque, Mayte Bolean, et al
Volume
9
Issue
2
Pages
e89374
DOI
https://dx.plos.org/10.1371/journal.pone.0089374
Publisher URL
http://journals.plos.org/plosone/article?id=10.1371%2Fjournal.pone.0089374
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/24586729
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3933536
Europe PMC
http://europepmc.org/abstract/MED/24586729
Web of Science
000331880700034
Scopus
84897904300
Mendeley
http://www.mendeley.com/research/catalytic-signature-heatstable-chimeric-human-alkaline-phosphatase-therapeutic-potential
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Mendeley | Further Information

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Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1396044"], "description"=>"<p>*Calculated from the exponential decay phase in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0089374#pone-0089374-g004\" target=\"_blank\"><b>Figure 4A</b></a> of main paper. ND: not determined. Computed inactivation rates for the exponential denaturation rates for IAP and ChimAP were similar (see text).</p>", "links"=>[], "tags"=>["biotechnology", "Bioengineering", "developmental biology", "exposed", "guanidinium", "chloride"], "article_id"=>942554, "categories"=>["Biological Sciences"], "users"=>["Tina Kiffer-Moreira", "Campbell R. Sheen", "Kellen Cristina da Silva Gasque", "Mayte Bolean", "Pietro Ciancaglini", "Andrea van Elsas", "Marc F. Hoylaerts", "Jose Luis Millán"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0089374.t004", "stats"=>{"downloads"=>9, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Enzyme_stability_when_exposed_to_guanidinium_chloride_GndCl_or_heat_/942554", "title"=>"Enzyme stability when exposed to guanidinium chloride (GndCl) or heat.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-02-24 02:45:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/1396045"], "description"=>"<p>*p<0.005 vs corresponding IC<sub>50</sub> for IAP and PLAP.</p>", "links"=>[], "tags"=>["biotechnology", "Bioengineering", "developmental biology", "inhibition", "l-amino"], "article_id"=>942555, "categories"=>["Biological Sciences"], "users"=>["Tina Kiffer-Moreira", "Campbell R. Sheen", "Kellen Cristina da Silva Gasque", "Mayte Bolean", "Pietro Ciancaglini", "Andrea van Elsas", "Marc F. Hoylaerts", "Jose Luis Millán"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0089374.t003", "stats"=>{"downloads"=>5, "page_views"=>19, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Uncompetitive_inhibition_with_L_amino_acids_expressed_at_IC_50_177_SD_/942555", "title"=>"Uncompetitive inhibition with L-amino acids, expressed at IC<sub>50</sub> (± SD).", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-02-24 02:45:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/1396046"], "description"=>"1<p>k<sub>cat</sub> values were determined from the rate of P<sub>i</sub> formation.</p>2<p>As the detection of two P<sub>i</sub> corresponds to one cleavage event, the actual rate is only half of the calculated number of P<sub>i</sub> molecules released.</p>", "links"=>[], "tags"=>["biotechnology", "Bioengineering", "developmental biology", "recombinant", "enzymes", "physiological", "substrates"], "article_id"=>942556, "categories"=>["Biological Sciences"], "users"=>["Tina Kiffer-Moreira", "Campbell R. Sheen", "Kellen Cristina da Silva Gasque", "Mayte Bolean", "Pietro Ciancaglini", "Andrea van Elsas", "Marc F. Hoylaerts", "Jose Luis Millán"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0089374.t002", "stats"=>{"downloads"=>1, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Kinetic_parameters_177_SD_of_recombinant_enzymes_with_physiological_substrates_at_physiological_pH_/942556", "title"=>"Kinetic parameters (± SD) of recombinant enzymes with physiological substrates at physiological pH.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-02-24 02:45:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/1396047"], "description"=>"<p>*Historical values, used as internal standards, were taken from our previous study<a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0089374#pone.0089374-Hoylaerts3\" target=\"_blank\">[50]</a>. k<sub>cat</sub> ∼123 s<sup>−1</sup> and ∼5,000 s<sup>−1</sup> for highly active bIAP II at pH 7.4 and pH 9.8, respectively<a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0089374#pone.0089374-Manes1\" target=\"_blank\">[32]</a>. k<sub>cat</sub> values were determined from the rate of p-NPP formation at pH 9.8 and from the rate of P<sub>i</sub> formation at pH 7.4.</p>", "links"=>[], "tags"=>["biotechnology", "Bioengineering", "developmental biology", "constants", "substrate", "p-nitrophenylphosphate", "alkaline", "physiological"], "article_id"=>942557, "categories"=>["Biological Sciences"], "users"=>["Tina Kiffer-Moreira", "Campbell R. Sheen", "Kellen Cristina da Silva Gasque", "Mayte Bolean", "Pietro Ciancaglini", "Andrea van Elsas", "Marc F. Hoylaerts", "Jose Luis Millán"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0089374.t001", "stats"=>{"downloads"=>5, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Enzyme_constants_177_SD_using_the_artificial_substrate_p_nitrophenylphosphate_pNPP_at_alkaline_and_physiological_pH_/942557", "title"=>"Enzyme constants (± SD) using the artificial substrate p-nitrophenylphosphate (pNPP) at alkaline and physiological pH", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2014-02-24 02:45:11"}

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