Construction of a Xylanase A Variant Capable of Polymerization
Publication Date
September 23, 2011
Journal
PLOS ONE
Authors
Veronika Szabó, Adél Muskotál, Balázs Tóth, Marko D. Mihovilovic, et al
Volume
6
Issue
9
Pages
e25388
DOI
https://dx.plos.org/10.1371/journal.pone.0025388
Publisher URL
http://journals.plos.org/plosone/article?id=10.1371%2Fjournal.pone.0025388
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/21966517
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3179519
Europe PMC
http://europepmc.org/abstract/MED/21966517
Web of Science
000295267100054
Scopus
80053098632
Mendeley
http://www.mendeley.com/research/construction-xylanase-variant-capable-polymerization
Events
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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/732582"], "description"=>"<p>The hypervariable D3 domain of Salmonella flagellin (residues 190–284) was replaced by xylanase A from <i>B. subtilis</i>. The C<sub>α</sub> backbone trace of flagellin and XynA is rainbow-colored from blue to red representing the sequence from the NH<sub>2</sub>- to COOH terminus.</p>", "links"=>[], "tags"=>["fusion"], "article_id"=>402929, "categories"=>["Biotechnology", "Biochemistry", "Biophysics"], "users"=>["Veronika Szabó", "Adél Muskotál", "Balázs Tóth", "Marko D. Mihovilovic", "Ferenc Vonderviszt"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025388.g001", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Design_of_the_FliC_XynA_fusion_construct_/402929", "title"=>"Design of the FliC(XynA) fusion construct.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 14:30:24"}
  • {"files"=>["https://ndownloader.figshare.com/files/732797"], "description"=>"<p>(A) Copolymers of flagellin and FliC(XynA) obtained by 0.6 M AS at 1∶1 mixing ratio (w/w) were incubated with trypsin at a 30∶1 (w/w) ratio. (B) Proteolysis of monomeric FliC(XynA) at a protein to protease ratio of 300∶1 (w/w). At the indicated time points, portions were removed from the reaction mixtures, mixed with electrophoresis sample buffer and boiled for 3 min. Experiments were done in 20 mM Tris–HCl, 150 mM NaCl (pH 7.8) at room temperature at a 1 mg/ml protein concentration.</p>", "links"=>[], "tags"=>["polymeric", "monomeric"], "article_id"=>403149, "categories"=>["Biotechnology", "Biochemistry", "Biophysics"], "users"=>["Veronika Szabó", "Adél Muskotál", "Balázs Tóth", "Marko D. Mihovilovic", "Ferenc Vonderviszt"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025388.g003", "stats"=>{"downloads"=>1, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Proteolytic_sensitivity_of_FliC_XynA_in_the_polymeric_and_monomeric_form_/403149", "title"=>"Proteolytic sensitivity of FliC(XynA) in the polymeric and monomeric form.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 14:31:34"}
  • {"files"=>["https://ndownloader.figshare.com/files/732863"], "description"=>"<p>Measurements were done at 1.2 µM enzyme (catalytic unit) concentration in 50 mM phosphate buffer (pH 6.0) at 37°C. The amount of FliC(XynA) subunits incorporated into the copolymers was estimated by densitometric analysis of SDS-PA gels of filament samples.</p>", "links"=>[], "tags"=>["recombinant", "xylanase", "fusion", "monomeric", "polymeric"], "article_id"=>403213, "categories"=>["Biotechnology", "Biochemistry", "Biophysics"], "users"=>["Veronika Szabó", "Adél Muskotál", "Balázs Tóth", "Marko D. Mihovilovic", "Ferenc Vonderviszt"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025388.t001", "stats"=>{"downloads"=>1, "page_views"=>31, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Catalytic_activity_of_recombinant_xylanase_A_and_the_FliC_XynA_fusion_protein_in_the_monomeric_and_polymeric_forms_/403213", "title"=>"Catalytic activity of recombinant xylanase A and the FliC(XynA) fusion protein in the monomeric and polymeric forms.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-20 14:31:54"}
  • {"files"=>["https://ndownloader.figshare.com/files/732680"], "description"=>"<p>Dark-field light micrographs of (A) FliC(XynA) filaments (0.6 M AS) and (B) copolymers of flagellin and FliC(XynA) at 1∶1 (w∶w) mixing ratio (0.4 M AS). Polymerization experiments were done in 20 mM Tris-HCl (pH 7.8) containing 150 mM NaCl at 1 to 1.5 mg/ml protein concentration, and 4 M AS was added to a final concentration indicated in parentheses to initiate filament formation. (C) SDS/PAGE analysis of copolymer samples polymerized at FliC(XynA) to flagellin ratios of 1∶1 and 1∶2. After AS-induced (0.6 M) polymerization, samples were centrifuged and the pellet was dissolved in 20 mM Tris-HCl (pH 7.8) buffer containing 150 mM NaCl. The molecular masses of flagellin and FliC(XynA) are 51.5 kDa and 64 kDa, respectively. Band intensities determined by densitometry were {49.3 (1∶1); 50.7 (1∶2)} and {49.6 (1∶1) and 34.2 (1∶2)} for FliC and FliC(XynA), respectively. (D) Copolymers observed by atomic force microscopy.</p>", "links"=>[], "tags"=>["polymerization"], "article_id"=>403039, "categories"=>["Biotechnology", "Biochemistry", "Biophysics"], "users"=>["Veronika Szabó", "Adél Muskotál", "Balázs Tóth", "Marko D. Mihovilovic", "Ferenc Vonderviszt"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0025388.g002", "stats"=>{"downloads"=>1, "page_views"=>41, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Products_of_the_polymerization_of_FliC_XynA_subunits_/403039", "title"=>"Products of the polymerization of FliC(XynA) subunits.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-20 14:30:59"}

PMC Usage Stats | Further Information

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Relative Metric

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