Enzymatic data underpinning S5B Fig in Excel format.

<p>Enzymatic data underpinning <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003427#pbio.3003427.s008" target="_blank">S5B Fig</a> in Excel format.</p>

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Autor Principal: Martin B. L. McAndrew (22683641) (author)
Outros autores: Jonathan Cook (3435386) (author), Amy Gill (14910614) (author), Kavya Sahoo (22683644) (author), Clare Thomas (7943747) (author), Phillip J. Stansfeld (1267617) (author), Allister Crow (263807) (author)
Publicado: 2025
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author Martin B. L. McAndrew (22683641)
author2 Jonathan Cook (3435386)
Amy Gill (14910614)
Kavya Sahoo (22683644)
Clare Thomas (7943747)
Phillip J. Stansfeld (1267617)
Allister Crow (263807)
author2_role author
author
author
author
author
author
author_facet Martin B. L. McAndrew (22683641)
Jonathan Cook (3435386)
Amy Gill (14910614)
Kavya Sahoo (22683644)
Clare Thomas (7943747)
Phillip J. Stansfeld (1267617)
Allister Crow (263807)
author_role author
dc.creator.none.fl_str_mv Martin B. L. McAndrew (22683641)
Jonathan Cook (3435386)
Amy Gill (14910614)
Kavya Sahoo (22683644)
Clare Thomas (7943747)
Phillip J. Stansfeld (1267617)
Allister Crow (263807)
dc.date.none.fl_str_mv 2025-11-25T18:40:08Z
dc.identifier.none.fl_str_mv 10.1371/journal.pbio.3003427.s029
dc.relation.none.fl_str_mv https://figshare.com/articles/dataset/Enzymatic_data_underpinning_S5B_Fig_in_Excel_format_/30714845
dc.rights.none.fl_str_mv CC BY 4.0
info:eu-repo/semantics/openAccess
dc.subject.none.fl_str_mv Biophysics
Biochemistry
Microbiology
Cell Biology
Molecular Biology
Biotechnology
Developmental Biology
Cancer
Hematology
Biological Sciences not elsewhere classified
Chemical Sciences not elsewhere classified
Information Systems not elsewhere classified
tolc efflux pump
multifunctional hydrolytic enzyme
extracts hydrophobic compounds
extracting hydrophobic molecules
capture implied long
bacterial cell envelope
active site residues
lipid hydrolase complex
escherichia coli </
data suggests ybbap
abc superfamily ’
div >< p
coli </
abc superfamily
thioester substrates
tesa complex
structural characterization
remarkable diversity
new function
mechanotransmission mechanism
inner membrane
extensively characterized
experimentally confirm
complete ybbap
>, three
dc.title.none.fl_str_mv Enzymatic data underpinning S5B Fig in Excel format.
dc.type.none.fl_str_mv Dataset
info:eu-repo/semantics/publishedVersion
dataset
description <p>Enzymatic data underpinning <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003427#pbio.3003427.s008" target="_blank">S5B Fig</a> in Excel format.</p>
eu_rights_str_mv openAccess
id Manara_793304ec89ab60c799445e4dbdd025c6
identifier_str_mv 10.1371/journal.pbio.3003427.s029
network_acronym_str Manara
network_name_str ManaraRepo
oai_identifier_str oai:figshare.com:article/30714845
publishDate 2025
repository.mail.fl_str_mv
repository.name.fl_str_mv
repository_id_str
rights_invalid_str_mv CC BY 4.0
spelling Enzymatic data underpinning S5B Fig in Excel format.Martin B. L. McAndrew (22683641)Jonathan Cook (3435386)Amy Gill (14910614)Kavya Sahoo (22683644)Clare Thomas (7943747)Phillip J. Stansfeld (1267617)Allister Crow (263807)BiophysicsBiochemistryMicrobiologyCell BiologyMolecular BiologyBiotechnologyDevelopmental BiologyCancerHematologyBiological Sciences not elsewhere classifiedChemical Sciences not elsewhere classifiedInformation Systems not elsewhere classifiedtolc efflux pumpmultifunctional hydrolytic enzymeextracts hydrophobic compoundsextracting hydrophobic moleculescapture implied longbacterial cell envelopeactive site residueslipid hydrolase complexescherichia coli </data suggests ybbapabc superfamily ’div >< pcoli </abc superfamilythioester substratestesa complexstructural characterizationremarkable diversitynew functionmechanotransmission mechanisminner membraneextensively characterizedexperimentally confirmcomplete ybbap>, three<p>Enzymatic data underpinning <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003427#pbio.3003427.s008" target="_blank">S5B Fig</a> in Excel format.</p>2025-11-25T18:40:08ZDatasetinfo:eu-repo/semantics/publishedVersiondataset10.1371/journal.pbio.3003427.s029https://figshare.com/articles/dataset/Enzymatic_data_underpinning_S5B_Fig_in_Excel_format_/30714845CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/307148452025-11-25T18:40:08Z
spellingShingle Enzymatic data underpinning S5B Fig in Excel format.
Martin B. L. McAndrew (22683641)
Biophysics
Biochemistry
Microbiology
Cell Biology
Molecular Biology
Biotechnology
Developmental Biology
Cancer
Hematology
Biological Sciences not elsewhere classified
Chemical Sciences not elsewhere classified
Information Systems not elsewhere classified
tolc efflux pump
multifunctional hydrolytic enzyme
extracts hydrophobic compounds
extracting hydrophobic molecules
capture implied long
bacterial cell envelope
active site residues
lipid hydrolase complex
escherichia coli </
data suggests ybbap
abc superfamily ’
div >< p
coli </
abc superfamily
thioester substrates
tesa complex
structural characterization
remarkable diversity
new function
mechanotransmission mechanism
inner membrane
extensively characterized
experimentally confirm
complete ybbap
>, three
status_str publishedVersion
title Enzymatic data underpinning S5B Fig in Excel format.
title_full Enzymatic data underpinning S5B Fig in Excel format.
title_fullStr Enzymatic data underpinning S5B Fig in Excel format.
title_full_unstemmed Enzymatic data underpinning S5B Fig in Excel format.
title_short Enzymatic data underpinning S5B Fig in Excel format.
title_sort Enzymatic data underpinning S5B Fig in Excel format.
topic Biophysics
Biochemistry
Microbiology
Cell Biology
Molecular Biology
Biotechnology
Developmental Biology
Cancer
Hematology
Biological Sciences not elsewhere classified
Chemical Sciences not elsewhere classified
Information Systems not elsewhere classified
tolc efflux pump
multifunctional hydrolytic enzyme
extracts hydrophobic compounds
extracting hydrophobic molecules
capture implied long
bacterial cell envelope
active site residues
lipid hydrolase complex
escherichia coli </
data suggests ybbap
abc superfamily ’
div >< p
coli </
abc superfamily
thioester substrates
tesa complex
structural characterization
remarkable diversity
new function
mechanotransmission mechanism
inner membrane
extensively characterized
experimentally confirm
complete ybbap
>, three