Your browser doesn't support javascript.
loading
Enzyme promiscuity shapes adaptation to novel growth substrates.
Guzmán, Gabriela I; Sandberg, Troy E; LaCroix, Ryan A; Nyerges, Ákos; Papp, Henrietta; de Raad, Markus; King, Zachary A; Hefner, Ying; Northen, Trent R; Notebaart, Richard A; Pál, Csaba; Palsson, Bernhard O; Papp, Balázs; Feist, Adam M.
Affiliation
  • Guzmán GI; Department of Bioengineering, University of California, San Diego, La Jolla, CA, USA.
  • Sandberg TE; Department of Bioengineering, University of California, San Diego, La Jolla, CA, USA.
  • LaCroix RA; Department of Bioengineering, University of California, San Diego, La Jolla, CA, USA.
  • Nyerges Á; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Papp H; Virological Research Group, Szentágothai Research Centre University of Pécs, Pécs, Hungary.
  • de Raad M; Environmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory Berkeley, Berkeley, CA, USA.
  • King ZA; Department of Bioengineering, University of California, San Diego, La Jolla, CA, USA.
  • Hefner Y; Department of Bioengineering, University of California, San Diego, La Jolla, CA, USA.
  • Northen TR; Environmental Genomics and Systems Biology Division, Lawrence Berkeley National Laboratory Berkeley, Berkeley, CA, USA.
  • Notebaart RA; Laboratory of Food Microbiology, Wageningen University and Research, Wageningen, The Netherlands.
  • Pál C; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Palsson BO; Department of Bioengineering, University of California, San Diego, La Jolla, CA, USA.
  • Papp B; Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Lyngby, Denmark.
  • Feist AM; Department of Pediatrics, University of California, San Diego, La Jolla, CA, USA.
Mol Syst Biol ; 15(4): e8462, 2019 04 08.
Article in En | MEDLINE | ID: mdl-30962359
Subject(s)
Key words
Fulltext
Add to My VHL
Print
XML
PubMed Links
Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Escherichia coli K12 / Enzymes / Mutation Type of study: Prognostic_studies Language: En Journal: Mol Syst Biol Journal subject: BIOLOGIA MOLECULAR / BIOTECNOLOGIA Year: 2019 Document type: Article Affiliation country: Country of publication:
Fulltext
Add to My VHL
Print
XML
PubMed Links
Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Escherichia coli K12 / Enzymes / Mutation Type of study: Prognostic_studies Language: En Journal: Mol Syst Biol Journal subject: BIOLOGIA MOLECULAR / BIOTECNOLOGIA Year: 2019 Document type: Article Affiliation country: Country of publication: