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  • team
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  • center
  • program_project
  • nrc
  • whocc
  • project
  • software
  • tool
  • patent
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  • Assistant Professor
  • Associate Professor
  • Clinical Research Assistant
  • Clinical Research Nurse
  • Clinician Researcher
  • Department Manager
  • Dual-education Student
  • Full Professor
  • Honorary Professor
  • Lab assistant
  • Master Student
  • Non-permanent Researcher
  • Nursing Staff
  • Permanent Researcher
  • Pharmacist
  • PhD Student
  • Physician
  • Post-doc
  • Prize
  • Project Manager
  • Research Associate
  • Research Engineer
  • Retired scientist
  • Technician
  • Undergraduate Student
  • Veterinary
  • Visiting Scientist
  • Deputy Director of Center
  • Deputy Director of Department
  • Deputy Director of National Reference Center
  • Deputy Head of Facility
  • Director of Center
  • Director of Department
  • Director of Institute
  • Director of National Reference Center
  • Group Leader
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  • Head of Operations
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  • Labex Coordinator
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© Ce graphique présente, pour chaque date d'observation depuis 2018, le taux d'accès ouvert des publications scientifiques de l'Institut Pasteur, avec un DOI Crossref, parues durant l'année précédente.
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Scientific reports - 04 Nov 2019

Nozeret K, Boucharlat A, Agou F, Buddelmeijer N

Link to Pubmed [PMID] – 31685855

Link to DOI – 10.1038/s41598-019-52106-8

Sci Rep 2019 Nov; 9(1): 15978

Lipoprotein modification is an essential process in Gram-negative bacteria. The action of three integral membrane proteins that catalyze the transfer of fatty acids derived from membrane phospholipids or cleave the signal peptide of the lipoprotein substrate result in the formation of mature triacylated proteins. Inactivation of the enzymes leads to mis-localization of immature lipoproteins and consequently cell death. Biochemical studies and the development of in vitro assays are challenging due to the fact that the enzymes and substrates are all membrane-embedded proteins difficult to overproduce and purify. Here we describe a sensitive fluorescence-based assay to monitor bacterial apolipoprotein N-acyltransferase activity.