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@ARTICLE{Sengupta:57344,
      author       = {Sengupta, K. and Limozin, L. and Tristl, M. and Haase, I.
                      and Fischer, M. and Sackmann, E.},
      title        = {{C}oupling artificial actin cortices to bio-functionalised
                      lipid monolayers},
      journal      = {Langmuir},
      volume       = {22},
      issn         = {0743-7463},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {PreJuSER-57344},
      pages        = {5776 - 5785},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {We report the assembly of protein supramolecular structures
                      at an air-water interface and coupling of artificial actin
                      cortices to such structures. The coupling strategies adopted
                      include electrostatic binding of actin to monolayers doped
                      with lipids, exposing positively charged poly(ethylene
                      glycol) headgroups; binding of biotinylated actin to lipids
                      carrying biotin headgroups through avidin; binding of actin
                      to membranes through biotinylated hisactophilin (a cellular
                      actin-membrane coupler) using an avidin-biotin linkage; and
                      coupling of actin to membranes carrying chelating lipids
                      through a 15-nm-diameter protein capsid (bacterial lumazine
                      synthase or LuSy) exhibiting histidine tags (which bind both
                      to actin and to the chelating lipid). The distribution of
                      the proteins in a direction normal to the interface was
                      measured by neutron reflectivity under different conditions
                      of pH and ionic strength. In the case of the first three
                      binding methods, the thickness of the actin film was found
                      to correspond to a single actin filament. Multilayers of
                      actin could be formed only by using the multifunctional LuSy
                      couplers that exhibit 60 hexahistidine tags and can thus act
                      as actin cross-linkers. The LuSy-mediated binding can be
                      reversibly switched by pH variations.},
      keywords     = {Actins: chemistry / Animals / Binding Sites / Lipid
                      Bilayers: chemistry / Lipids: chemistry / Microfilament
                      Proteins: chemistry / Models, Molecular / Multienzyme
                      Complexes: chemistry / Multiprotein Complexes: chemistry /
                      Neutrons / Protein Binding / Protozoan Proteins: chemistry /
                      Static Electricity / Surface Properties / Actins (NLM
                      Chemicals) / Lipid Bilayers (NLM Chemicals) / Lipids (NLM
                      Chemicals) / Microfilament Proteins (NLM Chemicals) /
                      Multienzyme Complexes (NLM Chemicals) / Multiprotein
                      Complexes (NLM Chemicals) / Protozoan Proteins (NLM
                      Chemicals) / hisactophilin protein, Protozoan (NLM
                      Chemicals) / 6,7-dimethyl-8-ribityllumazine synthase (NLM
                      Chemicals) / J (WoSType)},
      cin          = {ISG-4},
      ddc          = {670},
      cid          = {I:(DE-Juel1)VDB421},
      pnm          = {Kondensierte Materie},
      pid          = {G:(DE-Juel1)FUEK414},
      shelfmark    = {Chemistry, Multidisciplinary / Chemistry, Physical /
                      Materials Science, Multidisciplinary},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16768508},
      UT           = {WOS:000238217000044},
      doi          = {10.1021/la053310+},
      url          = {https://juser.fz-juelich.de/record/57344},
}