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000058488 0247_ $$2pmid$$apmid:17609177
000058488 0247_ $$2pmc$$apmc:PMC2705973
000058488 0247_ $$2DOI$$a10.1098/rsif.2007.1094
000058488 0247_ $$2WOS$$aWOS:000251628300006
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000058488 041__ $$aeng
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000058488 084__ $$2WoS$$aMultidisciplinary Sciences
000058488 1001_ $$0P:(DE-Juel1)VDB17030$$aWrobel, G.$$b0$$uFZJ
000058488 245__ $$aTransmission electron microscopy study of the cell-sensor interface
000058488 260__ $$aLondon$$bThe Royal Society$$c2007
000058488 300__ $$a1094 - 1098
000058488 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000058488 440_0 $$017801$$aJournal of the Royal Society Interface$$v10$$x1742-5689
000058488 500__ $$aRecord converted from VDB: 12.11.2012
000058488 520__ $$aAn emerging number of micro- and nanoelectronics-based biosensors have been developed for non-invasive recordings of physiological cellular activity. The interface between the biological system and the electronic devices strongly influences the signal transfer between these systems. Little is known about the nanoscopic structure of the cell-sensor interface that is essential for a detailed interpretation of the recordings. Therefore, we analysed the interface between the sensor surface and attached cells using transmission electron microscopy (TEM). The maximum possible resolution of our TEM study, however, was restricted by the quality of the interface preparation. Therefore, we complemented our studies with imaging ellipsometry. We cultured HEK293 cells on substrates, which had been precoated with different types of proteins. We found that contact geometry between attached cell membrane and substrate was dependent on the type of protein coating used. In the presence of polylysine, the average distance of the membrane-substrate interface was in the range of 35-40 nm. However, the cell membrane was highly protruded in the presence of other proteins like fibronectin, laminin or concanavalin-A. The presented method allows the nanoscopic characterization of the cell-sensor interface.
000058488 536__ $$0G:(DE-Juel1)FUEK414$$2G:(DE-HGF)$$aKondensierte Materie$$cP54$$x0
000058488 588__ $$aDataset connected to Web of Science, Pubmed
000058488 650_2 $$2MeSH$$aCell Adhesion: physiology
000058488 650_2 $$2MeSH$$aCell Line
000058488 650_2 $$2MeSH$$aCell Membrane: chemistry
000058488 650_2 $$2MeSH$$aCell Membrane: ultrastructure
000058488 650_2 $$2MeSH$$aEpithelial Cells: cytology
000058488 650_2 $$2MeSH$$aHumans
000058488 650_2 $$2MeSH$$aMicroscopy, Electron, Transmission
000058488 650_2 $$2MeSH$$aProteins: metabolism
000058488 650_2 $$2MeSH$$aSilicon
000058488 650_2 $$2MeSH$$aSurface Properties
000058488 650_7 $$00$$2NLM Chemicals$$aProteins
000058488 650_7 $$07440-21-3$$2NLM Chemicals$$aSilicon
000058488 650_7 $$2WoSType$$aJ
000058488 65320 $$2Author$$abio-electronic interface
000058488 65320 $$2Author$$acell adhesion
000058488 65320 $$2Author$$atransmission electron microscopy
000058488 65320 $$2Author$$aextracellular recording
000058488 65320 $$2Author$$acoupling strength
000058488 65320 $$2Author$$aseal resistance
000058488 7001_ $$0P:(DE-HGF)0$$aHöller, M.$$b1
000058488 7001_ $$0P:(DE-Juel1)VDB5728$$aIngebrandt, S.$$b2$$uFZJ
000058488 7001_ $$0P:(DE-Juel1)VDB5493$$aDieluweit, S.$$b3$$uFZJ
000058488 7001_ $$0P:(DE-Juel1)VDB46736$$aSommerhage, F.$$b4$$uFZJ
000058488 7001_ $$0P:(DE-Juel1)VDB13385$$aBochem, H. P.$$b5$$uFZJ
000058488 7001_ $$0P:(DE-Juel1)128713$$aOffenhäusser, A.$$b6$$uFZJ
000058488 773__ $$0PERI:(DE-600)2156283-0$$a10.1098/rsif.2007.1094$$gVol. 5, p. 1094 - 1098$$p1094 - 1098$$q5<1094 - 1098$$tInterface$$v5$$x1742-5689$$y2007
000058488 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2705973
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000058488 9141_ $$y2007
000058488 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000058488 9201_ $$0I:(DE-Juel1)IBN-2-20090406$$d31.12.2010$$gIBN$$kIBN-2$$lBioelektronik$$x1
000058488 9201_ $$0I:(DE-Juel1)VDB802$$d31.12.2010$$gIBN$$kIBN-4$$lBiomechanik$$x0
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