Demonstration of the Protein Involvement in Cell Electropermeabilization using Confocal Raman Microspectroscopy
Confocal Raman microspectroscopy was used to study the interaction between pulsed electric fields and live cells from a molecular point of view in a non-invasive and label-free manner. Raman signatures of live human adipose-derived mesenchymal stem cells exposed or not to pulsed electric fields (8 p...
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| Veröffentlicht in: | Scientific reports 2017-01, Vol.7 (1), p.40448-40448, Article 40448 |
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| creator | Azan, Antoine Untereiner, Valérie Gobinet, Cyril Sockalingum, Ganesh D. Breton, Marie Piot, Olivier Mir, Lluis M. |
| description | Confocal Raman microspectroscopy was used to study the interaction between pulsed electric fields and live cells from a molecular point of view in a non-invasive and label-free manner. Raman signatures of live human adipose-derived mesenchymal stem cells exposed or not to pulsed electric fields (8 pulses, 1 000 V/cm, 100 μs, 1 Hz) were acquired at two cellular locations (nucleus and cytoplasm) and two spectral bands (600–1 800 cm
−1
and 2 800–3 100 cm
−1
). Vibrational modes of proteins (phenylalanine and amide I) and lipids were found to be modified by the electropermeabilization process with a statistically significant difference. The relative magnitude of four phenylalanine peaks decreased in the spectra of the pulsed group. On the contrary, the relative magnitude of the amide I band at 1658 cm
−1
increased by 40% when comparing pulsed and control group. No difference was found between the control and the pulsed group in the high wavenumber spectral band. Our results reveal the modification of proteins in living cells exposed to pulsed electric fields by means of confocal Raman microspectroscopy. |
| doi_str_mv | 10.1038/srep40448 |
| format | Article |
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−1
and 2 800–3 100 cm
−1
). Vibrational modes of proteins (phenylalanine and amide I) and lipids were found to be modified by the electropermeabilization process with a statistically significant difference. The relative magnitude of four phenylalanine peaks decreased in the spectra of the pulsed group. On the contrary, the relative magnitude of the amide I band at 1658 cm
−1
increased by 40% when comparing pulsed and control group. No difference was found between the control and the pulsed group in the high wavenumber spectral band. Our results reveal the modification of proteins in living cells exposed to pulsed electric fields by means of confocal Raman microspectroscopy.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep40448</identifier><identifier>PMID: 28102326</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>14/63 ; 631/1647/527/1821 ; 631/57/2283 ; Adipose Tissue - cytology ; Biochemistry, Molecular Biology ; Biological Physics ; Biophysics ; Cancer ; Cell Behavior ; Cell Count ; Cell Survival ; Cellular Biology ; Cytoplasm ; Electric fields ; Electrodes ; Electroporation - methods ; Engineering Sciences ; Humanities and Social Sciences ; Humans ; Life Sciences ; Lipids ; Mesenchymal Stromal Cells - cytology ; Mesenchymal Stromal Cells - metabolism ; Mesenchyme ; Microscopy, Fluorescence ; multidisciplinary ; Nuclei ; Optics ; Phenylalanine ; Photonic ; Physics ; Plasma ; Principal Component Analysis ; Proteins - metabolism ; Science ; Signal and Image processing ; Spectrum Analysis, Raman - methods ; Statistical analysis ; Stem cells ; Subcellular Processes</subject><ispartof>Scientific reports, 2017-01, Vol.7 (1), p.40448-40448, Article 40448</ispartof><rights>The Author(s) 2017</rights><rights>Copyright Nature Publishing Group Jan 2017</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>Copyright © 2017, The Author(s) 2017 The Author(s)</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c538t-189036a94b2f20a92cb2ce7fc46eccf580885365647cebbf68484c063a39ce113</citedby><cites>FETCH-LOGICAL-c538t-189036a94b2f20a92cb2ce7fc46eccf580885365647cebbf68484c063a39ce113</cites><orcidid>0000-0002-2702-3697 ; 0000-0001-7869-5242 ; 0000-0002-3360-0171 ; 0000-0002-8671-9467</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5244372/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5244372/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28102326$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.univ-reims.fr/hal-02929412$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Azan, Antoine</creatorcontrib><creatorcontrib>Untereiner, Valérie</creatorcontrib><creatorcontrib>Gobinet, Cyril</creatorcontrib><creatorcontrib>Sockalingum, Ganesh D.</creatorcontrib><creatorcontrib>Breton, Marie</creatorcontrib><creatorcontrib>Piot, Olivier</creatorcontrib><creatorcontrib>Mir, Lluis M.</creatorcontrib><title>Demonstration of the Protein Involvement in Cell Electropermeabilization using Confocal Raman Microspectroscopy</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Confocal Raman microspectroscopy was used to study the interaction between pulsed electric fields and live cells from a molecular point of view in a non-invasive and label-free manner. Raman signatures of live human adipose-derived mesenchymal stem cells exposed or not to pulsed electric fields (8 pulses, 1 000 V/cm, 100 μs, 1 Hz) were acquired at two cellular locations (nucleus and cytoplasm) and two spectral bands (600–1 800 cm
−1
and 2 800–3 100 cm
−1
). Vibrational modes of proteins (phenylalanine and amide I) and lipids were found to be modified by the electropermeabilization process with a statistically significant difference. The relative magnitude of four phenylalanine peaks decreased in the spectra of the pulsed group. On the contrary, the relative magnitude of the amide I band at 1658 cm
−1
increased by 40% when comparing pulsed and control group. No difference was found between the control and the pulsed group in the high wavenumber spectral band. Our results reveal the modification of proteins in living cells exposed to pulsed electric fields by means of confocal Raman microspectroscopy.</description><subject>14/63</subject><subject>631/1647/527/1821</subject><subject>631/57/2283</subject><subject>Adipose Tissue - cytology</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological Physics</subject><subject>Biophysics</subject><subject>Cancer</subject><subject>Cell Behavior</subject><subject>Cell Count</subject><subject>Cell Survival</subject><subject>Cellular Biology</subject><subject>Cytoplasm</subject><subject>Electric fields</subject><subject>Electrodes</subject><subject>Electroporation - methods</subject><subject>Engineering Sciences</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Lipids</subject><subject>Mesenchymal Stromal Cells - cytology</subject><subject>Mesenchymal Stromal Cells - metabolism</subject><subject>Mesenchyme</subject><subject>Microscopy, Fluorescence</subject><subject>multidisciplinary</subject><subject>Nuclei</subject><subject>Optics</subject><subject>Phenylalanine</subject><subject>Photonic</subject><subject>Physics</subject><subject>Plasma</subject><subject>Principal Component Analysis</subject><subject>Proteins - metabolism</subject><subject>Science</subject><subject>Signal and Image processing</subject><subject>Spectrum Analysis, Raman - methods</subject><subject>Statistical analysis</subject><subject>Stem cells</subject><subject>Subcellular Processes</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNplUV1rFDEUDWKxpfbBPyABX1RYm6_JJC9CWastbFFEn0Mm3tlNmUnGZGah_nozbl23NS_5uOeek3sOQi8oeUcJV-c5wSCIEOoJOmFEVAvGGXt6cD5GZznfkrIqpgXVz9AxU5SUkjxB8QP0MeQx2dHHgGOLxw3gLymO4AO-DtvYbaGHMOJyXULX4csO3JjiAKkH2_jO_9q1TtmHNV7G0EZnO_zV9jbgG-9SzMOfjuzicPccHbW2y3B2v5-i7x8vvy2vFqvPn66XF6uFq7gaF1RpwqXVomEtI1Yz1zAHdeuEBOfaShGlKi4rKWoHTdNKJZRwRHLLtQNK-Sl6v-MdpqaHH65MkGxnhuR7m-5MtN48rAS_Meu4NRUTgtesELzZEWwetV1drMz8Rpie7WTbWez1vViKPyfIo-l9dsUsGyBO2VAlaVULLXmBvnoEvY1TCsWKgtJa1JXm-p_47F4JuN3_gBIzp272qRfsy8NJ98i_GRfA2x0gl1JYQzqQ_I_tNw8Bt9c</recordid><startdate>20170119</startdate><enddate>20170119</enddate><creator>Azan, Antoine</creator><creator>Untereiner, Valérie</creator><creator>Gobinet, Cyril</creator><creator>Sockalingum, Ganesh D.</creator><creator>Breton, Marie</creator><creator>Piot, Olivier</creator><creator>Mir, Lluis M.</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>1XC</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-2702-3697</orcidid><orcidid>https://orcid.org/0000-0001-7869-5242</orcidid><orcidid>https://orcid.org/0000-0002-3360-0171</orcidid><orcidid>https://orcid.org/0000-0002-8671-9467</orcidid></search><sort><creationdate>20170119</creationdate><title>Demonstration of the Protein Involvement in Cell Electropermeabilization using Confocal Raman Microspectroscopy</title><author>Azan, Antoine ; Untereiner, Valérie ; Gobinet, Cyril ; Sockalingum, Ganesh D. ; Breton, Marie ; Piot, Olivier ; Mir, Lluis M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c538t-189036a94b2f20a92cb2ce7fc46eccf580885365647cebbf68484c063a39ce113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>14/63</topic><topic>631/1647/527/1821</topic><topic>631/57/2283</topic><topic>Adipose Tissue - cytology</topic><topic>Biochemistry, Molecular Biology</topic><topic>Biological Physics</topic><topic>Biophysics</topic><topic>Cancer</topic><topic>Cell Behavior</topic><topic>Cell Count</topic><topic>Cell Survival</topic><topic>Cellular Biology</topic><topic>Cytoplasm</topic><topic>Electric fields</topic><topic>Electrodes</topic><topic>Electroporation - methods</topic><topic>Engineering Sciences</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Lipids</topic><topic>Mesenchymal Stromal Cells - cytology</topic><topic>Mesenchymal Stromal Cells - metabolism</topic><topic>Mesenchyme</topic><topic>Microscopy, Fluorescence</topic><topic>multidisciplinary</topic><topic>Nuclei</topic><topic>Optics</topic><topic>Phenylalanine</topic><topic>Photonic</topic><topic>Physics</topic><topic>Plasma</topic><topic>Principal Component Analysis</topic><topic>Proteins - metabolism</topic><topic>Science</topic><topic>Signal and Image processing</topic><topic>Spectrum Analysis, Raman - methods</topic><topic>Statistical analysis</topic><topic>Stem cells</topic><topic>Subcellular Processes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Azan, Antoine</creatorcontrib><creatorcontrib>Untereiner, Valérie</creatorcontrib><creatorcontrib>Gobinet, Cyril</creatorcontrib><creatorcontrib>Sockalingum, Ganesh D.</creatorcontrib><creatorcontrib>Breton, Marie</creatorcontrib><creatorcontrib>Piot, Olivier</creatorcontrib><creatorcontrib>Mir, Lluis M.</creatorcontrib><collection>Springer_OA刊</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>ProQuest_Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Azan, Antoine</au><au>Untereiner, Valérie</au><au>Gobinet, Cyril</au><au>Sockalingum, Ganesh D.</au><au>Breton, Marie</au><au>Piot, Olivier</au><au>Mir, Lluis M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Demonstration of the Protein Involvement in Cell Electropermeabilization using Confocal Raman Microspectroscopy</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2017-01-19</date><risdate>2017</risdate><volume>7</volume><issue>1</issue><spage>40448</spage><epage>40448</epage><pages>40448-40448</pages><artnum>40448</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Confocal Raman microspectroscopy was used to study the interaction between pulsed electric fields and live cells from a molecular point of view in a non-invasive and label-free manner. Raman signatures of live human adipose-derived mesenchymal stem cells exposed or not to pulsed electric fields (8 pulses, 1 000 V/cm, 100 μs, 1 Hz) were acquired at two cellular locations (nucleus and cytoplasm) and two spectral bands (600–1 800 cm
−1
and 2 800–3 100 cm
−1
). Vibrational modes of proteins (phenylalanine and amide I) and lipids were found to be modified by the electropermeabilization process with a statistically significant difference. The relative magnitude of four phenylalanine peaks decreased in the spectra of the pulsed group. On the contrary, the relative magnitude of the amide I band at 1658 cm
−1
increased by 40% when comparing pulsed and control group. No difference was found between the control and the pulsed group in the high wavenumber spectral band. Our results reveal the modification of proteins in living cells exposed to pulsed electric fields by means of confocal Raman microspectroscopy.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>28102326</pmid><doi>10.1038/srep40448</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-2702-3697</orcidid><orcidid>https://orcid.org/0000-0001-7869-5242</orcidid><orcidid>https://orcid.org/0000-0002-3360-0171</orcidid><orcidid>https://orcid.org/0000-0002-8671-9467</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 14/63 631/1647/527/1821 631/57/2283 Adipose Tissue - cytology Biochemistry, Molecular Biology Biological Physics Biophysics Cancer Cell Behavior Cell Count Cell Survival Cellular Biology Cytoplasm Electric fields Electrodes Electroporation - methods Engineering Sciences Humanities and Social Sciences Humans Life Sciences Lipids Mesenchymal Stromal Cells - cytology Mesenchymal Stromal Cells - metabolism Mesenchyme Microscopy, Fluorescence multidisciplinary Nuclei Optics Phenylalanine Photonic Physics Plasma Principal Component Analysis Proteins - metabolism Science Signal and Image processing Spectrum Analysis, Raman - methods Statistical analysis Stem cells Subcellular Processes |
| title | Demonstration of the Protein Involvement in Cell Electropermeabilization using Confocal Raman Microspectroscopy |
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