A Novel Model System for Design of Biomaterials Based on Recombinant Analogs of Spider Silk Proteins
Spider dragline silk possesses impressive mechanical and biochemical properties. It is synthesized by a couple of major ampullate glands in spiders and comprises of two major structural proteins—spidroins 1 and 2. The relationship between structure and mechanical properties of spider silk is not wel...
Gespeichert in:
| Veröffentlicht in: | Journal of neuroimmune pharmacology 2009-03, Vol.4 (1), p.17-27 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 27 |
|---|---|
| container_issue | 1 |
| container_start_page | 17 |
| container_title | Journal of neuroimmune pharmacology |
| container_volume | 4 |
| creator | Bogush, Vladimir G. Sokolova, Olga S. Davydova, Lyubov I. Klinov, Dmitri V. Sidoruk, Konstantin V. Esipova, Natalya G. Neretina, Tatyana V. Orchanskyi, Igor A. Makeev, Vsevolod Yu Tumanyan, Vladimir G. Shaitan, Konstantin V. Debabov, Vladimir G. Kirpichnikov, Mikhail P. |
| description | Spider dragline silk possesses impressive mechanical and biochemical properties. It is synthesized by a couple of major ampullate glands in spiders and comprises of two major structural proteins—spidroins 1 and 2. The relationship between structure and mechanical properties of spider silk is not well understood. Here, we modeled the complete process of the spider silk assembly using two new recombinant analogs of spidroins 1 and 2. The artificial genes sequence of the hydrophobic core regions of spidroin 1 and 2 have been designed using computer analysis of existing databases and mathematical modeling. Both proteins were expressed in
Pichia pastoris
and purified using a cation exchange chromatography. Despite the absence of hydrophilic N- and C-termini, both purified proteins spontaneously formed the nanofibrils and round micelles of about 1 μm in aqueous solutions. The electron microscopy study has revealed the helical structure of a nanofibril with a repeating motif of 40 nm. Using the electrospinning, the thin films with an antiparallel β-sheet structure were produced. In summary, we were able to obtain artificial structures with characteristics that are perspective for further biomedical applications, such as producing three-dimensional matrices for tissue engineering and drug delivery. |
| doi_str_mv | 10.1007/s11481-008-9129-z |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_66934874</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1950826142</sourcerecordid><originalsourceid>FETCH-LOGICAL-c401t-adbb1361b26ae9b614623043d2c4785f6d0f2a173fe04c16f071ce1a69185bbb3</originalsourceid><addsrcrecordid>eNqFkV2L1DAUhoMo7jr6A7yRgOBd9Zw0TZPL2fUT1g8cvQ5JezpkbZsx6Qi7v94MM6II4k0SyPO--XgYe4zwHAHaFxlRaqwAdGVQmOr2DjvHpmkrNCDv_lprA2fsQc7XAFJKgPvsDLWuTY3ynPVr_iH-oJG_j30ZNzd5oYkPMfGXlMN25nHgFyFObqEU3Jj5hcvU8zjzz9TFyYfZzQtfz26M23yAN7vQU-KbMH7jn1JcKMz5Ibs3lCw9Os0r9vX1qy-Xb6urj2_eXa6vqk4CLpXrvcdaoRfKkfEKpRI1yLoXnWx1M6geBuGwrQcC2aEaoMWO0CmDuvHe1yv27Ni7S_H7nvJip5A7Gkc3U9xnq5SppW7lf0GB2BhVvmjFnv4FXsd9Kq_NFk0DWpRLikLhkepSzDnRYHcpTC7dWAR7MGWPpmwxZQ-m7G3JPDk17_1E_e_ESU0BxBHIZWveUvrj6H-2_gQCKJ1e</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1950826142</pqid></control><display><type>article</type><title>A Novel Model System for Design of Biomaterials Based on Recombinant Analogs of Spider Silk Proteins</title><source>MEDLINE</source><source>SpringerLink Journals</source><creator>Bogush, Vladimir G. ; Sokolova, Olga S. ; Davydova, Lyubov I. ; Klinov, Dmitri V. ; Sidoruk, Konstantin V. ; Esipova, Natalya G. ; Neretina, Tatyana V. ; Orchanskyi, Igor A. ; Makeev, Vsevolod Yu ; Tumanyan, Vladimir G. ; Shaitan, Konstantin V. ; Debabov, Vladimir G. ; Kirpichnikov, Mikhail P.</creator><creatorcontrib>Bogush, Vladimir G. ; Sokolova, Olga S. ; Davydova, Lyubov I. ; Klinov, Dmitri V. ; Sidoruk, Konstantin V. ; Esipova, Natalya G. ; Neretina, Tatyana V. ; Orchanskyi, Igor A. ; Makeev, Vsevolod Yu ; Tumanyan, Vladimir G. ; Shaitan, Konstantin V. ; Debabov, Vladimir G. ; Kirpichnikov, Mikhail P.</creatorcontrib><description>Spider dragline silk possesses impressive mechanical and biochemical properties. It is synthesized by a couple of major ampullate glands in spiders and comprises of two major structural proteins—spidroins 1 and 2. The relationship between structure and mechanical properties of spider silk is not well understood. Here, we modeled the complete process of the spider silk assembly using two new recombinant analogs of spidroins 1 and 2. The artificial genes sequence of the hydrophobic core regions of spidroin 1 and 2 have been designed using computer analysis of existing databases and mathematical modeling. Both proteins were expressed in
Pichia pastoris
and purified using a cation exchange chromatography. Despite the absence of hydrophilic N- and C-termini, both purified proteins spontaneously formed the nanofibrils and round micelles of about 1 μm in aqueous solutions. The electron microscopy study has revealed the helical structure of a nanofibril with a repeating motif of 40 nm. Using the electrospinning, the thin films with an antiparallel β-sheet structure were produced. In summary, we were able to obtain artificial structures with characteristics that are perspective for further biomedical applications, such as producing three-dimensional matrices for tissue engineering and drug delivery.</description><identifier>ISSN: 1557-1890</identifier><identifier>EISSN: 1557-1904</identifier><identifier>DOI: 10.1007/s11481-008-9129-z</identifier><identifier>PMID: 18839314</identifier><language>eng</language><publisher>Boston: Springer US</publisher><subject>Animals ; Araneae ; Biocompatible Materials - chemistry ; Biomedical and Life Sciences ; Biomedicine ; Cell Biology ; Circular Dichroism ; Immunology ; Microscopy, Atomic Force ; Microscopy, Electron, Scanning ; Microscopy, Electron, Transmission ; Models, Molecular ; Models, Statistical ; Nanotechnology ; Neurosciences ; Original Article ; Pharmacology/Toxicology ; Pichia pastoris ; Proteins ; Recombinant Proteins - chemistry ; Silk ; Silk - chemistry ; Silk - genetics ; Silk - ultrastructure ; Solutions ; Spectrometry, Mass, Electrospray Ionization ; Spectrophotometry, Infrared ; Spiders ; Spiders - chemistry ; Spiders - genetics ; Tissue Engineering ; Virology</subject><ispartof>Journal of neuroimmune pharmacology, 2009-03, Vol.4 (1), p.17-27</ispartof><rights>Springer Science+Business Media, LLC 2008</rights><rights>Journal of Neuroimmune Pharmacology is a copyright of Springer, 2009.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c401t-adbb1361b26ae9b614623043d2c4785f6d0f2a173fe04c16f071ce1a69185bbb3</citedby><cites>FETCH-LOGICAL-c401t-adbb1361b26ae9b614623043d2c4785f6d0f2a173fe04c16f071ce1a69185bbb3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11481-008-9129-z$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11481-008-9129-z$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18839314$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bogush, Vladimir G.</creatorcontrib><creatorcontrib>Sokolova, Olga S.</creatorcontrib><creatorcontrib>Davydova, Lyubov I.</creatorcontrib><creatorcontrib>Klinov, Dmitri V.</creatorcontrib><creatorcontrib>Sidoruk, Konstantin V.</creatorcontrib><creatorcontrib>Esipova, Natalya G.</creatorcontrib><creatorcontrib>Neretina, Tatyana V.</creatorcontrib><creatorcontrib>Orchanskyi, Igor A.</creatorcontrib><creatorcontrib>Makeev, Vsevolod Yu</creatorcontrib><creatorcontrib>Tumanyan, Vladimir G.</creatorcontrib><creatorcontrib>Shaitan, Konstantin V.</creatorcontrib><creatorcontrib>Debabov, Vladimir G.</creatorcontrib><creatorcontrib>Kirpichnikov, Mikhail P.</creatorcontrib><title>A Novel Model System for Design of Biomaterials Based on Recombinant Analogs of Spider Silk Proteins</title><title>Journal of neuroimmune pharmacology</title><addtitle>J Neuroimmune Pharmacol</addtitle><addtitle>J Neuroimmune Pharmacol</addtitle><description>Spider dragline silk possesses impressive mechanical and biochemical properties. It is synthesized by a couple of major ampullate glands in spiders and comprises of two major structural proteins—spidroins 1 and 2. The relationship between structure and mechanical properties of spider silk is not well understood. Here, we modeled the complete process of the spider silk assembly using two new recombinant analogs of spidroins 1 and 2. The artificial genes sequence of the hydrophobic core regions of spidroin 1 and 2 have been designed using computer analysis of existing databases and mathematical modeling. Both proteins were expressed in
Pichia pastoris
and purified using a cation exchange chromatography. Despite the absence of hydrophilic N- and C-termini, both purified proteins spontaneously formed the nanofibrils and round micelles of about 1 μm in aqueous solutions. The electron microscopy study has revealed the helical structure of a nanofibril with a repeating motif of 40 nm. Using the electrospinning, the thin films with an antiparallel β-sheet structure were produced. In summary, we were able to obtain artificial structures with characteristics that are perspective for further biomedical applications, such as producing three-dimensional matrices for tissue engineering and drug delivery.</description><subject>Animals</subject><subject>Araneae</subject><subject>Biocompatible Materials - chemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cell Biology</subject><subject>Circular Dichroism</subject><subject>Immunology</subject><subject>Microscopy, Atomic Force</subject><subject>Microscopy, Electron, Scanning</subject><subject>Microscopy, Electron, Transmission</subject><subject>Models, Molecular</subject><subject>Models, Statistical</subject><subject>Nanotechnology</subject><subject>Neurosciences</subject><subject>Original Article</subject><subject>Pharmacology/Toxicology</subject><subject>Pichia pastoris</subject><subject>Proteins</subject><subject>Recombinant Proteins - chemistry</subject><subject>Silk</subject><subject>Silk - chemistry</subject><subject>Silk - genetics</subject><subject>Silk - ultrastructure</subject><subject>Solutions</subject><subject>Spectrometry, Mass, Electrospray Ionization</subject><subject>Spectrophotometry, Infrared</subject><subject>Spiders</subject><subject>Spiders - chemistry</subject><subject>Spiders - genetics</subject><subject>Tissue Engineering</subject><subject>Virology</subject><issn>1557-1890</issn><issn>1557-1904</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkV2L1DAUhoMo7jr6A7yRgOBd9Zw0TZPL2fUT1g8cvQ5JezpkbZsx6Qi7v94MM6II4k0SyPO--XgYe4zwHAHaFxlRaqwAdGVQmOr2DjvHpmkrNCDv_lprA2fsQc7XAFJKgPvsDLWuTY3ynPVr_iH-oJG_j30ZNzd5oYkPMfGXlMN25nHgFyFObqEU3Jj5hcvU8zjzz9TFyYfZzQtfz26M23yAN7vQU-KbMH7jn1JcKMz5Ibs3lCw9Os0r9vX1qy-Xb6urj2_eXa6vqk4CLpXrvcdaoRfKkfEKpRI1yLoXnWx1M6geBuGwrQcC2aEaoMWO0CmDuvHe1yv27Ni7S_H7nvJip5A7Gkc3U9xnq5SppW7lf0GB2BhVvmjFnv4FXsd9Kq_NFk0DWpRLikLhkepSzDnRYHcpTC7dWAR7MGWPpmwxZQ-m7G3JPDk17_1E_e_ESU0BxBHIZWveUvrj6H-2_gQCKJ1e</recordid><startdate>20090301</startdate><enddate>20090301</enddate><creator>Bogush, Vladimir G.</creator><creator>Sokolova, Olga S.</creator><creator>Davydova, Lyubov I.</creator><creator>Klinov, Dmitri V.</creator><creator>Sidoruk, Konstantin V.</creator><creator>Esipova, Natalya G.</creator><creator>Neretina, Tatyana V.</creator><creator>Orchanskyi, Igor A.</creator><creator>Makeev, Vsevolod Yu</creator><creator>Tumanyan, Vladimir G.</creator><creator>Shaitan, Konstantin V.</creator><creator>Debabov, Vladimir G.</creator><creator>Kirpichnikov, Mikhail P.</creator><general>Springer US</general><general>Springer Nature B.V</general><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>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7QO</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20090301</creationdate><title>A Novel Model System for Design of Biomaterials Based on Recombinant Analogs of Spider Silk Proteins</title><author>Bogush, Vladimir G. ; Sokolova, Olga S. ; Davydova, Lyubov I. ; Klinov, Dmitri V. ; Sidoruk, Konstantin V. ; Esipova, Natalya G. ; Neretina, Tatyana V. ; Orchanskyi, Igor A. ; Makeev, Vsevolod Yu ; Tumanyan, Vladimir G. ; Shaitan, Konstantin V. ; Debabov, Vladimir G. ; Kirpichnikov, Mikhail P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-adbb1361b26ae9b614623043d2c4785f6d0f2a173fe04c16f071ce1a69185bbb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Animals</topic><topic>Araneae</topic><topic>Biocompatible Materials - chemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cell Biology</topic><topic>Circular Dichroism</topic><topic>Immunology</topic><topic>Microscopy, Atomic Force</topic><topic>Microscopy, Electron, Scanning</topic><topic>Microscopy, Electron, Transmission</topic><topic>Models, Molecular</topic><topic>Models, Statistical</topic><topic>Nanotechnology</topic><topic>Neurosciences</topic><topic>Original Article</topic><topic>Pharmacology/Toxicology</topic><topic>Pichia pastoris</topic><topic>Proteins</topic><topic>Recombinant Proteins - chemistry</topic><topic>Silk</topic><topic>Silk - chemistry</topic><topic>Silk - genetics</topic><topic>Silk - ultrastructure</topic><topic>Solutions</topic><topic>Spectrometry, Mass, Electrospray Ionization</topic><topic>Spectrophotometry, Infrared</topic><topic>Spiders</topic><topic>Spiders - chemistry</topic><topic>Spiders - genetics</topic><topic>Tissue Engineering</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bogush, Vladimir G.</creatorcontrib><creatorcontrib>Sokolova, Olga S.</creatorcontrib><creatorcontrib>Davydova, Lyubov I.</creatorcontrib><creatorcontrib>Klinov, Dmitri V.</creatorcontrib><creatorcontrib>Sidoruk, Konstantin V.</creatorcontrib><creatorcontrib>Esipova, Natalya G.</creatorcontrib><creatorcontrib>Neretina, Tatyana V.</creatorcontrib><creatorcontrib>Orchanskyi, Igor A.</creatorcontrib><creatorcontrib>Makeev, Vsevolod Yu</creatorcontrib><creatorcontrib>Tumanyan, Vladimir G.</creatorcontrib><creatorcontrib>Shaitan, Konstantin V.</creatorcontrib><creatorcontrib>Debabov, Vladimir G.</creatorcontrib><creatorcontrib>Kirpichnikov, Mikhail P.</creatorcontrib><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>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</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 Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</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 China</collection><collection>Biotechnology Research Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of neuroimmune pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bogush, Vladimir G.</au><au>Sokolova, Olga S.</au><au>Davydova, Lyubov I.</au><au>Klinov, Dmitri V.</au><au>Sidoruk, Konstantin V.</au><au>Esipova, Natalya G.</au><au>Neretina, Tatyana V.</au><au>Orchanskyi, Igor A.</au><au>Makeev, Vsevolod Yu</au><au>Tumanyan, Vladimir G.</au><au>Shaitan, Konstantin V.</au><au>Debabov, Vladimir G.</au><au>Kirpichnikov, Mikhail P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Novel Model System for Design of Biomaterials Based on Recombinant Analogs of Spider Silk Proteins</atitle><jtitle>Journal of neuroimmune pharmacology</jtitle><stitle>J Neuroimmune Pharmacol</stitle><addtitle>J Neuroimmune Pharmacol</addtitle><date>2009-03-01</date><risdate>2009</risdate><volume>4</volume><issue>1</issue><spage>17</spage><epage>27</epage><pages>17-27</pages><issn>1557-1890</issn><eissn>1557-1904</eissn><abstract>Spider dragline silk possesses impressive mechanical and biochemical properties. It is synthesized by a couple of major ampullate glands in spiders and comprises of two major structural proteins—spidroins 1 and 2. The relationship between structure and mechanical properties of spider silk is not well understood. Here, we modeled the complete process of the spider silk assembly using two new recombinant analogs of spidroins 1 and 2. The artificial genes sequence of the hydrophobic core regions of spidroin 1 and 2 have been designed using computer analysis of existing databases and mathematical modeling. Both proteins were expressed in
Pichia pastoris
and purified using a cation exchange chromatography. Despite the absence of hydrophilic N- and C-termini, both purified proteins spontaneously formed the nanofibrils and round micelles of about 1 μm in aqueous solutions. The electron microscopy study has revealed the helical structure of a nanofibril with a repeating motif of 40 nm. Using the electrospinning, the thin films with an antiparallel β-sheet structure were produced. In summary, we were able to obtain artificial structures with characteristics that are perspective for further biomedical applications, such as producing three-dimensional matrices for tissue engineering and drug delivery.</abstract><cop>Boston</cop><pub>Springer US</pub><pmid>18839314</pmid><doi>10.1007/s11481-008-9129-z</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1557-1890 |
| ispartof | Journal of neuroimmune pharmacology, 2009-03, Vol.4 (1), p.17-27 |
| issn | 1557-1890 1557-1904 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_66934874 |
| source | MEDLINE; SpringerLink Journals |
| subjects | Animals Araneae Biocompatible Materials - chemistry Biomedical and Life Sciences Biomedicine Cell Biology Circular Dichroism Immunology Microscopy, Atomic Force Microscopy, Electron, Scanning Microscopy, Electron, Transmission Models, Molecular Models, Statistical Nanotechnology Neurosciences Original Article Pharmacology/Toxicology Pichia pastoris Proteins Recombinant Proteins - chemistry Silk Silk - chemistry Silk - genetics Silk - ultrastructure Solutions Spectrometry, Mass, Electrospray Ionization Spectrophotometry, Infrared Spiders Spiders - chemistry Spiders - genetics Tissue Engineering Virology |
| title | A Novel Model System for Design of Biomaterials Based on Recombinant Analogs of Spider Silk Proteins |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-05T04%3A41%3A17IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20Novel%20Model%20System%20for%20Design%20of%20Biomaterials%20Based%20on%20Recombinant%20Analogs%20of%20Spider%20Silk%20Proteins&rft.jtitle=Journal%20of%20neuroimmune%20pharmacology&rft.au=Bogush,%20Vladimir%20G.&rft.date=2009-03-01&rft.volume=4&rft.issue=1&rft.spage=17&rft.epage=27&rft.pages=17-27&rft.issn=1557-1890&rft.eissn=1557-1904&rft_id=info:doi/10.1007/s11481-008-9129-z&rft_dat=%3Cproquest_cross%3E1950826142%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1950826142&rft_id=info:pmid/18839314&rfr_iscdi=true |