Functionalization of viral protein assemblies by self-assembly reactions

Viral protein assemblies have been recently shown to hold promise as molecular templates for applications in sensing, imaging, and catalysis of several biochemical reactions by combinations of self-assembly, chemical modifications and mutagenesis. Several strategies based on self-assembly reactions...

Full description

Saved in:
Bibliographic Details
Published in:Journal of materials chemistry 2008-01, Vol.18 (32), p.3741-3745
Main Author: Ueno, Takafumi
Format: Article
Language:English
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c368t-d026b243800f96aa68f40686a40c97c556e1b64994ea10c71d8f29179e4554163
cites cdi_FETCH-LOGICAL-c368t-d026b243800f96aa68f40686a40c97c556e1b64994ea10c71d8f29179e4554163
container_end_page 3745
container_issue 32
container_start_page 3741
container_title Journal of materials chemistry
container_volume 18
creator Ueno, Takafumi
description Viral protein assemblies have been recently shown to hold promise as molecular templates for applications in sensing, imaging, and catalysis of several biochemical reactions by combinations of self-assembly, chemical modifications and mutagenesis. Several strategies based on self-assembly reactions of homo- and heterolytic viral monomer proteins are highlighted and future applications in nanomaterials science and biotechnology are discussed.
doi_str_mv 10.1039/b806296j
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_34184064</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>34184064</sourcerecordid><originalsourceid>FETCH-LOGICAL-c368t-d026b243800f96aa68f40686a40c97c556e1b64994ea10c71d8f29179e4554163</originalsourceid><addsrcrecordid>eNo1UMFKAzEUDKJgrYKfkJN4WX1vk7xNjlLUCgUvel6yaQIp6W5NtkL9eltbTzMMM8MwjN0iPCAI89hpoNrQ6oxNUJCslAI8ZxMwylRG1vqSXZWyAkBsSE3Y_GXbuzEOvU3xxx4IHwL_jtkmvsnD6GPPbSl-3aXoC-92vPgUqpO049nbv3i5ZhfBpuJvTjhlny_PH7N5tXh_fZs9LSonSI_VEmrqaik0QDBkLekggTRZCc40Tiny2JE0RnqL4Bpc6lAbbIyXSkkkMWV3x979uq-tL2O7jsX5lGzvh21phUS9b5R74_3R6PJQSvah3eS4tnnXIrSHq9r_q8Qv39lbPA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>34184064</pqid></control><display><type>article</type><title>Functionalization of viral protein assemblies by self-assembly reactions</title><source>Royal Society of Chemistry</source><creator>Ueno, Takafumi</creator><creatorcontrib>Ueno, Takafumi</creatorcontrib><description>Viral protein assemblies have been recently shown to hold promise as molecular templates for applications in sensing, imaging, and catalysis of several biochemical reactions by combinations of self-assembly, chemical modifications and mutagenesis. Several strategies based on self-assembly reactions of homo- and heterolytic viral monomer proteins are highlighted and future applications in nanomaterials science and biotechnology are discussed.</description><identifier>ISSN: 0959-9428</identifier><identifier>EISSN: 1364-5501</identifier><identifier>DOI: 10.1039/b806296j</identifier><language>eng</language><ispartof>Journal of materials chemistry, 2008-01, Vol.18 (32), p.3741-3745</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-d026b243800f96aa68f40686a40c97c556e1b64994ea10c71d8f29179e4554163</citedby><cites>FETCH-LOGICAL-c368t-d026b243800f96aa68f40686a40c97c556e1b64994ea10c71d8f29179e4554163</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Ueno, Takafumi</creatorcontrib><title>Functionalization of viral protein assemblies by self-assembly reactions</title><title>Journal of materials chemistry</title><description>Viral protein assemblies have been recently shown to hold promise as molecular templates for applications in sensing, imaging, and catalysis of several biochemical reactions by combinations of self-assembly, chemical modifications and mutagenesis. Several strategies based on self-assembly reactions of homo- and heterolytic viral monomer proteins are highlighted and future applications in nanomaterials science and biotechnology are discussed.</description><issn>0959-9428</issn><issn>1364-5501</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><recordid>eNo1UMFKAzEUDKJgrYKfkJN4WX1vk7xNjlLUCgUvel6yaQIp6W5NtkL9eltbTzMMM8MwjN0iPCAI89hpoNrQ6oxNUJCslAI8ZxMwylRG1vqSXZWyAkBsSE3Y_GXbuzEOvU3xxx4IHwL_jtkmvsnD6GPPbSl-3aXoC-92vPgUqpO049nbv3i5ZhfBpuJvTjhlny_PH7N5tXh_fZs9LSonSI_VEmrqaik0QDBkLekggTRZCc40Tiny2JE0RnqL4Bpc6lAbbIyXSkkkMWV3x979uq-tL2O7jsX5lGzvh21phUS9b5R74_3R6PJQSvah3eS4tnnXIrSHq9r_q8Qv39lbPA</recordid><startdate>20080101</startdate><enddate>20080101</enddate><creator>Ueno, Takafumi</creator><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope></search><sort><creationdate>20080101</creationdate><title>Functionalization of viral protein assemblies by self-assembly reactions</title><author>Ueno, Takafumi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-d026b243800f96aa68f40686a40c97c556e1b64994ea10c71d8f29179e4554163</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ueno, Takafumi</creatorcontrib><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Journal of materials chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ueno, Takafumi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functionalization of viral protein assemblies by self-assembly reactions</atitle><jtitle>Journal of materials chemistry</jtitle><date>2008-01-01</date><risdate>2008</risdate><volume>18</volume><issue>32</issue><spage>3741</spage><epage>3745</epage><pages>3741-3745</pages><issn>0959-9428</issn><eissn>1364-5501</eissn><abstract>Viral protein assemblies have been recently shown to hold promise as molecular templates for applications in sensing, imaging, and catalysis of several biochemical reactions by combinations of self-assembly, chemical modifications and mutagenesis. Several strategies based on self-assembly reactions of homo- and heterolytic viral monomer proteins are highlighted and future applications in nanomaterials science and biotechnology are discussed.</abstract><doi>10.1039/b806296j</doi><tpages>5</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0959-9428
ispartof Journal of materials chemistry, 2008-01, Vol.18 (32), p.3741-3745
issn 0959-9428
1364-5501
language eng
recordid cdi_proquest_miscellaneous_34184064
source Royal Society of Chemistry
title Functionalization of viral protein assemblies by self-assembly reactions
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-29T02%3A47%3A32IST&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=Functionalization%20of%20viral%20protein%20assemblies%20by%20self-assembly%20reactions&rft.jtitle=Journal%20of%20materials%20chemistry&rft.au=Ueno,%20Takafumi&rft.date=2008-01-01&rft.volume=18&rft.issue=32&rft.spage=3741&rft.epage=3745&rft.pages=3741-3745&rft.issn=0959-9428&rft.eissn=1364-5501&rft_id=info:doi/10.1039/b806296j&rft_dat=%3Cproquest_cross%3E34184064%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c368t-d026b243800f96aa68f40686a40c97c556e1b64994ea10c71d8f29179e4554163%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=34184064&rft_id=info:pmid/&rfr_iscdi=true