Loading…
Tighter ties that bind
A stepwise process of mutation and structural analysis has modulated a flexible binding interface of an immune-cell signalling protein, interleukin-2, and generated mutant proteins with enhanced anticancer activity. See Article p.529 Engineering an interleukin-2 'superkine' Chris Garcia an...
Saved in:
Published in: | Nature (London) 2012-04, Vol.484 (7395), p.463-464 |
---|---|
Main Author: | |
Format: | Article |
Language: | English |
Subjects: | |
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-c220a-a8a7bbbe28f7b8a1c008bf4ef83be6f53be2a5189f1f4ed6191fb4665a0134d83 |
---|---|
cites | cdi_FETCH-LOGICAL-c220a-a8a7bbbe28f7b8a1c008bf4ef83be6f53be2a5189f1f4ed6191fb4665a0134d83 |
container_end_page | 464 |
container_issue | 7395 |
container_start_page | 463 |
container_title | Nature (London) |
container_volume | 484 |
creator | Boder, Eric T. |
description | A stepwise process of mutation and structural analysis has modulated a flexible binding interface of an immune-cell signalling protein, interleukin-2, and generated mutant proteins with enhanced anticancer activity.
See Article
p.529
Engineering an interleukin-2 'superkine'
Chris Garcia and colleagues elucidate the molecular mechanism that underlies the sensitization of T cells to the immunostimulatory cytokine interleukin-2 (IL-2). They use this information to engineer a single-chain IL-2 superkine that functions independent of its α-receptor (IL-2Rα or CD25). This new superkine is more efficacious than IL-2 in inducing antitumour T-cell responses and has fewer toxic side effects. |
doi_str_mv | 10.1038/484463a |
format | article |
fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_journals_1014267186</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A630208543</galeid><sourcerecordid>A630208543</sourcerecordid><originalsourceid>FETCH-LOGICAL-c220a-a8a7bbbe28f7b8a1c008bf4ef83be6f53be2a5189f1f4ed6191fb4665a0134d83</originalsourceid><addsrcrecordid>eNpt0EtLAzEQAOAgCtYq3jwXPaiH1cljs-mxFB-FgqD1HJI02aa0u22Sgv57Iy3YgpcZGD7mhdAlhgcMVDwywRin6gh1MKt4wbiojlEHgIgCBOWn6CzGOQCUuGIddDXx9SzZ0Evexl6aqdTTvpmeoxOnFtFe7HIXfT4_TYavxfjtZTQcjAtDCKhCCVVprS0RrtJCYQMgtGPWCaotd2WORJVY9B3O1SnHfew047xUgCmbCtpFN9u-q9CuNzYmOW83ockjJQbMCK-w4H-qVgsrfePaFJRZ-mjkgFMgIEpGs7r-R5mVX8t9dH-ATNsk-5VqtYlRjj7eDxvebq0JbYzBOrkKfqnCd95N_v5a7n6d5d1Wxiya2ob9Mw7pDz_xeAg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1014267186</pqid></control><display><type>article</type><title>Tighter ties that bind</title><source>Nature</source><creator>Boder, Eric T.</creator><creatorcontrib>Boder, Eric T.</creatorcontrib><description>A stepwise process of mutation and structural analysis has modulated a flexible binding interface of an immune-cell signalling protein, interleukin-2, and generated mutant proteins with enhanced anticancer activity.
See Article
p.529
Engineering an interleukin-2 'superkine'
Chris Garcia and colleagues elucidate the molecular mechanism that underlies the sensitization of T cells to the immunostimulatory cytokine interleukin-2 (IL-2). They use this information to engineer a single-chain IL-2 superkine that functions independent of its α-receptor (IL-2Rα or CD25). This new superkine is more efficacious than IL-2 in inducing antitumour T-cell responses and has fewer toxic side effects.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/484463a</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/45/535 ; 631/553/1886 ; 692/699/67 ; 692/700/565 ; Cancer ; Crystallography ; Humanities and Social Sciences ; Immune response ; Immune system ; Interleukins ; multidisciplinary ; Mutation ; news-and-views ; Physiological aspects ; Proteins ; Science ; Structural analysis</subject><ispartof>Nature (London), 2012-04, Vol.484 (7395), p.463-464</ispartof><rights>Springer Nature Limited 2012</rights><rights>COPYRIGHT 2012 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Apr 26, 2012</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c220a-a8a7bbbe28f7b8a1c008bf4ef83be6f53be2a5189f1f4ed6191fb4665a0134d83</citedby><cites>FETCH-LOGICAL-c220a-a8a7bbbe28f7b8a1c008bf4ef83be6f53be2a5189f1f4ed6191fb4665a0134d83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Boder, Eric T.</creatorcontrib><title>Tighter ties that bind</title><title>Nature (London)</title><addtitle>Nature</addtitle><description>A stepwise process of mutation and structural analysis has modulated a flexible binding interface of an immune-cell signalling protein, interleukin-2, and generated mutant proteins with enhanced anticancer activity.
See Article
p.529
Engineering an interleukin-2 'superkine'
Chris Garcia and colleagues elucidate the molecular mechanism that underlies the sensitization of T cells to the immunostimulatory cytokine interleukin-2 (IL-2). They use this information to engineer a single-chain IL-2 superkine that functions independent of its α-receptor (IL-2Rα or CD25). This new superkine is more efficacious than IL-2 in inducing antitumour T-cell responses and has fewer toxic side effects.</description><subject>631/45/535</subject><subject>631/553/1886</subject><subject>692/699/67</subject><subject>692/700/565</subject><subject>Cancer</subject><subject>Crystallography</subject><subject>Humanities and Social Sciences</subject><subject>Immune response</subject><subject>Immune system</subject><subject>Interleukins</subject><subject>multidisciplinary</subject><subject>Mutation</subject><subject>news-and-views</subject><subject>Physiological aspects</subject><subject>Proteins</subject><subject>Science</subject><subject>Structural analysis</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><recordid>eNpt0EtLAzEQAOAgCtYq3jwXPaiH1cljs-mxFB-FgqD1HJI02aa0u22Sgv57Iy3YgpcZGD7mhdAlhgcMVDwywRin6gh1MKt4wbiojlEHgIgCBOWn6CzGOQCUuGIddDXx9SzZ0Evexl6aqdTTvpmeoxOnFtFe7HIXfT4_TYavxfjtZTQcjAtDCKhCCVVprS0RrtJCYQMgtGPWCaotd2WORJVY9B3O1SnHfew047xUgCmbCtpFN9u-q9CuNzYmOW83ockjJQbMCK-w4H-qVgsrfePaFJRZ-mjkgFMgIEpGs7r-R5mVX8t9dH-ATNsk-5VqtYlRjj7eDxvebq0JbYzBOrkKfqnCd95N_v5a7n6d5d1Wxiya2ob9Mw7pDz_xeAg</recordid><startdate>20120426</startdate><enddate>20120426</enddate><creator>Boder, Eric T.</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope></search><sort><creationdate>20120426</creationdate><title>Tighter ties that bind</title><author>Boder, Eric T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c220a-a8a7bbbe28f7b8a1c008bf4ef83be6f53be2a5189f1f4ed6191fb4665a0134d83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>631/45/535</topic><topic>631/553/1886</topic><topic>692/699/67</topic><topic>692/700/565</topic><topic>Cancer</topic><topic>Crystallography</topic><topic>Humanities and Social Sciences</topic><topic>Immune response</topic><topic>Immune system</topic><topic>Interleukins</topic><topic>multidisciplinary</topic><topic>Mutation</topic><topic>news-and-views</topic><topic>Physiological aspects</topic><topic>Proteins</topic><topic>Science</topic><topic>Structural analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Boder, Eric T.</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>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>Psychology Database (Alumni)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Research Library (Alumni Edition)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>eLibrary</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agriculture Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Psychology Database</collection><collection>ProQuest research library</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Engineering Database</collection><collection>Research Library (Corporate)</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest advanced technologies & aerospace journals</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>Materials science collection</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 One Psychology</collection><collection>Engineering collection</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>University of Michigan</collection><collection>Genetics Abstracts</collection><collection>SIRS Editorial</collection><collection>Environment Abstracts</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Boder, Eric T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tighter ties that bind</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><date>2012-04-26</date><risdate>2012</risdate><volume>484</volume><issue>7395</issue><spage>463</spage><epage>464</epage><pages>463-464</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>A stepwise process of mutation and structural analysis has modulated a flexible binding interface of an immune-cell signalling protein, interleukin-2, and generated mutant proteins with enhanced anticancer activity.
See Article
p.529
Engineering an interleukin-2 'superkine'
Chris Garcia and colleagues elucidate the molecular mechanism that underlies the sensitization of T cells to the immunostimulatory cytokine interleukin-2 (IL-2). They use this information to engineer a single-chain IL-2 superkine that functions independent of its α-receptor (IL-2Rα or CD25). This new superkine is more efficacious than IL-2 in inducing antitumour T-cell responses and has fewer toxic side effects.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><doi>10.1038/484463a</doi><tpages>2</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0028-0836 |
ispartof | Nature (London), 2012-04, Vol.484 (7395), p.463-464 |
issn | 0028-0836 1476-4687 |
language | eng |
recordid | cdi_proquest_journals_1014267186 |
source | Nature |
subjects | 631/45/535 631/553/1886 692/699/67 692/700/565 Cancer Crystallography Humanities and Social Sciences Immune response Immune system Interleukins multidisciplinary Mutation news-and-views Physiological aspects Proteins Science Structural analysis |
title | Tighter ties that bind |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T11%3A26%3A40IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Tighter%20ties%20that%20bind&rft.jtitle=Nature%20(London)&rft.au=Boder,%20Eric%20T.&rft.date=2012-04-26&rft.volume=484&rft.issue=7395&rft.spage=463&rft.epage=464&rft.pages=463-464&rft.issn=0028-0836&rft.eissn=1476-4687&rft.coden=NATUAS&rft_id=info:doi/10.1038/484463a&rft_dat=%3Cgale_proqu%3EA630208543%3C/gale_proqu%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c220a-a8a7bbbe28f7b8a1c008bf4ef83be6f53be2a5189f1f4ed6191fb4665a0134d83%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1014267186&rft_id=info:pmid/&rft_galeid=A630208543&rfr_iscdi=true |