Sialylated endogenous glycoconjugates in plant cells
Bioengineered plants are emerging as promising systems for the production of therapeutically valuable proteins. It has been commonly accepted that plants do not perform mammalian-like post-translational modifications, particularly sialylation of glycoconjugates, and no evidence has previously been r...
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Veröffentlicht in: | Nature biotechnology 2003-12, Vol.21 (12), p.1470-1471 |
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container_title | Nature biotechnology |
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creator | Shah, Miti M Fujiyama, Kazuhito Flynn, C Robert Joshi, Lokesh |
description | Bioengineered plants are emerging as promising systems for the production of therapeutically valuable proteins. It has been commonly accepted that plants do not perform mammalian-like post-translational modifications, particularly sialylation of glycoconjugates, and no evidence has previously been reported to suggest that they have such capabilities. Here we report the presence of sialylated glycoconjugates in suspension-cultured cells of
Arabidopsis thaliana
and suggest that a genetic and enzymatic basis for sialylation exists in plants. |
doi_str_mv | 10.1038/nbt912 |
format | Article |
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Arabidopsis thaliana
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Arabidopsis thaliana
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Psychology</subject><subject>glycoconjugates</subject><subject>Glycoconjugates - analysis</subject><subject>Glycoconjugates - metabolism</subject><subject>Glycoproteins</subject><subject>Glycosylation</subject><subject>Lactose</subject><subject>Lectins</subject><subject>Life Sciences</subject><subject>Mammals</subject><subject>N-Acetylneuraminic Acid - analysis</subject><subject>N-Acetylneuraminic Acid - metabolism</subject><subject>Proteins</subject><subject>sialylation</subject><issn>1087-0156</issn><issn>1546-1696</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqN0VFr3SAUAGAZK2vXbT9hhME29pDWo-YYH0tpu0Kh0K57FWNMyMVr7jSB3X9fLzdwaV82fVD0O-rxEPIJ6BlQXp-HZlLA3pATqASWgArf5jmtZUmhwmPyPqUVpRQF4jtyDAJpzVGeEPE4GL_1ZnJt4UI79i6Mcyp6v7WjHcNq7vNWKoZQbLwJU2Gd9-kDOeqMT-7jMp6Sp-urX5c_y7v7m9vLi7vSVlxNZcdZ05jOiMZJxqhsEHiTF1EpVnFmauUqZxFBVFaAAaykMKq1KGWrOqn4Kfm2P3cTxz-zS5NeD2n3AhNcfqWWIARgzf8JQQGyWrAMv7yCq3GOISehWW5cgqQZne1Rb7zTQ-jGKRqbe-vWQ_4U1w15_QIUhZpxugv48SIgm8n9nXozp6RvHx_-397_fmmXtGwcU4qu05s4rE3caqB6V3a9L3uGn5e05mbt2gNb6pzB1wWYZI3vogl2SAeHtEJGMbvve5fyVuhdPPzPqyufAQ_xvX4</recordid><startdate>20031201</startdate><enddate>20031201</enddate><creator>Shah, Miti M</creator><creator>Fujiyama, Kazuhito</creator><creator>Flynn, C Robert</creator><creator>Joshi, Lokesh</creator><general>Nature Publishing Group US</general><general>Nature</general><general>Nature Publishing Group</general><scope>IQODW</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</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>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20031201</creationdate><title>Sialylated endogenous glycoconjugates in plant cells</title><author>Shah, Miti M ; Fujiyama, Kazuhito ; Flynn, C Robert ; Joshi, Lokesh</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c539t-f32bbafa4be72207b613bf326992532a89e5ec66145c41a16574a9dc677d9f793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Acids</topic><topic>Agriculture</topic><topic>Arabidopsis - metabolism</topic><topic>Arabidopsis thaliana</topic><topic>Asialoglycoproteins - analysis</topic><topic>Asialoglycoproteins - metabolism</topic><topic>Bioinformatics</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedical Engineering/Biotechnology</topic><topic>Biomedicine</topic><topic>Biotechnology</topic><topic>brief-communication</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. 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Academic</collection><jtitle>Nature biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shah, Miti M</au><au>Fujiyama, Kazuhito</au><au>Flynn, C Robert</au><au>Joshi, Lokesh</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sialylated endogenous glycoconjugates in plant cells</atitle><jtitle>Nature biotechnology</jtitle><stitle>Nat Biotechnol</stitle><addtitle>Nat Biotechnol</addtitle><date>2003-12-01</date><risdate>2003</risdate><volume>21</volume><issue>12</issue><spage>1470</spage><epage>1471</epage><pages>1470-1471</pages><issn>1087-0156</issn><eissn>1546-1696</eissn><coden>NABIF9</coden><abstract>Bioengineered plants are emerging as promising systems for the production of therapeutically valuable proteins. It has been commonly accepted that plants do not perform mammalian-like post-translational modifications, particularly sialylation of glycoconjugates, and no evidence has previously been reported to suggest that they have such capabilities. Here we report the presence of sialylated glycoconjugates in suspension-cultured cells of
Arabidopsis thaliana
and suggest that a genetic and enzymatic basis for sialylation exists in plants.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>14608367</pmid><doi>10.1038/nbt912</doi><tpages>2</tpages></addata></record> |
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subjects | Acids Agriculture Arabidopsis - metabolism Arabidopsis thaliana Asialoglycoproteins - analysis Asialoglycoproteins - metabolism Bioinformatics Biological and medical sciences Biomedical and Life Sciences Biomedical Engineering/Biotechnology Biomedicine Biotechnology brief-communication Enzymes Fundamental and applied biological sciences. Psychology glycoconjugates Glycoconjugates - analysis Glycoconjugates - metabolism Glycoproteins Glycosylation Lactose Lectins Life Sciences Mammals N-Acetylneuraminic Acid - analysis N-Acetylneuraminic Acid - metabolism Proteins sialylation |
title | Sialylated endogenous glycoconjugates in plant cells |
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