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HOMOGENEOUS GLYCOPEPTIDES AND GLYCOPROTEINS FOR BIOLOGICAL INVESTIGATION
Protein glycosylation is widely recognized as a modulator of protein structure, localization, and cell-cell recognition in multicellular systems. Glycoproteins are typically expressed as mixtures of glycoforms, their oligosaccharides being generated by a template-independent biosynthetic process. In...
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| Published in: | Annual review of biochemistry 2002-01, Vol.71 (1), p.593-634 |
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| container_end_page | 634 |
| container_issue | 1 |
| container_start_page | 593 |
| container_title | Annual review of biochemistry |
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| creator | Grogan, Michael J Pratt, Matthew R Marcaurelle, Lisa A Bertozzi, Carolyn R |
| description | Protein glycosylation is widely recognized as a modulator of protein
structure, localization, and cell-cell recognition in multicellular systems.
Glycoproteins are typically expressed as mixtures of glycoforms, their
oligosaccharides being generated by a template-independent biosynthetic
process. Investigation of their function has been greatly assisted by sources
of homogeneous material. This review summarizes current efforts to obtain
homogeneous glycopeptide and glycoprotein materials by a variety of methods
that draw from the techniques of recombinant expression, chemical synthesis,
enzymatic transformation, and chemoselective ligation. Some of these techniques
remove obstacles to glycoprotein synthesis by installing nonnative linkages and
other modifications for facilitated assembly. The end purpose of the described
approaches is the production of glycosylated materials for experiments relevant
to the biological investigation of glycoproteins, although the strategies
presented apply to other posttranslational modifications as well. |
| doi_str_mv | 10.1146/annurev.biochem.71.110601.135334 |
| format | article |
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structure, localization, and cell-cell recognition in multicellular systems.
Glycoproteins are typically expressed as mixtures of glycoforms, their
oligosaccharides being generated by a template-independent biosynthetic
process. Investigation of their function has been greatly assisted by sources
of homogeneous material. This review summarizes current efforts to obtain
homogeneous glycopeptide and glycoprotein materials by a variety of methods
that draw from the techniques of recombinant expression, chemical synthesis,
enzymatic transformation, and chemoselective ligation. Some of these techniques
remove obstacles to glycoprotein synthesis by installing nonnative linkages and
other modifications for facilitated assembly. The end purpose of the described
approaches is the production of glycosylated materials for experiments relevant
to the biological investigation of glycoproteins, although the strategies
presented apply to other posttranslational modifications as well.</description><identifier>ISSN: 0066-4154</identifier><identifier>EISSN: 1545-4509</identifier><identifier>DOI: 10.1146/annurev.biochem.71.110601.135334</identifier><identifier>PMID: 12045107</identifier><identifier>CODEN: ARBOAW</identifier><language>eng</language><publisher>Palo Alto, CA 94303-0139: Annual Reviews</publisher><subject>Amino Acid Sequence ; Chemical synthesis ; chemoselective ligation ; Glycopeptides - chemical synthesis ; Glycopeptides - chemistry ; Glycopeptides - metabolism ; Glycoproteins ; Glycoproteins - chemical synthesis ; Glycoproteins - chemistry ; Glycoproteins - metabolism ; Glycosylation ; Glycosylphosphatidylinositols - metabolism ; GPI anchor ; Humans ; Membrane Glycoproteins - genetics ; Membrane Glycoproteins - metabolism ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Mucins - chemistry ; N-linked ; O-linked ; oligosaccharide ; P-Selectin - metabolism ; Proteins ; Serine - chemistry ; Threonine - chemistry</subject><ispartof>Annual review of biochemistry, 2002-01, Vol.71 (1), p.593-634</ispartof><rights>Copyright © 2002 by Annual Reviews. All rights reserved</rights><rights>Copyright Annual Reviews, Inc. 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a513t-6f73acfb6510f24932411e20901288390c83d2edec2cb73789b048ed27117db43</citedby><cites>FETCH-LOGICAL-a513t-6f73acfb6510f24932411e20901288390c83d2edec2cb73789b048ed27117db43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.annualreviews.org/content/journals/10.1146/annurev.biochem.71.110601.135334?crawler=true&mimetype=application/pdf$$EPDF$$P50$$Gannualreviews$$H</linktopdf><linktohtml>$$Uhttps://www.annualreviews.org/content/journals/10.1146/annurev.biochem.71.110601.135334$$EHTML$$P50$$Gannualreviews$$H</linktohtml><link.rule.ids>70,314,780,784,4179,27922,27923,78024,78025</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12045107$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Grogan, Michael J</creatorcontrib><creatorcontrib>Pratt, Matthew R</creatorcontrib><creatorcontrib>Marcaurelle, Lisa A</creatorcontrib><creatorcontrib>Bertozzi, Carolyn R</creatorcontrib><title>HOMOGENEOUS GLYCOPEPTIDES AND GLYCOPROTEINS FOR BIOLOGICAL INVESTIGATION</title><title>Annual review of biochemistry</title><addtitle>Annu Rev Biochem</addtitle><description>Protein glycosylation is widely recognized as a modulator of protein
structure, localization, and cell-cell recognition in multicellular systems.
Glycoproteins are typically expressed as mixtures of glycoforms, their
oligosaccharides being generated by a template-independent biosynthetic
process. Investigation of their function has been greatly assisted by sources
of homogeneous material. This review summarizes current efforts to obtain
homogeneous glycopeptide and glycoprotein materials by a variety of methods
that draw from the techniques of recombinant expression, chemical synthesis,
enzymatic transformation, and chemoselective ligation. Some of these techniques
remove obstacles to glycoprotein synthesis by installing nonnative linkages and
other modifications for facilitated assembly. The end purpose of the described
approaches is the production of glycosylated materials for experiments relevant
to the biological investigation of glycoproteins, although the strategies
presented apply to other posttranslational modifications as well.</description><subject>Amino Acid Sequence</subject><subject>Chemical synthesis</subject><subject>chemoselective ligation</subject><subject>Glycopeptides - chemical synthesis</subject><subject>Glycopeptides - chemistry</subject><subject>Glycopeptides - metabolism</subject><subject>Glycoproteins</subject><subject>Glycoproteins - chemical synthesis</subject><subject>Glycoproteins - chemistry</subject><subject>Glycoproteins - metabolism</subject><subject>Glycosylation</subject><subject>Glycosylphosphatidylinositols - metabolism</subject><subject>GPI anchor</subject><subject>Humans</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Molecular Structure</subject><subject>Mucins - chemistry</subject><subject>N-linked</subject><subject>O-linked</subject><subject>oligosaccharide</subject><subject>P-Selectin - metabolism</subject><subject>Proteins</subject><subject>Serine - chemistry</subject><subject>Threonine - chemistry</subject><issn>0066-4154</issn><issn>1545-4509</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><recordid>eNqVkV1r2zAUhkVZabK2f2GYXYzdOD1Hki35bmnqJobUKo1T2JXwh0xTkjiz4pX--6rYUOjN2NWBl4f3lXgI-YkwQeThVb7fd635Oyk2TflkdhOBLocQ3GEBY_yEjDHggc8DiL6QMUAY-twlI_LV2mcAYBGnZ2SEFHiAIMZksVB3ah6nsVqvvPny90zdx_dZchOvvGl6MyQPKouTdOXdqgfvOlFLNU9m06WXpI_xKkvm0yxR6QU5rfOtNZfDPSfr2zibLfyB9vMA2dEPa8Hysi5CN19THjHKEQ2FCJBKySIoJauoqUxJy0IwIaMCuDQVFYiiKjg7Jz_63kPb_OmMPerdxpZmu833pumsFiikkIz9E0QpUEoBDvz-CXxuunbvPqEpZWHEHOegXz1Uto21ran1od3s8vZVI-h3N3pwowc37iG6d6N7N67i27DTFTtTfRQMMhwQ98B7Vb51ZRvzYv9_6A3VkJ8x</recordid><startdate>20020101</startdate><enddate>20020101</enddate><creator>Grogan, Michael J</creator><creator>Pratt, Matthew R</creator><creator>Marcaurelle, Lisa A</creator><creator>Bertozzi, Carolyn R</creator><general>Annual Reviews</general><general>Annual Reviews, Inc</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FD</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>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20020101</creationdate><title>HOMOGENEOUS GLYCOPEPTIDES AND GLYCOPROTEINS FOR BIOLOGICAL INVESTIGATION</title><author>Grogan, Michael J ; Pratt, Matthew R ; Marcaurelle, Lisa A ; Bertozzi, Carolyn R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a513t-6f73acfb6510f24932411e20901288390c83d2edec2cb73789b048ed27117db43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Sequence</topic><topic>Chemical synthesis</topic><topic>chemoselective ligation</topic><topic>Glycopeptides - chemical synthesis</topic><topic>Glycopeptides - chemistry</topic><topic>Glycopeptides - metabolism</topic><topic>Glycoproteins</topic><topic>Glycoproteins - chemical synthesis</topic><topic>Glycoproteins - chemistry</topic><topic>Glycoproteins - metabolism</topic><topic>Glycosylation</topic><topic>Glycosylphosphatidylinositols - metabolism</topic><topic>GPI anchor</topic><topic>Humans</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Molecular Structure</topic><topic>Mucins - chemistry</topic><topic>N-linked</topic><topic>O-linked</topic><topic>oligosaccharide</topic><topic>P-Selectin - metabolism</topic><topic>Proteins</topic><topic>Serine - chemistry</topic><topic>Threonine - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Grogan, Michael J</creatorcontrib><creatorcontrib>Pratt, Matthew R</creatorcontrib><creatorcontrib>Marcaurelle, Lisa A</creatorcontrib><creatorcontrib>Bertozzi, Carolyn R</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Complete (ProQuest Database)</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>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</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</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</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 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>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</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>ProQuest Science Journals</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science 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 Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Annual review of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Grogan, Michael J</au><au>Pratt, Matthew R</au><au>Marcaurelle, Lisa A</au><au>Bertozzi, Carolyn R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>HOMOGENEOUS GLYCOPEPTIDES AND GLYCOPROTEINS FOR BIOLOGICAL INVESTIGATION</atitle><jtitle>Annual review of biochemistry</jtitle><addtitle>Annu Rev Biochem</addtitle><date>2002-01-01</date><risdate>2002</risdate><volume>71</volume><issue>1</issue><spage>593</spage><epage>634</epage><pages>593-634</pages><issn>0066-4154</issn><eissn>1545-4509</eissn><coden>ARBOAW</coden><abstract>Protein glycosylation is widely recognized as a modulator of protein
structure, localization, and cell-cell recognition in multicellular systems.
Glycoproteins are typically expressed as mixtures of glycoforms, their
oligosaccharides being generated by a template-independent biosynthetic
process. Investigation of their function has been greatly assisted by sources
of homogeneous material. This review summarizes current efforts to obtain
homogeneous glycopeptide and glycoprotein materials by a variety of methods
that draw from the techniques of recombinant expression, chemical synthesis,
enzymatic transformation, and chemoselective ligation. Some of these techniques
remove obstacles to glycoprotein synthesis by installing nonnative linkages and
other modifications for facilitated assembly. The end purpose of the described
approaches is the production of glycosylated materials for experiments relevant
to the biological investigation of glycoproteins, although the strategies
presented apply to other posttranslational modifications as well.</abstract><cop>Palo Alto, CA 94303-0139</cop><cop>4139 El Camino Way, P.O. Box 10139</cop><cop>USA</cop><pub>Annual Reviews</pub><pmid>12045107</pmid><doi>10.1146/annurev.biochem.71.110601.135334</doi><tpages>42</tpages></addata></record> |
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| identifier | ISSN: 0066-4154 |
| ispartof | Annual review of biochemistry, 2002-01, Vol.71 (1), p.593-634 |
| issn | 0066-4154 1545-4509 |
| language | eng |
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| source | Annual Reviews : Complete Collection of 50 |
| subjects | Amino Acid Sequence Chemical synthesis chemoselective ligation Glycopeptides - chemical synthesis Glycopeptides - chemistry Glycopeptides - metabolism Glycoproteins Glycoproteins - chemical synthesis Glycoproteins - chemistry Glycoproteins - metabolism Glycosylation Glycosylphosphatidylinositols - metabolism GPI anchor Humans Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Models, Molecular Molecular Sequence Data Molecular Structure Mucins - chemistry N-linked O-linked oligosaccharide P-Selectin - metabolism Proteins Serine - chemistry Threonine - chemistry |
| title | HOMOGENEOUS GLYCOPEPTIDES AND GLYCOPROTEINS FOR BIOLOGICAL INVESTIGATION |
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