Peng Wu
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Peng Wu has a total of 13 co-authors. Here are the top co-authors by number of shared publications:
Tianshun Hu
Department of Biochemistry and
3 shared publicationsAlexander Xenakis
Departments of Chemistry and Molecular Cell Biology and Howard Hughes Medical Institute, University of California, Berkeley, and The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720 (USA), Fax: (+1) 510‐643‐2628
2 shared publications- Carolyn R. Bertozzi
Department of Chemistry, Stanford University, Stanford, CA 94305, USA
2 shared publications Chris Smyrniotis
Departments of Chemistry and Molecular Cell Biology and Howard Hughes Medical Institute, University of California, Berkeley, and The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720 (USA), Fax: (+1) 510‐643‐2628
2 shared publicationsPamela V. Chang
Department of Chemistry and Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA 94720, USA
2 shared publicationsXing Chen
Departments of Chemistry and Molecular Cell Biology and Howard Hughes Medical Institute, University of California, Berkeley, and The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720 (USA), Fax: (+1) 510‐643‐2628
2 shared publications
Latest Publications
- 22 September 2009
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 106 (38) , 16096-16101
Chemoenzymatic synthesis of GDP- l -fucose and the Lewis X glycan derivatives
Lewis X (Le x )-containing glycans play important roles in numerous cellular processes. However, the absence of robust, facile, and cost-effective methods for the synthesis of Le x and its structurally related analogs has severely hampered the elucidation of the specific functions of these glycan epitopes. Here we demonstrate that chemically defined guanidine 5′-diphosphate-β- l -fucose (GDP-fucose), the universal fucosyl donor, the Le x trisaccharide, and their C-5 substituted derivatives can be synthesized on preparative scales, using a chemoenzymatic approach. This method exploits l -fucokinase/GDP-fucose pyrophosphorylase (FKP), a bifunctional enzyme isolated from Bacteroides fragilis 9343, which converts l -fucose into GDP-fucose via a fucose-1-phosphate (Fuc-1-P) intermediate. Combining the activities of FKP and a Helicobacter pylori α1,3 fucosyltransferase, we prepared a library of Le x trisaccharide glycans bearing a wide variety of functional groups at the fucose C-5 position. These neoglycoconjugates will be invaluable tools for studying Le x -mediated biological processes.
- 22 September 2009
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 106 (38) , 16096-16101
Chemoenzymatic synthesis of GDP- l -fucose and the Lewis X glycan derivatives
Lewis X (Le x )-containing glycans play important roles in numerous cellular processes. However, the absence of robust, facile, and cost-effective methods for the synthesis of Le x and its structurally related analogs has severely hampered the elucidation of the specific functions of these glycan epitopes. Here we demonstrate that chemically defined guanidine 5′-diphosphate-β- l -fucose (GDP-fucose), the universal fucosyl donor, the Le x trisaccharide, and their C-5 substituted derivatives can be synthesized on preparative scales, using a chemoenzymatic approach. This method exploits l -fucokinase/GDP-fucose pyrophosphorylase (FKP), a bifunctional enzyme isolated from Bacteroides fragilis 9343, which converts l -fucose into GDP-fucose via a fucose-1-phosphate (Fuc-1-P) intermediate. Combining the activities of FKP and a Helicobacter pylori α1,3 fucosyltransferase, we prepared a library of Le x trisaccharide glycans bearing a wide variety of functional groups at the fucose C-5 position. These neoglycoconjugates will be invaluable tools for studying Le x -mediated biological processes.
- 12 May 2009
- Published by Wiley in Angewandte Chemie International Edition
- Vol. 48 (22) , 4030-4033
Metabolic Labeling of Sialic Acids in Living Animals with Alkynyl Sugars
Sialome sweet sialome: As sialic acids are involved in many host–pathogen recognition events and are markers of embryonic and malignant tissues, there is great interest in methods for the enrichment and identification of sialylated glycoproteins from complex tissues. Now N‐(4‐pentynoyl)mannosamine can be used to metabolically label sialylated glycoproteins in living animals, enabling future identification of new biomarkers. magnified image
- 12 May 2009
- Published by Wiley in Angewandte Chemie International Edition
- Vol. 48 (22) , 4030-4033
Metabolic Labeling of Sialic Acids in Living Animals with Alkynyl Sugars
Sialome sweet sialome: As sialic acids are involved in many host–pathogen recognition events and are markers of embryonic and malignant tissues, there is great interest in methods for the enrichment and identification of sialylated glycoproteins from complex tissues. Now N‐(4‐pentynoyl)mannosamine can be used to metabolically label sialylated glycoproteins in living animals, enabling future identification of new biomarkers. magnified image
- 12 May 2009
- Published by Wiley in Angewandte Chemie
- Vol. 121 (22) , 4090-4093
Metabolic Labeling of Sialic Acids in Living Animals with Alkynyl Sugars
- 12 May 2009
- Published by Wiley in Angewandte Chemie
- Vol. 121 (22) , 4090-4093
Metabolic Labeling of Sialic Acids in Living Animals with Alkynyl Sugars