Feixia Chu, Ph.D.

Feixia Chu, Ph.D.

Associate Professor

Educational Background:

Ph.D. University of California, San Francisco, 2004

Courses Taught:

 Proteomics for Biological Discoveries; Biochemistry

Description of current research and/or professional activities:

Mass spectrometry-based proteomics & epigenomics

As our understanding on the cell deepens, we appreciate more and more the sophisticated orchestration of cellular processes, where exchanges of protein components, addition and removal of posttranslational modifications take place in a highly ordered, dynamic manner.  Since modern mass spectrometry excels in both characterization of protein complexes and elucidation of posttranslational modifications, we see a great opportunity to use and develop mass spectrometric techniques to shed light on those complex, dynamic cellular processes.  In particular, we are interested in the molecular recognition among proteins in protein assemblies, the nature and function of posttranslational modifications in chromatin.

Most cellular processes are carried out by protein assemblies, where strong protein interactions constitute stable architecture of the assemblies to ensure efficiency; while weak protein interactions regulate transient function of the assemblies to achieve plasticity.  Conceivably, the molecular recognition among proteins dictates the organization, function and modulation of protein assemblies.  We are interested in structural characterization of protein assemblies with an integrated chemical cross-linking and mass spectrometric approach.  Chemical cross-linking of protein assemblies, followed by mass spectrometric identification of the cross-linked species provides valuable spatial constrains that can be used in conjunction with computational modeling to reveal surfaces involved in protein interactions.  Since chemical cross-linking can covalently ‘lock’ various conformers in the conformational equilibrium of protein    assemblies, we have used this approach to elucidate the structural dynamics of protein complexes.  In addition, we are interested in developing mass spectrometric techniques to facilitate sensitive detection and confident identification of the cross-linked species.  Thus far, we have developed tools and strategies that have proved robust for most binary complexes we have attempted.  Equipped with these tools, we are expanding to the structural characterization of multi-subunit protein assemblies, a challenging domain yet to be tackled by this promising, integrative approach.

The largest macromolecular assembly inside the cell might be chromatin, though little is known about its spatial organization.  The function of structure alterations in chromatin is prominently manifested during the development of multi-cellular organisms, in which a variety of phenotypes are achieved from a singular genotype.  As an epigenetic regulation mechanism, posttranslational modification of chromatin proteins can either recruit or exclude the binding of effector proteins to indirectly, or directly modulate chromatin structure.  The ability for sensitive detection and specific structural elucidation, as well as the compatibility with upstream biochemical purification has made mass spectrometry ideal for the characterization of posttranslational modifications.  We have developed a biochemical technique for rapid, one-step purification of large quantities of low abundance histone vairants and histone-associated proteins. Using this technique, we have elucidated multiple novel histone modifications.  We are also interested in using comparative quantification during mass spectrometric analysis to elucidate dynamic changes in chromatin modifications.  Quantitative profiling of chromatin modifications can serves as a starting point to study their function.  Using a label-free quantitation strategy, we have revealed a significant increase in histone acetylation after UV irradiation, in concert with chromatin de-condensation and chromatin remodeling.

Publications:

Anna Rodina, Tai Wang, Pengrong Yan, Erica DaGama Gomes, Mark P. S. Dunphy, Nagavarakishore Pillarsetty, John Koren, John F. Gerecitano, Tony Taldone, Hongliang Zong, Eloisi Caldas-Lopes, Mary Alpaugh, Adriana Corben, Matthew Riolo, Brad Beattie, Christina Pressl, Radu I. Peter, Chao Xu, Robert Trondl, Hardik J. Patel, Fumiko Shimizu, Alexander Bolaender, Chenghua Yang, Palak Panchal, Mohammad F. Farooq, Sarah Kishinevsky, Shanu Modi, Oscar Lin, Feixia Chu, Sujata Patil, Hediye Erdjument-Bromage, Pat Zanzonico, Clifford Hudis, Lorenz Studer, Gail J. Roboz, Ethel Cesarman, Leandro Cerchietti, Ross Levine, Ari Melnick, Steven M. Larson, Jason S. Lewis, Monica L. Guzman and Gabriela Chiosis. The epichaperome is an integrated chaperome network that facilitates tumour survival. Nature, 538 (7625), 397-401 (2016).

Thomas L. Williams, Christopher W. DiBona, Sean R. Dinneen, Stephanie F. Jones Labadie, Feixia Chu and Leila F. Deravi. Identification of phenoxazone-based pigments in the nanostructured granules of squid chromatophores, Langmuir, 32 (15), 3754-3759 (2016).

Ethan Baker, Yang Tang, Feixia Chu and Louis S. Tisa. Molecular Responses of Frankia sp. strain QA3 to Naphthalene Stress, Can. J. Microbiol., 61 (4), 281-292 (2015).

Xiaohui Zeng-Elmore, Xiong-Zhuo Gao, Riccardo Pellarin, Dina Schneidman-Duhovny, Xiu-Jun Zhang, Katie A. Kozacka, Yang Tang, Andrej Sali, Robert J. Chalkley, Rick H. Cote and Feixia Chu. Molecular architecture of photoreceptor phosphodiesterase elucidated by chemical cross-linking and integrative modeling, J. Mol. Biol., 426 (22), 3713-3728 (2014).

Medhat Rehan, Teal Furnholm, Ryan H. Finethy, Feixia Chu, Gomaah El-Fadly, and Louis S. Tisa. Copper Tolerance by Frankia involves Surface-Binding and Copper Transport, Appl Microbiol Biotechnol., 98 (18), 8005-8015 (2014).

Timothy O. Street, Xiaohui Zeng, Riccardo Pellarin, Massimiliano Bonomi, Andrej Sali, Mark J.S. Kelly, Feixia Chu and David A. Agard.  Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone, J. Mol. Biol., 426 (12), 2393-2404 (2014).

Poshen B. Chen, Jui-Hung Hung, Taylor L. Hickman, Andrew H. Coles, James F. Carey, Zhiping Weng, Feixia Chu, and Thomas G. Fazzio. Hdac6 is a stem-cell specific modulator of Tip60-p400 function, eLife, 2:01557 (2013).

Bin Wu, Alys Peisley, Claire Richards, Hui Yao, Xiaohui Zeng, Cecilie Lin, Feixia Chu, Thomas Walz and Sun Hur. Structural Basis for Viral dsRNA Recognition by MDA5, Cell, 152, 276-89 (2013).

Donna G. Brickner, Sara Ahmed, Lauren Meldi, Abbey Thompson, Will Light, Matthew Young, Taylor L. Hickman, Feixia Chu, Emmanuelle Fabre, Jason H. Brickner. DNA zip codes control gene positioning and interchromosomal clustering at the nuclear periphery, Developmental Cell, 22, 1234-46 (2012). (Previewed in Developmental Cell, 22, 1119-1120)

Huiqing Hu, Liu Hu, Zhonglian Yu, Amanda E. Chasse, Feixia Chu, and Ziyin Li. An orphan kinesin in trypanosomes cooperates with a kinetoplastid-specific kinesin to maintain cell morphology through regulating subpellicular microtubules, J Cell Sci., 125, 4126-4136 (2012).

Gary B. Smejkal, George O. Poinar Jr., Pier Giorgio Righetti, Feixia Chu. Revisiting Jurassic Park:  the isolation of proteins from amber encapsulated organisms millions of years old. Sample Preparation in Biological Mass Spectrometry, 2011, Part 14, 925-938.  DOI 10.1007/978-94-007-0828-0_45.

Miki S. Park, Feixia Chu, Jinghang Xie, Yu Wang, Pompeya Bhattacharya, William K. Chan. Identification of cyclophilin-40 interacting proteins reveals potential cellular function of cyclophilin-40, Analytical Biochemistry, 410, 257-265 (2011). PMC303427.

Feixia Chu, Xuefeng Ren, Amanda Chasse, Taylor Hickman, Luoping Zhang, Jessica Yuh, Martyn T. Smith, Alma L. Burlingame. Quantitative mass spectrometry reveals the epigenome as a target of arsenic, Chemico-Biological Interactions, 192(1-2), 113-117 (2011).       

Feixia Chu, Peter Baker, Robert J. Chalkley, and Alma L. Burlingame. Finding chimeras: a bioinformatic strategy for identification of cross-linked peptides. Mol Cell Proteomics, 9, 25-31 (2010).  (Featured by Journal of Proteome Research: Online News October 27, 2009; by ASBMB Today, December, 2009).

William Jaime Jo, Xuefeng Ren, Feixia Chu, Maria Aleshin, Henri Wintz, Alma Burlingame, Martyn Thomas Smith, Chris Dillon Vulpe, and Luoping Zhang. Acetylated H4K16 by MYST1 protects UROtsa cells from arsenic toxicity and is decreased following chronic arsenic exposure, Toxicology and Applied Pharmacology, 241, 294-302 (2009).

Kathleen A. Worringer, Feixia Chu, and Barbara Panning. The zinc finger protein Zn72D and DEAD box helicase Belle interact and control maleless mRNA and protein levels, BMC Molecular Biology, DOI:10.1186/1471-2199-10-33 (2009).

Ziyin Li, Ju Huck Lee, Feixia Chu, Alma L. Burlingame, Arthur Günzl, and Ching C. Wang. Identification of a Novel Chromosomal Passenger Complex and Its Unique Localization during Cytokinesis in Trypanosoma brucei, PLoS ONE., 3, e2354 (2008).

Paula Casati, Mabel Campi, Feixia Chu, Nagi Suzuki, David Maltby, Shenheng Guan, Alma L. Burlingame, and Virginia Walbot. Targeted histone acetylation and chromatin remodeling are required for UV-B dependent transcriptional activation of regulated genes in maize, Plant Cell, 20, 827-42 (2008).

Mathivanan S, et al. Human Proteinpedia enables sharing of human protein data, Nat Biotechnol., 26, 164-7(2008).

Tobias C. Walther, Pablo S. Aguilar, Florian Froehlich, Feixia Chu, Karen Moreira, Alma L. Burlingame, and Peter Walter. Pkh-kinases control eisosome assembly and organization, EMBO J., 26, 4946-55 (2007).

Daniel R. Hostetter, Carly R.K. Loeb, Feixia Chu, and Charles S. Craik. HIP is a pro-survival substrate of Granzyme B, J. Biol. Chem.282, 27865-74 (2007).

Matthew D. Simon, Feixia Chu, Lisa R. Racki, Cecile C. de la Cruz, Alma L.   Burlingame, Barbara   Panning, Geeta J. Narlikar, and Kevan M. Shokat. The site-specific installation of methyl lysine analogues into recombinant histone, Cell, 128, 1003-1012 (2007).  (Cover story for that issue of Cell).

Feixia Chu, Sami Mahrus, Charles S. Craik, and Alma L. Burlingame.  Isotope-coded and affinity-tagged cross-linking (ICATXL): an efficient strategy   to probe protein interaction surfaces, J Am Chem Soc, 128, 10362-3 (2006).

Feixia Chu, Jason C. Maynard, Gabriela Chiosis, Christopher V. Nicchitta, and Alma L. Burlingame. Identification of novel quaternary domain interactions in the Hsp90 chaperon, GRP94, Protein Science, 15, 1260-9 (2006).

Feixia Chu, Dmitri A. Nusinow, Robert J. Chalkley, Kathrin Plath, Barbara Panning, and Alma L. Burlingame.  Mapping post-translational modifications of the histone variant macroH2A1 using tandem mass spectrometry. Mol Cell Proteomics, 5, 194-203 (2006).

Feixia Chu, Shu-ou Shan, Demetri T. Moustakas, Frank Alber, Pascal F. Egea, Robert M. Stroud, Peter Walter, and Alma L. Burlingame.  Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry. PNAS, 101, 16454-16459 (2004).

Jean-Luc Wolfender, Feixia Chu, Haydn Ball, Florence Wolfender, Michael Fainzilber, Michael A. Baldwin, and Alma L. Burlingame.  Identification of tyrosine sulfation in Conus pennaceus conotoxins a-PnIA and a-PnIB: further investigation of labile sulfo- and phosphopeptides by electrospray, matrix-assisted laser desorption/ionization (MALDI) and atomospheric pressure MALDI mass spectrometry, J. Mass Spec., 34, 447-454 (1999).

Ralph N. Salvatore, Feixia Chu, Advait S. Nalgle, Elona A. Kapxhiu, Richard M. Cross, and Kyung Woon Jung.  Efficient Cs2CO3-promoted solution and Solid Synthesis of Carbonates and Carbamates in the Presence of TBAI, Tetrahedron, 58, 3329-3347 (2002).

Seok-In Kim, Feixia Chu, Eric Duendo, and Kyung Woon Jung.  Alkyl carbonate: efficient three component coupling of aliphatic alcohols, CO2, and alkyl halides in the presence of Cs2CO3, J. Org. Chem., 64, 4578-4579 (1999).

Eric Dueno, Feixia Chu, Seok-In Kim, and Kyung Woon Jung.  Cesium promoted O-alkylation of alcohols for the efficient ether synthesis, Tetrahedron Letters, 40, 1843-1846 (1999).

Feixia Chu, Eric Dueno, and Kyung Woon Jung.  Cs2CO3 promoted O-alkylation of alcohols for the preparation of mixed alkyl carbonates, Tetrahedron Letters, 40, 1847-1850 (1999).

 

 

Educational Background:

   Ph.D. University of California, San Francisco, 2004

   Courses Taught:

   Proteomics for Biological Discoveries; Biochemistry

   Description of current research and/or professional activities:

   Mass spectrometry-based proteomics & epigenomics

   As our understanding on the cell deepens, we appreciate more and more the sophisticated orchestration of cellular processes, where
   exchanges of protein components, addition and removal of posttranslational modifications take place in a highly ordered, dynamic
   manner.  Since modern mass spectrometry excels in both characterization of protein complexes and elucidation of posttranslational
   modifications, we see a great opportunity to use and develop mass spectrometric techniques to shed light on those complex, dynamic
   cellular processes.  In particular, we are interested in the molecular recognition among proteins in protein assemblies, the nature and
   function of posttranslational modifications in chromatin.

   Most cellular processes are carried out by protein assemblies, where strong protein interactions constitute stable architecture of the
   assemblies to ensure efficiency; while weak protein interactions regulate transient function of the assemblies to achieve plasticity. 
   Conceivably, the molecular recognition among proteins dictates the organization, function and modulation of protein assemblies.  We
   are interested in structural characterization of protein assemblies with an integrated chemical cross-linking and mass spectrometric
   approach.  Chemical cross-linking of protein assemblies, followed by mass spectrometric identification of the cross-linked species
   provides valuable spatial constrains that can be used in conjunction with computational modeling to reveal surfaces involved in protein
   interactions.  Since chemical cross-linking can covalently ‘lock’ various conformers in the conformational equilibrium of protein
   assemblies, we have used this approach to elucidate the structural dynamics of protein complexes.  In addition, we are interested in
   developing mass spectrometric techniques to facilitate sensitive detection and confident identification of the cross-linked species. 
   Thus far, we have developed tools and strategies that have proved robust for most binary complexes we have attempted.  Equipped
   with these tools, we are expanding to the structural characterization of multi-subunit protein assemblies, a challenging domain yet to
   be tackled by this promising, integrative approach.

   The largest macromolecular assembly inside the cell might be chromatin, though little is known about its spatial organization.  The
   function of structure alterations in chromatin is prominently manifested during the development of multi-cellular organisms, in which a
   variety of phenotypes are achieved from a singular genotype.  As an epigenetic regulation mechanism, posttranslational modification of
   chromatin proteins can either recruit or exclude the binding of effector proteins to indirectly, or directly modulate chromatin structure. 
   The ability for sensitive detection and specific structural elucidation, as well as the compatibility with upstream biochemical purification
   has made mass spectrometry ideal for the characterization of posttranslational modifications.  We have developed a biochemical
   technique for rapid, one-step purification of large quantities of low abundance histone vairants and histone-associated proteins. Using
   this technique, we have elucidated multiple novel histone modifications.  We are also interested in using comparative quantification
   during mass spectrometric analysis to elucidate dynamic changes in chromatin modifications.  Quantitative profiling of chromatin
   modifications can serves as a starting point to study their function.  Using a label-free quantitation strategy, we have revealed a
   significant increase in histone acetylation after UV irradiation, in concert with chromatin de-condensation and chromatin remodeling.
 

   Publications:

    Xiaohui Zeng-Elmore, Xiong-Zhuo Gao, Riccardo Pellarin, Dina Schneidman-Duhovny, Xiu-Jun Zhang, Katie A. Kozacka, Yang Tang, Andrej
    Sali, Robert J. Chalkley, Rick H. Cote and Feixia Chu. Molecular architecture of photoreceptor phosphodiesterase elucidated by chemical
    cross-linking and integrative modeling, J. Mol. Biol., accepted.

   Medhat Rehan, Teal Furnholm, Ryan H. Finethy, Feixia Chu, Gomaah El-Fadly, and Louis S. Tisa. Copper Tolerance by Frankia involves
   Surface-Binding and Copper Transport, Appl Microbiol Biotechnol., accepted.

   Timothy O. Street, Xiaohui Zeng, Riccardo Pellarin, Massimiliano Bonomi, Andrej Sali, Mark J.S. Kelly, Feixia Chu and David A. Agard. 
   Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone, J. Mol. Biol., 426 (12), 2393-2404
   (2014).

   Poshen B. Chen, Jui-Hung Hung, Taylor L. Hickman, Andrew H. Coles, James F. Carey, Zhiping Weng, Feixia Chu, and Thomas G.
   Fazzio. Hdac6 is a stem-cell specific modulator of Tip60-p400 function, eLife, 2:01557 (2013).

   Bin Wu, Alys Peisley, Claire Richards, Hui Yao, Xiaohui Zeng, Cecilie Lin, Feixia Chu, Thomas Walz and Sun Hur. Structural Basis for
   Viral dsRNA Recognition by MDA5, Cell, 152, 276-89 (2013).

   Donna G. Brickner, Sara Ahmed, Lauren Meldi, Abbey Thompson, Will Light, Matthew Young, Taylor L. Hickman, Feixia Chu,
   Emmanuelle Fabre, Jason H. Brickner. DNA zip codes control gene positioning and interchromosomal clustering at the nuclear periphery,
   Developmental Cell, 22, 1234-46 (2012). (Previewed in Developmental Cell, 22, 1119-1120)

   Huiqing Hu, Liu Hu, Zhonglian Yu, Amanda E. Chasse, Feixia Chu, and Ziyin Li. An orphan kinesin in trypanosomes cooperates with a
   kinetoplastid-specific kinesin to maintain cell morphology through regulating subpellicular microtubules, J Cell Sci., 125, 4126-4136
   (2012).

   Gary B. Smejkal, George O. Poinar Jr., Pier Giorgio Righetti, Feixia Chu. Revisiting Jurassic Park:  the isolation of proteins from amber
   encapsulated organisms millions of years old. Sample Preparation in Biological Mass Spectrometry, 2011, Part 14, 925-938.  DOI
   10.1007/978-94-007-0828-0_45.

   Miki S. Park, Feixia Chu, Jinghang Xie, Yu Wang, Pompeya Bhattacharya, William K. Chan. Identification of cyclophilin-40 interacting
   proteins reveals potential cellular function of cyclophilin-40, Analytical Biochemistry, 410, 257-265 (2011). PMC303427.

   Feixia Chu, Xuefeng Ren, Amanda Chasse, Taylor Hickman, Luoping Zhang, Jessica Yuh, Martyn T. Smith, Alma L. Burlingame.
   Quantitative mass spectrometry reveals the epigenome as a target of arsenic, Chemico-Biological Interactions, 192(1-2), 113-117
   (2011).       

   Feixia Chu, Peter Baker, Robert J. Chalkley, and Alma L. Burlingame. Finding chimeras: a bioinformatic strategy for identification of
   cross-linked peptides. Mol Cell Proteomics, 9, 25-31 (2010).  (Featured by Journal of Proteome Research: Online News October 27,
   2009; by ASBMB Today, December, 2009).

   William Jaime Jo, Xuefeng Ren, Feixia Chu, Maria Aleshin, Henri Wintz, Alma Burlingame, Martyn Thomas Smith, Chris Dillon Vulpe, and
   Luoping Zhang. Acetylated H4K16 by MYST1 protects UROtsa cells from arsenic toxicity and is decreased following chronic arsenic
   exposure, Toxicology and Applied Pharmacology, 241, 294-302 (2009).

   Kathleen A. Worringer, Feixia Chu, and Barbara Panning. The zinc finger protein Zn72D and DEAD box helicase Belle interact and
   control maleless mRNA and protein levels, BMC Molecular Biology, DOI:10.1186/1471-2199-10-33 (2009).

   Ziyin Li, Ju Huck Lee, Feixia Chu, Alma L. Burlingame, Arthur Günzl, and Ching C. Wang. Identification of a Novel Chromosomal
   Passenger Complex and Its Unique Localization during Cytokinesis in Trypanosoma brucei, PLoS ONE., 3, e2354 (2008).

    Paula Casati, Mabel Campi, Feixia Chu, Nagi Suzuki, David Maltby, Shenheng Guan, Alma L. Burlingame, and Virginia Walbot. Targeted
   histone acetylation and chromatin remodeling are required for UV-B dependent transcriptional activation of regulated genes in maize,
   Plant Cell, 20, 827-42 (2008).

   Mathivanan S, et al. Human Proteinpedia enables sharing of human protein data, Nat Biotechnol., 26, 164-7(2008).

   Tobias C. Walther, Pablo S. Aguilar, Florian Froehlich, Feixia Chu, Karen Moreira, Alma L. Burlingame, and Peter Walter. Pkh-kinases
   control eisosome assembly and organization, EMBO J., 26, 4946-55 (2007).

   Daniel R. Hostetter, Carly R.K. Loeb, Feixia Chu, and Charles S. Craik. HIP is a pro-survival substrate of Granzyme B, J. Biol. Chem.,
   282, 27865-74 (2007).

   Matthew D. Simon, Feixia Chu, Lisa R. Racki, Cecile C. de la Cruz, Alma L.   Burlingame, Barbara   Panning, Geeta J. Narlikar, and
   Kevan M. Shokat. The site-specific installation of methyl lysine analogues into recombinant histone, Cell, 128, 1003-1012 (2007).
   (Cover story for that issue of Cell).

   Feixia Chu, Sami Mahrus, Charles S. Craik, and Alma L. Burlingame.  Isotope-coded and affinity-tagged cross-linking (ICATXL): an
   efficient strategy   to probe protein interaction surfaces, J Am Chem Soc, 128, 10362-3 (2006).

   Feixia Chu, Jason C. Maynard, Gabriela Chiosis, Christopher V. Nicchitta, and Alma L. Burlingame. Identification of novel quaternary
   domain interactions in the Hsp90 chaperon, GRP94, Protein Science, 15, 1260-9 (2006).

   Feixia Chu, Dmitri A. Nusinow, Robert J. Chalkley, Kathrin Plath, Barbara Panning, and Alma L. Burlingame.  Mapping post-translational
   modifications of the histone variant macroH2A1 using tandem mass spectrometry. Mol Cell Proteomics, 5, 194-203 (2006).

   Feixia Chu, Shu-ou Shan, Demetri T. Moustakas, Frank Alber, Pascal F. Egea, Robert M. Stroud, Peter Walter, and Alma L.
   Burlingame.  Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass
   spectrometry. PNAS, 101, 16454-16459 (2004).

   Jean-Luc Wolfender, Feixia Chu, Haydn Ball, Florence Wolfender, Michael Fainzilber, Michael A. Baldwin, and Alma L. Burlingame. 
   Identification of tyrosine sulfation in Conus pennaceus conotoxins a-PnIA and a-PnIB: further investigation of labile sulfo- and  
   phosphopeptides by electrospray, matrix-assisted laser desorption/ionization (MALDI) and atomospheric pressure MALDI mass
   spectrometry, J. Mass Spec., 34, 447-454 (1999).

   Ralph N. Salvatore, Feixia Chu, Advait S. Nalgle, Elona A. Kapxhiu, Richard M. Cross, and Kyung Woon Jung.  Efficient Cs2CO3-
   promoted solution and Solid Synthesis of Carbonates and Carbamates in the Presence of TBAI, Tetrahedron, 58, 3329-3347 (2002).

   Seok-In Kim, Feixia Chu, Eric Duendo, and Kyung Woon Jung.  Alkyl carbonate: efficient three component coupling of aliphatic
   alcohols, CO2, and alkyl halides in the presence of Cs2CO3, J. Org. Chem., 64, 4578-4579 (1999).

   Eric Dueno, Feixia Chu, Seok-In Kim, and Kyung Woon Jung.  Cesium promoted O-alkylation of alcohols for the efficient ether
   synthesis, Tetrahedron Letters, 40, 1843-1846 (1999).

   Feixia Chu, Eric Dueno, and Kyung Woon Jung.  Cs2CO3 promoted O-alkylation of alcohols for the preparation of mixed alkyl
   carbonates, Tetrahedron Letters, 40, 1847-1850 (1999).

Feixia Chu, Ph.D.
Rudman Hall, Room 306
Durham, NH 03824
Phone: 
(603) 862-2436