Past Student Publications

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Last Names A-E
Last Names F-K
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Current Student Publications

A-E

John R. Androsavich (Walter Lab)

  1. Wisén S., Androsavich J., Evans C.G., Chang L., Gestwicki J.E., "Chemical modulators of heat shock protein 70 (Hsp70) by sequential, microwave-accelerated reactions on solid phase.", Bioorg Med Chem Lett. 2008, 18, 60. [Full Text]

Victoria A. Assimon (Gestwicki Lab)

  1. Cech, D.L., Wang, P.F., Holt, M.C., Assimon, V.A., Schaub, J. M., Holler, T.P. , Woodward, R.W. “A novel Glucose 6-Phosphate Isomerase from Listeria monocytogenes .” 2014, Protein J. 33(5)447-456.
  2. Connarn, J. N., Assimon, V. A., Reed, R. A., Tse, E., Southworth, D. R., Zuiderweg, E. R. P., Gestwicki, J. E., Sun, S. “The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5) by binding the tetratricopeptide repeat (TPR) domain.” 2013, J Biol Chem. 289(5)2908-2917.
  3. Smith, M. C., Scaglione, K. M., Assimon, V. A., Patury, S., Thompson, A. D., Dickey, C. A., Southworth, D. R., Paulson, H. L., Gestwicki, J. E., Zuiderweg, E. R. P. 2013, Biochemistry. 52(32):5354-5364.
  4. Assimon, V. A., Gillies, A. T., Rauch, J. N., Gestwicki, J. E.  “Hsp70 Protein Complexes as Drug Targets.” 2012, Curr Pharm Design. 19(3):404-417.

Steffen Bernard (J. Smith Lab)

  1. Thompson, A.D., Bernard, S.M., Skiniotis, G., and Gestwicki, J.E. (2012). Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK). Cell Stress Chaperones 17, 313-327.
  2. Akey DL, Li S, Konwerski JR, Confer LA, Bernard SM, Anzai Y, Kato F, Sherman DH, Smith JL. (2011). A New Structural Form in the SAM/Metal-Dependent O‐Methyltransferase Family: MycE from the Mycinamicin Biosynthetic Pathway. J Mol Bio. 413, 438-450.

Devayani P. Bhave (Carroll Lab)

  1. Bhave, D., Muse, W., and Carroll, K., “Drug Targets in Mycobacterial sulfur metabolism”, Infect. Disord. Drug Targets, 2007, 7, 140. [Full Text]
  2. Belokon, Y.N., Bhave, D., D'Addario, D., Groaz, E., North, M. and Tagliazucca, V., "Copper(II)salen catalysed, asymmetric synthesis of α,α-disubstituted amino acids", Tetrahedron, 2003, 60, 1849. [Full Text]
  3. Belokon, Y.N., Bhave, D., D'Addario, D., Groaz, E., Maleev, V., North, M. and Pertrosyan, A., "Catalytic, asymmetric synthesis of α,α-disubstituted amino acids", Tetrahedron Lett., 2003, 44, 2045. [Full Text]

Tonia J. Buchholz (Sherman Lab)

  1. Buchholz, T.J., Geders, T.W., Bartley, F.E., Reynolds, K.A., Smith,J.L., and Sherman, D.H., "Structural basis for binding specificity between subclasses of modular polyketide synthase docking domains", ACS Chem. Biol., 2009, 4, 41-52. [Full Text]
  2. Lopanik, N.B., Shields,J.A., Buchholz, T.J., Rath, C.M., Hothersoll, J., Haygood, M.G., Hakansson, K., Thomas, C.M., and Sherman, D.H., "In vivo and in vitro trans-acylation by BryP, the putative bryostatin pathway acyltransferase derived from an uncultured marine symbiont", Chem. Biol, 2008, 15, 1175-1186. [Full Text]
  3. Buchholz, T.J., Kittendorf, J.D., Sherman, D.H., "Polyketide Biosynthesis, Modular Polyketide Synthases: Nature's Platform for the Expansion of Structural Diversity?", Wiley Encyclopedia of Chemical Biology, 2008
  4. Kittendorf, J.D., Beck, B.J., Buchholz, T.J., Seufert, W., and Sherman, D.H., "Interrogating the Molecular Basis for Multiple Macrolactone Ring Formation by the Pikromycin Polyketide Synthase", Chemistry and Biology, 2007, 14, 944. [Full Text]
  5. Demo, S.D., Kirk, C.J., Aujay, M.A., Buchholz, T.J., Dajee, M., Ho, M.N., Jiang, J., Laidig, G.J., Lewis, E.R., Parlati, F., Shenk, K.D., Smyth, M.S., Sun, C.M., Vallone, M.K., Woo, T.M., Molineaux, C.J. and Bennett, M.K., "Antitumor Activity of PR-171, a Novel Irreversuble Inhibitor of the Proteasome", Cancer Res., 2007, 67, 6383. [Full Text]
  6. Grüschow, S., Buchholz, T.J., Seufert, W., Dordick, J.S. and Sherman, D.H., "Substrate Profile Analysis and ACP-Mediated Acyl Transfer in Streptomyces coelicolor Type III Polyketide Synthases", ChemBioChem, 2007, 8, 863. [Full Text]
  7. Bennett, M.K., Buchholz, T.J., Demo, S.D., Laidig, G.J., Lewis, E.R. and Smyth, M.S., "Compounds for Enzyme Inhibition", U.S./International Patent Applications, 2006 [Full Text]
  8. Schuster, M.C., Mann, D.A., Buchholz, T.J., Johnson, K.M., Thomas, W.D., and Kiessling, L.L., "Parallel Synthesis of Glycomimetic Libraries: Targeting a C-Type Lectin", Org. Lett., 2003, 5, 1407. [Full Text]
  9. Buchholz, T.J., and Burke, T. J., "Methods and Kits for Assays Utilizing Fluorescence Polarization", U.S./International Patent Applications, 2003 [Full Text]

Benjamin C. Buer (Marsh Lab)

  1. Buer BC, Meagher JL, Stuckey JA, Marsh EN. Structural basis for the enhanced stability of highly fluorinated proteins. Proc Natl Acad Sci USA. 2012;109(13):4810-5.
  2. Buer BC, Marsh EN. Fluorine: A new element in protein design. Protein Sci. 2012; 21(4):453-62.
  3. Suzuki Y, Buer BC, Al-Hashimi HM, Marsh EN. Using fluorine nuclear magnetic resonance to probe changes in the structure and dynamics of membrane active peptides interacting with lipid bilayers. Biochemistry. 2011; 50(27):5979-87.
  4. Buer BC, Chugh J, Al-Hashimi HM, Marsh EN. Using fluorine nuclear magnetic resonance to probe the interaction of membrane-active peptides with the lipid bilayer. Biochemistry. 2010; 49(27):5760-5.
  5. Buer BC, de la Salud-Bea R, Al Hashimi HM, Marsh EN. Engineering protein stability and specificity using fluorous amino acids: the importance of packing effects. Biochemistry. 2009; 48(45):10810-7.
  6. Marsh EN, Buer BC, Ramamoorthy A. Fluorine--a new element in the design of membrane-active peptides. Mol Biosyst. 2009; 5(10): 1143-7.

James Carolan (Mapp Lab)

  1. Evans, C. G., Smith, M. C., Carolan, J.P., Gestwicki, J. E. “Improved synthesis of 15-deoxyspergualin analogs using the Ugi multicomponent reaction” Bioorgan. Med. Chem. Lett. 2011, 21, 2587.
  2. Olson, M.E.; Carolan, J.P.; Chiodo, M. V.; Lazzara, P. R.; Mohan, R. S. "Iron(III) Tosylate Catalyzed Deprotection of Aromatic Acetals in Water." Tetrahedron Lett. 2010, 51, 3969.
  3. Bothwell, J.M., Angeles, V.V., Carolan, J.P., Olson, M.E. and Mohan, R.S., "A mild and chemoselective method for the deprotection of tert-butyldimethylsilyl (TBDMS) ethers using iron(III) tosylate as a catalyst", Tetrahedron Letters, 2010, 51, 1056. [Full Text]

Chia Yin (Lyra) Chang (Gestwicki Lab)

  1. Chang, L., Thompson, A.D., Ung, P., Carlson, H.A., Gestwicki, J.E., "Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (HSP70/DNAK)", J. Biol. Chem., 2010. [Full Text]
  2. Evans, C.G., Chang, L., Gestwicki, J.E.,"Heat Shock Protein 70
    (Hsp70) as an Emerging Drug Target", J. Med. Chem., 2010. [Full Text]
  3. Bertelsen, E.B., Chang, L., Gestwicki, J.E., Zuiderweg, E.R., "Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate", Proc. Natl. Acad. Sci. U S A, 2009, 106(21), 8471. [Full Text]
  4. Jinwal, U.K., Miyata, Y., Koren, J. 3rd, Jones, J.R., Trotter, J.H., Chang, L., O'Leary, J., Morgan, D., Lee, D.C., Shults, C.L., Rousaki, A., Weeber, E.J., Zuiderweg, E.R., Gestwicki, J.E., and Dickey, C.A., "Chemical manipulation of hsp70 ATPase activity regulates tau stability", J. Neurosci., 2009, 29(39), 12079. [Full Text]
  5. Koren, J., Jinwal, U.K., Jin, Y., O'Leary, J., Jones, J.R., Johnson, A.G., Blair, L.J., Abisambra, J.F., Chang, L., Miyata, Y., Cheng, A.M., Guo, J., Cheng, J.Q., Gestwicki, J.E., and Dickey, C.A., "Facilitating Akt clearance via manipulation of Hsp70 activity and levels", J. Biol. Chem., 2009, Epub ahead of print. [Full Text]
  6. Wisen, S., Androsavich, J., Evans, C.G., Chang, L., Gestwicki, J.E., "Chemical modulators of heat shock protein 70 (Hsp70) by sequential, microwave-accelerated reactions on solid phase", Bioorgan. Med. Chem., 2008, 18, 60. [Full Text]
  7. Chang, L., Bertelsen, E.B., Wisen, S., Larsen, E.M., Zuiderweg, E.R.P., Gestwicki, J.E., "High throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone, DnaK", Anal. Biochem., 2008, 372, 167. [Full Text]
  8. Chang, C.Y., Hong, W.W., Chong, P. and Wu, S.C., "Influence of Intron and Exon Splicing Enhancers on Mammalian Cell Expression of a Truncated Spike Protein of SARS-CoV and its Implication for Subunit Vaccine Development", Vaccine, 2006, 24, 1132. [Full Text]

Wenjing Chen (Garneau-Tsodikova Lab)

  1. Chen, W., Biswas, T., Porter, V.R., Tsodikov, O.V., and Garneau-Tsodikova, S., "Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB", Proc. Nat. Acad. Scie., U.S.A., 2011, 108, 9804. [Full Text]
  2. Green, K.D., Chen, W., and Garneau-Tsodikova, S., "Effects of alteringaminoglycoside structures on bacterial resistance enzyme activities, Antimicrob", Agents Chemother., 2011, 55, 3207. [Full Text]
  3. Houghton, J.L., Green, K.D., Chen, W., and Garneau-Tsodikova, S., "The future of aminoglycosides: The end or renaissance", Chembiochem, 2010, 11, 800. [Full Text]
  4. Green, K.D., Chen, W., Houghton, J.L., Fridman, M., and Garneau-Tsodikova, S., "Exploring the Substrate Promiscuity of Drug-Modifying Enzymes for the Chemoenzymatic Generation of N-Acylated Aminoglycosides", Chembiochem, 2010, 11, 119. [Full Text]

John A. Conrad (Palfey Lab)

  1. Conrad JA, Moran GR., "The Interaction of Hydroxymandelate Synthase with the 4-Hydroxyphenylpyruvate Dioxygenase Inhibitor: NTBC", Inorganica Chim Acta., 2008, 361, 1197. [Full Text]

Brian T. DeVree (Sunahara Lab)

  1. Westfield, G.H., Rasmussen, S.G., Su, M., Dutta, S., DeVree, B.T., Chung, K.Y., Calinski, D., Velez-Ruiz, G., Oleskie, A.N., Pardon, E., Chae, P.S., Liu, T., Li, S., Woods, V.L. Jr., Steyaert, J., Kobilka, B.K., Sunahara, R.K., Skiniotis, G. “Structural flexibility of the G alpha s
    alpha-helical domain in the beta2-adrenoceptor Gs complex” PNAS 2011, 108, 16086-91.
  2. Rasmussen, S.G.*, DeVree, B.T.*, Zou, Y., Kruse, A.C., Chung, K.Y., Kobilka, T.S., Thian, F.S., Chae, P.S., Pardon, E., Calinski, D., Mathiesen, J.M., Shah, S.T., Lyons, J.A., Caffrey, M., Gellman, S.H., Steyaert, J., Skiniotis, G., Weis, W.I., Sunahara, R.K., Kobilka, B.K. “Crystal structure of the β2 adrenergic receptor-Gs protein complex” Nature, 2011 477, 549-55. [Full Text]
  3. Chung, K.Y., Rasmussen, S.G., Liu, T., Li, S., DeVree, B.T., Chae, P.S., Calinski, D., Kobilka, B.K., Woods, V.L. Jr., Sunahara, R.K. “Conformational changes in the G protein Gs induced by the β2 adrenergic receptor” Nature. 2011, 477, 611-5. [Full Text]
  4. Rasmussen, S.G., Choi, H.J., Fung, J.J., Pardon, E., Casarosa, P., Chae, P.S., DeVree, B.T., Rosenbaum, D.M., Thian, F.S., Kobilka, T.S., Schnapp, A., Konetzki, I., Sunahara, R.K., Gellman, S.H., Pautsch, A., Steyaert, J., Weis, W.I., Kobilka, B.K. "Structure of a nanobody-stabilized active state of the beta(2) adrenoceptor", Nature, 2011, 469,175-80. [Full Text]
  5. Rosenbaum, D.M., Zhang, C., Lyons, J.A., Holl, R., Aragao, D., Arlow, D.H., Rasmussen, S.G., Choi, H.J., DeVree, B.T., Sunahara, R.K., Chae, P.S., Gellman, S.H., Dror, R.O., Shaw, D.E., Weis, W.I., Caffrey, M., Gmeiner, P., Kobilka, B.K. "Structure and function of an irreversible agonist-beta(2) adrenoceptor complex", Nature, 2011, 469, 236-40. [Full Text]
  6. Fung, J.J., Deupi, X., Pardo, L., Yao, X.J., Velez-Ruiz, G.A., DeVree, B.T., Sunahara, R.K., Kobilka, B.K. "Ligand-regulated oligomerization of beta(2)-adrenoceptors in a model lipid bilayer", EMBO J., 2009, 28, 3315-28. [Full Text]
  7. Yao, X.J., Whorton, M.R., Velez-Ruiz, G., Rasmussen, S., DeVree, B., Deupi, X., Sunahara, R.K., and Kobilka, B. "The effect of ligand efficacy on the formation and stability of a GPCR-G protein complex", PNAS, 2009, 106, 9501. [Full Text]

Amanda Dugan (Mapp Lab)

  1. Krishnamurthy, M., Dugan, A., Nwokoye, A., Fung, Y-H, Lancia, J.K., Majmudar, C.Y. and Mapp, A.K. (2011) Caught in the Act: Covalent Cross-linking Captures Activator-Coactivator Interactions in Vivo. ACS Chem. Biol. 6; 1321-1326. [Full Text]

Christopher G. Evans (Gestwicki Lab)

  1. Evans, C.G., Chang, L., Gestwicki, J.E.,"Heat Shock Protein 70
    (Hsp70) as an Emerging Drug Target", J. Med. Chem., 2010. [Full Text]
  2. Wisen, S., Androsavich, J., Evans, C.G., Chang, L., Gestwicki, J.E., "Chemical modifiers of heat shock protein 70 (Hsp70) by sequential, microwave-accelerated reactions on solid phase", Bioorgan. Med. Chem., 2008, 18, 60. [Full Text]
  3. Evans, C.G., Wisen, S., and Gestwicki, J.E., "Heat shock protein 70 and 90 inhibit early stages of amyloid ß(1-42) aggregation in vitro", J Biol Chem, 2006, 281, 33182. [Full Text]

F-K

Tasha M. Francis (Glick Lab)

  1. Nicolaou, K.C., Brenzovich, W.E., Bulger, P.G. and Francis, T.M., "Synthesis of iso-epoxy-amphidinolide N and des-epoxy-caribenolide I Structures. Initial Forays", Org. & Biomol. Chem., 2006, 4, 2119. [Full Text]
  2. Francis, T.M., Sundberg, T.B., Cleary, J., Groendyke, T., Opipari, A.W. Jr. and Glick, G.D., "Identification of cytotoxic, T-cell-selective 1,4-benzodiazepine-2,5-diones", Bioorg. & Med. Chem. Lett., 2006, 16, 2423. [Full Text]
  3. Zhou, J., Zong, C., Francis, T.M. and Braun, C.L., "Radiative Exciplexes of 1,2,4,5-Tetracyanobenzene with Sterically Hindered Alkylbenzenes", J. Phys. Chem. A., 2003, 107, 8319. [Full Text]
  4. Bruckner, C., McCarthy, J.R., Daniell, H.W., Pendon, Z.D., Ilagan, R.P., Francis, T.M., Ren, L., Birge, R.R. and Frank, H.A., "A Spectroscopic and Computational Study of the Singlet and Triplet Excited States of Synthetic β-Functionalized Chlorins", Chemical Physics, 2003, 294, 285. [Full Text]
  5. Zhou, J., Findley, B.R., Francis, T.M., Nytko, E.A. and Braun, C.L., "The Solution Dynamics of Photoinduced Geminate Radical Ion Pairs: Free Ion Formation", Chem. Phys. Lett., 2002, 362, 63. [Full Text]

Anne Gillies (Gestwicki Lab)

  1. Assimon, V.A., Gillies, A.T., Rauch, J.N., Gestwicki, J.E. Hsp70 Protein Complexes as Drug Targets. Curr Pharm Des. 2012 (Manuscript accepted)
  2. Thompson, A.D., Scaglione, K.M., Prensner, J., Gillies, A.T., Chinnaiyan, A., Paulson, H.L., Jinwal, U.K., Dickey, C.A., Gestwicki, J.E. Analysis of the tau-associated proteome reveals that exchange of hsp70 for hsp90 is involved in tau degradation. ACS Chem Biol. 2012, 7(10), 1677-86.
  3. Srinivasan, S.R., Gillies, A.T., Chang, L., Thompson, A.D., Gestwicki, J.E. Molecular chaperones DnaK and DnaJ share predicted binding sites on most proteins in the E. coli proteome. Mol Biosyst. 2012, 8(9), 2323-33. 
  4. Gillies, A.T., Taylor, R., Gestwicki, J.E. Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones. Mol Biosyst. 2012, 8(11), 2901-8. [Full Text]
  5. Gillies, A.T., Gai, X.S., Buckwalter, B.L., Fenlon, E.F., Brewer, S.H., "(15)N NMR studies of a nitrile-modified nucleoside", J. Phys. Chem. B, 2010, 114, 17136-41. [Full Text]
  6. Watson, M.D., Gai, X.S., Gillies, A.T., Brewer, S.H., and Fenlon, E.E., "A vibrational probe for local nucleic acid environments: 5-cyano-2'-deoxyuridine", J. Phy. Chem. B., 2008, 112, 13188. [Full Text]

Alisa Glukhova (Tesmer Lab)

  1. Yokom AL, Morishima Y, Lau M, Su M, Glukhova A, Osawa Y, Southworth DR, Architecture of the Nitric Oxide Synthase Holoenzyme Reveals Large Conformational Changes and a Calmodulin-Driven Release of the FMN Domain. J Biol Chem. 2014 April 15.
  2. Bukach, O.V., Glukhova, A.E., Seit-Nebi, A.S., and Gusev, N.B., "Heterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20)", Biochim. Biophys. Acta., 2009, 1794, 486. [Full Text]

Felicia Gray (Cierpicki/Grembecka Labs)

  1. P. Mitra, D. Shultis, J.R Brender, J. Czajka, D. Marsh, F.L.V Gray, T. Cierpicki, Y. Zhang. “An evolution-based approach to de novo protein design and case study on Mycobacterium Tuberculosis.” PLoS Computational Biology, in press (2013).
  2. Gray FLV, Murai MJ, Grembecka J, Cierpicki T. "Detection of disordered regions in globular proteins using 13C-detected NMR" Protein Science 2012, 21, 1954-60. [Full Text]

Mark Hedglin (O'Brien Lab)

  1. Hedglin, M., Zhang, Y., O’Brien, P.J. (2015) Probing the DNA structural requirements for facilitated diffusion. Biochemistry 54:557-66. http://www.ncbi.nlm.nih.gov/pubmed/25495964
  2. Hedglin, M., Zhang, Y., O’Brien, P.J. (2013) Intersegmental transfer by a monomeric DNA repair glycosylase. J. Biol. Chem. 288:24550-9. http://www.ncbi.nlm.nih.gov/pubmed/23839988
  3. Hedglin, M., O’Brien, P.J. (2010) Hopping enables a DNA repair glycosylase to efficiently search both strands and bypass a bound protein. ACS Chem. Biol. 5:427-36. http://www.ncbi.nlm.nih.gov/pubmed/20201599
  4. Hedglin, M. and O'Brien, PJ., "Hopping Enables a DNA Repair Glycosylase To Search Both Strands and Bypass a Bound Protein ", ACS Chemical Biology, DOI: 10.1021/cb1000185. Full Text
  5. Hedglin, M. and O'Brien, PJ., "Human Alkyladenine DNA glucosylase employs a Processive Search for DNA damage", Biochemistry, 2008, 47, 11434. [Full Text]
  6. KrennHrubec, K., Marshall, B.L., Hedglin, M., Verdin, E. and Ulrich, S.M., "Design and Evaluation of 'Linkerless' hydroxamic acids as selective HDAC8 inhibitors," Bioorg. Med. Chem. Lett., 2007, 17, 2874. [Full Text]

Leshern Karamchand (Kopelman Lab)

  1. Karamchand, L., Dawood, H., and Chuturgoon, A. A., "Lymphocyte mitochondrial depolarization and apoptosis in HIV-1-infected HAART patients", J. Acquir. Immune. Defic. Syndr., 2008, 48, 381. [Full Text]
  2. Karamchand L, Kim G, Wang S, Hah HJ, Ray A, Jiddou R, Koo Lee YE, Philbert MA, Kopelman R., "Modulation of hydrogel nanoparticle intracellular trafficking by multivalent surface engineering with tumor targeting peptide.", Nanoscale. 2013 Nov 7;5(21):10327-44. doi: 10.1039/c3nr00908d. Epub 2013 Sep 11.

Cesar Kenaan (Hollenberg Lab)

  1. Kenaan, C., Zhang, H., and Hollenberg, P.F., "High-Throughput Fluorescence Assay for Cytochrome P450 Mechanism-Based Inactivators." Methods in Molecular Biology, 2012.
  2. Zin, H.L., Kenaan, C., and Hollenberg, P.F. "Identification of the Residue in Human CYP3A4 that is Covalently Modified by Bergamottin and the Reactive Intermediate that Contributes to the Grapefruit Juice Effect." Drug Metab Dispos., 2012.
  3. Zhang, H., Sridar, C., Kenaan, C., Amunugama, H., Ballou, D.P., and Hollenberg, P.F. "Polymorphic Variants Of Cytochrome P450 2B6 (CYP2B6.4 - CYP2B6.9) Exhibit Altered Rates Of Metabolism For Bupropion And Efavirenz: A Charge-Reversal Mutation In The K139E Variant (CYP2B6.8) Impairs Formation Of A Functional P450-Reductase Complex." J. Pharmacol. Expt. Ther., 2011.
  4. Kenaan, C., Zhang, H., Shea. E.V. and Hollenberg, P.F. "Uncovering the Role of Hydrophobic Residues in Cytochrome P450 - Cytochrome P450 Reductase Interactions." Biochemistry, 2011 50 (19), pp 3957-3967 [Full Text]
  5. Zhang, H., Lin, H.L., Kenaan, C., and Hollenberg, P.F."Targeting of the highly conserved threonine 302 residue of cytochromes P450 2B family during mechanism-based inactivation by aryl acetylenes", Archives of Biochemistry and Biophysics, 2011, 507(1):135-43. [Full Text]
  6. Kenaan, C., Zhang, H., and Hollenberg, P.F., "A Quantitative High-Throughput 96-well plate Fluorescence Assay for Mechanism-Based Inactivators of Cytochromes P450 Exemplified using CYP2B6." Nature Protocols, 2010, 5, 10. [Full Text]
  7. Zhang, H., Kenaan, C., Hamdane, D., Hui Bon Hoa, G., Hollenberg, P.F., "Effect of Conformational Dynamics on Substrate Recognition and Specificity as Probed by the introduction of a De Novo Disulfide bond into Cytochrome P450 2B1", J. Biol. Chem., 2009, 284, 25678. [Full Text]
  8. Marsili, R. and Kenaan, C., "Identification of Iris Scent Volatiles Using Dynamic Headspace with PDMS foam Trapping and GC-TOFMS", Perf. Flav., 2007, 32, 18. [Full Text]
  9. Marsili, R.T., Laskonis, L.C. and Kenaan, C., "Evaluation of PDMS-based Extraction Techniques and GC-TOFMS for the Analysis of Off-flavor Chemicals in Beer", Amer. Soc. of Brewing Chemists, 2007, 65, 129. [Full Text]

Byung Chul Kim (Fierke Lab)

  1. Kim, B.C., Lee, J.M., Ahn, J.S., and Kim, B.S., "Cloning, Sequencing, and characterization of the Pradimicin Biosynthetic Gene Cluster of Actinomadura hibisca P157-2", J. Microbiol. Biotechnol., 2007, 17, 830-839. [Full Text]

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Jody K. Lancia (Mapp Lab)

  1. Marinec, P.S., Lancia, J. K., and Gestwicki, J. E., "Bifunctional molecules evade cytochrome P450 metabolism by forming protective complexes with FK506-binding protein.", Mol. BioSyst., 2008, 4, 571. [Full Text]
  2. Fischer, J.L., Lancia, J.K., Mathur, A. and Smith, M.L., "Selenium protection from DNA damage involves a Ref1/p53/Brca1 protein complex", Anticancer Res., 2006, 26, 899.
  3. Smith, M.L., Lancia, J.K., Mercer, T.I., Ip, C., "Selenium compounds regulate p53 by common and distinctive mechanisms", Anticancer Res., 2004, 24, 1401.

Stephen E. Leonard (Carroll Lab)

  1. Depuydt, M., Leonard, S.E., Vertommen, D., Denoncin, K., Morsomme, P., Wahni, K. and Carroll, K.S., "A Periplasmic Reducing System Protects Single Cysteine Residues from Oxidation", Science., 2009, 326, 1109. [Full Text]
  2. Leonard, S.E., Reddie, K.G and Carroll, K.S., "Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells", ACS Chem. Biol., 2009. [Full Text]
  3. Reddie, K.G, Seo, Y.H., Muse III, W.B., Leonard, S.E. and Carroll, K.S., "A chemical approach for detecting sulfenic acid-modified proteins in living cells", Mol. BioSyst., 2008. [Full Text]

Paul Lund (Walter Lab)

  1. Fung, K. L.; Pan, J.; Ohnuma, S.; Lund, P. E.; Pixley, J. N.; Kimchi-Sarfaty, C.; Ambudkar, S. V.; Gottesman, M. M. MDR1 synonymous polymorphisms alter transporter specificity and protein stability in a stable epithelial monolayer. Cancer Res. 2014, 74, 598-608.
  2. Macadangdang, B.; Zhang, N.; Lund, P. E.; Marple, A. H.; Okabe, M.; Gottesman, M. M.; Appella, D. H.; Kimchi-Sarfaty, C. Inhibition of multidrug resistance by SV40 pseudovirion delivery of an antigene peptide nucleic acid (PNA) in cultured cells. PLoS ONE 2011, 6, e17981.
  3. Lund, P., Hunt, R., Gottesman, M.M. and Kimchi-Sarfaty, C., "Pseudovirions as Vehicles for the Delivery of siRNA ", Pharmaceutical Research, 2010, 27, 400. [Full Text]
  4. Amit, P., Watson, R.M., Lund, P., Xing, Y., Burke, K., He, Y., Borguet, E., Achim, C. and Waldeck, D.H., "Charge Transfer through Single-Stranded Peptide Nucleic Acid Composed of Thymine Nucleotides", J. Phy. Chem. C, 2008, 112, 7233. [Full Text]

Yoshi Miyata (Gestwicki Lab)

  1. Koren, J., Jinwal, U.K., Jin, Y., O'Leary, J., Jones, J.R., Johnson, A.G., Blair, L.J., Abisambra, J.F., Chang, L., Miyata, Y., Cheng, A.M., Guo, J., Cheng, J.Q., Gestwicki, J.E. and Dickey, C.A., "Facilitating Akt Clearance via Manipulation of Hsp70 Activity and Levels.", J. Biol. Chem., 2010, 285, 2498. Full Text
  2. Patury, S., Miyata, Y. and Gestwicki, J.E., "Pharmacological Targeting of the Hsp70 Chaperone.", Curr. Top. Med. Chem., 2009 ;9(15):1337-51. Full Text
  3. Jinwal, U.K., Miyata, Y., Koren, J., Jones, J.R., Trotter, J.H., Chang, L., O'Leary, J., Morgan, D., Lee, D.C., Shults, C.L., Rousaki, A., Weeber, E.J., Zuiderweg, E.R.P., Gestwicki, J.E. and Dickey, C.A., "Chemical Manipulation of Hsp70 ATPase Activity Regulates Tau Stability.", J.Neurosci., 2009, 29, 12079. Full Text
  4. Miyata, Y. and Matsunaga, S., "Structure Elucidation of 21,22-dihydroxyonnamides A(1)-A(4) from the Marine Sponge Theonella swinhoei: an Empirical Rule to Assign the Relative Stereochemistry of Linear 1,5-diols.", Tetrahedron Lett., 2008, 49, 6334. Full Text
  5. Miyata, Y., Diyabalanage, T., Amsler, C.D., McClintock, J.B., Valerioote, F.A., Baker, B.J., "Ecdysteroids from the Antarctic Tunicate Synoicum adareanum.", J. Nat. Prod., 2007, 70, 1859. Full Text
  6. Kobayashi, H., Miyata, Y., Okada, K., Fujita, T., Iwashita, T., Nakao, Y., Fusetani, N. and Matsunaga, S., "The Structures of Three New Shishididemniols from a Tunicate of the Family Didemnida.", Tetrahedron, 2007, 63, 6748. Full Text
  7. Matsunaga, S., Miyata, Y., van Soest, R.W.M. and Nobuhiro, F., "Tetradehydrohalicyclamine A and 22-Hydroxyhalicyclamine A, New Cytotoxic Bis-piperdine Alkaloids from a Marine Sponge Amphimedon sp.", J. Nat. Prod., 2004, 67, 1758. [Full Text]

Evgenia Nikolova (Al-Hashimi Lab)

  1. Nikolova, E.N., Kim, E., Wise, A.A., O’Brien, P., Andricioaei, I., and Al-Hashimi, H. M. “Transient Hoogsteen Base-pairs in Canonical Duplex DNA”, Nature, Published online 2011 Jan 26
  2. Nikolova, E.N. and Al-Hashimi, H.M. “Thermodynamics of RNA melting, one base pair at a time.” RNA. 2010 Sep;16(9):1687-91. Epub 2010 Jul 21.
  3. Nikolova, E.N. and Al-Hashimi, H.M. “Preparation, resonance assignment, and preliminary dynamics characterization of residue specific 13C/15N-labeled elongated DNA for the study of sequence-directed dynamics by NMR.” J. Biomol. NMR. 2009 Sep;45(1-2):9-16. Epub 2009 Jul 28.
  4. Hansen, A.L., Nikolova, E.N., Casiano-Negroni, A., and Al-Hashimi, H.M., "Extending the range of microsecond-to-millisecond chemical exchange detected in labeled and unlabeled nucleic acids by selective carbon R(1rho) NMR spectroscopy", J. Am. Chem. Soc., 2009, 131, 3818. [Full Text]
  5. Pereira, M.J.B., Nikolova, E. N., Hiley, S. L., Jaikaran, D., Collins, R. A. and Walter, N. G., "Single VS Ribozyme Molecules Reveal Dynamic and Hierarchical Folding Toward Catalysis", J. Mol. Biol., 2008, 382, 496. [Full Text]

Tad Ogorzalek (Marsh Lab)

  1. Gramer, M.J., and Ogorzalek, T, "A semi-empirical mathematical model useful for describing the relationship between Carbon Dioxide, pH, Lactate, and base in a bicarbonate-buffered cell-culture process", Biotechnol. Appl. Biochem., 2007, 47, 197-204. [Full Text]

Candice E. Paulsen (Carroll Lab)

  1. Paulsen, C.E., and Carroll, K.S., "Orchestrating Redox Signaling Networks through Regulatory Cysteine Switches", ACS Chem. Biol., 2010, 5, 47. [Full Text]
  2. Paulsen, C.E., and Carroll, K.S., “Chemical dissection of an essential redox switch in yeast”, Chem. Biol., 2009, 16, 217. [Full Text]

Carol Ann Pitcairn (Fierke Lab)

  1. Olson DE, Udeshi ND, Wolfson NA, Pitcairn CA, Sullivan ED, Jaffe JD, Svinkina T, Natoli T, Lu X, Paulk J, McCarren P, Wagner FF, Barker D, Howe E, Lazzaro F, Gale JP, Zhang YL, Subramanian A, Fierke CA, Carr SA, Holson EB. An Unbiased Approach To Identify Endogenous Substrates of “Histone” Deacetylase 8. ACS Chem Biol. 2014, [Epub ahed of print.]
  2. Wolfson, N. A.; Pitcairn, C. A.; Sullivan, E. D.; Joseph, C. G.; Fierke, C. A., An enzyme-coupled assay measuring acetate production for profiling histone deacetylase specificity. Analytical Biochemistry 2014, 456 (0), 61-69.
  3. Wolfson, N. A.; Pitcairn, C. A.; Fierke, C. A., HDAC8 substrates: Histones and beyond. Biopolymers. 2013, 99 (2), 112-126.

 

Q-T

Christopher M. Rath (Sherman Lab)

  1. Lopanik, N.B., Shields,J.A., Buchholz, T.J., Rath, C.M., Hothersoll, J., Haygood, M.G., Hakansson, K., Thomas, C.M., and Sherman, D.H., "In vivo and in vitro trans-acylation by BryP, the putative bryostatin pathway acyltransferase derived from an uncultured marine symbiont", Chem. Biol, 2008, 15, 1175-1186. [Full Text]
  2. Pfleger, B.F., Kim, Y., Nusca, T.D., Maltseva, N., Lee, J.Y., Rath, C.M., Scaglione, J.B., Janes, B.K., Anderson, A.C., Bergman, N.H., Hanna, P.C., Joachimiak, A., and Sherman, D.H.,"Structural and functional analysis of AsbF: Origin of the stealth 3,4-dihydroxybenzoic acid subunit for petrobactin biosynthesis", Proc. Nat'l. Acad. Sci., 2008, 105, 17133-17138. [Full Text]
  3. Amagata, T., Rath, C., Rigot, J.F., Tarlov, N., Tenney, K., Valeriote, F.A. and Crews, P., "Structures and cytoxic properties of trichoverriods and their macrolide analogues produced by saltwater culture of Myrothecium verrucaria", J. Med. Chem., 2003, 46, 4342. [Full Text]

Chenxi Shen (Nikolovska-Coleska Lab)

  1. Pfisterer PH, Shen C, Nikolovska-Coleska Z, Schyschka L, Schuster D, Rudy A, Wolber G, Vollmar AM, Rollinger JM, Stuppner H. "In silico discovery of acylated flavonol monorhamnosides from Eriobotrya japonica as natural, small-molecular weight inhibitors of XIAP BIR3". Bioorg Med Chem. 2011 19(2):1002-9.
  2. Shen C., Li Z, Yang X, Wang K., "La(3+) binds to BiP/GRP78 and induces unfolded protein response in HepG2 cells", Chem. Biol. Interact., 2008, 176, 196. [Full Text]

Andrew C. Stelzer (Al-Hashimi Lab)

  1. Frank, A.T.*, Stelzer, A.C.*, Al-Hashimi, H.M., and Andricioaei, I., "Constructing RNA dynamical ensembles by combining MD and motionally decoupled NMR RDCs: new insights into RNA dynamics and adaptive ligand recognition", Nucleic Acids Res., 2009, 37, 3670. (*authors contributed equally) [Full Text]
  2. Fisher, C.K., Zhang, Q., Stelzer, A., and Al-Hashimi, H.M., "Ultrahigh Resolution Characterization of Domain Motions and Correlations by Multialignment and Multireference Residual Dipolar Coupling NMR", J. Phys. Chem. B., 2008, 112, 16815. [Full Text]
  3. Zhang, Q., Stelzer, A.C., Fisher, C.K. and Al-Hashimi, H.M., "Visualizing spatially correlated dynamics that directs RNA conformational transitions", Nature, 2007, 450, 1263. [Full Text]

Bethany S. Strunk (Karbstein Lab)

  1. Strunk, B., Struffi, P., Wright, K., Pabst, B., Thomas, J., Qin, L. and Arnosti, D.N., "Role of CtBP in Transcriptional Repression by the Drosophila giant Protein", Dev. Biology, 2001, 239, 229. [Full Text]
  2. Hewitt, G.F., Strunk, B.S., Marguilies, C., Priputin, T., Wang, X.D., Amey, R., Pabst, B.A., Kosman, D., Reinitz, J. and Arnosti, D.N., "Transcriptional repression by the Drosophila giant protein: cis element positioning provides an alternative means of interpreting an effector gradient", Development, 1999, 126, 1201. [Full Text]

Frederick Stull (Palfey Lab)

  1. Martin, D.F., Aguinaldo, J.S., Kondis, N.P., Stull F.W., O'Donnell, L.F., Martin, B.B., and Alldredge, R.L., "Comparison of effectiveness of removal of nuisance anions by metalloligs, metal derivatives of Octolig", J. Environ. Sci. Health A. Tox. Hazard. Subst. Environ. Eng., 2008, 43, 1296. [Full Text]

Jia Sun (Lei Lab)

  1. Sun, J. *, Yu, E.Y*, et al. Analyses of Candida Cdc13 orthologues revealed a novel OB fold dimer arrangement, dimerization-assisted DNA-binding, and substantial structural differences between Cdc13 and RPA70, Molecular and Cellular Biology, 2011. [Full Text]
  2. Sun, J., Yang, Y., et al. Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase α, Cell Research, 2010. 21(2): p. 258-74. [Full Text]
  3. Sun, J., Yu, E.Y., Yang, Y., et al. "Stn1-Ten1 is an Rpa2-Rpa3-like complex at telomeres", Genesdev., 2009, 23, 2900. [Full Text]

Wendy Tay (Walter Lab)

  1. Carr, G., Tay, W., Bottriell, H., Andersen, S.K., Mauk, A.G. and Andersen, R.J., "Plectosphaeroic Acids A, B, and C, Indoleamine 2,3-Dioxygenase Inhibitors Produced in Culture by a Marine Isolate of the Fungus Plectosphaerella cucumerina" Org Lett, 2009, 11, 2996. Full Text

David M. Thal (Tesmer Lab)

  1. Shankaranarayanan A., Thal D.M., Tesmer V.M., Roman D.L., Neubig R.R., Kozasa T and Tesmer J.J., "Assembly of high order G alpha q-effector complexes with RGS
    proteins", J. Biol. Chem., 2008. [Full Text]
  2. Gu, S., He, J., Ho, W.T., Ramineni, S., Thal, D.M., Natesh, R., Tesmer, J.J.G., Hepler, J.R. and Heximer, S.P., "Unique hydrophobic extension of the RGS2 amphipathic helix domain imparts increased plasma membrane binding and function relative to other RGS R4/B subfamily members", J. Biol. Chem., 2007. [Full Text]
  3. Hanes, J.W., Thal, D.M. and Johnson, K.A., "Incorporation and Replication of 8-Oxo-deoxyguanosine by the Human
    Mitochondrial DNA Polymerase", J. Biol. Chem., 2006, 281, 36241. [Full Text]

Andrea Thompson (Gestwicki Lab)

  1. Thompson AD, Bernard S, Skiniotis G, Gestwicki JE. Function and Oligomeric States of Escherichia coli Heat Shock Protein 70 (Hsp70/DnaK). Cellular Stress & Chaperones 2011 [Epub ahead of print] PMID 22076723. [Full Text]
  2. Wisén S*, Bertelsen EB*, Thompson AD, Patury S, Ung P, Chang L, Evans CG, Walter GM, Wipf P, Carlson HA, Brodsky JL, Zuiderweg ER, Gestwicki JE. Binding of a Small Molecule at a Protein-Protein Interface Regulates the Chaperone Activity of Hsp70-Hsp40. ACS Chem Biol 2010 Jun 18;5(6):611-22.
    PMID 20481474. [Full Text]
  3. Chang, L., Thompson, A.D., Ung, P., Carlson, H.A., Gestwicki, J.E., "Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (HSP70/DNAK)", J. Biol. Chem., 2010. [Full Text]
  4. Kawamoto SA, Thompson AD, Coleska A, Nikolovska-Coleska Z, Yi H, Wang S. Analysis of the BCL9 interaction with beta-catenin and development of fluorescence polarization and surface plasmon resonance binding assays for this interaction. (2009) Biochemistry. 48(40):9534-41. PMID 19715304. [Full Text]
  5. Dooley, A.J., Taggart, B., Shindo, N., Park, J.G. and Pang, Y.-P., "Genome to Drug Lead: Identification of a Small-Molecule Inhibitor for SARS", Bioorg. Med. Chem. Lett., 2006, 16, 830. [Full Text]
  6. Lipinski, C.A., Tran, N.L., Dooley, A., Pang, Y.-P., Rohl, C., Kloss, J., McDonough, W., Craig, D., Berens, M.E. and Loftus, J.C., "Critical Role of the FERM Domain in Pyk2 Stimulated Glioma Cell Migration", Biochem. Biophys. Res. Commun., 2006, 349, 939. [Full Text]

Gabrielle Todd (Walter Lab)

  1. Mo, J., Todd, G.C., and Hakansson, K., "Characterization of nucleic acid higher order structure by gas-phase H/D exchange in a quadrupole-FT-ICR mass spectrometer", Biopolymers, 2009, 91, 256. [Full Text]
  2. Todd G, Karbstein K., "RNA takes center stage." Biopolymers. 2007, 87, 275. [Full Text]

Hong Tran (Sherman Lab)

  1. Li, S., Anand, K., Tran, H., Yu, F., Finefield, J. M., Sunderhaus, J. D., Timothy, J., Tsukamoto, S., Williams, R. M., Sherman, D. H., Arbor, A., and Collins, F. (2012) Comparative analysis of the biosynthetic systems for fungal bicyclo[2.2.2]diazaoctane indole alkaloids: the (+)/(-)-notoamide, paraherquamide and malbrancheamide pathways, MedChemComm 1-23.

 

U-Z

Daniel R. Wahl (Glick Lab)

  1. Luikart, S., Masri, M., Wahl, D., Hinkel, T, Beck, J.M., Gyetko M.R., Gupta, P., Oegema, T. "Urokinase is required for the formation of mactinin, an alpha-actinin fragment that promotes monocyte/macrophage maturation", Biochem, Biophys. Acta., 2002,1591, 99. [Full Text]

Ningkun Wang (Mapp Lab)

  1. Pomerantz, W. C.; Wang, N.; Lipinski, A. K.; Wang, R.; Cierpicki, T.; Mapp, A. K. “Profiling Transcription Complexes by Protein-Observed 19F NMR”. ACS Chemical Biology 2012, 7, 1345–50.
  2. Wands, A. M.; Wang, N.; Lum, J. K.; Hsieh, J.; Fierke, C. A.; Mapp, A. K. “Transient-State Kinetic Analysis of Transcriptional Activator-DNA Complexes Interacting with a Key Coactivator”.  J. Biol. Chem. 2011, 286, 16238-16245.

Jonas Westergaard Hojfeldt (Mapp Lab)

  1. Hansen, M.H., Blakskjaer, P., Petersen, L.K., Hansen, T.H., Hojfeldt, J.W., Gothelf, K.V., and Hansen, N.J., "A yoctoliter-scale DNA reactor for small-molecule evolution", J. Am. Chem. Soc., 2009, 131, 1322. [Full Text]
  2. Casey, R.J., Desaulniers, J.P., Hojfeldtb, J.W. and Mapp, A.K., "Expanding the repertoire of small molecule transcriptional activation domains", Bioorg. Med. Chem., 2008. [Full Text]
  3. Hojfeldt, J.W., Blakskjaer, P. and Gothelf, K.V., "A cleavable amino-thiol linker for reversible linking of amines to DNA", J. Org. Chem., 2006, 71, 9556. [Full Text]

Jonathan R. Whicher (J. Smith Lab)

  1. Structural rearrangements of a polyketide synthase module during its catalytic cycle. J. R. Whicher, S. Dutta, D. A. Hansen, W. A. Hale, J. A. Chemler, A. M. Dosey, A. R. Narayan, K. Håkansson, D. H. Sherman, J. L. Smith and G. Skiniotis. (2014) Nature 510, 560-564. PMICD in process. PMC4074775.
  2. Structure of a modular polyketide synthase.  S. Dutta, J. R. Whicher, D. A. Hansen, W. A. Hale, J. A. Chemler, G. R. Congdon, A. R. Narayan, K. Håkansson, D. H. Sherman, J. L. Smith and G. Skiniotis. (2014) Nature 510, 512-517. PMICD in process.
  3. Cyanobacterial polyketide synthase docking domains: A tool for engineering natural product biosynthesis. J. R. Whicher, S. S. Smaga, D. A. Hansen, W. C. Brown, W. H. Gerwick, D. H. Sherman and J. L. Smith. (2013) Chem. Biol. 20, 1340-1351. PMC3870462.
  4. Structural and stereochemical analysis of a modular polyketide synthase ketoreductase domain required for the generation of a cis-alkene.  S. A. Bonnett, J. R. Whicher, K. Papireddy, G. Florova, J. L. Smith and K. A. Reynolds. (2013) Chem Biol. 20, 772-783. PMC3875705.
  5. Structure and function of RedJ, a thioesterase from the prodiginine biosynthetic pathway in Streptomyces coelicolorJ. R. Whicher, G. Florova, P. K. Sydor, R. Singh, M. Alhamadsheh, G. L. Challis, K. A. Reynolds and J. L. Smith. (2011) J. Biol. Chem. 286, 22558-22569.  PMC3121400.
  6. Disruption of the proton relay network in the class 2 dihydroorotate dehydrogenase from Escherichia coli. R. L. Kow, J. R.  Whicher, C. A. McDonald, B. A. Palfey and R. L. Fagan R. (2009) Biochemistry 48, 9801-9809.

Joel A. Yates (Bochar Lab)

  1. Menon, T., Yates, J.A. and Bochar, D.A., , "Regulation of Androgen-Responsive Transcription by the Chromatin Remodeling Factor CHD8", Mol Endocrinol, 2010, In Press. [Full Text]
  2. Yates, J.A., Menon, T., Thompson, B.A. and Bochar, D.A., "Regulation of HOXA2 gene expression by the ATP-dependent chromatin remodeling enzyme CHD8", FEBS Lett., 2010, 584, 689. [Full Text]
  3. Li, Y., Yates, J.A., Chen, J.J.L., "Identification and characterization of sea squirt telomerase reverse transcriptase", Gene, 2007, 400, 16. [Full Text]

Yaru Zhang (O'Brien Lab)

  1. Zhang, Y., O'Brien, P.J. (2015) Repair of alkylation damage in eukaryotic chromatin depends on searching ability of alkyladenine DNA glycosylase ACS Chem. Biol. epub Sept 4, 2015 http://www.ncbi.nlm.nih.gov/pubmed/26317160
  2. Hedglin, M., Zhang, Y., O’Brien, P.J. (2015) Probing the DNA structural requirements for facilitated diffusion. Biochemistry 54:557-66. http://www.ncbi.nlm.nih.gov/pubmed/25495964
  3. Hedglin, M., Zhang, Y., O’Brien, P.J. (2013) Intersegmental transfer by a monomeric DNA repair glycosylase. J. Biol. Chem. 288:24550-9. http://www.ncbi.nlm.nih.gov/pubmed/23839988
  4. Bao, R., Zhang, Y., Lou, X. C., Zhou, C. Z. and Chen, Y., "Structural and kinetic analysis of Saccharomyces cerevisiae thioredoxin Trx1: Implications for the catalytic mechanism of GSSG reduced by thioredoxin", Biochim Biophys Acta, 2009, 1794, 1218.[Full Text]
  5. Bao, R., Zhang, Y., Zhou, C. Z. and Chen, Y., "Structural and mechanistic analyses of yeast mitochondrial thioredoxin Trx3 reveal putative function of its additional cysteine residues", Biochim Biophys Acta, 2009, 1794, 716. [Full Text]
  6. Zhang, Z., Bao, R., Zhang, Y., Yu, J., Zhou, C. Z. and Chen, Y., "Crystal structure of Saccharomyces cerevisiae cytoplasmic thioredoxin reductase Trr1 reveals the structural basis for species-specific recognition of thioredoxin", Biochim Biophys Acta, 2009, 1794, 124. [Full Text]
  7. Lou, X., Zhang, Y., Bao, R., Zhou, C.Z., and Chen, Y., "Purification, Crystallization and Preliminary X-ray diffraction analysis of glutathionylated Trx1 C33S mutant from yeast", Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009, 65, 39-41.[Full Text]
  8. Zhang, Y., Bao, R., Zhou, C. Z. and Chen, Y., "Expression, purification, crystallization and preliminary X-ray diffraction analysis of thioredoxin Trx1 from Saccharomyces cerevisiae", Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008, 64, 323. [Full Text]
  9. Bao, R., Chen, Y.X., Zhang, Y., and Zhou, C.Z., "Expression, purification, Crystallization and preliminary X-Ray diffraction analysis of mitochondrial thioredoxin Trx3 from Sacchromyces cerevisiae", Acta. Crystallogr. Sect. F. Struct. Biol. Cryst. Commun., 2006, 62, 1161-1163. [Full Text]