Student Publications

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Last Names A-E
Last Names F-K
Last Names L-P
Last Names Q-T
Last Names U-Z

Previous Student Publications

A-E

Victoria A. Assimon (Gestwicki Lab)

  1. 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.
  2. 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.

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]

Laura Cesa (Mapp Lab)

  1. Cesa LC*, Patury S*, Komiyama T, Ahmad A, Zuiderweg, ER, Gestwicki JE (2013). Inhibitors of protein-protein interactions identified by high-throughput screening of multi-protein complexes. ACS Chem Biol. 8(9): 1988-1997. [PDF]
  2. Majmudar, C. Y.; Højfeldt, J. W.; Arevang, C. J.; Pomerantz, W. C.; Gagnon, J. K.; Schultz, P. J.; Cesa, L. C.; Doss, C. H.; Rowe, S. P.; Vásquez, V.; Tamayo-Castillo, G.; Cierpicki, T.; Brooks, C. L. 3rd; Sherman, D. H.; Mapp, A. K. (2012). Sekikaic acid and lobaric acid target a dynamic interface of the coactivator CBP/p300. Angew. Chem. Int. Ed. Engl. 51(45): 11258-11262. [PDF]
  3. Cesa LC, Higgins CA, Sando SR, Kuo DW, Levandoski MM (2012). Specificity Determinants of Allosteric Modulation in the Neuronal Nicotinic Acetylcholine Receptor: A Fine Line between Inhibition and Potentiation. Molecular Pharmacology 81(2): 239-249. [PDF]

*authors contributed equally

Osvaldo Cruz (Sunahara Lab)

  1. Bifunctional Ligands Allow Deliberate Extrinsic Reprogramming of the Glucocorticoid Receptor. Højfeldt JW, Cruz-Rodríguez O, Imaeda Y, Van Dyke AR, Carolan JP, Mapp AK, Iñiguez-Lluhí JA. Mol Endocrinol. 2014 Jan 1:me20131343. [Epub ahead of print]
  2. The in vivo role of androgen receptor SUMOylation as revealed by androgen insensitivity syndrome and prostate cancer mutations targeting the proline/glycine residues of synergy control motifs.
    Mukherjee S, Cruz-Rodríguez O, Bolton E, Iñiguez-Lluhí JA.
    J Biol Chem. 2012 Sep 7;287(37):31195-206. doi: 10.1074/jbc.M112.395210. Epub 2012 Jul 24.
  3. Small ubiquitin-like modifier (SUMO) modification mediates function of the inhibitory domains of developmental regulators FOXC1 and FOXC2. Danciu TE, Chupreta S, Cruz O, Fox JE, Whitman M, Iñiguez-Lluhí JA. J Biol Chem. 2012 May 25;287(22):18318-29. doi: 10.1074/jbc.M112.339424. Epub 2012 Apr 5.

Matthew DeMars (Sherman Lab)

  1. Zhang, K.; Shafer, B. M.; Demars II, M. D.; Stern, H. A.; Fasan, R. Controlled oxidation of remote sp3 C-H bonds in artemisinin via P450 catalysts with fine-tuned regio- and stereoselectivity. J. Am. Chem. Soc. 2012, 134, 18695.

 

F-K

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]

Carrie Johnson (Iniguez Lab)

  1. Johnson, A.R., Johnson, C.M., Stoll, D.R., Vitha, M.F.  Identifying orthogonal and similar reversed phase liquid chromatography stationary phases using the system selectivity cube and the hydrophobic subtraction model.  J Chromatogr. A 2012, 1249, 62-82. [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.

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]

 

L-P

Daniel Lorenz (Garner Lab)

  1. Lockshon D, Olsen CP, Brett CL, Chertov A, Merz AJ, Lorenz DA, Van Gilst MR, Kennedy BK. (2012) Rho Signaling Participates in Membrane Fluidity Homeostasis. PLoS ONE 7(10): e45049. doi:10.1371/journal.pone.0045049

Paul Lund (Walter Lab)

  1. 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]
  2. 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]

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]

Carol Ann Pitcairn (Fierke Lab)

  1. 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.
  2. Wolfson, N. A.; Pitcairn, C. A.; Fierke, C. A., HDAC8 substrates: Histones and beyond. Biopolymers. 2013, 99 (2), 112-126.

Rachel Pricer (Mapp Lab)

  1. Pricer, R.E., Houghton, J.L., Green, K.D., Mayhoub, A.S., &
    Garneau-Tsodikova, S.  (2012). Biochemical and structural analysis of aminoglycoside acetyltransferase Eis from Anabaena variabilis. Mol. BioSyst., 8, 3305-3313.
  2. Houghton, J.L., Green, K.D., Pricer, R.E., Mayhoub, A.S., &
    Garneau-Tsodikova, S.  (2013). Unexpected N-acetylation of capreomycin by mycobacterial Eis enzymes. J. Antimicrob. Chemother., 68, 800-805.
  3. Lancia, J.K., Nwokoye, A., Dugan, A., Joiner, C., Pricer, R.,
    & Mapp, A.K. (2013). Sequence context and crosslinking mechanism affect the efficiency of in vivo capture of a protein-protein interaction. Biopolymers, Accepted.
  4. Rashidian, M., Song, J. M., Pricer, R. E., Distefano, M. D., "Chemoenzymatic Reversible Immobilization and Labeling of Proteins without Prior Purification." Journal of the American Chemical Society, 2012.

 

Q-T

James Song (Garner Lab)

  1. Rashidian, M., Song, J. M., Pricer, R. E., Distefano, M. D., "Chemoenzymatic Reversible Immobilization and Labeling of Proteins without Prior Purification." Journal of the American Chemical Society, 2012. [PDF]

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]

Eric Sullivan (Fierke Lab)

  1. Kincaid, V. A., E. D. Sullivan, et al. (2011). "Structure and Catalytic Mechanism of Nicotinate (Vitamin B3) Degradative Enzyme Maleamate Amidohydrolase from Bordetella bronchiseptica RB50." Biochemistry 51(1): 545-554.

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

Adam Yokom (Southworth 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.

Yaru Zhang (O'Brien Lab)

  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]