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  1. Deka R.K., Brautigam C.A., Liu W.Z., Tomchick D.R., Norgard M.V. (2016) Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm. MicrobiologyOpen 5:21-38. PMID: 26626129
  2. Dodd D.W., Tomchick D.R., Corey D.R., Gagnon K.T. (2016) Pathogenic C9ORF72 antisense repeat RNA forms a double helix with tandem C:C mismatches. Biochemistry 55:1283-6. PMID: 26878348
  3. Ouyang Z., Zheng G., Tomchick D.R., Luo X., Yu H. (2016) Structural basis and IP6 requirement for Pds5-dependent cohesion dynamics. Mol Cell 62:248-59. PMID: 26971492
  4. Kokkonda S., Deng X., White K.L., Coterón J.M., Marco M., de Las Heras L., White J., El Mazouni F., Tomchick D.R., Manjalanagara K., Rudra K.R., Chen G., Morizzi J., Ryan E., Kaminsky W., Leroy D., Martínez-Martínez M.S., Jimenez Diaz M.B., Bazaga S.F., Angulo-Barturen I., Waterson D., Burrows J.N., Matthews D., Charman S.A., Phillips M.A., Rathod P.K. (2016) Tetrahydro-2-napthyl and 2-indanyl triazolopyrimidines targeting Plasmodium falciparum dihydroorotate dehydrogenase display potent and selective antimalarial activity. J Med Chem 59:5416-31. PMID: 27127993
  5. Nguyen K.B., Sreelatha A., Durrant E., Lopez-Garrido J., Muszewska A., Dudkiewicz M., Grynberg M., Yee S.S., Pogliano K., Tomchick D.R., Pawlowski K., Dixon J.E., Tagliabracci V.S. (2016) Phosphorylation of spore coat proteins by a new family of kinases. Proc Natl Acad Sci USA 113:E3482-E3491. PMID: 27185916



  1. Guo Y., Scheuermann T.H., Partch C.L., Tomchick D.R., Gardner, K.H. (2015) Coiled-coil coactivators play a structural role mediating interactions in hypoxia inducible factor heterodimerization. J Biol Chem 290:7707-7721. PMID: 25627682
  2. Deka R.K., Brautigam C.A., Liu W.Z., Tomchick D.R., Norgard M.V. (2015) Evidence for posttranslational protein flavinylation in the syphilis spirochete Treponema pallidum: structural and biochemical insights from the catalytic core of periplasmic flavin-trafficking protein. mBio 6:e00519-15. PMID: 25944861
  3. Brewer K.D., Bacaj T., Cavalli A., Camilloni C., Swarbrick J.D., Liu J., Zhou A., Zhou P., Barlow N., Xu J., Seven A.B., Prinslow E.A., Voleti R., Häussinger D., Bonvin A.M.J.J., Tomchick D.R., Vendruscolo M., Graham B., Südhof T.C., Rizo J. (2015) Dynamic synaptotagmin-1-SNARE complex binding mode in solution. Nat Struct Mol Biol 22:555-64. PMID: 26030874
  4. Phillips M.A., Lotharius J., Marsh K., White J., Dayan A., White K.L., Njoroge J.W., El Mazouni F., Lao Y., Kokkonda S., Tomchick D.R., Deng X., Laird T., Bhatia S.N., March S., Ng C.L., Fidock D.A., Wittlin S., Lafuente-Monasterio M., Benito F.J., Alonso L.M., Martinez M.S., Jimenez-Diaz M.B., Bazaga S.F., Angulo-Barturen I., Haselden J.N., Louttit J., Cui Y., Sridhar A., Zeeman A.M., Kocken C., Sauerwein R., Dechering K., Avery V.M., Duffy S., Delves M., Sinden R., Ruecker A., Wickham K.S., Rochford R., Gahagen J., Iyer L., Riccio E., Mirsalis J., Bathhurst I., Rueckle T., Ding X., Campo B., Leroy D., Rogers M.J., Rathod P.K., Burrows J.N., Charman S.A. (2015) A long-duration dihydroorotate dehydrogenase inhibitor (DSM265) for prevention and treatment of malaria. Sci Transl Med 7:296ra111. PMID: 26180101
  5. Pascoe, H.G., Gutowski, S., Chen, H., Brautigam, C.A., Chen, Z., Sternweis, P.C. and Zhang, X. (2015) “Secondary PDZ domain-binding site on class B plexins enhances the affinity for PDZ-RhoGEF” Proc. Natl. Acad. Sci..112 (48): 14852-57.



  1. Fortune D.E., Lin Y.-P., Deka R.K., Groshong A.M., Hagman K.E., Leong J.M., Tomchick D.R., Blevins J.S. (2014) Identification of lysine residues in the Borrelia burgdorferi DbpA adhesin required for murine infection. Infect Immun 82:3186-3198. PMID: 24842928
  2. Hara K., Zheng G., Qu Q., Liu H., Ouyang Z., Chen Z., Tomchick D.R., Yu H. (2014) Structure of cohesion subcomplex pinpoints direct shugoshin-Wapl antagonism in centromeric cohesion. Nat Struct Mol Biol 21:864-870. PMID: 25173175
  3. Lin Z., Jia L., Tomchick D.R., Luo X., Yu H. (2014) Substrate-specific activation of the mitotic kinase Bub1 through intramolecular autophosphorylation and kinetochore targeting. Structure 22:1616-1627. PMID: 25308863
  4. Rivera-Cancel G., Ko W.-H., Tomchick D.R., Correa F., Gardner K.H. (2014) Full-length structure of a monomeric histidine kinase reveals basis for sensory regulation. Proc Natl Acad Sci USA 111:17839-44. PMID: 25468971
  5. Hunter, J., Gurbani, D., Ficarro, S.B., Carrasco, M., Lim, S.M., Choi, H.G., Xie, T., Marto, J.A., Chen, Z., Gray, N.S. and Westover, K.D. (2014) “In situ Selectivity Profiling and Crystal Structure of SML-8-73-1, an Active Site Inhibitor of Oncogenic K-Ras G12C” Proc. Natl. Acad. Sci. 111(24): 8895-8900.
  6. Zhang, X., Wu, J., Du, F., Xu, H., Sun, L., Chen, Z., Brautigam, C. A., Zhang, X. and Chen, Z. J. (2014) “The Cytosolic DNA Sensor cGAS Forms An Oligomeric Complex with DNA and Undergoes Switch-like Conformational Changes in the Activation Loop” Cell Report 6(3): 421-30.



  1. Deka R.K., Brautigam C.A., Liu W.Z., Tomchick D.R., Norgard M.V. (2013). The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis. J Biol Chem 16:11106-11121. PMID: 23447540
  2. Ouyang Z., Zheng G., Song J., Borek D.M., Otwinowski Z., Brautigam C.A., Tomchick D.R., Rankin S., Yu H. (2013) Structure of the human cohesion inhibitor Wapl. Proc Natl Acad Sci USA110: 11355-60. PMID: 23776203
  3. Ni L., Li S., Yu J., Min J., Brautigam C.A., Tomchick D.R., Pan D., Luo X. (2013) Structural basis for autoactivation of human Mst2 kinase and its regulation by RASSF5. Structure 21: 1757-68. PMID: 23972470. PMID: 23972470
  4. Zahm J.A., Padrick S.B., Chen Z., Pak C.W., Yunus A.A., Henry L., Tomchick D.R., Chen Z., Rosen M.K. (2013) The bacterial effector VopL organizes actin into filament-like structures. Cell 155: 423-434. PMID: 24120140
  5. Medina, F., Carter, A., Dada, O., Gutowski, S., Hadas, J., Chen, Z. and Sternweis, P. C. (2013) "Activated RhoA Is a Positive Feedback Regulator of the Lbc Family of Rho Guanine Nucleotide Exchange Factor Proteins” J. Biol Chem 288: 11325-33.



  1. Thompson J.W., Salahudeen A.A., Chollangi S., Ruiz J.C., Brautigam C.A., Makris T.M., Lipscomb J.D., Tomchick D.R., Bruick R.K. (2012) Structural and molecular characterization of the iron-sensing hemerythrin-like domain within F-box and Leucine-rich Repeat Protein 5 (FBXL5). J Biol Chem 287:7357-7365. PMID: 22253436
  2. Deka R.K., Brautigam C.A., Goldberg M., Schuck P., Tomchick D.R., Norgard M.V. (2012) Structural, bioinformatic, and in vivo analyses of two Treponema pallidum lipoproteins reveal a unique TRAP transporter. J Mol Biol 416:678-696. PMID: 22306465
  3. Matos M.M., Xu Y., Dulubova I., Otwinowski Z., Richardson J.M., Tomchick D.R., Rizo J., Ho A. (2012) Autoinhibition of Mint1 adaptor protein regulates APP binding and processing. Proc Natl Acad Sci USA 109:3802-3807. PMID: 22355143
  4. Kim S., Sun H., Tomchick D.R., Yu H., Luo X. (2012) Structure of human Mad1 C-terminal domain reveals its involvement in kinetochore targeting. Proc Natl Acad Sci USA 109:6549-6554. PMID: 22493223
  5. Brautigam C.A., Deka R.K., Schuck P. Tomchick D.R., Norgard M.V. (2012) Structural and thermodynamic characterization of the interaction between two periplasmic Treponema pallidum lipoproteins that are components of a TPR-protein-associated TRAP transporter (TPAT). J Mol Biol 420:70-86. PMID: 22504226
  6. Brautigam C.A., Deka R.K., Ouyang Z., Machius M., Knutsen G., Tomchick D.R., Norgard M.V. (2012). Biophysical and bioinformatics analyses implicate the Treponema pallidum Tp34 lipoprotein in transition metal homeostasis. J Bacteriol 194:6771-6781. PMID 23042995
  7. Tian W., Li B., Warrington R., Tomchick D.R., Yu H., Luo X. (2012) Structural analysis of human Cdc20 supports multi-site degron recognition by APC/C. Proc Natl Acad Sci USA 109:18419-24. PMID 23091007
  8. Chen, Z., Guo, L., Hadas, J., Sprang, S. R. and Sternweis, P. C. (2012) "Activation of the Guanine Nucleotide Exchange Activity of p115-RhoGEF Requires Direct Association of Ga13 and the Dbl-homology Domain" J. Biol Chem 287: 16369-77.



Li W., Ma C., Guan R., Xu Y., Tomchick D.R., Rizo J. (2011). The crystal structure of a Munc13 C-terminal module exhibits a remarkable similarity to vesicle tethering factors. Structure, 19, 1443-1455. [PubMed]

Haines, D.C., Hegde, A., Chen, B., Zhao, W., Bondlela, M., Humphreys, J.M., Mullin, D.A., Tomchick, D.R., Machius, M., Peterson, J.A. (2011). A single active-site mutation of P450BM-3 dramatically enhances substrated binding and rate of product formations. Biochemistry, 50, 8333-8341.[PubMed]

Yu, B., Cheng ,H.C., Brautigam, C.A., Tomchick ,D.R., Rosen, M.K. (2011). Mechanism of actin filament nucleation by the bacteral effector VopL. Nat. Struct. Molec. Biol., 18, 1068-1074. [PubMed]

Padrick, S.B., Doolittle, L.K., Brautigam, C.A., King, D.S., Rosen, M.K. (2011). Arp2/3 complex is bound and activated by two WASP proteins. Proc. Natl. Acad. Sci., 108, E472-E479. [PubMed]

Brautigam, C.A., Wynn, R.M., Chuang, J.L., Naik, M.T., Young, B.B., Huang, T. & Chuang, D.T. (2011). Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex. J. Biol. Chem., 286, 23478-23488. [PubMed]

Kang, J., Chaudhury, J. Dong, H., Brautigam, C.A., & Yu, H. (2011). INCENP-mediated mitotic centromere targeting and Sgo1 binding of HP1 are dispensible for sister-chromatid cohesion in human cells. Mol. Biol. Cell, 22, 1181-1190. [PubMed]

Padrick, S.B. & Brautigam, C.A. (2011). Evaluating the stoichiometry of macromolecular complexes using multisignal sedimentation velocity. Methods, in press. [PubMed]

Brautigam, C.A. (2011). Using Lamm-Equation modeling of sedimentation velocity data to determine the kinetic and thermodynamic properties of macromolecular interactions. Methods, in press. [PubMed]

Hoopman, T.C., Liu, W., Joslin, S.N., Pybus, C., Brautigam, C.A., & Hansen, E.J. (2011). Identification of gene products involved in the oxidative stress response of Moraxella catarrhalis. Infect. Immun., 79, 745-755. [PubMed]

Selyunin, A.S., Sutton, S.E., Weigele, B.A., Reddick, L.E., Orchard, R.C., Bresson, S.M. Tomchick, D.R., & Alto, N.M. (2011). The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold. Nature, 469, 107-111. [PubMed]

Chen, Z., Guo, L., Sprang, S. R. and Sternweis, P. C. (2011) "Modulation of a GEF Switch: Autoinhibition of the Intrinsic Guanine Nucleotide Exchange Activity of p115-RhoGEF." Protein Science 20: 107-117.


Dorwart, M.R., Wray, R., Brautigam, C.A., Jiang, Y. & Blount, P. (2010). S. aureus MscL is a pentamer in vivo but of variable stoichiometries in vitro: implications for detergent-solubilized membrane proteins. PLoS Biology, 8, e1000555. [Link]

Otomo, T., Tomchick, D.R., Otomo, C, Machius, M., & Rosen, M.K. (2010). Crystal structure of the Formin mDia1 in autoinhibited conformation. PLoS One, 5, e12896. [Link]

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Labandeira-Rey, M., Brautigam, C.A., & Hansen, E.J. (2010) Initial characterization of the CpxRA proteins and the associated regulon in Haemophilus ducreyi. Infect. Immun., 78, 4779-4791. [PubMed]

Padrick, S.B., Deka, R.K., Chuang, J.L., Wynn, R.M., Chuang, D.T., Norgard, M.V., Rosen, M.K., & Brautigam, C.A. (2010). Determination of protein complex stoichiometry through multisignal sedimentation velocity experiments. Anal. Biochem., 407, 89-103. [PubMed]

Deng, X., Lee, J., Michael, A.J., Tomchick, D.R., Goldsmith, E.J., & Phillips, M.A. (2010). Evolution of substrate specificity within a diverse family of b/a-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine. J. Biol. Chem., 285, 25708-25719. [PubMed]

Luong, P., Kinch, L.N, Brautigam, C.A., Grishin, N.V., Tomchick, D.R., & Orth, K. (2010). Kinetic and structural insights into the mechanism of AMPylation by VopS FIC domain. J. Biol. Chem., 285, 20155-20163. [PubMed]

Tian, W., Yu, J., Tomchick, D.R., Pan, D., & Luo, X. (2010). Structural and functional analysis of the YAP-binding domain of human TEAD2. Proc. Natl. Acad. Sci (USA), 107, 7293-7298. [PDF]

Shin O.H., Lu, J. Rhee, J.S., Tomchick, D.R. Pang, Z.P., Wojcik, S.M., Camacho-Preez, M., Brose, N., Machius, M., Rizo, J., Rosenmund, C., & Sudhof, T.C. (2010). Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic exocytosis. Nat. Struct. Mol. Biol., 17, 280-288. [PDF]

Yu, B., Martins, I.R., Li, P., Amarasinghe G.K., Umetani, J., Fernandez-Zapico, M.E., Billadeau, D.D., Machius, M., Tomchick, D.R., & Rosen, M.K. (2010). Structural and energetic mechanisms of cooperative autoinhibition and activation of Vav1. Cell, 140, 246-256. [PDF]


Attia, A.S., Sedillo, J.L., Hoopman, T.C., Liu, W., Liu, L., Brautigam, C.A., & Hansen, E.J. (2009). Identification of a bacteriocin and its cognate immunity factor expressed by Moraxella catarrhalis. BMC Microbiol., 9, 207. [PDF]

Huerta, C., Borek, D., Machius, M., Grishin, N.V., & Zhang, H. (2009). Structure and mechanism of a eukaryotic FMN adenylyltransferase. J. Mol. Biol., 389, 388-400. [PDF]

Brautigam, C.A., Wynn, R.M., Chuang, J.L., & Chuang, D.T. (2009). Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex. J. Biol. Chem., 284, 13086-13098. [PDF]

Davis, L., Abdi, K., Machius, M., Brautigam, C., Tomchick, D.R., Bennett, V., Michaely, P. (2009). Localization and structure of the ankyrin-binding site on beta2-spectrin. J. Biol. Chem., 284, 6982-6987. [PDF]

Scheuermann, T.H., Tomchick, D.R., Machius, M., Guo, Y., Bruick, R.K., Gardner, K.H. (2009). Artificial ligand binding within the HIF2alpha PAS-B domain of the HIF2 transcription factor. Proc. Natl. Acad. Sci. USA, 106, 450-455. [PDF]


Kato, M., Wynn, R.M., Chuang, J.L., Tso, S.C., Machius, M., Li, J., & Chuang, D.T. (2008). Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops. Structure, 16, 1849-1859. [PDF]

Padrick, S.B., Cheng, H.C., Ismail, A.M., Panchal, S.C., Doolittle L.K., Kim, S., Skehan, B.M., Umetani, J., Brautigam, C.A., Leong, J.M., Rosen, M.K. (2008). Hierarchical regulation of WASP/WAVE proteins. Mol. Cell, 32, 426-438. [PDF]

Kang, J., Yang, M., Li, B., Qi, W., Zhang, C., Shokat, K.M., Tomchick, D.R., Machius, M., & Yu, H. (2008). Structure and substrate recruitment of the human spindle checkpoint kinase Bub1. Mol. Cell, 32, 394-405. [PDF]

Rezacova, P., Kozisek, M., Moy, S.F., Sieglova, I., Joachimiak, A., Machius, M., & Otwinowski, Z. (2008). Crystal structures of the effoector -binding domain of repressor CggR from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates. Mol. Microbiol., 69, 895-910. [PDF]

Attia, A.S., Sedillo, J.L., Wang, W., Liu, W., Brautigam, C.A., Winkler, W., & Hansen, E.J. (2008). Moraxella catarrhalis expresses an unusual Hfq protein. Infect. Immun., 76, 2520-2530. [PDF]

Lee, J., Tomchick, D.R., Brautigam, C.A., Machius, M., Kort, R., Hellingwerf, H.J., & Gardner, K.H. (2008). Changes at the KinA PAS-A dimerization interface influence histidine kinase function. Biochemistry, 47, 4051-4064. [PDF]

Yang, M., Li, B. Liu, C.J., Tomchick, D.R., Machius, M., Rizo, J., Yu, H., Luo, X. (2008). Insights into mad2 regulation in the spindle checkpoint revealed by the crystal structure of the symmetric mad2 dimer. PLoS Biol., 6, e50. [PDF]

Haines, D.C., Chen, B., Tomchick, D.R., Bondlela, M., Hegde, A., Machius, M., & Peterson, J.A. (2008). Crystal structure of inhibitor-bound P450BM-3 reveals open conformation of substrate access channel. Biochemistry, 47, 3662-3670. [PDF]

Huang, N., Sorci, L., Zhang, X., Brautigam, C., Li, X., Raffaelli, N., Magni, G., Grishin, N.V., Osterman, A., & Zhang, H. (2008). Bifunctional NMN adenylyltransferase/ADP ribose pyrophosphatase: structure and function in bacterial NAD metabolism. Structure, 16, 196-209. [PDF]

Hoopman, T.C., Wang, W., Brautigam, C.A., Reilly, T.J., and Hansen, E.J. (2008). Moraxella catarrhalis synthesizes an autotransporter that is an acid phosphatase. J. Bacteriol., 190, 1459-1472. [PDF]


Hegde, A., Haines, D.C., Bondlela, M., Chen, B., Schaffer, N., Tomchick, D.R., Machius, M., Nguyen, H., Chowdhary, P.K., Stewart, L, Lopez, C., and Peterson, J.A. (2007). Interactions of substrates at the surface of P450s can greatly enhance substrate potency. Biochemistry, 46, 14010-14017. [PDF]

Yang, M., Li, B., Tomchick, D.R., Machius, M., Rizo, J., Yu, H., and Luo, X. (2007). p31(comet) blocks Mad2 activation through structural mimicry. Cell, 131, 744-755. [PDF]

Guan, R., Dai, H., Tomchick, D.R., Dulubova, I., Machius, M., Sudhof, T.C., and Rizo, J. (2007). Crystal structure of the RIM1alpha domain at 1.7 A. Biochemistry, 46, 8988-8998. [PDF]

Yang, M., Culhane, J.C., Szewczuk, L.M., Jalili, P., Ball, H.L., Machius, M., Cole, P.A., and Yu, H. (2007). Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine. Biochemistry, 46, 8058-8065. [PDF]

Machius, M., Brautigam, C.A., Tomchick, D.R., Ward, P., Otwinowski, Z., Blevins, J.S., Deka, R.K., & Norgard, M.V. (2007). Structural and biochemical basis for polyamine binding to the Tp0655 lipoprotein of Treponema pallidum: putative role for Tp0655 (TpPotD) as a polyamine receptor. J. Mol. Biol., 373, 681-694. [PDF]

Yang, M., Culhane, J.C., Szewczuk, L.M., Gocke, C.B., Brautigam, C.A., Tomchick, D.R., Machius, M., Cole, P.A., & Yu, H. (2007). Structural basis of histone demethylation by LSD1 revealed by suicide inactivation. Nat. Struct. Molec. Biol., 14, 535-539. [PDF]

Li, J., Machius, M., Chuang, J.L., Wynn, R.M., and Chuang, D.T. (2007). The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism. J. Biol. Chem., 282, 11904-11913. [PDF]

Chosed, R., Tomchick, D.R., Brautigam, C.A., Mukherjee, S., Negi, V.S., Machius, M., and Orth, K. (2007). Structural analysis of Xanthomonas XopD provides insights into substrate specificity of ULPs. J. Biol. Chem., 282, 6773-6782. [PDF]

Deka, R.K., Brautigam, C.A., Tomson, F.L., Machius, M., Tomchick, D.R., and Norgard, M.V. (2007). Crystal structure of the Tp34 (TP0971) lipoprotein of Treponema pallidum: biological implications of its metal-bound state and affinity for human lactoferrin. J. Biol. Chem., 282, 5944-5958. [PDF]


Yang, M., Gocke, C.B., Luo, X., Borek, D., Tomchick, D.R., Machius, M., Otwinowski, Z., and Yu, H. (2006). Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase. Mol. Cell, 23, 377-387. [PDF]

Gilles-Gonzalez, M.-A., Caceres, A.I., Sousa, E.H.S., Tomchick, D.R., Brautigam, C., Gonzalez, C., and Machius, M. (2006). A proximal arginine R206 participates in switching of the Bradyrhizobium japonicum FixL oxygen sensor. J. Mol. Biol., 360, 80-89. [PDF]

Lu, J., Machius, M., Dulubova, I., Dai, H., Sudhof, T.C., Tomchick, D.R., and Rizo, J. (2006). Structural basis for a Munc13-1 homodimer to Munc13-1/RIM heterodimer switch. PLoS Biol., 4, e192. [PDF]

Machius, M., Wynn, R.M., Chuang, J.L., Li, J., Kluger, R., Yu, D., Tomchick, D.R., Brautigam, C.A., and Chuang, D.T. (2006). A versitile conformational switch regulates reactivity in human branched-chain a-ketoacid dehydrogenase. Structure, 14, 287-298. [PDF]

Brautigam, C.A., Wynn, R.M., Chuang, J.L., Machius, M., Tomchick, D.R., and Chuang, D.T. (2006). Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex. Structure, 14, 611-621. [PDF]

Deka, R.K., Brautigam, C.A., Yang, X.F., Blevins, J.S., Machius, M., Tomchick, D.R., and Norgard, M.V. (2006). The PnrA (Tp0319; TmpC) lipoprotein represents a new family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC)-like operon in Treponema pallidum. J. Biol. Chem., 281, 8072-8081. [PDF]


Dai, H., Tomchick, D.R., Garcia, J., Sudhof, T.C., Machius, M., and Rizo, J. (2005). Crystal structure of the RIM2 C2A-domain at 1.4 A resolution. Biochemistry, 44, 13533-13542. [PDF]

Brautigam, C.A., Chuang, J.L., Tomchick, D.R., Machius, M., and Chuang, D.T. (2005). Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. J. Mol. Biol., 350, 543-552. [PDF]

Otomo, T., Otomo, C., Tomchick, D.R., Machius, M., and Rosen, M.K. (2005). Structural basis of Rho GTP-ase-mediated activation of the formin mDia1. Mol. Cell, 18, 273-281. [PDF]

Otomo, T., Tomchick, D.R., Otomo, C., Panchal, S.C., Machius, M., and Rosen, M.K. (2005). Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature, 433, 488-494. [PDF]

Thibodeau, P.H., Brautigam, C.A., Machius, M., and Thomas, P.J. (2005). Side chain and backbone contributions of Phe508 to CFTR folding. Nat. Struct. Molec. Biol., 12, 10-16. [PDF]



Deka, R.K., Neil, L., Hagman, K.E., Machius, M., Tomchick, D.R., Brautigam, C.A., and Norgard, M.V. (2004). Structural evidence that the 32-Kilodalton lipoprotein (Tp32) of Treponema pallidum is a L-Methionine-binding protein. J. Biol. Chem., 279, 55644-55650. [PDF]

Wynn, R.M., Kato, M., Machius, M., Chuang, J.L., Li, J., Tomchick, D.R., & Chuang, D.T. (2004). Moleuclar mechanism for regulation of the human mitochondrial branched-chain a-ketoacid dehydrogenase complex by phosphorylation. Structure, 12, 2185-2196. [PDF]

Li, J., Wynn, R.M., Machius, M., Chuang, J.L., Karthikeyan, S., Tomchick, D.R. and Chuang, D.T. (2004). Cross-talk between Thiamin Diphosphate Binding and Phosphorylation Loop Conformation in Human Branched-chain a-Keto Acid Decarboxylase/Dehydrogenase. J. Biol. Chem., 279, 32968-32978. [PDF]

Dai, H., Shin, O.-H., Machius, M., Tomchick, D.R., & Rizo, J. (2004). Structural Basis for the Evolutionary Inactivation of Ca2+ Binding to Synaptotagmin 4. Nat. Struct. Molec. Biol., 11, 844-849. [PDF]




Wynn, R.W., Machius, M., Chuang, J., Li, J., Tomchick, D.R., and Chuang, D.T. (2003). Roles of His291-a and His146-b' in the Reductive Acylation Reaction Catalyzed by Human Branched-chain a-Ketoacid Dehydrogenase. J. Biol. Chem., 278, 43402-43410. [PDF]

Hu, X., Machius, M., and Yang, W. (2003). Monovalent Cation Dependence and Preference of GHKL ATPases and Kinases. FEBS Lett., 544, 268-273. [PDF]




Michaely, P., Tomchick, D.R., Machius, M., and Anderson, R.G.W. (2002). Crystal Structure of a 12 ANK Repeat Stack from Human AnkyrinR. EMBO J., 21, 6387-6396. [PDF]

Deka, R.K., Machius, M., Norgard, M.V., and Tomchick, D.R. (2002). Crystal Structure of the 47-kDa Lipoprotein of Treponema pallidum Reveals a Novel Penicillin-binding Protein. J. Biol. Chem., 277, 41857-41862. [PDF]

Chen, X., Tomchick, D.R., Kovrigin, E., Arac, D., Machius, M., Sudhof, T.C., and Rizo, J. (2002). Three-dimensional Structure of the Complexin/SNARE Complex. Neuron, 33, 397-409. [PDF]

Zhou, T., Kurnasov, O., Tomchick, D.R., Binns, D.D., Grishin, N.V., Marquez, V.E., Osterman, A.L., and Zhang, H. (2002). Structure of Human Nicotinamide/Nicotinic Acid Mononucleotide Adenylyltransferase: Basis for the Dual Substrate Specificity and Activation of the Oncolytic Agent Tiazofurin. J. Biol. Chem., 277, 13148-13154. [PDF]




Haines, D.C., Tomchick, D.R., Machius, M., and Peterson, J.A. (2001). Pivotal Role of Water in the Mechanism of P450-BM3. Biochemistry, 40, 13456-13465. [PDF]

Machius, M., Chuang, J.L., Wynn, R.W., Tomchick, D.R., and Chuang, D.T. (2001). Structure of Rat BCKD Kinase: Nucleotide-induced Domain Communication in a Mitochondrial Protein Kinase. Proc. Natl. Acad. Sci. USA, 98, 11218-11213. [PDF]

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