Publications
2017
61 Sharma, P., Maklashina, E., Cecchini, G., Iverson, T.M. (2017) Crystal structure of an assembly intermediate of respiratory Complex II. Nat Commun. 2018 Jan 18;9(1):274.
60 Chen, Q., Perry, N.A., Vishnivetskiy, S.A., Berndt, S., Gilbert, N.C., Zhuo, Y., Singh, P.K., Tholen, J., Ohi, M.D., Gurevich, E.V., Brautigam, C.A., Klug, C.S., Gurevich, V.V., Iverson, T.M. (2017) Structural basis of arrestin-3 activation and signaling. Nat Commun. 2017 Nov 10;8(1):1427.
59 Starbird, C.A., Tomasiak, T.M., Singh, P.K., Yankovskaya, V., Maklashina, E., Eisenbach, M., Cecchini, G., Iverson, T.M. (2017) New crystal forms of the integral membrane Escherichia coli quinol:fumarate reductase suggest that ligands control domain movement. J Struct Biol. 2017 Nov 20.
58 Tso, S.C., Chen, Q., Vishnivetskiy, S.A., Gurevich, V.V., Iverson, T.M., Brautigam, C.A. (2017) Using two-site binding models to analyze microscale thermophoresis data. Anal Biochem. 2017 Oct 17.
57 Starbird, C.A., Maklashina, E., Sharma, P., Qualls-Histed, S., Cecchini, G., Iverson, T.M. (2017) Structural and biochemical analyses reveal insights into covalent flavinylation of the Escherichia coli Complex II homolog quinol:fumarate reductase. J Biol Chem. 2017 Aug 4;292(31):12921-12933.
56 Prokop, S., Perry, N.A., Vishnivetskiy, S.A., Toth, A.D., Inoue, A., Milligan, G., Iverson, T.M., Hunyady, L., Gurevich, V.V. (2017) Differential manipulation of arrestin-3 binding to basal and agonist-activated G protein-coupled receptors. Cell Signal. 2017 Aug;36:98-107.
2016
55 Loukachevitch, L.V., Bensing, B.A., Yu, H., Zeng, J., Chen, X., Sullam, P.M., Iverson, T. M. (2016) Structures of the Streptococcus sanguinis SrpA Binding Region with Human Sialoglycans Suggest Features of the Physiological Ligand. Biochemistry. 2016 Oct 11.
54 Bensing, B.A., Loukachevitch, L.V., McCulloch, K.M., Yu ,H., Vann, K.R., Wawrzak, Z., Anderson, S., Chen, X., Sullam, P.M., Iverson, T.M. (2016) Structural Basis for Sialoglycan Binding by the Streptococcus sanguinis SrpA Adhesin. J. Biol. Chem. 291(14):7230-40.
53 Maklashina, E., Rajagukguk, S., Starbird, C.A., McDonald, W.H., Koganitsky, A., Eisenbach, M., Iverson, T.M., Cecchini, G. (2016) Binding of the Covalent Flavin Assembly Factor to the Flavoprotein Subunit of Complex II. J. Biol. Chem. 291(6):2904-16
52 Zhan, X., Stoy, H., Kaoud, T. S., Perry, N. A., Chen, Q., Perez, A., Els-Heindl, S., Slagis, J.V., Iverson, T.M., Beck-Sickinger, A.G., Gurevich, E.V., Dalby, K.N., Gurevich, V. V. (2016). Peptide mini-scaffold facilitates JNK3 activation in cells. Scientific Reports, 6, 21025.
51 Bensing, B.A., Khedri, Z., Deng, L., Yu, H., Prakobphol, A., Fisher, S.J., Chen, X., Iverson, T.M., Varki, A., and Sullam, P.M. (2016) Novel aspects of sialoglycan recognition by the Siglec-like domains of streptococcal SRR glycoproteins. Glycobiology. 2016 Nov;26(11):1222-1234.
50 Kaya, A.I., Lokits, A.D., Gilbert, J.A., Iverson, T.M., Meiler, J., Hamm, H.E. (2016) A conserved hydrophobic core in Gαi1 regulates G protein activation and release from activated receptor. J. Biol. Chem. 2016 Sep 9;291(37):19674-86.
2015
49 McCulloch, K.M., McCranie, E.K., Smith, J.A., Sarwar, M., Mathieu, J.L., Gitschlag, B.L., Du, Y., Bachmann, B.O., and Iverson, T.M. (2015) Oxidative cyclizations in orthosomycin biosynthesis expand the known chemistry of an oxygenase superfamily. Proc Natl Acad Sci USA. 112(37):11547-52.
48 Starbird, C. A., Maklashina, E., Cecchini, G. and Iverson, T.M. (2015) Flavoenzymes: Covalent versus Noncovalent. eLS. 1–11.
47 Chen, Q., Vishnivetskiy, S.A., Zhuang, T., Cho, M.K., Thaker, T.M., Sanders, C.R., Gurevich, V.V., and Iverson, T.M. (2015) The rhodopsin-arrestin-1 interaction in bicelles. Methods Mol. Biol. 1271:77-95
46 Kaya, A.I., Iverson T.M., and Hamm, H.E. (2015) Functional stability of rhodopsin in a bicelle system: evaluating G protein activation by rhodopsin in bicelles. Methods Mol. Biol. 1271:67-76
2014
45 Birmingham, W.R., Nannemann, D.P., Starbird, C.A., Panosian, T.D., Iverson T.M., and Bachmann, B.O. (2014) Bioretrosynthetic construction of a didanosine biosynthetic pathway. Nat. Chem. Biol. 10(5):392-399
44 Kaya, A.I., Lokits, A.D., Gilbert, J.A., Iverson, T.M., Meiler, J., and Hamm, H.E. (2014) A conserved phenylalanine as a relay between the α5 helix and the GDP binding region of heterotrimeric Gi protein α subunit. J. Biol. Chem. 289(35):24475-24487
43 Thaker, T.M., Preininger, A.M., Sarwar, M., Hamm, H.E., and Iverson T.M. (2014) A transient interaction between the P-loop and Switch I contributes to the allosteric network between receptor and nucleotide in Gαi1. J. Biol. Chem. 289(16):11331-11341
42 Vishnivetskiy, S.A., Zhan, X., Chen, Q., Iverson, T.M., and Gurevich, V.V. (2014) Arrestin expression in E. coli and purification. Curr. Protoc. Pharmacol. 67(Unit 2.11)
2013
41 Zhuang T., Chen Q., Cho M.K., Vishnivetskiy S.A., Iverson T.M., Gurevich V.V., and Sanders C.R. (2013) Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin. Proc Natl Acad Sci USA 110(3): 942-947
40 Seo, H.S., Misanov, G., Seepersaud, R., Doran, K.S., Dubrovska, I., Shuvalova, L., Anderson, W.F., Iverson T.M., and Sullam, P.M. (2013) Characterization of Fibrinogen Binding by Glycoproteins Srr1 and Srr2 of Streptococcus agalactiae. J. Biol. Chem. 288(50): 35982-35996
39 Singh P.K., Sarwar M., Maklashina E., Kotlyar V., Rajaqukquk S., Tomasiak T.M., Cecchini G., Iverson T.M. (2013) Plasticity of the Quinone-Binding Site of the Complex II Homolog Quinol:Fumarate Reductase. J. Biol Chem.
38 Vishnivetskiy S.A., Chen Q., Palazzo M.C., Brooks E.K., Altenbach C., Iverson T.M., Hubbell W.L., and Gurevich V.V. (2013) Engineering visual arrestin-1 with special functional characteristics. J Biol Chem 288(5): 3394-405.
37 Thaker T.M., Tanabe M., Fowler M.L., Preininger A.M., Ingram-Smith C., Smith K.S., and Iverson T.M. (2013) Crystal structures of acetate kinases from the eukaryotic pathogens Entamoeba histolytica and Cryptococcus neoformans. J Struct Biol. 181(2):185-9.
2012
36 Iverson T.M., Panosian, T.D., Birmingham, W., Nannemann, D. P., and Bachmann, B.O. (2012) Molecular differences between a mutase and a phosphatase: investigations of the activation step in Bacillus cereus phosphopentomutase. Biochemistry. 51(9): 1964-1975.
35 Iverson T.M. (2012) Catalytic mechanisms of complex II enzymes: A structural perspective. Biochim Biophys Acta. Sep 18. pii: S0005-2728(12) 01031-6.
34 Iverson T.M., Maklashina E., and Cecchini G. (2012) Structural basis for malfunction in complex II. J Biol Chem. 287(42): 35430-8.
2011
33 Pyburn, T.M., Bensing, B.A., Melancon, B.J., Tomasiak, T.M., Yankovskaya, V., Oliver, K., Ward, N.J., Sulikowski, G.A., Cecchini, G., Tyska, M.J., Sullam, P.M., and Iverson, T.M. (2011) A structural model for binding of the serine-rich repeat adhesin GspB to host carbohydrate receptors. PLoS Pathogens. 7(7): e1002112.
32 Kuchtey, J., Olson, L.M., Rinkoski, T., MacKay, E.O., Iverson, T.M.,Gelatt, K.N., Haines, J.L. and Kuchtey, R.W. (2011) Mutation in ADAMTS10 in a canine model of primary open angle glaucoma. PLoS Genetics. 7(2): e1001306.
31 Kaya, A.I., Thaker, T.M., Preininger, A.M., Iverson, T.M., and Hamm, H.E. (2011) Coupling efficiency of rhodopsin and transducin in bicelles. Biochemistry. 50(15): 3193-3203.
30 Thaker, T.M., Kaya, A.I., Preininger, A.M., Hamm, H.E., and Iverson, T.M., (2011) Allosteric Mechanisms of G protein Coupled Receptor Signaling: A Structural Perspective, in A. Fenton (ed.) Methods in Molecular Biology – Allostery: Methods and Protocols, Humana Press, New York, NY. (2011) Part II, Chapter 8, pp. 133-174.
29 Panosian, T.D., Nannemann, D.P., Watkins, G., Wadzinski, B., Bachmann, B.O., and Iverson, T.M. (2011) Bacillus cereus phosphopentomutase is an alkaline phosphatase family member that exhibits an altered catalytic cycle. J. Biol Chem. 286(10): 8043-8054.
28 Tomasiak, T.M., Archuleta, T.L., Andréll, J., Luna-Chavez, C., Davis, T., Sarwar, M., Ham, A.J., McDonald, H., Yankovskaya, V., Maklashina, E., Stern, H.A., Johnston, J.N., Cecchini, G., and Iverson, T.M. (2011) Geometric restraints drive on- and off-pathway catalysis in the Escherichia coli menaquinol:fumarate reductase. J. Biol. Chem. 286(4): 3047-3056.
2010
27 Tanabe M., Nimigean C.M., Iverson, T.M. (2010) Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Proc. Natl. Acad. Sci. USA. 107(15): 6811-6816.
26 Vey J.L., Al-Mestarihi A., Funk M.A., Bachmann B.O., Iverson T.M. (2010) Structure and mechanism of ORF36, an amino sugar oxidizing enzyme in everninomicin biosynthesis. Biochemistry. 49(43): 9306-9317.
25 Pyburn T., Bensing B., Yankovskaya V., Sullam P.M., Iverson T.M. (2010) Purification, crystallization, and preliminary x-ray diffraction analysis of the carbohydrate binding region of the Streptococcus gordonii adhesin GspB. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Nov 1;66(Pt 11):1503-7.
24 Panosian T.D., Nannemann D.P., Bachmann B.O., Iverson T.M. (2010) Crystallization and preliminary X-ray analysis of a phosphopentomutase from Bacillus cereus. Acta Crystallogr. F66(7): 811-814.
2009
23 Thompson A.N., Kim I., Panosian T.D., Iverson T.M., Allen W.A., Nimigean C.M. (2009) Mechanism of potassium-channel selectivity revealed by Na+ and Li+ binding sites within the KcsA pore. Nat. Struct. & Molec Biol. 16(12): 1317-U1143. PMCID:PMC2825899
22 Adler D.H., Phillips J.A., Cogan J.D., Iverson T.M., Stein J.A., et al. (2009) The enteropathy of prostaglandin deficiency. J. Gastroenterol. 44(Suppl 19): 1-7.
21 Preininger, A. M., Funk, M. A., Meier, S. M., Oldham, W. M., Johnston, C. A., Adhikary, S., … Iverson, T. M. (2009). Helix dipole movement and conformational variability contribute to allosteric GDP release in Gαi subunits. Biochemistry, 48(12), 2630–2642.
20 Tanabe M., Iverson T.M. (2009) Expression, purification and preliminary X-ray analysis of the Neisseria meningitidis outer membrane protein PorB. Acta Crystallogr. F65(10): 996-1000.
19 Tanabe M., Iverson T.M. (2009) A Practical Guide to X-Ray Crystallography of beta-barrel Membrane Proteins: Expression, Purification, Detergent Selection, and Crystallization. Membrane Protein Crystallization: 63, 229-267.
2008
18 Tomasiak T.M., Maklashina E., Cecchin, G., Iverson, T.M. (2008) A threonine on the active site loop controls transition state formation in Escherichia coli respiratory complex II. J. Biol Chem. 283(22): 15460-15468.
17 Cecchini G., Maklashina E., Tomasiak T.M., Iverson T.M. Conformational Changes at the Dicarboxylate Binding Site of Succinate Dehydrogenase (Complex II) and Fumarate Reductase, in Frago S., Gomez-Moeno C, Medina M. (eds.) Flavins and Flavoproteins, Prensas Universitarias de Zaragoza (2008) pp. 17-26.
16 Adler D.H., Cogan J.D., Phillips J.A., Schnetz-Boutaud N., Milne G.L, Iverson T.M., Stein J.A., Brenner D.A., Morrow J.D., Boutaud O., Oates J.A. (2008) Inherited human cPLA2α deficiency is associated with impaired eicosanoid biosynthesis, small intestinal ulceration, and platelet dysfunction. J. Clin. Invest. 118:2121-2131.
2007
15 Tomasiak, T, Cecchini, G, Iverson, T.M. 2007. Succinate as Donor; Fumarate as Acceptor, EcoSal Plus 2007; doi:10.1128/ecosal.3.2.6 ASM Press, Washington, D.C.
2006
14 Iverson T.M. (2006) Evolution and unique bioenergetic mechanisms in oxygenic photosynthesis. Curr Opin Chem Biol. 10(2): 91-100.
13 Maklashina E., Iverson T.M., Sher Y., Kotlyar V., Andréll J., Mirza O., Hudson J.M., Armstrong F.A., Rothery R.A., Weiner J.H., Cecchini G. (2006) Fumarate reductase and succinate oxidase activity of Escherichia coli complex II homologs are perturbed differently by mutation of the flavin binding domain. J. Biol. Chem. 281(16): 11357-11365.
2004
12 Ferreira K.N.*, Iverson T.M.*, Maghaloui K., Iwata S, and Barber J. (2004) Architecture of the oxygen evolving centre of photosystem II. Science, 303(5665): 1831-1838.
2003
11 Cecchini G., Maklashina E., Yankovskaya V., Iverson T.M., Iwata S. (2003) Variation in proton donor/acceptor pathways in succinate:quinone oxidoreductases. FEBS Lett. 545(1), 31-8.
2002
10 Doukov T.I., Iverson T.M., Seravalli J., Ragsdale S.W., Drennan C.L. (2002) A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science, 298(5593), 567-72.
9 Iyer R., Iverson T.M., Accardi A., Miller C. (2002) A biological role for prokaryotic ClC chloride channels. Nature, 419(6908), 715-8.
8 Iverson T.M., Luna-Chavez C., Croal L.R., Cecchini G., Rees D.C. (2002) Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. J Biol Chem, 277(18), 16124-30.
2001
7 Iverson T.M., Arciero D.M., Hooper A.B., Rees D.C. (2001) High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea. J Biol Inorg Chem, 6(4), 390-7.
6 Strop P., Smith K.S., Iverson T.M., Ferry J.G., Rees D.C. (2001) Crystal structure of the 'cab'-type beta class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum. J Biol Chem, 276(13), 10299-305.
2000
5 Iverson T.M., Alber B.E., Kisker C., Ferry J.G., Rees D.C. (2000) A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry, 39(31), 9222-31.
4 Iverson, T.M., Luna-Chavez, C, Schröder, I, Cecchini, G, Rees, D C. (2000) Analyzing your complexes: structure of the quinol-fumarate reductase respiratory complex. Curr Opin Struct Biol, 10(4), 448-55.
3 Luna-Chavez C., Iverson T. M., Rees D.C., Cecchini G. (2000) Overexpression, purification, and crystallization of the membrane-bound fumarate reductase from Escherichia coli. Protein Expr Purif, 19(1), 188-96.
1999
2 Iverson T.M., Luna-Chavez C., Cecchini G., Rees D.C. (1999) Structure of the Escherichia coli fumarate reductase respiratory complex. Science, 284(5422), 1961-6.
1998
1 Iverson T.M., Arciero D.M., Hsu B.T., Logan M.S., Hooper A.B., Rees D C. (1998) Heme packing motifs revealed by the crystal structure of the tetra-heme cytochrome c554 from Nitrosomonas europaea. Nat Struct Biol, 5(11), 1005-12.
* Authors contributed equally.