Publications

Capelluto D.G.S., Hellman U, Cazzulo J.J. and Cannata J.J.B. Purification and partial characterization of three isoforms of serine hydroxymethyltransferase from Crithidia fasciculata. Mol. Biochem. Parasitol., 98(2),187-201(1999). pdf

Capelluto D.G.S. Presence of a natural occurring inhibitor of Trypanosoma cruzi serine hydroxymethyltransferase. J. Arg. Chem. Soc., 87(1/2), 43-50 (1999).

Capelluto D.G.S., Hellman U, Cazzulo J.J. and Cannata J.J.B.. Serine hydroxymethyltransferase of Trypanosoma cruzi: Purification and some properties. Eur. J. Biochem., 267, 1-9 (2000). pdf

Capelluto D.G.S., Kutateladze T.G., Habas R., Finkielstein C.V., He X. and Overduin M. DIX domain targets Dishevelled to actin stress fibers and vesicular membranes. Nature, 419, 726-729 (2002). pdf

Kutateladze T.G., Capelluto D.G.S., Ferguson C.G, Cheever M., Kutateladze, A, Prestwich G.D. and Overduin M. Multivalent mechanism of membrane insertion by the FYVE domain. J. Biol Chem. 279, 3050-3057(2004). pdf

Capelluto D.G.S. and Overduin M. Secondary structure, 1H, 13C and 15N resonance assignments and molecular interactions of the Dishevelled DIX domain. J. Biochem Mol. Biol., 38, 243-247 (2005). pdf

Finkielstein C.V., Overduin M and Capelluto D.G.S. Cell migration and signaling specificity is determined by the phosphatidylserine recognition motif of Rac1, J. Biol. Chem., 281(37):27317-26 (2006). pdf

Tokonzaba E., Capelluto D.G.S., Kutateladze T. and Overduin M. Phosphoinositide, phosphopeptide and pyridone interactions of the Abl SH2 domain, Chem. Biol. Drug Des., 67:230-237 (2006). pdf

Sweede M, Ankem G, Chutvirasakul B, Azurmendi H, Chbeir S., Watkins J, Helm R, Finkielstein C.V. and Capelluto D.G.S. Structural and membrane binding properties of the Prickle PET domain. Biochemistry, 47(51): 13524-36 (2008). pdf

Yang J., Kim K., Lucas, A, Drahos, K., Santos, C, Mury, S, Capelluto D.G.S. and Finkielstein C.V. A Novel Heme Regulatory Motif Is Essential for Heme-Mediated Degradation of the Circadian Transcription Factor Period 2. Mol. Cell Biol. 15:4697-4711 (2008). pdf

Finkielstein C.V. and Capelluto D.G.S., International research internships for the high school students. Book Chapter (2008). In Education Outreach and Public Engagement. Series: Mentoring in Academia and Industry, Vol. 1. Erin Dolan, editor Ed. Springer.

Drahos K.E, Welsh J.E., Finkielstein C.V. and Capelluto D.G.S. Sulfatides Partition Disabled-2 in Response to Platelet Activation. PLoS ONE 4(11): e8007. Doi:10.1371/journal.pone.0008007 (2009).

Kale S., Gu B, Capelluto D.G.S., Dou D., Feldman, E, Rumore A, Arredondo FD, Hanlon R, Fudal I, Rouxel T, Lawrence C., Shan W. and Tyler B.M. Effector host-targeting signals of eukaryotic pathogens bind phosphoinositides. Cell 142:284-295 (2010).

Allen WJ, Capelluto D.G.S., Finkielstein C.V and Bevan D.R. Modeling the Relationship between the p53 C-terminal Domain and Binding Partners Using Molecular Dynamics. J. of Phys Chem. 114: 13201-13213 (2010).

Azurmendi H., Mitra S., Ayala I., Li L., Finkielstein C.V. and Capelluto D.G.S. Backbone 1H, 13C and 15N resonance assignments and secondary structure of the Tollip CUE domain. Mol. Cells, 30(6), 581-585 (2010).

Ankem G., Mitra S., Sun F., Moreno A.C., Chutvirasakul B., Azurmendi H.F., Li L. and Capelluto D.G.S. The C2 domain of Tollip, a Toll-like receptor signaling regulator, exhibits a broad preference to phosphoinositides. Biochem J, 435: 597-608 (2011).

Welsh J.D., Charonko J.J., Salmanzadeh-Dozdabi A., Drahos K.E., Shafiee H., Stremler M.A., Davalos R., Capelluto D.G.S., Vlachos P. and Finkielstein C.V. Disabled-2 negative regulates homotypic and heterotypic platelet aggregation by binding to sulfatides. British J Hematol. 154: 122-133 (2011).

Alajlouni R., Drahos, K.E., Finkielstein C.V. and Capelluto D.G.S. Lipid-mediated membrance binding properties of Disabled-2. Biochim Biophys Acta-Biomembranes, 1808://2734-2744 (2011).

Gotoh T., Villa L., Capelluto D.G.S. and Finkielstein C.V. Regulatory pathways coordinating cell cycle progression in early Xenopus development. Results Probl. Cell Differ. 53: 171-199. (2011).

Kale, S.D., C., R.A., Gu, B., Shan, W., Lawrence, C.B., Capelluto, D., and Tyler, B.M. Unraveling the entry mechanism of oomycete and fungal effector proteins into host cells. In Borlaug Global Rust Initiative (BGRI) Technical Workshop. 82-88 (2011).

Capelluto D.G.S. Tollip: a multitasking protein in innate immunity and protein trafficking. Microbes Infect., 14(2): 140-7 (2012).

Maitra U., Deng H., Glaros T., Baker B., Capelluto D.G.S., Li Z., Li L. Molecular mechanisms responsible for the selective and low-grade induction of pro-inflammatory mediators by lipopolysaccharide. J. Immunol., 189: 1014-1023 (2012).

Xiao S., Charonko J.J., Fu X., Salmanzadeh-Dozdabi A., Davaloss R.V., Vlachos P.P., Finkielstein C.V., and Capelluto D.G.S. Structure, sulfatide binding properties, and inhibition of platelet aggregation by a Disabled-2 protein-derived peptide. J. Biol. Chem., 287: 37691-37702 (2012).

Sun F., Kale S.D., Azurmendi H.F., Li D., Tyler B.M., and Capelluto D.G.S. Structural basis for interactions of the Phytophthora sojae RSLR effector Avh5 with phosphatidylinositol 3-phosphate and for host cell entry. Mol Plant Microbe Interact, 26: 331-344 (2013).

Xiao S., Finkielstein C.V., and Capelluto D.G.S. The enigmatice role of sulfatides: new insights in cellular functions and mechanisms of protein recognition. Chapter 3. In Lipid-mediated Protein Signaling. Daniel G.S. Capelluto, editor, Adv Exp Biol Med. Ed. Springer, 991:27-40. (2013)

Mitra S., Traughber C.A., Brannon M.K., Gomez S., and Capelluto D.G.S. Ubiquitin interacts with the Tollip C2 and CUE domains and inhibits binding of Tollip to phosphoinositides. J Biol Chem, 288:25780-91

Xiao S., Zhao X., Finkielstein C.V., and Capelluto D.G.S. A rapid procedure to isolate isotopically-labeled peptides for NMR studies: Application to the Disabled-2 sulfatide-binding motif. J. Pept. Sci., 20:216-222 (2014).

Capelluto D.G.S., Zhao X., Lucas A., Lemkul J., Xiao S., Fu X., Sun F., Bevan D., and Finkielstein C.V. Biophysical and molecular simulations studies of phosphatidic acid binding by the Dishevelled-2 DEP domain, Biophys. J., 106:1101-1111 (2014).

Xiao S., Brannon M.K., Zhao X., Fread K., Ellena J.F., Bushweller J.H., Finkielstein C.V., Armstrong G., and Capelluto D.G.S. Tom1 negatively modulates binding of Tollip to phosphatidylinositol 3-phosphate via a coupled folding and binding mechanism. Structure, 23:1910-1920 (2015)

Selfridge J.M., Moyer K., Capelluto D.G.S., and Finkielstein C.V*. Opening the debate: How to fulfill the need for physicians’ training in circadian-related topics in a full medical school curriculum. J Circadian Rhythms, 13:Art. 7 (2015).

Xiao S., Ellena J.F., Armstrong G., and Capelluto D.G.S. Structure of the GAT domain of the endosomal adaptor protein Tom1. Data in Brief, 344-348 (2016).

Finkielstein C.V., and Capelluto D.G.S. Disabled-2: a modular scaffold protein with multifaceted functions in signaling. Bioessays, 1:S45-55 (2016).

Selfridge J., Gotoh T., Schiffhauer S., Liu, JJ, Stauffer P., Li A., Capelluto D.G.S., and Finkielstein C.V. Chronotherapy: intuitive, sound, founded…but not broadly applied, Drugs 76:1507-1521 (2016).

George D., Charkhesht A., Hull O., Mishra A., Capelluto D.G.S., Mitchell-Koch K., and  Vinh N. Hydration Dynamics and Micelle-Water Interactions in Zwitterionic Micelles. J Phys Chem, Part B 120:10757-10767 (2016).

Ellena J.F., Xiong W., Zhao X., Shanaiah, N. and Capelluto D.G.S. Backbone 1H, 15N, and 13C resonance assignments of the Tom1 VHS domain, Biol NMR Assign 11:1-4 (2017).

Tang TX., Xiong W., Finkielstein C.V., and Capelluto D.G.S. Identification of ligand-binding modulators using the protein-lipid overlay assay, Meth Mol Biol (2017), in press.

Cortes D.F., Tang TX., Capelluto D.G.S., and Lazar I.M. Nanoflow valve for the removal of trapped air in microfluidic structures. Sensors & Actuators: B. Chemical, 243:650-257 (2017).

Zhao X., Xiong W., Xiao S., Tang, T-X., Ellena J.F., Armstrong G., Finkielstein, C.V., and Capelluto D.G.S. Membrane targeting of TIRAP is negatively regulated by phosphorylation in its phosphoinositide-binding motif, Sci Rep 7:43043 (2017).

Tang T-X., Jo A., Deng J., Ellena J.F., Lazar I.M., David R., and Capelluto D.G.S.*, Structural, thermodynamic, and phosphatidylinositol 3-phosphate binding properties of Phafin2, Prot Sci 26:814-823 (2017).

 

Daniel G. S. Capelluto
Associate Professor
Biological Sciences Department
Biocomplexity Institute 263C
1015 Life Science Circle
Blacksburg, VA 24061-0477
E-mail: capellut@vt.edu
Phone: (540) 231-0974

College of Science

 

 

Department of Biological Sciences
2125 Derring Hall
Mail Code 0406
Virginia Tech
Blacksburg, VA 24061-0406
Phone: (540) 231-8930
Fax: (540) 231-9307

Last Update 31 May 2017