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HEINRICH RODER lab
Protein folding, dynamics and function

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Fox Chase Cancer Center

Scientific Report:  2006 / 2005 / 2004 / 2003 / 2002 / 2001 / 2000 / 1999  / 1998 / 1997 / 1996 / 1995 / 1994  

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Lab members

Heiner Roder (Biosketch) | Hong Cheng | Hossein Fazelinia | Ruzaliya Fazlieva | Harvey H. Hensley | Ming Xu | Agnieszka Lewandowska

Former lab members

 

Recent Papers

Cheng, H., Li, J., Fazlieva, R., Dai, Z., Bu, Z. & Roder, H. (2009). Autoinhibitory Interactions between the PDZ2 and C-terminal Domains in the Scaffolding Protein NHERF1. Structure 17, 660-669. (pdf)

Tzul, F.O., Kurchan, E., Roder, H., and Bowler, B.E. (2009). Competition between reversible aggregation and loop formation in denatured iso-1-cytochrome c. Biochemistry 48, 481-491. (pdf)

Latypov, R.F., Maki, K., Cheng, H., Luck, S.D., and Roder, H. (2008). Folding mechanism of reduced Cytochrome c: equilibrium and kinetic properties in the presence of carbon monoxide. J. Mol. Biol. 383, 437-453. (pdf)

Srimathi, T., Robbins, S.L., Dubas, R.L., Chang, H., Cheng, H., Roder, H., and Park, Y.C. (2008). Mapping of POP1-binding site on pyrin domain of ASC. J. Biol. Chem. 283, 15390-15398. (pdf)

D. Samuel, H. Cheng, P. W. Riley, A. A. Canutescu, C. Nagaswami, J. W. Weisel, Z. Bu, P. N. Walsh, and H. Roder (2007) Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation. Proc. Natl. Acad. Sci. USA, 104:15693-98. (pdf)

Bender, G.M., Lehmann, A., Zou, H., Cheng, H., Fry, H.C., Engel, D., Therien, M.J., Blasie, J.K., Roder, H., Saven, J.G., and Degrado, W.F. (2007). De Novo Design of a Single-Chain Diphenylporphyrin Metalloprotein. J. Am. Chem. Soc. 129:10732-10740. (pdf)

Maki, K., Cheng, H., Dolgikh, D. A. & Roder, H. (2007) Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods. J. Mol. Biol., 368:244-255. (pdf)

Abel, C.J., Goldbeck, R.A., Latypov, R.F., Roder, H., & Kliger, D.S. (2007) Conformational equilibration time of unfolded protein chains and the folding speed limit. Biochemistry, 46:4090-4099. (pdf)

Riley, P. W., Cheng, H., Samuel, D., Roder, H. & Walsh, P. N. (2007). Dimer Dissociation and Unfolding Mechanism of Coagulation Factor XI Apple 4 Domain: Spectroscopic and Mutational Analysis. J. Mol. Biol. 367:558-573. (pdf)

Apetri, A. C., Maki, K., Roder, H. & Surewicz, W. K. (2006) Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments. J. Am. Chem. Soc. 128:11673-8. (pdf)

Roder, H., Maki,K. & Cheng, H. (2006). Early events in protein folding explored by rapid mixing methods. Chem. Rev. 106(5): 1836-1861. (pdf)

Latypov, R. F., Cheng, H., Roder, N. A., Zhang, J. & Roder, H. (2006). Structural Characterization of an Equilibrium Unfolding Intermediate in Cytochrome c. J. Mol. Biol. 357:1009-1025 (pdf)

Kurchan, E., Roder, H. & Bowler, B.E. (2005) Kinetics of Loop Formation and Breakage in the Denatured State of Iso-1-cytochrome c. J. Mol. Biol. 353:730-43. (pdf)

Roder, H., Maki, K., Latypov, R. F., Cheng, H. & Shastry, M. C. R. (2005). Early events in protein folding explored by rapid mixing methods. In Protein Foldign Handbook, Vol. Part I, pp. 491-535. Wiley-VCH, Weinheim. (pdf)

Garcia, P., Bruix, M., Rico, M., Ciofi-Baffoni, S., Banci, L., Ramachandra Shastry, M. C., Roder, H., de Lumley Woodyear, T., Johnson, C. M., Fersht, A. R., et al. (2005). Effects of Heme on the Structure of the Denatured State and Folding Kinetics of Cytochrome b(562). J. Mol. Biol. 346:331-344. (pdf)

 

Any questions? Problems? Comments? Send mail to: roder@fccc.edu

Designed by J M. Sauder. Last updated 11/11/09 by H. Roder

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