Carl C. Correll, Ph.D.

Associate Professor
Chicago Medical School
Biochemistry and Molecular Biology
Room: 3.128
Building: BSB
Phone: 847.578.8611
Fax: 847.578.3240
Carl.Correll@rosalindfranklin.edu
Publications

For e-Print (PDF file) contact Carl Correll

Sardana R., Liu, X., Granneman S., Zhu J., Gill, M., Papoulas, O., Marcotte, E.M., Tollervey, D., Correll, C.C., Johnson, A.W. (In Press) The DEAH-box helicase Dhr1 Dissociates U3 from the pre-rRNA to promote formation of the Central Pseudoknot. PLOS Biology.

Shah, B.N., Liu X., Correll CC. (2013) Imp3 unfolds stem structures in pre-rRNA and U3 snoRNA to form a duplex essential for small subunit processing. RNA 19, 1372-1383. [medline]

Plantinga, M.J., Korennykh, A.V., Piccirilli, J.A. Correll, C.C. (2011) The ribotoxin restrictocin recognizes its RNA substrate by selective engagement of active site residues. Biochemistry 50, 3004-3013. [medline]

Gérczei, T., Shah, B.N., Anthony J. Manzo, A.J., Walter, N.G. and Correll, C.C. (2009) RNA chaperones stimulate formation and yield of the U3 snoRNA-pre-rRNA duplexes needed for ribosome biogenesis. Journal of Molecular Biology 390, 991-1006. [medline]

Plantinga, M.J., Korennykh, A.V., Piccirilli, J.A. and Correll, C.C. (2008) Electrostatic interactions guide the active site face of a structure-specific ribonuclease to its RNA substrate. Biochemistry 47, 8912-8918. [medline]

Korennykh AV, Plantinga MJ, Correll CC, Piccirilli JA. (2007) Abstract Linkage between Substrate Recognition and Catalysis during Cleavage of Sarcin/Ricin Loop RNA by Restrictocin. Biochemistry 46, 12744-12756. [medline]

Korennykh, A.V., Correll, C.C. and Piccirilli, J.A. (2007) Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins. RNA 13, 1391-1396. [medline]

Korennykh, A.V., Piccirilli, J.A. and Correll, C.C. (2006) The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins. Nature Structural & Molecular Biology 13, 436-443. [medline]

Gérczei, T. and Correll, C.C. (2004) Imp3p and Imp4p mediate formation of essential U3-pre-rRNA duplexes, possibly to recruit the small subunit processome to the pre-rRNA. PNAS 101, 15301-15306. [medline]

Correll, C.C., Beneken, J., Plantinga, M.J., Lubbers, M and Chan, Y-L (2003) The common and the distinctive features of the bulged-G motif based on a 1.04 Å resolution RNA structure. Nucleic Acids Research 31, 6806-6818.[medline]

Correll, C.C. and Swinger, K. (2003) Common and distinctive features of GNRA tetraloops based on a GUAA tetraloop structure at 1.4 Å resolution. RNA 9 355-363.[medline]

Yang, X., Gérczei, T., Glover, L. and Correll, C.C. (2001) Crystal structures of restrictocin-inhibitor complexes with implications for RNA recognition and base flipping. Nature Structural Biology 8, 968-973.[medline]

Correll, C.C., Wool, I.G. and Munishkin, A. (1999) The two faces of the Escherichia coli 23 S rRNA sarcin/ricin domain: the structure at 1.11 Å resolution. Journal of Molecular Biology 292 275-287.[medline]

Correll, C.C., Munishkin, A., Chan, Y., Ren, Z., Wool, I.R. and Steitz, T.A. (1998) Crystal structure of the ribosomal RNA loop essential for binding both elongation factors. Proc. Natl. Acad. Sci. USA 95, 13436-14341.

Correll, C.C., Freeborn, B., Moore, P.B., Steitz, T.A. (1997) Metals, motifs, and recognition in the crystal structure of a 5S rRNA domain. Cell 91, 705-712.

Correll, C.C., Ludwig, M.L., Bruns, C.M. and Karplus, P.A. (1993) Structural prototypes for an extended family of flavoprotein reductases: Comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin. Protein Science 2, 2112-2113.

Correll, C.C., Batie, C.J., Ballou, D.P. and Ludwig, M.L. (1992) Phthalate dioxygenase reductase: A modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]. Science 258, 1604-1610.

Correll, C.C., Batie, C.J., Ballou P.D. and Ludwig, M.L. (1985)  Crystallographic characterization of phthalate oxygenase reductase, an iron-sulfur flavoprotein from Pseudomanoas cepacia. Journal of Biological Chemistry 260, 14633-14635.

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