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SELECTED REFERENCES:

 

Chapman, S, Schrader, J, and Uhlenbeck, OC. "Histidine 66 in E. coli Elongation Factor TU Selectively Stabilitizes Aminoacyl-tRNAs" J Biol Chem, 287, 1229-1234 (2012)

Schrader, J. and Uhlenbeck, OC. “Is the sequence-specific binding of aminoacyl-tRNAs by EF-Tu universal among bacteria?" Nucleic Acids Res, doi: 10.1093/nar/gkr641 (2011)

Saks, M, Sanderson, L, Choi, D, Crosby, C, and Uhlenbeck, OC. “Functional consequences of T-stem mutations in E. coli tRNAThrUCU in vitro and in vivoRNA, 17, 1038-47 (2011).

Schrader, J, Chapman, S, and Uhlenbeck, OC. “Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding” Proc. Natl. Acad. Sci. U.S.A., 108, 5215-20 (2011).

Schrader, J, Saks, M, & Uhlenbeck OC. “The specific interaction between aminoacyl-tRNAs and elongation factor Tu” in Ribosomes: Structure, Function, and Dynamics Springer-Verlag Wien New York (2011).

Shepotinovskaya IV, Uhlenbeck, OC. “Enhanced product stability in the hammerhead ribozyme" Biochemistry, 49 4494–4500 (2010).

Elles-Sharpe L, Sykes M, Williamson J, Uhlenbeck OC. “A dominant negative mutant of the E. Coli RNA helicase DbpA blocks assembly of the 50S ribosomal subunit.” Nucleic Acids Res., 37, 6503-6514 (2009).

Uhlenbeck, OC. “RNA biophysics has come of age.” Biopolymers. 91, 811-4 (2009).

Ledoux S, Olejniczak M, & Uhlenbeck OC. “A sequence element that tunes E. coli tRNAAlaGGC to ensure accurate decoding.” Nat. Struct. Mol. Biol.,16, 359 – 364 (2009).

Schrader, J, Chapman, S, & Uhlenbeck OC. “Understanding the sequence wpecificity of tRNA binding to EF-Tu by tRNA mutagenesis.” JMB, 386, 1255-1264 (2009).

Dale T, Olejniczak M, Fahlman R, & Uhlenbeck OC. “Specificity of the ribosomal A site for aminoacyl-tRNAs” Nucleic Acids Res., 37, 1202-1210 (2008).

Garcia I & Uhlenbeck OC. “Differential RNA-dependent ATPase activities of four rRNA processing yeast DEAD-box proteins.” Biochemistry, 47, 12562–12573 (2008).

Shepotinovskaya I & Uhlenbeck OC.  “Catalytic diversity in natural hammerhead ribozymes”.  Biochemistry, 47, 7034–7042 (2008).

Nelson JA & Uhlenbeck OC.  “Hammerhead redux: Does the new structure fit the old biochemical data?”  RNA, 14, 605-615 (2008).

Ledoux S & Uhlenbeck OC. “[3'-(32)P]-labeling tRNA with nucleotidyltransferase for assaying aminoacylation and peptide bond formation.”  Methods,  44, 74-80  (2008)

Elles LM & Uhlenbeck OC.  “Mutation of the arginine finger in the active site of Escherichia coli DbpA abolishes ATPase and helicase activity and confers a dominant slow growth phenotype.”  Nucleic Acids. Res., 36, 41-50 (2007).

Nelson JA & Uhlenbeck OC. “Minimal and extended hammerheads utilize a similar dynamic reaction mechanism for catalysis”.  RNA, 14, 43-54 (2007).

Sanderson LE & Uhlenbeck OC.  “The 51-63 base pair of tRNA confers specificity for binding by EF-Tu”.  RNA 13,  835-840 (2007).

Sanderson LE & Uhlenbeck OC.  “Exploring the specificity of bacterial elongation factor Tu for different tRNAs”.  Biochemistry,  46, 6194-6200 (2007). 

Sanderson LE & Uhlenbeck OC. “Directed mutagenesis identifies amino acid residues involved in elongation factor Tu binding to yeast Phe-tRNAPhe”.  JMB, 368, 119-130 (2007).

Nelson JA & Uhlenbeck OC.  “When to believe what you see.”  Mol. Cell,  4, 447-450  (2006).

Olejniczak M & Uhlenbeck OC.  “tRNA residues that have coevolved with their anticodon to ensure uniform and accurate codon recognition.”  Biochemie,  8, 943-50  (2006).

Wang S, Hu Y, Overgaard MT, Karginov FV, Uhlenbeck OC & McKay DB.  “The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold.”  RNA, 12, 956-967  (2006).

Hobson D & Uhlenbeck OC.  “Alanine scanning of MS2 coat protein reveals protein-phosphate contacts Involved in thermodynamic hot spots.”  JMB, 356, 613-24  (2005).

Fahlman RP, Olejniczak M & Uhlenbeck OC.  “Quantitative analysis of deoxynucleotide substitutions in the codon-anticodon helix.”  JMB, 355, 887-892  (2005).

 

View Publications by Olke C. Uhlenbeck listed in the National Library of Medicine (PubMed).

 

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