Skip to main content

URMC Logo

URMC / Structural Biology & Biophysics Facility / Recent Facility Publications

Recent Facility Publications

Miralem T, Lerner-Marmarosh N, Gibbs PE, Jenkins JL, Heimiller C, Maines MD (2016). Interaction of human biliverdin reductase with Akt/protein kinase B and phosphatidylinositol-dependent kinase 1 regulates glycogen synthase kinase 3 activity: a novel mechanism of Akt activation. FASEB J. 2016 May 10. pii: fj.201600330RR. [Epub ahead of print].

Agrawal AA, Salsi E, Chatrikhi R, Henderson S, Jenkins JL, Green MR, Ermolenko DN, Kielkopf CL(2016). An extended U2AF(65)-RNA-binding domain recognizes the 3' splice site signal. Nat Commun. 2016 Mar 8;7:10950. doi: 10.1038/ncomms10950.

Liberman JA, Suddala KC, Aytenfisu A, Chan D, Belashov IA, Salim M, Mathews DH, Spitale RC, Walter NG, Wedekind JE (2015). Structural analysis of a class III preQ1 riboswitch reveals an aptamer distant from a ribosome-binding site regulated by fast dynamics. Proc Natl Acad Sci U S A. 2015 Jul 7;112(27):E3485-94.

Liberman JA, Bogue JT, Jenkins JL, Salim M, Wedekind JE (2014). ITC analysis of ligand binding to preQ₁ riboswitches. Methods Enzymol. 2014;549:435-50.

Agrawal AA, McLaughlin KJ, Jenkins JL, Kielkopf CL (2014). Structure-guided U2AF65 variant improves recognition and splicing of a defective pre-mRNA. Proc Natl Acad Sci U S A. 2014 Dec 9;111(49):17420-5.

Loerch S, Maucuer A, Manceau V, Green MR, Kielkopf CL (2014). Cancer-relevant splicing factor CAPERα engages the essential splicing factor SF3b155 in a specific ternary complex. J Biol Chem. 2014 Jun 289(25):17325-37.

Smith JM, Frost JR, Fasan R (2014). Designer macrocyclic organo-peptide hybrids inhibit the interaction between p53 and HDM2/X by accommodating a functional α-helix. Chem Commun (Camb). 2014 May 21;50(39):5027-30.

Suddala KC, Rinaldi AJ, Feng J, Mustoe AM, Eichhorn CD, Liberman JA, Wedekind JE, Al-Hashimi HM, Brooks CL 3rd, Walter NG (2013). Single transcriptional and translational preQ1 riboswitches adopt similar pre-folded ensembles that follow distinct folding pathways into the same ligand-bound structure. Nucleic Acids Res. 2013 Dec;41(22):10462-75.

Griffiths AE, Rydkin I, Fay PJ (2013). Factor VIIIa A2 Subunit Shows a High Affinity Interaction with Factor IXa: CONTRIBUTION OF A2 SUBUNIT RESIDUES 707-714 TO THE INTERACTION WITH FACTOR IXa J. Biol Chem. 288(21).

Liberman JA, Salim M, Krucinska J, Wedekind JE (2013). Structure of a class II preQ1 riboswitch reveals ligand recognition by a new fold. Nature Chem. Biol. 10.1038/NChemBio.1231.

Gleghorn ML, Gong C, Kielkopf CL, Maquat LE (2013). Staufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRNA decay. Nat Struct Mol Biol. 20, 515-24.

Jenkins JL, Agrawal AA, Gupta A, Green MR, Kielkopf CL (2013). U2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs. Nucleic Acids Res. 41, 3859-73.

Wang W, Maucuer A, Gupta A, Manceau V, Thickman KR, Bauer WJ, Kennedy SD, Wedekind JE, Green MR, Kielkopf CL (2013). Structure of phosphorylated SF1 bound to U2AF65 in an essential splicing factor complex. Structure 21, 197-208.

Daddacha W, Noble E, Nguyen LA, Kennedy EM, Kim B (2013). Effect of Ribonucleotides Embedded in DNA Template on HIV-1 Reverse Transcription Kinetics and Fidelity. J. Biol. Chem. Epub 2013 Mar 11.

Jenkins JL, Agarwal AA, Gupta A, Green MR, Kielkopf CL (2013). U2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs. Nucl. Acids. Res. 41(6), 3859-3873.

Takeyama M, Wakabayashi H, Fay PJ (2012). Factor VIII light chain contains a binding site for factor X that contributes to the catalytic efficiency of factor Xase. Biochemistry 51(3), 820-828.

Salter JD, Lippa GM, Belashov IA, Wedekind JE (2012). Core-binding factor β increases the affinity between human Cullin 5 and HIV-1 Vif within an E3 ligase complex. Biochemistry 51(44) 8702-8704

Bauer WJ, Heath J, Jenkins JL, Kielkopf CL (2012). Three RNA Recognition Motifs Participate in RNA Recognition and Structural Organization by the Pro-apoptotic Splicing Factor TIA-1. J. Mol. Biol. 415(4), 727-740.

Jenkins JL, Krucinska J, McCarty RM, Bandarian V, Wedekind JE (2011). Comparison of a preQ1 riboswitch aptamer in the metabolite-bound and free states with implications for gene regulation. J. Biol. Chem. 286(28), 24626-24637.

Williams KJ, Jenkins JL, Kielkopf CL (2011). Large Favorable Enthalpy Changes Drive Specific RNA Recognition by RNA Recognition Motif Proteins. Biochemistry. 50(9), 1429-1431.

Gupta A, Jenkins JL, Kielkopf CL (2011). RNA induces conformational changes in SF1/U2AF65 splicing factor complex. J. Mol. Biol. 405(5), 1128-1138.

Jenkins JL, Shen H, Green MR, Kielkopf CL (2008). Solution Conformation and Thermodynamic Characteristics of RNA binding by Splicing Factor U2AF65. J. Biol. Chem. 283(48), 33641-33649.