| Year |
Citation |
Score |
| 2014 |
Thapar R. Contribution of protein phosphorylation to binding-induced folding of the SLBP-histone mRNA complex probed by phosphorus-31 NMR. Febs Open Bio. 4: 853-7. PMID 25379382 DOI: 10.1016/J.Fob.2014.10.002 |
0.414 |
|
| 2013 |
Bansal N, Zhang M, Bhaskar A, Itotia P, Lee E, Shlyakhtenko LS, Lam TT, Fritz A, Berezney R, Lyubchenko YL, Stafford WF, Thapar R. Assembly of the SLIP1-SLBP complex on histone mRNA requires heterodimerization and sequential binding of SLBP followed by SLIP1. Biochemistry. 52: 520-36. PMID 23286197 DOI: 10.1021/Bi301074R |
0.387 |
|
| 2012 |
Krishnan N, Lam TT, Fritz A, Rempinski D, O'Loughlin K, Minderman H, Berezney R, Marzluff WF, Thapar R. The prolyl isomerase Pin1 targets stem-loop binding protein (SLBP) to dissociate the SLBP-histone mRNA complex linking histone mRNA decay with SLBP ubiquitination. Molecular and Cellular Biology. 32: 4306-22. PMID 22907757 DOI: 10.1128/Mcb.00382-12 |
0.353 |
|
| 2012 |
Zhang M, Lam TT, Tonelli M, Marzluff WF, Thapar R. Interaction of the histone mRNA hairpin with stem-loop binding protein (SLBP) and regulation of the SLBP-RNA complex by phosphorylation and proline isomerization. Biochemistry. 51: 3215-31. PMID 22439849 DOI: 10.1021/Bi2018255 |
0.388 |
|
| 2006 |
Kupsco JM, Wu MJ, Marzluff WF, Thapar R, Duronio RJ. Genetic and biochemical characterization of Drosophila Snipper: A promiscuous member of the metazoan 3'hExo/ERI-1 family of 3' to 5' exonucleases. Rna (New York, N.Y.). 12: 2103-17. PMID 17135487 DOI: 10.1261/Rna.186706 |
0.33 |
|
| 2006 |
Borchers CH, Thapar R, Petrotchenko EV, Torres MP, Speir JP, Easterling M, Dominski Z, Marzluff WF. Combined top-down and bottom-up proteomics identifies a phosphorylation site in stem-loop-binding proteins that contributes to high-affinity RNA binding. Proceedings of the National Academy of Sciences of the United States of America. 103: 3094-9. PMID 16492733 DOI: 10.1073/Pnas.0511289103 |
0.373 |
|
| 2005 |
Heo J, Thapar R, Campbell SL. Recognition and activation of Rho GTPases by Vav1 and Vav2 guanine nucleotide exchange factors. Biochemistry. 44: 6573-85. PMID 15850391 DOI: 10.1021/Bi047443Q |
0.566 |
|
| 2004 |
Thapar R, Williams JG, Campbell SL. NMR characterization of full-length farnesylated and non-farnesylated H-Ras and its implications for Raf activation. Journal of Molecular Biology. 343: 1391-408. PMID 15491620 DOI: 10.1016/J.Jmb.2004.08.106 |
0.5 |
|
| 2004 |
Thapar R, Marzluff WF, Redinbo MR. Electrostatic contribution of serine phosphorylation to the Drosophila SLBP--histone mRNA complex. Biochemistry. 43: 9401-12. PMID 15260483 DOI: 10.1021/Bi036315J |
0.397 |
|
| 2004 |
Thapar R, Mueller GA, Marzluff WF. The N-terminal domain of the Drosophila histone mRNA binding protein, SLBP, is intrinsically disordered with nascent helical structure. Biochemistry. 43: 9390-400. PMID 15260482 DOI: 10.1021/Bi036314R |
0.415 |
|
| 2003 |
Thapar R, Moore CD, Campbell SL. Backbone 1H, 13C, and 15N resonance assignments for the 21 kDa GTPase Rac1 complexed to GDP and Mg2+. Journal of Biomolecular Nmr. 27: 87-8. PMID 12878844 DOI: 10.1023/A:1024774230562 |
0.481 |
|
| 2002 |
Thapar R, Karnoub AE, Campbell SL. Structural and biophysical insights into the role of the insert region in Rac1 function. Biochemistry. 41: 3875-83. PMID 11900529 DOI: 10.1021/Bi0120087 |
0.619 |
|
| 1999 |
Peterson RW, Nicholson EM, Thapar R, Klevit RE, Scholtz JM. Increased helix and protein stability through the introduction of a new tertiary hydrogen bond. Journal of Molecular Biology. 286: 1609-19. PMID 10064718 DOI: 10.1006/Jmbi.1999.2574 |
0.557 |
|
| 1996 |
Thapar R, Nicholson EM, Rajagopal P, Waygood EB, Scholtz JM, Klevit RE. Influence of N-cap mutations on the structure and stability of Escherichia coli HPr. Biochemistry. 35: 11268-77. PMID 8784180 DOI: 10.1021/Bi960349S |
0.577 |
|
| 1995 |
Peterkofsky A, Seok YJ, Amin N, Thapar R, Lee SY, Klevit RE, Waygood EB, Anderson JW, Gruschus J, Huq H. The Escherichia coli adenylyl cyclase complex: requirement of PTS proteins for stimulation by nucleotides. Biochemistry. 34: 8950-9. PMID 7619794 DOI: 10.1021/Bi00028A003 |
0.615 |
|
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