☰

Clara L. Kielkopf, Ph.D. - Publications

Affiliations: 
2000 California Institute of Technology, Pasadena, CA 
Area:
Protein Structure and Energetics; X-ray Crystallography
Tree Info Similar researchers PubMed Report error

60 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2022 Galardi JW, Bela VN, Jeffery N, He X, Glasser E, Loerch S, Jenkins JL, Pulvino MJ, Boutz PL, Kielkopf CL. A UHM - ULM interface with unusual structural features contributes to U2AF2 and SF3B1 association for pre-mRNA splicing. The Journal of Biological Chemistry. 102224. PMID 35780835 DOI: 10.1016/j.jbc.2022.102224  0.45
2022 Glasser E, Maji D, Biancon G, Puthenpeedikakkal AMK, Cavender CE, Tebaldi T, Jenkins JL, Mathews DH, Halene S, Kielkopf CL. Pre-mRNA splicing factor U2AF2 recognizes distinct conformations of nucleotide variants at the center of the pre-mRNA splice site signal. Nucleic Acids Research. PMID 35524551 DOI: 10.1093/nar/gkac287  0.492
2021 Chatrikhi R, Feeney CF, Pulvino MJ, Alachouzos G, MacRae AJ, Falls Z, Rai S, Brennessel WW, Jenkins JL, Walter MJ, Graubert TA, Samudrala R, Jurica MS, Frontier AJ, Kielkopf CL. A synthetic small molecule stalls pre-mRNA splicing by promoting an early-stage U2AF2-RNA complex. Cell Chemical Biology. PMID 33689684 DOI: 10.1016/j.chembiol.2021.02.007  0.315
2020 Maji D, Glasser E, Henderson S, Galardi J, Pulvino MJ, Jenkins JL, Kielkopf CL. Representative cancer-associated U2AF2 mutations alter RNA interactions and splicing. The Journal of Biological Chemistry. 295: 17148-17157. PMID 33453965 DOI: 10.1074/jbc.RA120.015339  0.432
2020 Maji D, Glasser E, Henderson S, Galardi J, Pulvino MJ, Jenkins JL, Kielkopf CL. Representative cancer-associated U2AF2 mutations alter RNA interactions and splicing. The Journal of Biological Chemistry. PMID 33020180 DOI: 10.1074/jbc.RA120.015339  0.42
2020 Warnasooriya C, Feeney CF, Laird KM, Ermolenko DN, Kielkopf CL. A splice site-sensing conformational switch in U2AF2 is modulated by U2AF1 and its recurrent myelodysplasia-associated mutation. Nucleic Acids Research. PMID 32343311 DOI: 10.1093/Nar/Gkaa293  0.515
2019 Maji D, Grossfield AM, Kielkopf CL. Structures of SF3b1 reveal a dynamic Achilles heel of spliceosome assembly: Implications for cancer-associated abnormalities and drug discovery. Biochimica Et Biophysica Acta. Gene Regulatory Mechanisms. 194440. PMID 31707043 DOI: 10.1016/J.Bbagrm.2019.194440  0.411
2019 Talkish J, Igel H, Hunter O, Horner SW, Jeffery NN, Leach JR, Jenkins JL, Kielkopf CL, Ares M. Cus2 enforces the first ATP-dependent step of splicing by binding to yeast SF3b1 through a UHM-ULM interaction. Rna (New York, N.Y.). PMID 31110137 DOI: 10.1261/Rna.070649.119  0.478
2019 Kennedy SD, Bauer WJ, Wang W, Kielkopf CL. Dynamic stacking of an expected branch point adenosine in duplexes containing pseudouridine-modified or unmodified U2 snRNA sites. Biochemical and Biophysical Research Communications. PMID 30797552 DOI: 10.1016/J.Bbrc.2019.02.073  0.486
2019 Biancon G, Joshi P, Hunck T, Gao Y, Botti V, Qin A, Sadykov M, Wang X, Viero G, Neuenkirchen N, Taylor A, Huang J, Ardasheva A, Fu X, Lin H, ... ... Kielkopf CL, et al. U2AF1 Driver Mutations in Hematopoietic Disorders Alter but Do Not Abrogate RNA Binding and Enlighten Structural Dependencies of the U2AF-RNA Complex Blood. 134: 1230-1230. DOI: 10.1182/Blood-2019-130759  0.544
2019 Kielkopf CL, Feeney CF, Chatrikhi R, MacRae A, Alachouzos G, Falls Z, Laird KM, Jenkins JL, Samudrala R, Frontier AJ, Jurica MS. A synthetic molecule stalls pre-mRNA splicing by enhancing cancer-relevant U2AF2–RNA complexes Acta Crystallographica Section a Foundations and Advances. 75: a103-a103. DOI: 10.1107/S0108767319098969  0.302
2019 Maji D, Grossfield A, Kielkopf CL. Structural analysis shows spliceosome-induced closure of an α-helical super-helix in the proto-oncogenic splicing factor SF3b1 Acta Crystallographica Section a Foundations and Advances. 75: a130-a130. DOI: 10.1107/S0108767319098696  0.34
2019 Glasser E, Maji D, Henderson S, Pulvino M, Jenkins JL, Kielkopf CL. The essential pre-mRNA splicing factor U2AF65 accommodates divergent nucleotides at the central position of the polypyrimidine 3′ splice site signal Acta Crystallographica Section a Foundations and Advances. 75: a134-a134. DOI: 10.1107/S0108767319098659  0.411
2018 Loerch S, Leach JR, Horner SW, Maji D, Jenkins JL, Pulvino M, Kielkopf CL. The pre-mRNA splicing and transcription factor Tat-SF1 is a functional partner of the spliceosome SF3b1 subunit via a U2AF homology motif interface. The Journal of Biological Chemistry. PMID 30567737 DOI: 10.2210/Pdb6N3D/Pdb  0.485
2018 Kielkopf CL, Warnasooriya CM, Ermolenko DN. Emerging views of U2AF at the 3′ splice site: a disease-relevant step of gene expression Acta Crystallographica Section a Foundations and Advances. 74: a186-a186. DOI: 10.1107/S0108767318098136  0.339
2018 Maji D, Glasser E, Jenkins JL, Kielkopf CL. Cancer-associated mutations of the pre-mRNA splicing factor U2AF2 alter splice site signal recognition Acta Crystallographica Section a Foundations and Advances. 74: a232-a232. DOI: 10.1107/S0108767318097672  0.397
2017 Kielkopf CL. Insights from structures of cancer-relevant pre-mRNA splicing factors. Current Opinion in Genetics & Development. 48: 57-66. PMID 29128695 DOI: 10.1016/J.Gde.2017.10.008  0.416
2017 Glasser E, Agrawal A, Jenkins JL, Kielkopf CL. Cancer-associated mutations mapped on high resolution structures of the U2AF2 RNA recognition motifs. Biochemistry. PMID 28850223 DOI: 10.1021/Acs.Biochem.7B00551  0.419
2017 Jenkins JL, Kielkopf CL. Splicing Factor Mutations in Myelodysplasias: Insights from Spliceosome Structures. Trends in Genetics : Tig. PMID 28372848 DOI: 10.1016/J.Tig.2017.03.001  0.467
2016 Chatrikhi R, Wang W, Gupta A, Loerch S, Maucuer A, Kielkopf CL. SF1 Phosphorylation Enhances Specific Binding to U2AF(65) and Reduces Binding to 3'-Splice-Site RNA. Biophysical Journal. 111: 2570-2586. PMID 28002734 DOI: 10.1016/J.Bpj.2016.11.007  0.51
2016 Loerch S, Kielkopf CL. Unmasking the U2AF homology motif family: a bona fide protein-protein interaction motif in disguise. Rna (New York, N.Y.). 22: 1795-1807. PMID 27852923 DOI: 10.1261/Rna.057950.116  0.386
2016 Fei DL, Motowski H, Chatrikhi R, Prasad S, Yu J, Gao S, Kielkopf CL, Bradley RK, Varmus H. Wild-Type U2AF1 Antagonizes the Splicing Program Characteristic of U2AF1-Mutant Tumors and Is Required for Cell Survival. Plos Genetics. 12: e1006384. PMID 27776121 DOI: 10.1371/Journal.Pgen.1006384  0.345
2016 Agrawal AA, Salsi E, Chatrikhi R, Henderson S, Jenkins JL, Green MR, Ermolenko DN, Kielkopf CL. An extended U2AF(65)-RNA-binding domain recognizes the 3' splice site signal. Nature Communications. 7: 10950. PMID 26952537 DOI: 10.1038/Ncomms10950  0.559
2015 Loerch S, Kielkopf CL. Dividing and Conquering the Family of RNA Recognition Motifs: A Representative Case Based on hnRNP L. Journal of Molecular Biology. 427: 2997-3000. PMID 26101840 DOI: 10.1016/J.Jmb.2015.06.009  0.492
2015 Okeyo-Owuor T, White BS, Chatrikhi R, Mohan DR, Kim S, Griffith M, Ding L, Ketkar-Kulkarni S, Hundal J, Laird KM, Kielkopf CL, Ley TJ, Walter MJ, Graubert TA. U2AF1 mutations alter sequence specificity of pre-mRNA binding and splicing. Leukemia. 29: 909-17. PMID 25311244 DOI: 10.1038/Leu.2014.303  0.478
2014 Agrawal AA, McLaughlin KJ, Jenkins JL, Kielkopf CL. Structure-guided U2AF65 variant improves recognition and splicing of a defective pre-mRNA. Proceedings of the National Academy of Sciences of the United States of America. 111: 17420-5. PMID 25422459 DOI: 10.1073/Pnas.1412743111  0.728
2014 Loerch S, Maucuer A, Manceau V, Green MR, Kielkopf CL. Cancer-relevant splicing factor CAPERα engages the essential splicing factor SF3b155 in a specific ternary complex. The Journal of Biological Chemistry. 289: 17325-37. PMID 24795046 DOI: 10.1074/Jbc.M114.558825  0.479
2014 Agrawal A, Kielkopf C. Human U2AF65 Recognizing the Major Polypyrimidine Splice Site Signal Acta Crystallographica Section a Foundations and Advances. 70: C1163-C1163. DOI: 10.1107/S2053273314088366  0.537
2013 Gleghorn ML, Gong C, Kielkopf CL, Maquat LE. Staufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRNA decay Nature Structural and Molecular Biology. 20: 515-524. PMID 23524536 DOI: 10.1038/Nsmb.2528  0.529
2013 Jenkins JL, Agrawal AA, Gupta A, Green MR, Kielkopf CL. U2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs. Nucleic Acids Research. 41: 3859-73. PMID 23376934 DOI: 10.1093/Nar/Gkt046  0.536
2013 Wang W, Maucuer A, Gupta A, Manceau V, Thickman KR, Bauer WJ, Kennedy SD, Wedekind JE, Green MR, Kielkopf CL. Structure of phosphorylated SF1 bound to U2AF⁶⁵ in an essential splicing factor complex. Structure (London, England : 1993). 21: 197-208. PMID 23273425 DOI: 10.1016/J.Str.2012.10.020  0.448
2012 Jenkins JL, Laird KM, Kielkopf CL. A Broad range of conformations contribute to the solution ensemble of the essential splicing factor U2AF(65). Biochemistry. 51: 5223-5. PMID 22702716 DOI: 10.1021/Bi300277T  0.478
2012 Bauer WJ, Heath J, Jenkins JL, Kielkopf CL. Three RNA recognition motifs participate in RNA recognition and structural organization by the pro-apoptotic factor TIA-1. Journal of Molecular Biology. 415: 727-40. PMID 22154808 DOI: 10.1016/J.Jmb.2011.11.040  0.516
2011 Gupta A, Kielkopf CL. Purification, crystallization and preliminary X-ray crystallographic analysis of a central domain of human splicing factor 1. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 67: 486-90. PMID 21505248 DOI: 10.1107/S1744309111004623  0.429
2011 McLaughlin KJ, Jenkins JL, Kielkopf CL. Large favorable enthalpy changes drive specific RNA recognition by RNA recognition motif proteins. Biochemistry. 50: 1429-31. PMID 21261285 DOI: 10.1021/Bi102057M  0.725
2011 Gupta A, Jenkins JL, Kielkopf CL. RNA induces conformational changes in the SF1/U2AF65 splicing factor complex. Journal of Molecular Biology. 405: 1128-38. PMID 21146534 DOI: 10.1016/J.Jmb.2010.11.054  0.469
2010 McLaughlin KJ, Strain-Damerell CM, Xie K, Brekasis D, Soares AS, Paget MS, Kielkopf CL. Structural basis for NADH/NAD+ redox sensing by a Rex family repressor. Molecular Cell. 38: 563-75. PMID 20513431 DOI: 10.1016/J.Molcel.2010.05.006  0.708
2009 Gupta A, Kielkopf CL. A Novel Domain Implicated in the Interactions between pre-mRNA Splicing Factors Biophysical Journal. 96: 600a. DOI: 10.1016/J.Bpj.2008.12.3141  0.43
2009 Williams KJ, Jenkins JL, Kielkopf CL. Thermodynamic Characteristics of pre-mRNA Splice Site Recognition Biophysical Journal. 96: 63a-64a. DOI: 10.1016/J.Bpj.2008.12.226  0.531
2009 Kielkopf CL. Structural and Thermodynamic Means for Adaptable 3′ Splice Site Recognition Biophysical Journal. 96: 366a. DOI: 10.1016/J.Bpj.2008.12.1973  0.551
2008 Jenkins JL, Shen H, Green MR, Kielkopf CL. Solution conformation and thermodynamic characteristics of RNA binding by the splicing factor U2AF65. The Journal of Biological Chemistry. 283: 33641-9. PMID 18842594 DOI: 10.1074/Jbc.M806297200  0.55
2008 Manceau V, Kielkopf CL, Sobel A, Maucuer A. Different requirements of the kinase and UHM domains of KIS for its nuclear localization and binding to splicing factors. Journal of Molecular Biology. 381: 748-62. PMID 18588901 DOI: 10.1016/J.Jmb.2008.06.026  0.42
2008 Lin Y, Kielkopf CL. X-ray structures of U2 snRNA-branchpoint duplexes containing conserved pseudouridines. Biochemistry. 47: 5503-14. PMID 18435545 DOI: 10.1021/Bi7022392  0.505
2008 Kumar AO, Swenson MC, Benning MM, Kielkopf CL. Structure of the central RNA recognition motif of human TIA-1 at 1.95A resolution. Biochemical and Biophysical Research Communications. 367: 813-9. PMID 18201561 DOI: 10.1016/J.Bbrc.2008.01.027  0.499
2007 Swenson MC, Paranawithana SR, Miller PS, Kielkopf CL. Structure of a DNA repair substrate containing an alkyl interstrand cross-link at 1.65 A resolution. Biochemistry. 46: 4545-53. PMID 17375936 DOI: 10.1021/Bi700109R  0.376
2007 Thickman KR, Sickmier EA, Kielkopf CL. Alternative conformations at the RNA-binding surface of the N-terminal U2AF(65) RNA recognition motif. Journal of Molecular Biology. 366: 703-10. PMID 17188295 DOI: 10.1016/J.Jmb.2006.11.077  0.504
2006 Sickmier EA, Frato KE, Shen H, Paranawithana SR, Green MR, Kielkopf CL. Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65. Molecular Cell. 23: 49-59. PMID 16818232 DOI: 10.1016/J.Molcel.2006.05.025  0.564
2006 Sickmier EA, Frato KE, Kielkopf CL. Crystallization and preliminary X-ray analysis of a U2AF65 variant in complex with a polypyrimidine-tract analogue by use of protein engineering. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 62: 457-9. PMID 16682775 DOI: 10.1107/S1744309106012504  0.477
2006 Manceau V, Swenson M, Le Caer JP, Sobel A, Kielkopf CL, Maucuer A. Major phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65. The Febs Journal. 273: 577-87. PMID 16420481 DOI: 10.1111/J.1742-4658.2005.05091.X  0.437
2006 Thickman KR, Swenson MC, Kabogo JM, Gryczynski Z, Kielkopf CL. Multiple U2AF65 binding sites within SF3b155: thermodynamic and spectroscopic characterization of protein-protein interactions among pre-mRNA splicing factors. Journal of Molecular Biology. 356: 664-83. PMID 16376933 DOI: 10.1016/J.Jmb.2005.11.067  0.519
2006 Sickmier EA, Frato KE, Paranawithana S, Shen H, Green MR, Kielkopf CL. Structural basis of polypyrimidine tract recognition by the essential splicing factor U2AF65. Molecular Cell. 23: 49-59. DOI: 10.2210/Pdb2G4B/Pdb  0.398
2005 Sickmier EA, Brekasis D, Paranawithana S, Bonanno JB, Paget MS, Burley SK, Kielkopf CL. X-ray structure of a Rex-family repressor/NADH complex insights into the mechanism of redox sensing. Structure (London, England : 1993). 13: 43-54. PMID 15642260 DOI: 10.1016/J.Str.2004.10.012  0.422
2004 Kielkopf CL, Lücke S, Green MR. U2AF homology motifs: protein recognition in the RRM world. Genes & Development. 18: 1513-26. PMID 15231733 DOI: 10.1101/Gad.1206204  0.412
2002 Kielkopf CL, Burley SK. X-ray structures of threonine aldolase complexes: structural basis of substrate recognition. Biochemistry. 41: 11711-20. PMID 12269813 DOI: 10.1021/Bi020393+  0.313
2001 Kielkopf CL, Rodionova NA, Green MR, Burley SK. A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer. Cell. 106: 595-605. PMID 11551507 DOI: 10.1016/S0092-8674(01)00480-9  0.487
2000 Kielkopf CL, Ding S, Kuhn P, Rees DC. Conformational flexibility of B-DNA at 0.74 A resolution: d(CCAGTACTGG)(2). Journal of Molecular Biology. 296: 787-801. PMID 10677281 DOI: 10.1006/Jmbi.1999.3478  0.59
2000 Kielkopf CL, Erkkila KE, Hudson BP, Barton JK, Rees DC. Structure of a photoactive rhodium complex intercalated into DNA. Nature Structural Biology. 7: 117-21. PMID 10655613 DOI: 10.1038/72385  0.571
2000 Kielkopf CL, Bremer RE, White S, Szewczyk JW, Turner JM, Baird EE, Dervan PB, Rees DC. Structural effects of DNA sequence on T.A recognition by hydroxypyrrole/pyrrole pairs in the minor groove. Journal of Molecular Biology. 295: 557-67. PMID 10623546 DOI: 10.1006/Jmbi.1999.3364  0.604
1998 Kielkopf CL, White S, Szewczyk JW, Turner JM, Baird EE, Dervan PB, Rees DC. A structural basis for recognition of A.T and T.A base pairs in the minor groove of B-DNA. Science (New York, N.Y.). 282: 111-5. PMID 9756473 DOI: 10.1126/Science.282.5386.111  0.548
1998 Kielkopf CL, Baird EE, Dervan PB, Rees DC. Structural basis for G.C recognition in the DNA minor groove. Nature Structural Biology. 5: 104-9. PMID 9461074 DOI: 10.1038/Nsb0298-104  0.594
Show low-probability matches.