Year |
Citation |
Score |
2022 |
Hunsicker-Wang LM, Vogt MJ, Hoogstraten CG, Cosper NJ, Davenport AM, Hendon CH, Scott RA, Britt RD, DeRose VJ. Spectroscopic characterization of Mn and Cd coordination to phosphorothioates in the conserved A9 metal site of the hammerhead ribozyme. Journal of Inorganic Biochemistry. 230: 111754. PMID 35219138 DOI: 10.1016/j.jinorgbio.2022.111754 |
0.481 |
|
2021 |
Hoogstraten CG, Terrazas M, Aviñó A, White NA, Sumita M. Dynamics-Function Analysis in Catalytic RNA Using NMR Spin Relaxation and Conformationally Restricted Nucleotides. Methods in Molecular Biology (Clifton, N.J.). 2167: 183-202. PMID 32712921 DOI: 10.1007/978-1-0716-0716-9_11 |
0.477 |
|
2018 |
Kamba PF, Dickson DA, White NA, Ekstrom JL, Koslowsky DJ, Hoogstraten CG. The 27 kDa Trypanosoma brucei Pentatricopeptide Repeat Protein is a G-tract Specific RNA Binding Protein. Scientific Reports. 8: 16989. PMID 30451852 DOI: 10.1038/S41598-018-34377-9 |
0.421 |
|
2018 |
White NA, Sumita M, Marquez VE, Hoogstraten CG. Coupling Between Conformational Dynamics and Catalytic Function at the Active Site of the Lead-Dependent Ribozyme. Rna (New York, N.Y.). PMID 30111534 DOI: 10.1261/Rna.067579.118 |
0.46 |
|
2017 |
White NA, Hoogstraten CG. Thermodynamics and kinetics of RNA tertiary structure formation in the junctionless hairpin ribozyme. Biophysical Chemistry. 228: 62-68. PMID 28710920 DOI: 10.1016/J.Bpc.2017.07.001 |
0.461 |
|
2016 |
Ochieng PO, White NA, Feig M, Hoogstraten CG. Intrinsic Base-Pair Rearrangement in the Hairpin Ribozyme Directs RNA Conformational Sampling and Tertiary Interface Formation. The Journal of Physical Chemistry. B. PMID 27701852 DOI: 10.1021/Acs.Jpcb.6B05606 |
0.44 |
|
2015 |
Ochieng PO, Wang B, Feig M, Hoogstraten CG. Alternative Base-Pairing and Conformational Sampling in Loop a of the Hairpin Ribozyme Biophysical Journal. 108: 238a. DOI: 10.1016/J.Bpj.2014.11.1318 |
0.321 |
|
2014 |
Hoogstraten CG, Sumita M, White NA. Unraveling the thermodynamics and kinetics of RNA assembly: surface plasmon resonance, isothermal titration calorimetry, and circular dichroism. Methods in Enzymology. 549: 407-32. PMID 25432758 DOI: 10.1016/B978-0-12-801122-5.00017-9 |
0.44 |
|
2013 |
Sumita M, White NA, Julien KR, Hoogstraten CG. Intermolecular domain docking in the hairpin ribozyme: metal dependence, binding kinetics and catalysis. Rna Biology. 10: 425-35. PMID 23324606 DOI: 10.4161/Rna.23609 |
0.461 |
|
2008 |
Johnson JE, Hoogstraten CG. Extensive backbone dynamics in the GCAA RNA tetraloop analyzed using 13C NMR spin relaxation and specific isotope labeling. Journal of the American Chemical Society. 130: 16757-69. PMID 19049467 DOI: 10.1021/Ja805759Z |
0.493 |
|
2008 |
Julien KR, Sumita M, Chen PH, Laird-Offringa IA, Hoogstraten CG. Conformationally restricted nucleotides as a probe of structure-function relationships in RNA. Rna (New York, N.Y.). 14: 1632-43. PMID 18596252 DOI: 10.1261/Rna.866408 |
0.486 |
|
2008 |
Hoogstraten CG, Johnson JE. Metabolic labeling: Taking advantage of bacterial pathways to prepare spectroscopically useful isotope patterns in proteins and nucleic acids Concepts in Magnetic Resonance Part a: Bridging Education and Research. 32: 34-55. DOI: 10.1002/Cmr.A.20103 |
0.368 |
|
2007 |
Hoogstraten CG, Sumita M. Structure-function relationships in RNA and RNP enzymes: recent advances. Biopolymers. 87: 317-28. PMID 17806104 DOI: 10.1002/Bip.20836 |
0.438 |
|
2006 |
Vogt M, Lahiri S, Hoogstraten CG, Britt RD, DeRose VJ. Coordination environment of a site-bound metal ion in the hammerhead ribozyme determined by 15N and 2H ESEEM spectroscopy. Journal of the American Chemical Society. 128: 16764-70. PMID 17177426 DOI: 10.1021/Ja057035P |
0.671 |
|
2006 |
Johnson JE, Julien KR, Hoogstraten CG. Alternate-site isotopic labeling of ribonucleotides for NMR studies of ribose conformational dynamics in RNA. Journal of Biomolecular Nmr. 35: 261-74. PMID 16937241 DOI: 10.1007/S10858-006-9041-X |
0.447 |
|
2002 |
Hoogstraten CG, Britt RD. Water counting: quantitating the hydration level of paramagnetic metal ions bound to nucleotides and nucleic acids. Rna (New York, N.Y.). 8: 252-60. PMID 11911370 DOI: 10.1017/S1355838202014826 |
0.61 |
|
2002 |
Hoogstraten CG, Grant CV, Horton TE, DeRose VJ, Britt RD. Structural analysis of metal ion ligation to nucleotides and nucleic acids using pulsed EPR spectroscopy. Journal of the American Chemical Society. 124: 834-42. PMID 11817959 DOI: 10.1021/Ja0112238 |
0.711 |
|
2001 |
Summers JS, Hoogstraten CG, Britt RD, Base K, Shaw BR, Ribeiro AA, Crumbliss AL. 31P NMR probes of chemical dynamics: paramagnetic relaxation enhancement of the (1)H and (31)P NMR resonances of methyl phosphite and methylethyl phosphate anions by selected metal complexes. Inorganic Chemistry. 40: 6547-54. PMID 11735462 DOI: 10.1021/ic010728w |
0.461 |
|
2000 |
Hoogstraten CG, Wank JR, Pardi A. Active site dynamics in the lead-dependent ribozyme. Biochemistry. 39: 9951-8. PMID 10933815 DOI: 10.1021/Bi0007627 |
0.62 |
|
1999 |
Morrissey SR, Horton TE, Grant CV, Hoogstraten CG, Britt RD, DeRose VJ. Mn2+-nitrogen interactions in RNA probed by electron spin-echo envelope modulation spectroscopy: Application to the hammerhead ribozyme Journal of the American Chemical Society. 121: 9215-9218. DOI: 10.1021/Ja9921571 |
0.688 |
|
1998 |
Hoogstraten CG, Legault P, Pardi A. NMR solution structure of the lead-dependent ribozyme: evidence for dynamics in RNA catalysis. Journal of Molecular Biology. 284: 337-50. PMID 9813122 DOI: 10.1006/Jmbi.1998.2182 |
0.656 |
|
1998 |
Legault P, Hoogstraten CG, Metlitzky E, Pardi A. Order, dynamics and metal-binding in the lead-dependent ribozyme. Journal of Molecular Biology. 284: 325-35. PMID 9813121 DOI: 10.1006/Jmbi.1998.2181 |
0.653 |
|
1998 |
Hoogstraten CG, Pardi A. Measurement of carbon-phosphorus J coupling constants in RNA using spin-echo difference constant-time HCCH-COSY. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 133: 236-40. PMID 9654495 DOI: 10.1006/Jmre.1998.1457 |
0.618 |
|
1998 |
Hoogstraten CG, Pardi A. Improved distance analysis in RNA using network-editing techniques for overcoming errors due to spin diffusion. Journal of Biomolecular Nmr. 11: 85-95. PMID 9566314 DOI: 10.1023/A:1008239625802 |
0.649 |
|
1996 |
Hoogstraten CG, Markley JL. Effects of experimentally achievable improvements in the quality of NMR distance constraints on the accuracy of calculated protein structures. Journal of Molecular Biology. 258: 334-48. PMID 8627630 DOI: 10.1006/Jmbi.1996.0254 |
0.529 |
|
1995 |
Hoogstraten CG, Westler WM, Mooberry ES, Macura S, Markley JL. Analysis of transverse cross relaxation in proteins within a simplified relaxation submatrix: BD-ROESY. Journal of Magnetic Resonance. Series B. 109: 76-9. PMID 8581311 DOI: 10.1006/Jmrb.1995.1149 |
0.441 |
|
1995 |
Hoogstraten CG, Choe S, Westler WM, Markley JL. Comparison of the accuracy of protein solution structures derived from conventional and network-edited NOESY data. Protein Science : a Publication of the Protein Society. 4: 2289-99. PMID 8563625 DOI: 10.1002/Pro.5560041106 |
0.604 |
|
1995 |
Hoogstraten CG, Westler WM, Macura S, Markley JL. NOE Measurements in the Absence of Spin Diffusion: Application to Methylene Groups in Proteins and Effects on Local Structural Parameters. [Erratum to document cited in CA122:310070] Journal of the American Chemical Society. 117: 8885-8885. DOI: 10.1021/Ja00139A037 |
0.496 |
|
1995 |
Hoogstraten CG, Westler WM, Macura SI, Markley JL. NOE Measurements in the Absence of Spin Diffusion: Application to Methylene Groups in Proteins and Effects on Local Structural Parameters Journal of the American Chemical Society. 117: 5610-5611. DOI: 10.1021/Ja00125A033 |
0.51 |
|
1993 |
Hoogstraten CG, Westler WM, Macura S, Markley JL. Improved Measurement of Longer Proton-Proton Distances in Proteins by Relaxation Network Editing Journal of Magnetic Resonance, Series B. 102: 232-235. DOI: 10.1006/Jmrb.1993.1090 |
0.48 |
|
1992 |
Macura S, Fejzo J, Hoogstraten CG, Westler WM, Markley JL. Topological Editing of Cross-Relaxation Networks Israel Journal of Chemistry. 32: 245-256. DOI: 10.1002/Ijch.199200031 |
0.489 |
|
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