| Year |
Citation |
Score |
| 2021 |
Delgadillo RF, Carnes KA, Zaleta-Rivera K, Olmos O, Parkhurst LJ. A FLIM Microscopy Based on Acceptor-Detected Förster Resonance Energy Transfer. Analytical Chemistry. PMID 33691398 DOI: 10.1021/acs.analchem.0c04492 |
0.75 |
|
| 2020 |
Delgadillo RF, Carnes KA, Valles-Villarreal N, Olmos O, Zaleta-Rivera K, Parkhurst LJ. Dual-Channel Stopped-Flow Apparatus for Simultaneous Fluorescence, Anisotropy, and FRET Kinetic Data Acquisition for Binary and Ternary Biological Complexes. Biosensors. 10. PMID 33227895 DOI: 10.3390/bios10110180 |
0.75 |
|
| 2019 |
Delgadillo RF, Mueser TC, Zaleta-Rivera K, Carnes KA, González-Valdez J, Parkhurst LJ. Detailed characterization of the solution kinetics and thermodynamics of biotin, biocytin and HABA binding to avidin and streptavidin. Plos One. 14: e0204194. PMID 30818336 DOI: 10.1371/Journal.Pone.0204194 |
0.775 |
|
| 2013 |
Glanzer JG, Carnes KA, Soto P, Liu S, Parkhurst LJ, Oakley GG. A small molecule directly inhibits the p53 transactivation domain from binding to replication protein A. Nucleic Acids Research. 41: 2047-59. PMID 23267009 DOI: 10.1093/Nar/Gks1291 |
0.459 |
|
| 2012 |
Delgadillo RF, Parkhurst LJ, Mueser TC, Carnes KA. Kinetics of Biotin Derivatives Binding to Avidin and Streptavidin Biophysical Journal. 102: 217a. DOI: 10.1016/J.Bpj.2011.11.1189 |
0.776 |
|
| 2010 |
Delgadillo RF, Parkhurst LJ. Spectroscopic properties of fluorescein and rhodamine dyes attached to DNA. Photochemistry and Photobiology. 86: 261-72. PMID 20003160 DOI: 10.1111/J.1751-1097.2009.00663.X |
0.778 |
|
| 2009 |
Delgadillo RF, Whittington JE, Parkhurst LK, Parkhurst LJ. The TATA-binding protein core domain in solution variably bends TATA sequences via a three-step binding mechanism. Biochemistry. 48: 1801-9. PMID 19199812 DOI: 10.1021/Bi8018724 |
0.759 |
|
| 2008 |
Whittington JE, Delgadillo RF, Attebury TJ, Parkhurst LK, Daugherty MA, Parkhurst LJ. TATA-binding protein recognition and bending of a consensus promoter are protein species dependent. Biochemistry. 47: 7264-73. PMID 18553934 DOI: 10.1021/Bi800139W |
0.757 |
|
| 2007 |
Whittington J, Wood T, Daugherty M, Parkhurst L, Parkhurst L. Full‐length human TBP (hTBP) shows markedly different TATA‐box binding kinetics and thermodynamics from yeast TBP The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A285-C |
0.739 |
|
| 2006 |
Williams SL, Parkhurst LK, Parkhurst LJ. Changes in DNA bending and flexing due to tethered cations detected by fluorescence resonance energy transfer. Nucleic Acids Research. 34: 1028-35. PMID 16481311 DOI: 10.1093/Nar/Gkj498 |
0.445 |
|
| 2004 |
Parkhurst LJ. Distance parameters derived from time-resolved Förster resonance energy transfer measurements and their use in structural interpretations of thermodynamic quantities associated with protein-DNA interactions. Methods in Enzymology. 379: 235-62. PMID 15051361 DOI: 10.1016/S0076-6879(04)79013-8 |
0.414 |
|
| 2003 |
Masters KM, Parkhurst KM, Daugherty MA, Parkhurst LJ. Native human TATA-binding protein simultaneously binds and bends promoter DNA without a slow isomerization step or TFIIB requirement. The Journal of Biological Chemistry. 278: 31685-90. PMID 12791683 DOI: 10.1074/Jbc.M305201200 |
0.551 |
|
| 2003 |
Hardwidge PR, Parkhurst KM, Parkhurst LJ, Maher LJ. Reflections on apparent DNA bending by charge variants of bZIP proteins. Biopolymers. 69: 110-7. PMID 12717726 DOI: 10.1002/Bip.10321 |
0.472 |
|
| 2002 |
Hardwidge PR, Wu J, Williams SL, Parkhurst KM, Parkhurst LJ, Maher LJ. DNA bending by bZIP charge variants: a unified study using electrophoretic phasing and fluorescence resonance energy transfer. Biochemistry. 41: 7732-42. PMID 12056905 DOI: 10.1021/Bi020213W |
0.587 |
|
| 2002 |
Powell RM, Parkhurst KM, Parkhurst LJ. Comparison of TATA-binding protein recognition of a variant and consensus DNA promoters. The Journal of Biological Chemistry. 277: 7776-84. PMID 11726667 DOI: 10.1074/Jbc.M110147200 |
0.716 |
|
| 2001 |
Parkhurst LJ, Parkhurst KM, Powell R, Wu J, Williams S. Time-resolved fluorescence resonance energy transfer studies of DNA bending in double-stranded oligonucleotides and in DNA-protein complexes. Biopolymers. 61: 180-200. PMID 11987180 DOI: 10.1002/Bip.10138 |
0.75 |
|
| 2001 |
Powell RM, Parkhurst KM, Brenowitz M, Parkhurst LJ. Marked stepwise differences within a common kinetic mechanism characterize TATA-binding protein interactions with two consensus promoters. The Journal of Biological Chemistry. 276: 29782-91. PMID 11387341 DOI: 10.1074/Jbc.M104099200 |
0.725 |
|
| 2001 |
Wu J, Parkhurst KM, Powell RM, Brenowitz M, Parkhurst LJ. DNA bends in TATA-binding protein-TATA complexes in solution are DNA sequence-dependent. The Journal of Biological Chemistry. 276: 14614-22. PMID 11278276 DOI: 10.1074/Jbc.M004402200 |
0.738 |
|
| 2001 |
Wu J, Parkhurst KM, Powell RM, Parkhurst LJ. DNA sequence-dependent differences in TATA-binding protein-induced DNA bending in solution are highly sensitive to osmolytes. The Journal of Biological Chemistry. 276: 14623-7. PMID 11278275 DOI: 10.1074/Jbc.M004401200 |
0.724 |
|
| 1999 |
Parkhurst KM, Richards RM, Brenowitz M, Parkhurst LJ. Intermediate species possessing bent DNA are present along the pathway to formation of a final TBP-TATA complex. Journal of Molecular Biology. 289: 1327-41. PMID 10373370 DOI: 10.1006/Jmbi.1999.2835 |
0.532 |
|
| 1996 |
Parkhurst KM, Brenowitz M, Parkhurst LJ. Simultaneous binding and bending of promoter DNA by the TATA binding protein: Real time kinetic measurements Biochemistry. 35: 7459-7465. PMID 8652523 DOI: 10.1021/Bi9530301 |
0.512 |
|
| 1996 |
Parkhurst KM, Parkhurst LJ. Detection of point mutations in DNA by fluorescence energy transfer Journal of Biomedical Optics. 1: 435-441. DOI: 10.1117/12.250674 |
0.403 |
|
| 1995 |
Parkhurst LJ. Donor- acceptor distance distributions in a double-labeled fluorescent oligonucleotide both as a single strand and in duplexes Biochemistry®. 34: 293-300. PMID 7819210 DOI: 10.1021/Bi00001A036 |
0.366 |
|
| 1995 |
Parkhurst LJ. Kinetic studies by fluorescence resonance energy transfer employing a double-labeled oligonucleotide: Hybridization to the oligonucleotide complement and to single-stranded DNA Biochemistry®. 34: 285-292. PMID 7819209 DOI: 10.1021/Bi00001A035 |
0.474 |
|
| 1994 |
Parkhurst LJ, Larsen TM, Lee HY. Effects of wavelength on fitting Adair constants for binding of oxygen to human hemoglobin Methods in Enzymology. 232: 606-632. PMID 8057883 DOI: 10.1016/0076-6879(94)32067-5 |
0.323 |
|
| 1994 |
Parkhurst KM, Hileman RE, Saha D, Gupta NK, Parkhurst LJ. Thermodynamic characterization of the cooperativity of 40S complex formation during the initiation of eukaryotic protein synthesis Biochemistry. 33: 15168-15177. PMID 7999777 DOI: 10.1021/Bi00254A028 |
0.301 |
|
| 1993 |
Mueser TC, Parkhurst LJ. Synthesis of dansyl ribonucleotides and their use in steady-state fluorescence anisotropy studies of nucleotide binding by initiation factor-2 (eif-2) and histone hi International Journal of Biochemistry. 25: 1689-1696. PMID 8288038 DOI: 10.1016/0020-711X(93)90529-N |
0.383 |
|
| 1992 |
Astatke M, McGee WA, Parkhurst LJ. A flow procedure to determine oxygen binding isotherms for low affinity and easily oxidized hemoglobins Comparative Biochemistry and Physiology -- Part B: Biochemistry And. 101: 683-688. PMID 1611887 DOI: 10.1016/0305-0491(92)90359-Y |
0.307 |
|
| 1991 |
Larsen TM, Mueser TC, Parkhurst LJ. Use of dual wavelength spectrophotometry and continuous enzymatic depletion of oxygen for determination of the oxygen binding constants of hemoglobin Analytical Biochemistry. 197: 231-246. PMID 1952070 DOI: 10.1016/0003-2697(91)90383-5 |
0.314 |
|
| 1990 |
Martin KD, Parkhurst LJ. A multipass cuvette for laser photolysis studies and its uses in studying hemoglobin kinetics and equilibria Analytical Biochemistry. 186: 288-295. PMID 2363502 DOI: 10.1016/0003-2697(90)90082-K |
0.316 |
|
| 1990 |
McGee WA, Parkhurst LJ. A combined nuclear magnetic resonance and absorbance stopped-flow apparatus for biochemical studies Analytical Biochemistry. 189: 267-273. PMID 2281872 DOI: 10.1016/0003-2697(90)90119-T |
0.313 |
|
| 1986 |
Dholakia JN, Mueser TC, Woodley CL, Parkhurst LJ, Wahba AJ. The association of NADPH with the guanine nucleotide exchange factor from rabbit reticulocytes: A role of pyridine dinucleotides in eukaryotic polypeptide chain initiation Proceedings of the National Academy of Sciences of the United States of America. 83: 6746-6750. PMID 3462724 DOI: 10.1073/Pnas.83.18.6746 |
0.303 |
|
| 1984 |
Goss DJ, Parkhurst LJ. Ligand binding kinetic studies on the hybrid hemoglobin alpha(carp):beta(human): a hemoglobin with a restricted allosteric range. Biochemistry. 23: 2174-9. PMID 6733080 DOI: 10.1021/Bi00305A011 |
0.342 |
|
| 1984 |
Goss DJ, Parkhurst LJ, Mehta AM, Wahba AJ. Cooperative interactions in the system ribosomes-ribosomal protein S1-polynucleotide triplets Biochemistry. 23: 6522-6529. PMID 6397227 DOI: 10.1021/Bi00321A038 |
0.39 |
|
| 1984 |
Schreiber JK, Parkhurst LJ. Ligand binding equilibrium and kinetic measurements on the dimeric myoglobin of Busycon canaliculatum and the comparative ligand binding of diverse non-cooperative heme proteins Comparative Biochemistry and Physiology -- Part a: Physiology. 78: 129-135. PMID 6146431 DOI: 10.1016/0300-9629(84)90104-X |
0.345 |
|
| 1983 |
Goss DJ, Parkhurst LJ, Mehta AM, Wahba AJ. The binding of ribosomal protein SI to Sl-depleted 30S and 70S ribosomes. A fluorescence anisotropy study of the effects of Mg2+ Nucleic Acids Research. 11: 5589-5602. PMID 6351011 DOI: 10.1093/Nar/11.16.5589 |
0.375 |
|
| 1982 |
Goss DJ, LaGow JB, Parkhurst LJ. The kinetics of ligand binding for diverse mammalian myoglobins and the effects of substitutions outside the heme cavity Comparative Biochemistry and Physiology -- Part B: Biochemistry And. 71: 229-233. PMID 7060346 DOI: 10.1016/0305-0491(82)90245-0 |
0.382 |
|
| 1980 |
Parkhurst LJ, Sima P, Goss DJ. Kinetics of oxygen and carbon monoxide binding to the hemoglobins of Glycera dibranchiata Biochemistry. 19: 2688-2692. PMID 7397098 DOI: 10.1021/Bi00553A023 |
0.312 |
|
| 1980 |
Goss DJ, Parkhurst LJ, Wahba AJ. Kinetic studies of the rates and mechanism of assembly of the protein synthesis initiation complex Biophysical Journal. 32: 283-293. PMID 7018606 DOI: 10.1016/S0006-3495(80)84957-5 |
0.416 |
|
| 1979 |
Parkhurst LJ, Steinmeier RC. Kinetics of carbon monoxide binding to the cooperative dimeric hemoglobin from Thyonella gemmata. Analysis of carbon monoxide equilibrium results Biochemistry. 18: 4651-4656. PMID 497158 DOI: 10.1021/Bi00588A028 |
0.414 |
|
| 1975 |
Parkhurst LJ, LaGow J. Kinetic and equilibrium studies of the ligand binding reactions of eight electrophoretic components of sperm whale ferrimyoglobin Biochemistry. 14: 1200-1205. PMID 1122276 DOI: 10.1021/Bi00677A016 |
0.396 |
|
| 1975 |
Steinmeier RC, Parkhurst LJ. Kinetic studies on the five principal components of normal adult human hemoglobin Biochemistry. 14: 1564-1572. PMID 235958 DOI: 10.1021/Bi00679A003 |
0.367 |
|
| 1975 |
Goss DJ, Parkhurst LJ, Görisch H. Kinetic light scattering studies on the dissociation of hemoglobin from Lumbricus terrestris Biochemistry. 14: 5461-5464. PMID 56 DOI: 10.1021/Bi00696A012 |
0.347 |
|
| 1974 |
Goss DJ, Parkhurst LJ. Ultra-rapid quantitative isolation of specific transfer ribonucleic acids a solid-phase method Biochemical and Biophysical Research Communications. 59: 181-187. PMID 4601813 DOI: 10.1016/S0006-291X(74)80191-9 |
0.342 |
|
| 1973 |
Geraci G, Parkhurst LJ. Effects of heme-globin and chain-chain interactions on the conformation of human hemoglobin. A kinetic study Biochemistry. 12: 3414-3418. PMID 4731185 DOI: 10.1021/Bi00742A008 |
0.325 |
|
| 1972 |
LaGow J, Parkhurst LJ. Kinetics of carbon monoxide and oxygen binding for eight electrophoretic components of sperm-whale myoglobin Biochemistry. 11: 4520-4525. PMID 4675876 DOI: 10.1021/Bi00774A014 |
0.376 |
|
| 1972 |
Wiechelman KJ, Parkhurst LJ. Kinetics of ligand binding in the hemoglobin of Lumbricus terrestris Biochemistry. 11: 4515-4520. PMID 4653126 DOI: 10.1021/Bi00774A013 |
0.379 |
|
| 1971 |
Boelts KJ, Parkhurst LJ. Ligand binding kinetics of hemoglobin from the earthworm Biochemical and Biophysical Research Communications. 43: 637-643. PMID 5563311 DOI: 10.1016/0006-291X(71)90662-0 |
0.357 |
|
| 1966 |
Parkhurst LJ, Anex BG. Polarization of the lowest-energy allowed transition of beta-ionylidene crotonic acid and the electronic structure of the polyenes. The Journal of Chemical Physics. 45: 862-73. PMID 5946286 DOI: 10.1063/1.1727696 |
0.673 |
|
| 1963 |
Anex BG, Parkhurst LJ. A new assignment of the polarization of the charge-transfer transition in crystalline quinhydrone [6] Journal of the American Chemical Society. 85: 3301-3302. DOI: 10.1021/Ja00903A059 |
0.663 |
|
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