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Results: 1-14 |
Results: 14
Kinetic trapping of DNA by transcription factor IIIB
Authors: Cloutier, TE Librizzi, MD Mollah, AKMM Brenowitz, M Willis, IM
Citation: Te. Cloutier et al., Kinetic trapping of DNA by transcription factor IIIB, P NAS US, 98(17), 2001, pp. 9581-9586
Marked stepwise differences within a common kinetic mechanism characterizeTATA-binding protein interactions with two consensus promoters
Authors: Powell, RM Parkhurst, KM Brenowitz, M Parkhurst, LJ
Citation: Rm. Powell et al., Marked stepwise differences within a common kinetic mechanism characterizeTATA-binding protein interactions with two consensus promoters, J BIOL CHEM, 276(32), 2001, pp. 29782-29791
DNA bends in TATA-binding protein center dot TATA complexes in solution are DNA sequence-dependent
Authors: Wu, J Parkhurst, KM Powell, RM Brenowitz, M Parkhurst, LJ
Citation: J. Wu et al., DNA bends in TATA-binding protein center dot TATA complexes in solution are DNA sequence-dependent, J BIOL CHEM, 276(18), 2001, pp. 14614-14622
Mg2+-linked oligomerization modulates the catalytic activiy of the Lon (La) protease from Mycobacterium smegmatis
Authors: Rudyak, SG Brenowitz, M Shrader, TE
Citation: Sg. Rudyak et al., Mg2+-linked oligomerization modulates the catalytic activiy of the Lon (La) protease from Mycobacterium smegmatis, BIOCHEM, 40(31), 2001, pp. 9317-9323
Stability and cooperativity of individual tertiary contacts in RNA revealed through chemical denaturation
Authors: Ralston, CY He, Q Brenowitz, M Chance, MR
Citation: Cy. Ralston et al., Stability and cooperativity of individual tertiary contacts in RNA revealed through chemical denaturation, NAT ST BIOL, 7(5), 2000, pp. 371-374
The early folding intermediates of the tetrahymena ribozyme are kinetically trapped
Authors: Ralston, CY Sclavi, B Brenowitz, M Sullivan, M Chance, MR
Citation: Cy. Ralston et al., The early folding intermediates of the tetrahymena ribozyme are kinetically trapped, J BIO STRUC, 2000, pp. 195-200
Time-resolved synchrotron X-ray footprinting and its application to RNA folding
Authors: Ralston, CY Sclavi, B Sullivan, M Deras, ML Woodson, SA Chance, MR Brenowitz, M
Citation: Cy. Ralston et al., Time-resolved synchrotron X-ray footprinting and its application to RNA folding, METH ENZYM, 317, 2000, pp. 353-368
A detailed interpretation of OH radical footprints in a TBP-DNA complex reveals the role of dynamics in the mechanism of sequence-specific binding
Authors: Pastor, N Weinstein, H Jamison, E Brenowitz, M
Citation: N. Pastor et al., A detailed interpretation of OH radical footprints in a TBP-DNA complex reveals the role of dynamics in the mechanism of sequence-specific binding, J MOL BIOL, 304(1), 2000, pp. 55-68
Folding mechanism of the Tetrahymena ribozyme P4-P6 domain
Authors: Deras, ML Brenowitz, M Ralston, CY Chance, MR Woodson, SA
Citation: Ml. Deras et al., Folding mechanism of the Tetrahymena ribozyme P4-P6 domain, BIOCHEM, 39(36), 2000, pp. 10975-10985
Participation of the amino-terminal domain in the self-association of the full-length yeast TATA binding protein
Authors: Daugherty, MA Brenowitz, M Fried, MG
Citation: Ma. Daugherty et al., Participation of the amino-terminal domain in the self-association of the full-length yeast TATA binding protein, BIOCHEM, 39(16), 2000, pp. 4869-4880
Quantitative DNase I kinetics footprinting
Authors: Mollah, AKMM Brenowitz, M
Citation: Akmm. Mollah et M. Brenowitz, Quantitative DNase I kinetics footprinting, PRACT APPR, 2000, pp. 281-290
Intermediate species possessing bent DNA are present along the pathway to formation of a final TBP-TATA complex
Authors: Parkhurst, KM Richards, RM Brenowitz, M Parkhurst, LJ
Citation: Km. Parkhurst et al., Intermediate species possessing bent DNA are present along the pathway to formation of a final TBP-TATA complex, J MOL BIOL, 289(5), 1999, pp. 1327-1341
The TATA-binding protein from Saccharomyces cerevisiae oligomerizes in solution at micromolar concentrations to form tetramers and octamers
Authors: Daugherty, MA Brenowitz, M Fried, MG
Citation: Ma. Daugherty et al., The TATA-binding protein from Saccharomyces cerevisiae oligomerizes in solution at micromolar concentrations to form tetramers and octamers, J MOL BIOL, 285(4), 1999, pp. 1389-1399
Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry
Authors: Maleknia, SD Brenowitz, M Chance, MR
Citation: Sd. Maleknia et al., Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry, ANALYT CHEM, 71(18), 1999, pp. 3965-3973
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