Detalhe da pesquisa
1.
Signal Transmission in Escherichia coli Cyclic AMP Receptor Protein for Survival in Extreme Acidic Conditions.
Biochemistry
; 60(40): 2987-3006, 2021 10 12.
Artigo
Inglês
| MEDLINE | ID: mdl-34605636
2.
NMR-based investigations into target DNA search processes of proteins.
Methods
; 148: 57-66, 2018 09 15.
Artigo
Inglês
| MEDLINE | ID: mdl-29753002
3.
Changes in conformational dynamics of basic side chains upon protein-DNA association.
Nucleic Acids Res
; 44(14): 6961-70, 2016 08 19.
Artigo
Inglês
| MEDLINE | ID: mdl-27288446
4.
Balancing between affinity and speed in target DNA search by zinc-finger proteins via modulation of dynamic conformational ensemble.
Proc Natl Acad Sci U S A
; 112(37): E5142-9, 2015 Sep 15.
Artigo
Inglês
| MEDLINE | ID: mdl-26324943
5.
Thermodynamic Additivity for Impacts of Base-Pair Substitutions on Association of the Egr-1 Zinc-Finger Protein with DNA.
Biochemistry
; 55(47): 6467-6474, 2016 Nov 29.
Artigo
Inglês
| MEDLINE | ID: mdl-27933778
6.
Stereospecific Effects of Oxygen-to-Sulfur Substitution in DNA Phosphate on Ion Pair Dynamics and Protein-DNA Affinity.
Chembiochem
; 17(17): 1636-42, 2016 09 02.
Artigo
Inglês
| MEDLINE | ID: mdl-27271797
7.
Entropic Enhancement of Protein-DNA Affinity by Oxygen-to-Sulfur Substitution in DNA Phosphate.
Biophys J
; 109(5): 1026-37, 2015 Sep 01.
Artigo
Inglês
| MEDLINE | ID: mdl-26331260
8.
Temperature dependence of internal motions of protein side-chain NH3(+) groups: insight into energy barriers for transient breakage of hydrogen bonds.
Biochemistry
; 54(2): 538-45, 2015 Jan 20.
Artigo
Inglês
| MEDLINE | ID: mdl-25489884
9.
Asymmetrical roles of zinc fingers in dynamic DNA-scanning process by the inducible transcription factor Egr-1.
Proc Natl Acad Sci U S A
; 109(26): E1724-32, 2012 Jun 26.
Artigo
Inglês
| MEDLINE | ID: mdl-22675124
10.
Real-time kinetics of high-mobility group box 1 (HMGB1) oxidation in extracellular fluids studied by in situ protein NMR spectroscopy.
J Biol Chem
; 288(17): 11621-7, 2013 Apr 26.
Artigo
Inglês
| MEDLINE | ID: mdl-23447529
11.
Effective strategy to assign ¹H- ¹5N heteronuclear correlation NMR signals from lysine side-chain NH33⺠groups of proteins at low temperature.
J Biomol NMR
; 60(1): 23-7, 2014 Sep.
Artigo
Inglês
| MEDLINE | ID: mdl-25129623
12.
Molecular basis of hUHRF1 allosteric activation for synergistic histone modification binding by PI5P.
Sci Adv
; 8(34): eabl9461, 2022 Aug 26.
Artigo
Inglês
| MEDLINE | ID: mdl-36001657
13.
Signature of mobile hydrogen bonding of lysine side chains from long-range 15N-13C scalar J-couplings and computation.
J Am Chem Soc
; 133(24): 9192-5, 2011 Jun 22.
Artigo
Inglês
| MEDLINE | ID: mdl-21591797
14.
Structural basis for allosteric PARP-1 retention on DNA breaks.
Science
; 368(6486)2020 04 03.
Artigo
Inglês
| MEDLINE | ID: mdl-32241924
15.
NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains.
Nat Commun
; 9(1): 844, 2018 02 27.
Artigo
Inglês
| MEDLINE | ID: mdl-29487285
16.
Hydrogen-Deuterium Exchange Coupled to Top- and Middle-Down Mass Spectrometry Reveals Histone Tail Dynamics before and after Nucleosome Assembly.
Structure
; 26(12): 1651-1663.e3, 2018 12 04.
Artigo
Inglês
| MEDLINE | ID: mdl-30293810
17.
Centromeres are maintained by fastening CENP-A to DNA and directing an arginine anchor-dependent nucleosome transition.
Nat Commun
; 8: 15775, 2017 06 09.
Artigo
Inglês
| MEDLINE | ID: mdl-28598437
18.
Residence Times of Molecular Complexes in Solution from NMR Data of Intermolecular Hydrogen-Bond Scalar Coupling.
J Phys Chem Lett
; 7(5): 820-4, 2016 Mar 03.
Artigo
Inglês
| MEDLINE | ID: mdl-26881297
19.
Physicochemical Properties of Ion Pairs of Biological Macromolecules.
Biomolecules
; 5(4): 2435-63, 2015 Sep 30.
Artigo
Inglês
| MEDLINE | ID: mdl-26437440
20.
Structural impact of complete CpG methylation within target DNA on specific complex formation of the inducible transcription factor Egr-1.
FEBS Lett
; 589(15): 1748-53, 2015 Jul 08.
Artigo
Inglês
| MEDLINE | ID: mdl-25999311