Stereospecific Nuclear Magnetic Resonance Assignments of the Methyl Groups of Valine and Leucine in the DNA-Binding Domain of the 434 Repressor by Biosynthetically Directed Fractional 13C Labeling

Magnetic Resonance ◽

Dna Binding ◽

Resonance Assignments ◽

Binding Domain ◽

Methyl Groups ◽

Dna Binding Domain ◽

13C Labeling ◽

434 Repressor ◽

Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional carbon-13 labeling

Biochemistry ◽

10.1021/bi00445a003 ◽

1989 ◽

Vol 28 (19) ◽

pp. 7510-7516 ◽

Cited By ~ 422

Author(s):

Dario Neri ◽

Thomas Szyperski ◽

Gottfried Otting ◽

Hans Senn ◽

Kurt Wuethrich

Keyword(s):

Magnetic Resonance ◽

Dna Binding ◽

Resonance Assignments ◽

Binding Domain ◽

Methyl Groups ◽

Dna Binding Domain ◽

434 Repressor ◽

Determination of the Nuclear Magnetic Resonance Structure of the DNA-binding Domain of the P22 c2 Repressor (1 to 76) in Solution and Comparison with the DNA-binding Domain of the 434 Repressor

Journal of Molecular Biology ◽

10.1006/jmbi.1994.1053 ◽

1994 ◽

Vol 235 (3) ◽

pp. 1003-1020 ◽

Cited By ~ 33

Author(s):

P. Sevilla-Sierra ◽

G. Otting ◽

K. Wüthrich

Keyword(s):

Magnetic Resonance ◽

Dna Binding ◽

Binding Domain ◽

Resonance Structure ◽

Nuclear Magnetic Resonance Structure ◽

Dna Binding Domain ◽

434 Repressor ◽

Secondary structure of the lac repressor DNA-binding domain by two-dimensional 1H nuclear magnetic resonance in solution.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.80.19.5837 ◽

1983 ◽

Vol 80 (19) ◽

pp. 5837-5841 ◽

Cited By ~ 70

Author(s):

E. R. Zuiderweg ◽

R. Kaptein ◽

K. Wuthrich

Keyword(s):

Magnetic Resonance ◽

Secondary Structure ◽

Dna Binding ◽

Binding Domain ◽

Lac Repressor ◽

Dna Binding Domain ◽

Two Dimensional ◽

1H Nuclear Magnetic Resonance ◽

Hydrogen Exchange of Individual Amide Protons in the E. ColilacRepressor DNA-binding Domain: A Nuclear Magnetic Resonance Study (29)

Journal of Biomolecular Structure and Dynamics ◽

10.1080/07391102.1985.10508416 ◽

1985 ◽

Vol 3 (2) ◽

pp. 269-280 ◽

Cited By ~ 14

Author(s):

R. Boelens ◽

P. Gros ◽

R. M. Scheek ◽

J. A. Verpoorte ◽

R. Kaptein

Keyword(s):

Magnetic Resonance ◽

Dna Binding ◽

Hydrogen Exchange ◽

Nuclear Magnetic Resonance Study ◽

Binding Domain ◽

Dna Binding Domain ◽

Magnetic Resonance Study ◽

Nuclear Magnetic ◽

Amide Protons

Dynamics of the DNA Binding Domain of the Fructose Repressor from the Analysis of Linear Correlations between the15N−1H Bond Spectral Densities Obtained by Nuclear Magnetic Resonance Spectroscopy

Biochemistry ◽

10.1021/bi971706h ◽

1998 ◽

Vol 37 (15) ◽

pp. 5060-5073 ◽

Cited By ~ 9

Author(s):

Carine van Heijenoort ◽

François Penin ◽

Eric Guittet

Keyword(s):

Magnetic Resonance ◽

Dna Binding ◽

Magnetic Resonance Spectroscopy ◽

Nuclear Magnetic Resonance Spectroscopy ◽

Binding Domain ◽

Resonance Spectroscopy ◽

Dna Binding Domain ◽

Spectral Densities ◽

Linear Correlations

Intrinsic Differences in Backbone Dynamics between Wild Type and DNA-Contact Mutants of the p53 DNA Binding Domain Revealed by Nuclear Magnetic Resonance Spectroscopy

Biochemistry ◽

10.1021/acs.biochem.7b00514 ◽

2017 ◽

Vol 56 (37) ◽

pp. 4962-4971 ◽

Cited By ~ 5

Author(s):

Juhi A. Rasquinha ◽

Aritra Bej ◽

Shraboni Dutta ◽

Sujoy Mukherjee

Keyword(s):

Magnetic Resonance ◽

Dna Binding ◽

Magnetic Resonance Spectroscopy ◽

Nuclear Magnetic Resonance Spectroscopy ◽

Binding Domain ◽

Backbone Dynamics ◽

Resonance Spectroscopy ◽

Dna Binding Domain ◽

Wild Type

Determination of the nuclear magnetic resonance solution structure of the DNA-binding domain (residues 1 to 69) of the 434 repressor and comparison with the X-ray crystal structure

Journal of Molecular Biology ◽

10.1016/0022-2836(92)90987-u ◽

1992 ◽

Vol 223 (3) ◽

pp. 743-767 ◽

Cited By ~ 45

Author(s):

Dario Neri ◽

Martin Billeter ◽

Kurt Wüthrich

Keyword(s):

Crystal Structure ◽

Magnetic Resonance ◽

Dna Binding ◽

Solution Structure ◽

Dna Binding Domain ◽

X Ray ◽

Resonance Solution ◽

434 Repressor

Nuclear magnetic resonance assignments and global fold of a CheY-binding domain in CheA, the chemotaxis-specific kinase of Escherichia coli

Biochemistry ◽

10.1021/bi00042a019 ◽

1995 ◽

Vol 34 (42) ◽

pp. 13871-13880 ◽

Cited By ~ 22

Author(s):

Megan M. McEvoy ◽

Hongjun Zhou ◽

Amy F. Roth ◽

David F. Lowry ◽

Tom B. Morrison ◽

...

Keyword(s):

Escherichia Coli ◽

Magnetic Resonance ◽

Resonance Assignments ◽

Binding Domain ◽

Global Fold ◽

ChemInform Abstract: CARBON-13 NUCLEAR MAGNETIC RESONANCE ASSIGNMENTS AND BIOSYNTHESIS OF VERSICOLORIN A IN ASPERGILLUS PARASITICUS

Chemischer Informationsdienst ◽

10.1002/chin.197850358 ◽

1978 ◽

Vol 9 (50) ◽

Author(s):

C. P. GORST-ALLMAN ◽

P. S. STEYN ◽

P. L. WESSELS ◽

D. B. SCOTT

Keyword(s):

Magnetic Resonance ◽

Aspergillus Parasiticus ◽

Resonance Assignments ◽

Versicolorin A ◽

Nuclear magnetic resonance studies of sperm whale myoglobin specifically enriched with 13C in the methionine methyl groups.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)32870-3 ◽

1976 ◽

Vol 251 (23) ◽

pp. 7452-7460 ◽

Cited By ~ 2

Author(s):

W C Jones ◽

T M Rothgeb ◽

F R Gurd

Keyword(s):

Magnetic Resonance ◽

Sperm Whale ◽

Methyl Groups ◽

Magnetic Resonance Studies ◽

Sperm Whale Myoglobin ◽