Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: evidence for an activating surface

M Nohaile, D Kern, D Wemmer, K Stedman… - Journal of molecular …, 1997 - Elsevier
The bacterial enhancer-binding protein NtrC activates transcription when phosphorylated on
aspartate 54 in its amino (N)-terminal regulatory domain or when altered by constitutively …
被引用次数：65 相关文章

Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: evidence for an activating surface.

M Nohaile, D Kern, D Wemmer… - Journal of Molecular …, 1997 - europepmc.org
The bacterial enhancer-binding protein NtrC activates transcription when phosphorylated on
aspartate 54 in its amino (N)-terminal regulatory domain or when altered by constitutively …

Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: evidence for an activating surface

M Nohaile, D Kern, D Wemmer… - … of molecular biology, 1997 - pubmed.ncbi.nlm.nih.gov
The bacterial enhancer-binding protein NtrC activates transcription when phosphorylated on
aspartate 54 in its amino (N)-terminal regulatory domain or when altered by constitutively …
[PDF] academia.edu

[PDF][PDF] Structural and Functional Analyses of Activating Amino Acid Substitutions in the Receiver Domain of NtrC: Evidence for an Activating Surface

M Nohaile, D Kern, D Wemmer, K Stedman, S Kustu - J. Mol. Biol, 1997 - academia.edu
Two-component systems are a large family of signal transduction proteins that have been
found in all domains of life (Woese et al., 1990): bacteria, archaea and eukarya, formerly …

Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: Evidence for an activating surface

M Nohaile, D Kern, D Wemmer… - Journal of …, 1997 - scholarworks.brandeis.edu
Structural and functional analyses of activating amino acid substitutions in the receiver domain of
NtrC: Evidence for an activating surface - Brandeis University Logo image Menu Scholarship …

Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: Evidence for an activating surface

M Nohaile, D Kern, D Wemmer, K Stedman… - Journal of Molecular …, 1997 - infona.pl
The bacterial enhancer-binding protein NtrC activates transcription when phosphorylated on
aspartate 54 in its amino (N)-terminal regulatory domain or when altered by constitutively …

Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: Evidence for an activating surface

M Nohaile, D Kern, D Wemmer… - Journal of …, 1997 - scholarworks.brandeis.edu
Structural and functional analyses of activating amino acid substitutions in the receiver domain of
NtrC: Evidence for an activating surface - Brandeis University Logo image Menu Scholarship …

[引用][C] STRUCTURAL AND FUNCTIONAL ANALYSES OF ACTIVATING AMINO ACID SUBSTITUTIONS IN THE RECEIVER DOMAIN OF NTRC: EVIDENCE FOR AN …

M NOHAILE, D KERN, D WEMMER… - Journal of molecular …, 1997 - Elsevier