-David S Waugh Researcher Activity Profile

Research Author Detailed Information 

David S Waugh Publication Rate By Year

David S Waugh has published 11 paper(s) in 2007, 2 paper(s) in 2008, for a total of 13 research publications in total.

David S Ds Waugh Author Information

LAST NAME: waugh

FIRST NAME: David S

INITIALS: ds

AFFILIATION:

Papers

David S Waugh's Publication Record

1. New protein fold revealed by a 1.65 A resolution crystal structure of Francisella tularensis pathogenicity island protein IglC. Year Published: 2007
Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, MD 21702-1201, USA.
2. Mutations that alter the equilibrium between open and closed conformations of Escherichia coli maltose-binding protein impede its ability to enhance the solubility of passenger proteins. Year Published: 2007
Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, P.O. Box B, Frederick, MD 21702-1201, USA.
3. Structure and activity of Yersinia pestis 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase as a novel target for the development of antiplague therapeutics. Year Published: 2007
Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA.
4. The High-Precision Solution Structure of Yersinia Modulating Protein YmoA Provides Insight into Interaction with H-NS. Year Published: 2007
Structural Biophysics Laboratory and Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, Maryland 21702-1201.
5. Mutations that alter the equilibrium between open and closed conformations of Escherichia coli maltose-binding protein impede its ability to enhance the solubility of passenger proteins. Year Published: 2007
Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, P.O. Box B, Frederick, MD 21702-1201, USA.
6. Mutations that alter the equilibrium between open and closed conformations of Escherichia coli maltose-binding protein impede its ability to enhance the solubility of passenger proteins. Year Published: 2007
Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, P.O. Box B, Frederick, MD 21702-1201, USA.
7. New protein fold revealed by a 1.65 A resolution crystal structure of Francisella tularensis pathogenicity island protein IglC. Year Published: 2007
Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, MD 21702-1201, USA.
8. The high-precision solution structure of Yersinia modulating protein YmoA provides insight into interaction with H-NS. Year Published: 2007
Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, Maryland 21702-1201, USA.
9. Structure and activity of Yersinia pestis 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase as a novel target for the development of antiplague therapeutics. Year Published: 2007
Macromolecular Crystallography Laboratory, National Cancer Institute, Frederick, MD 21702, USA.
10. Structural biophysics of the NusB:NusE antitermination complex. Year Published: 2008
Structural Biophysics Laboratory, National Cancer Institute, Frederick, MD 21702, USA.
11. The high-precision solution structure of Yersinia modulating protein YmoA provides insight into interaction with H-NS. Year Published: 2007
Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, Maryland 21702-1201, USA.
12. Structural biophysics of the NusB:NusE antitermination complex. Year Published: 2008
Structural Biophysics Laboratory, National Cancer Institute, Frederick, MD 21702, USA.
13. A generic protocol for the expression and purification of recombinant proteins in Escherichia coli using a combinatorial His6-maltose binding protein fusion tag. Year Published: 2007
Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, P.O. Box B, Frederick, Maryland 21702-1201, USA.