Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
7R01GM039928-02
Application #
3297220
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1988-10-01
Project End
1991-06-30
Budget Start
1988-10-01
Budget End
1989-06-30
Support Year
2
Fiscal Year
1988
Total Cost
Indirect Cost

  Institution

Name
Stanford University
Department
Type
Schools of Medicine
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305

  Publications

Xu, Xiaohua; Wang, Shuying; Hu, Yao-Xiong et al. (2007) The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues. J Mol Biol 373:367-81
Bitto, Eduard; McKay, David B (2004) Binding of phage-display-selected peptides to the periplasmic chaperone protein SurA mimics binding of unfolded outer membrane proteins. FEBS Lett 568:94-8
Kwon, Ae-Ran; Trame, Christine B; McKay, David B (2004) Kinetics of protein substrate degradation by HslUV. J Struct Biol 146:141-7
Trame, Christine B; McKay, David B (2003) Structure of the Yersinia enterocolitica molecular-chaperone protein SycE. Acta Crystallogr D Biol Crystallogr 59:389-92
Kwon, Ae-Ran; Kessler, Benedikt M; Overkleeft, Herman S et al. (2003) Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome. J Mol Biol 330:185-95
Bitto, Eduard; McKay, David B (2003) The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins. J Biol Chem 278:49316-22
Bitto, Eduard; McKay, David B (2002) Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Structure 10:1489-98
Sousa, Marcelo C; Kessler, Benedikt M; Overkleeft, Herman S et al. (2002) Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: corroboration of a proposed mechanism of allosteric activation of HslV by HslU. J Mol Biol 318:779-85
Wedekind, J E; Trame, C B; Dorywalska, M et al. (2001) Refined crystallographic structure of Pseudomonas aeruginosa exotoxin A and its implications for the molecular mechanism of toxicity. J Mol Biol 314:823-37
Sousa, M C; McKay, D B (2001) Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site. Acta Crystallogr D Biol Crystallogr 57:1950-4

Showing the most recent 10 out of 34 publications