Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Method to Extend Research in Time (MERIT) Award (R37)
Project #
4R37GM023152-26
Application #
6589579
Study Section
Special Emphasis Panel (NSS)
Program Officer
Preusch, Peter C
Project Start
1976-05-01
Project End
2006-06-30
Budget Start
2003-07-01
Budget End
2004-06-30
Support Year
26
Fiscal Year
2003
Total Cost
$384,581
Indirect Cost

  Institution

Name
Upstate Medical University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
058889106
City
Syracuse
State
NY
Country
United States
Zip Code
13210

  Publications

Bulygin, Vladimir V; Milgrom, Yakov M (2007) Studies of nucleotide binding to the catalytic sites of Escherichia coli betaY331W-F1-ATPase using fluorescence quenching. Proc Natl Acad Sci U S A 104:4327-31
Milgrom, Yakov M; Cross, Richard L (2005) Rapid hydrolysis of ATP by mitochondrial F1-ATPase correlates with the filling of the second of three catalytic sites. Proc Natl Acad Sci U S A 102:13831-6
Bulygin, Vladimir V; Duncan, Thomas M; Cross, Richard L (2004) Rotor/Stator interactions of the epsilon subunit in Escherichia coli ATP synthase and implications for enzyme regulation. J Biol Chem 279:35616-21
Cross, Richard L; Muller, Volker (2004) The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. FEBS Lett 576:1-4
Hutcheon, M L; Duncan, T M; Ngai, H et al. (2001) Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(O) sector of Escherichia coli ATP synthase. Proc Natl Acad Sci U S A 98:8519-24
Cross, R L (2000) The rotary binding change mechanism of ATP synthases. Biochim Biophys Acta 1458:270-5
Milgrom, Y M; Murataliev, M B; Boyer, P D (1998) Bi-site activation occurs with the native and nucleotide-depleted mitochondrial F1-ATPase. Biochem J 330 ( Pt 2):1037-43
Bulygin, V V; Duncan, T M; Cross, R L (1998) Rotation of the epsilon subunit during catalysis by Escherichia coli FOF1-ATP synthase. J Biol Chem 273:31765-9
Milgrom, Y M; Cross, R L (1997) Nucleotide-depleted beef heart F1-ATPase exhibits strong positive catalytic cooperativity. J Biol Chem 272:32211-4
Zhou, Y; Duncan, T M; Cross, R L (1997) Subunit rotation in Escherichia coli FoF1-ATP synthase during oxidative phosphorylation. Proc Natl Acad Sci U S A 94:10583-7

Showing the most recent 10 out of 37 publications