Allison WS - Search Results

1

A model for ATP hydrolysis catalysed by F1-ATPases based on kinetic and structural considerations.

Allison WS, Jault JM, Grodsky NB, Dou C. Allison WS, et al. Biochem Soc Trans. 1995 Nov;23(4):752-6. doi: 10.1042/bst0230752. Biochem Soc Trans. 1995. PMID: 8654831 No abstract available.

2

Functional sites in F1-ATPases: location and interactions.

Allison WS, Jault JM, Zhuo S, Paik SR. Allison WS, et al. J Bioenerg Biomembr. 1992 Oct;24(5):469-77. doi: 10.1007/BF00762364. J Bioenerg Biomembr. 1992. PMID: 1429541 Review.

3

Lowered temperature or binding of pyrophosphate to sites for noncatalytic nucleotides modulates the ATPase activity of the beef heart mitochondrial F1-ATPase by decreasing the affinity of a catalytic site for inhibitory MgADP.

Jault JM, Paik SR, Grodsky NB, Allison WS. Jault JM, et al. Among authors: allison ws. Biochemistry. 1994 Dec 20;33(50):14979-85. doi: 10.1021/bi00254a005. Biochemistry. 1994. PMID: 7999754

4

ADP tethered to tyrosine-beta 345 at the catalytic site of the bovine heart F1-ATPase is converted to tethered AMP by Mg(2+)-dependent hydrolysis when the enzyme is photoinactivated with 2-N3-ADP.

Jault JM, Allison WS. Jault JM, et al. Among authors: allison ws. FEBS Lett. 1994 Jun 20;347(1):13-6. doi: 10.1016/0014-5793(94)00497-8. FEBS Lett. 1994. PMID: 8013653 Free article.

5

Probing the specificity of nucleotide binding to the F1-ATPase from thermophilic Bacillus PS3 and its isolated alpha and beta subunits with 2-N3-[beta, gamma-32P]ATP.

Jault JM, Kaibara C, Yoshida M, Garrod S, Allison WS. Jault JM, et al. Among authors: allison ws. Arch Biochem Biophys. 1994 Apr;310(1):282-8. doi: 10.1006/abbi.1994.1168. Arch Biochem Biophys. 1994. PMID: 8161217

6

Hysteretic inhibition of the bovine heart mitochondrial F1-ATPase is due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP.

Jault JM, Allison WS. Jault JM, et al. Among authors: allison ws. J Biol Chem. 1994 Jan 7;269(1):319-25. J Biol Chem. 1994. PMID: 8276813 Free article.

7

Glutamine 170 to tyrosine substitution in yeast mitochondrial F1 beta-subunit increases catalytic site interaction with GDP and IDP and produces negative cooperativity of GTP and ITP hydrolysis.

Jault JM, Divita G, Allison WS, Di Pietro A. Jault JM, et al. Among authors: allison ws. J Biol Chem. 1993 Oct 5;268(28):20762-7. J Biol Chem. 1993. PMID: 8407901 Free article.

8

Slow binding of ATP to noncatalytic nucleotide binding sites which accelerates catalysis is responsible for apparent negative cooperativity exhibited by the bovine mitochondrial F1-ATPase.

Jault JM, Allison WS. Jault JM, et al. Among authors: allison ws. J Biol Chem. 1993 Jan 25;268(3):1558-66. J Biol Chem. 1993. PMID: 8420930 Free article.

9

The alpha 3 beta 3 gamma complex of the F1-ATPase from thermophilic Bacillus PS3 containing the alpha D261N substitution fails to dissociate inhibitory MgADP from a catalytic site when ATP binds to noncatalytic sites.

Jault JM, Matsui T, Jault FM, Kaibara C, Muneyuki E, Yoshida M, Kagawa Y, Allison WS. Jault JM, et al. Among authors: allison ws. Biochemistry. 1995 Dec 19;34(50):16412-8. doi: 10.1021/bi00050a023. Biochemistry. 1995. PMID: 8845368

10

The alpha3beta3gamma subcomplex of the F1-ATPase from the thermophilic bacillus PS3 with the betaT165S substitution does not entrap inhibitory MgADP in a catalytic site during turnover.

Jault JM, Dou C, Grodsky NB, Matsui T, Yoshida M, Allison WS. Jault JM, et al. Among authors: allison ws. J Biol Chem. 1996 Nov 15;271(46):28818-24. doi: 10.1074/jbc.271.46.28818. J Biol Chem. 1996. PMID: 8910526 Free article.

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