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Page 1
Pathway of processive ATP hydrolysis by kinesin.
Gilbert SP, Webb MR, Brune M, Johnson KA. Gilbert SP, et al. Among authors: brune m. Nature. 1995 Feb 23;373(6516):671-6. doi: 10.1038/373671a0. Nature. 1995. PMID: 7854446 Free PMC article.
Phosphate release during microtubule assembly: what stabilizes growing microtubules?
Vandecandelaere A, Brune M, Webb MR, Martin SR, Bayley PM. Vandecandelaere A, et al. Among authors: brune m. Biochemistry. 1999 Jun 22;38(25):8179-88. doi: 10.1021/bi9830765. Biochemistry. 1999. PMID: 10387063
Since this relationship remains controversial, we have re-examined the release of Pi upon microtubule assembly using a fluorometric assay for Pi, based on the phosphate-binding protein of Escherichia coli [Brune M., Hunter, J. L., Corrie, J. E. T., and Webb, M …
Since this relationship remains controversial, we have re-examined the release of Pi upon microtubule assembly using a fluorometric assay fo …
Kinetics of inorganic phosphate release during the interaction of p21ras with the GTPase-activating proteins, p120-GAP and neurofibromin.
Nixon AE, Brune M, Lowe PN, Webb MR. Nixon AE, et al. Among authors: brune m. Biochemistry. 1995 Nov 28;34(47):15592-8. doi: 10.1021/bi00047a026. Biochemistry. 1995. PMID: 7492562
The kinetic mechanism of this activation has been investigated by following the release of inorganic phosphate (Pi), using a fluorescent probe that is sensitive to Pi [Brune, M., Hunter, J., Corrie, J. E. T., & Webb, M. R. (1994) Biochemistry 33, 8262-827 …
The kinetic mechanism of this activation has been investigated by following the release of inorganic phosphate (Pi), using a fluorescent pro …
Time resolved measurements show that phosphate release is the rate limiting step on myofibrillar ATPases.
Lionne C, Brune M, Webb MR, Travers F, Barman T. Lionne C, et al. Among authors: brune m. FEBS Lett. 1995 May 1;364(1):59-62. doi: 10.1016/0014-5793(95)00356-e. FEBS Lett. 1995. PMID: 7750544 Free article.
When myofibrillar ATPase reaction mixtures are quenched in acid, there is a burst of Pi formation, due to AM.ADP.Pi or Pi, as shown in the scheme: AM+ATP<-->A.M.ATP<-->AM.ADP.Pi<-->AM.ADP+Pi<-->AM+ADP. Therefore, in the steady state, either AM.ADP.P …
When myofibrillar ATPase reaction mixtures are quenched in acid, there is a burst of Pi formation, due to AM.ADP.Pi or Pi, as shown in the s …
ATPase and shortening rates in frog fast skeletal myofibrils by time-resolved measurements of protein-bound and free Pi.
Barman T, Brune M, Lionne C, Piroddi N, Poggesi C, Stehle R, Tesi C, Travers F, Webb MR. Barman T, et al. Among authors: brune m. Biophys J. 1998 Jun;74(6):3120-30. doi: 10.1016/S0006-3495(98)78018-X. Biophys J. 1998. PMID: 9635765 Free PMC article.
The myofibrillar kF is higher than the fiber ATPase rates obtained previously in frog fast muscles but considerably lower than obtained in skinned fibers by the phosphate-binding protein method (Z. H. He, R. K. Chillingworth, M. Brune, J. E. T. Corrie, D. R. Trentha …
The myofibrillar kF is higher than the fiber ATPase rates obtained previously in frog fast muscles but considerably lower than obtained in s …
Time-resolved measurements of phosphate release by cycling cross-bridges in portal vein smooth muscle.
He ZH, Ferenczi MA, Brune M, Trentham DR, Webb MR, Somlyo AP, Somlyo AV. He ZH, et al. Among authors: brune m. Biophys J. 1998 Dec;75(6):3031-40. doi: 10.1016/S0006-3495(98)77744-6. Biophys J. 1998. PMID: 9826623 Free PMC article.
The rate of release of inorganic phosphate (Pi) from cycling cross-bridges in rabbit portal-anterior mesenteric vein smooth muscle was determined by following the fluorescence of the Pi-reporter, MDCC-PBP (Brune, M., J. L. Hunter, S. A. Howell, S. R. Martin, T. L. H …
The rate of release of inorganic phosphate (Pi) from cycling cross-bridges in rabbit portal-anterior mesenteric vein smooth muscle was deter …
594 results