Zobrazeno 1 - 10
of 55
pro vyhledávání: '"Tom Barman"'
Publikováno v:
Journal of Muscle Research and Cell Motility
Journal of Muscle Research and Cell Motility, Springer Verlag, 2017, 38 (2), pp.137-142. ⟨10.1007/s10974-017-9480-x⟩
Journal of Muscle Research and Cell Motility, 2017, 38 (2), pp.137-142. ⟨10.1007/s10974-017-9480-x⟩
Journal of Muscle Research and Cell Motility, Springer Verlag, 2017, 38 (2), pp.137-142. ⟨10.1007/s10974-017-9480-x⟩
Journal of Muscle Research and Cell Motility, 2017, 38 (2), pp.137-142. ⟨10.1007/s10974-017-9480-x⟩
International audience
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::300458aed39731dca1542963b59b76ea
https://hal.archives-ouvertes.fr/hal-02322680
https://hal.archives-ouvertes.fr/hal-02322680
Autor:
Engin H. Serpersu, Tom Barman, Nadia Leban, Corinne Lionne, Perrine Lallemand, Simone Kunzelmann, Martin R. Webb, Laurent Chaloin
Publikováno v:
Febs Letters
Highlights ► APH(3′)-IIIa is a bacterial kinase responsible for antibiotics resistance. ► Release of ADP is the rate limiting step of Kanamycin A phosphorylation. ► An ADP-enzyme complex is the main steady state intermediate. ► A strategy t
Autor:
Tom Barman, Perrine Lallemand, Nancy Adamek, Christian Valentin, Andrea Varga, Laurent Chaloin, Mária Vas, Judit Szabó, Corinne Lionne
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2009, 48 (29), pp.6998-7008. ⟨10.1021/bi900396h⟩
Biochemistry, American Chemical Society, 2009, 48 (29), pp.6998-7008. ⟨10.1021/bi900396h⟩
International audience; 3-Phosphoglycerate kinase (PGK) is a promising candidate for the activation of nucleotide analogues used in antiviral and anticancer therapies. PGK is a key enzyme in glycolysis; it catalyzes the reversible reaction 1,3-bispho
Publikováno v:
Protein Science. 11:117-128
Bovine pancreatic ribonuclease (RNase A, EC 3.1.27.5) has been studied extensively (e.g., see D'Alessio and Riordan 1997; Raines 1998). However, fine kinetic analysis of its specificity has always been hampered by the enormous complexity of its subst
Autor:
Beáta Flachner, Tom Barman, Christian Périgaud, Andrea Varga, Béatrice Roy, Judit Szabó, Corinne Lionne, Peter V. Konarev, Mária Vas, Péter Závodszky, Dmitri I. Svergun
Publikováno v:
Biochemical and Biophysical Research Communications
Biochemical and Biophysical Research Communications, Elsevier, 2008, 366 (4), pp.994-1000. ⟨10.1016/j.bbrc.2007.12.061⟩
Biochemical and Biophysical Research Communications, Elsevier, 2008, 366 (4), pp.994-1000. ⟨10.1016/j.bbrc.2007.12.061⟩
International audience; l-Nucleoside-analogues, mirror images of the natural d-nucleosides, are a new class of antiviral and anticancer agents. In the cell they have to be phosphorylated to pharmacologically active triphosphate forms, the last step s
At Physiological Temperatures the ATPase Rates of Shortening Soleus and Psoas Myofibrils Are Similar
Publikováno v:
Biophysical Journal. 85(5):3132-3141
We obtained the temperature dependences of the adenosine triphosphatase (ATPase) activities (calcium-activated and relaxed) of myofibrils from a slow muscle, which we compared with those from a fast muscle. We chose rabbit soleus and psoas because th
Autor:
Tom Barman, Franck Travers, Alexandra Belus, Bogdan I. Iorga, Corinne Lionne, Nicoletta Piroddi, Robin Candau, Martin R. Webb
Publikováno v:
Biochemistry. 41:13297-13308
It has been suggested that the mechanical condition determines the rate-limiting step of the ATPase of the myosin heads in fibers: when fibers are isometrically contracting, the ADP release kinetics are rate-limiting, but as the strain is reduced and
Publikováno v:
Biophysical Journal. 78(6):3093-3102
The kinetics of formation of the actin-myosin complex have 11/7/2008been reinvestigated on the minute and second time scales in sedimentation and chemical cross-linking experiments. With the sedimentation method, we found that the binding of the skel
Autor:
Robert Stehle, Corrado Poggesi, Martin Brune, Nicoletta Piroddi, Franck Travers, Corinne Lionne, Tom Barman, Martin R. Webb, Chiara Tesi
Publikováno v:
Biophysical Journal. 74:3120-3130
Shortening and ATPase rates were measured in Ca2+-activated myofibrils from frog fast muscles in unloaded conditions at 4 degrees C. ATPase rates were determined using the phosphate-binding protein method (free phosphate) and quench flow (total phosp
Publikováno v:
Journal of Muscle Research and Cell Motility. 19:381-392
We have exploited solvent perturbation to probe the coupling of Ca2+ and rigor activation of the ATPase of myofibrils from rabbit psoas. Three techniques were used: overall myofibrillar ATPases by the rapid-flow quench method; kinetics of the interac