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Showing results (61-70 of 64) with videos related to

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The Journal of Biological Chemistry|May 3, 1996
Structural basis of extended spectrum TEM beta-lactamases. Crystallographic, kinetic, and mass spectrometric investigations of enzyme mutantsL Maveyraud, I Saves, O Burlet-Schiltz, et al.
FEBS Letters|November 24, 1999
Discoupling the Ca(2+)-activation from the pore-forming function of the bi-component Panton-Valentine leucocidin in human PMNsL Baba Moussa, S Werner, D A Colin, et al.
Structure (London, England : 1993)|June 16, 1999
The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxinsJ D Pédelacq, L Maveyraud, G Prévost, et al.
The Journal of Biological Chemistry|October 3, 1998
X-ray analysis of the NMC-A beta-lactamase at 1.64-A resolution, a class A carbapenemase with broad substrate specificityP Swarén, L Maveyraud, X Raquet, et al.
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Showing results (61-70 of 64) with videos related to

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Pageof 7
You have reached the last page of results.This site can display upto 64 results.
The Journal of Biological Chemistry|May 3, 1996
Structural basis of extended spectrum TEM beta-lactamases. Crystallographic, kinetic, and mass spectrometric investigations of enzyme mutantsL Maveyraud, I Saves, O Burlet-Schiltz, et al.
FEBS Letters|November 24, 1999
Discoupling the Ca(2+)-activation from the pore-forming function of the bi-component Panton-Valentine leucocidin in human PMNsL Baba Moussa, S Werner, D A Colin, et al.
Structure (London, England : 1993)|June 16, 1999
The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxinsJ D Pédelacq, L Maveyraud, G Prévost, et al.
The Journal of Biological Chemistry|October 3, 1998
X-ray analysis of the NMC-A beta-lactamase at 1.64-A resolution, a class A carbapenemase with broad substrate specificityP Swarén, L Maveyraud, X Raquet, et al.
Pageof 7