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Results: 1-18 |
Results: 18
The molecular puzzle of two-component signaling cascades
Authors: Foussard, M Cabantous, S Pedelacq, JD Guillet, V Tranier, S Mourey, L Birck, C Samama, JP
Citation: M. Foussard et al., The molecular puzzle of two-component signaling cascades, MICROBES IN, 3(5), 2001, pp. 417-424
Further insights into the mechanism of function of the response regulator CheY from crystallographic studies of the CheY-CheA(124-257) complex
Authors: Gouet, P Chinardet, N Welch, M Guillet, V Cabantous, S Birck, C Mourey, L Samama, JP
Citation: P. Gouet et al., Further insights into the mechanism of function of the response regulator CheY from crystallographic studies of the CheY-CheA(124-257) complex, ACT CRYST D, 57, 2001, pp. 44-51
Critical involvement of a carbamylated lysine in catalytic function of class D beta-lactamases
Authors: Golemi, D Maveyraud, L Vakulenko, S Samama, JP Mobashery, S
Citation: D. Golemi et al., Critical involvement of a carbamylated lysine in catalytic function of class D beta-lactamases, P NAS US, 98(25), 2001, pp. 14280-14285
Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis
Authors: Mourey, L Da Re, S Pedelacq, JD Tolstykh, T Faurie, C Guillet, V Stock, JB Samama, JP
Citation: L. Mourey et al., Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis, J BIOL CHEM, 276(33), 2001, pp. 31074-31082
Crystal structure of the F component of the Panton-Valentine leucocidin
Authors: Pedelacq, JD Prevost, G Monteil, H Mourey, L Samama, JP
Citation: Jd. Pedelacq et al., Crystal structure of the F component of the Panton-Valentine leucocidin, INT J MED M, 290(4-5), 2000, pp. 395-401
Insights into class D beta-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa
Authors: Maveyraud, L Golemi, D Kotra, LP Tranier, S Vakulenko, S Mobashery, S Samama, JP
Citation: L. Maveyraud et al., Insights into class D beta-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa, STRUCTURE, 8(12), 2000, pp. 1289-1298
N-sulfonyloxy-beta-lactam inhibitors for beta-lactamases
Authors: Bulychev, A Bellettini, JR O'Brien, M Crocker, PJ Samama, JP Miller, MJ Mobashery, S
Citation: A. Bulychev et al., N-sulfonyloxy-beta-lactam inhibitors for beta-lactamases, TETRAHEDRON, 56(31), 2000, pp. 5719-5728
The high resolution crystal structure for class A beta-lactamase PER-1 reveals the bases for its increase in breadth of activity
Authors: Tranier, S Bouthors, AT Maveyraud, L Guillet, V Sougakoff, W Samama, JP
Citation: S. Tranier et al., The high resolution crystal structure for class A beta-lactamase PER-1 reveals the bases for its increase in breadth of activity, J BIOL CHEM, 275(36), 2000, pp. 28075-28082
6-(hydroxyalkyl)penicillanates as probes for mechanisms of beta-lactamases
Authors: Golemi, D Maveyraud, L Ishiwata, A Tranier, S Miyashita, K Nagase, T Massova, I Mourey, L Samama, JP Mobashery, S
Citation: D. Golemi et al., 6-(hydroxyalkyl)penicillanates as probes for mechanisms of beta-lactamases, J ANTIBIOT, 53(10), 2000, pp. 1022-1027
The first structural and mechanistic insights for class D beta-lactamases:Evidence for a novel catalytic process for turnover of beta-lactam antibiotics
Authors: Golemi, D Maveyraud, L Vakulenko, S Tranier, S Ishiwata, A Kotra, LP Samama, JP Mobashery, S
Citation: D. Golemi et al., The first structural and mechanistic insights for class D beta-lactamases:Evidence for a novel catalytic process for turnover of beta-lactam antibiotics, J AM CHEM S, 122(25), 2000, pp. 6132-6133
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 toxins
Authors: Pedelacq, JD Maveyraud, L Prevost, G Baba-Moussa, L Gonzalez, A Courcelle, E Shepard, W Monteil, H Samama, JP Mourey, L
Citation: Jd. Pedelacq et al., 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 toxins, STRUCT F D, 7(3), 1999, pp. 277-287
Conformational changes induced by phosphorylation of the FixJ receiver domain
Authors: Birck, C Mourey, L Gouet, P Fabry, B Schumacher, J Rousseau, P Kahn, D Samama, JP
Citation: C. Birck et al., Conformational changes induced by phosphorylation of the FixJ receiver domain, STRUCT F D, 7(12), 1999, pp. 1505-1515
Structural transitions in the FixJ receiver domain
Authors: Gouet, P Fabry, B Guillet, V Birck, C Mourey, L Kahn, D Samama, JP
Citation: P. Gouet et al., Structural transitions in the FixJ receiver domain, STRUCT F D, 7(12), 1999, pp. 1517-1526
Two-wavelength MAD phasing: in search of the optimal choice of wavelengths
Authors: Gonzalez, A Pedelacq, JD Sola, M Gomis-Ruth, FX Coll, M Samama, JP Benini, S
Citation: A. Gonzalez et al., Two-wavelength MAD phasing: in search of the optimal choice of wavelengths, ACT CRYST D, 55, 1999, pp. 1449-1458
Inhibition of the broad spectrum nonmetallocarbapenamase of class A (NMC-A) beta-lactamase from Enterobacter cloacae by monocyclic beta-lactams
Authors: Mourey, L Kotra, LP Bellettini, J Bulychev, A O'Brien, M Miller, MJ Mobashery, S Samama, JP
Citation: L. Mourey et al., Inhibition of the broad spectrum nonmetallocarbapenamase of class A (NMC-A) beta-lactamase from Enterobacter cloacae by monocyclic beta-lactams, J BIOL CHEM, 274(36), 1999, pp. 25260-25265
Discoupling the Ca2+-activation from the pore-forming function of the bi-component Panton-Valentine leucocidin in human PMNs
Authors: Moussa, LB Werner, S Colin, DA Mourey, L Pedelacq, JD Samama, JP Sanni, A Monteil, H Prevost, G
Citation: Lb. Moussa et al., Discoupling the Ca2+-activation from the pore-forming function of the bi-component Panton-Valentine leucocidin in human PMNs, FEBS LETTER, 461(3), 1999, pp. 280-286
X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 beta-lactamase: Direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid
Authors: Swaren, P Golemi, D Cabantous, S Bulychev, A Maveyraud, L Mobashery, S Samama, JP
Citation: P. Swaren et al., X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 beta-lactamase: Direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid, BIOCHEM, 38(30), 1999, pp. 9570-9576
Elucidation of mechanism of inhibition and x-ray structure of the TEM-1 beta-lactamase from Escherichia coli inhibited by a N-sulfonyloxy-beta-lactam
Authors: Swaren, P Massova, I Bellettini, JR Bulychev, A Maveyraud, L Kotra, LP Miller, MJ Mobashery, S Samama, JP
Citation: P. Swaren et al., Elucidation of mechanism of inhibition and x-ray structure of the TEM-1 beta-lactamase from Escherichia coli inhibited by a N-sulfonyloxy-beta-lactam, J AM CHEM S, 121(23), 1999, pp. 5353-5359
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