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M Le Maire

Showing results (71-80 of 85) with videos related to

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European Journal of Biochemistry|November 3, 1998
Spectroscopic studies of the interaction of Ca2+-ATPase-peptides with dodecyl maltoside and its brominated analogS Soulié, B de Foresta, J V Møller, et al.
Comptes Rendus De L'Academie Des Sciences. Serie III, Sciences De La Vie|January 1, 1987
[A variety of human autoantibodies recognizes in HeLa cells 2 proteins related to the TFIIIA factor of Xenopus laevis which regularizes the transcription of ribosomal 5S RNA]S Lagaye, J P Barque, V Della Valle, et al.
Biochimie|October 23, 1998
FhuA, an Escherichia coli outer membrane protein with a dual function of transporter and channel which mediates the transport of phage DNAM Bonhivers, L Plançon, A Ghazi, et al.
The Journal of Biological Chemistry|August 1, 1998
The cytoplasmic loop located between transmembrane segments 6 and 7 controls activation by Ca2+ of sarcoplasmic reticulum Ca2+-ATPaseT Menguy, F Corre, L Bouneau, et al.
Annals of the New York Academy of Sciences|May 24, 2003
Involvement of the cytoplasmic loop L6-7 in the entry mechanism for transport of Ca2+ through the sarcoplasmic reticulum Ca2+-ATPaseF Corre, C Jaxel, J Fuentes, et al.
Biochemistry|March 21, 1989
Membrane solubilization by detergent: use of brominated phospholipids to evaluate the detergent-induced changes in Ca2+-ATPase/lipid interactionB de Foresta, M le Maire, S Orlowski, et al.
The Journal of Biological Chemistry|May 16, 2000
The transmembrane domains of hepatitis C virus envelope glycoproteins E1 and E2 play a major role in heterodimerizationA Op De Beeck, R Montserret, S Duvet, et al.
The Journal of Biological Chemistry|August 25, 1995
Do transmembrane segments in proteolyzed sarcoplasmic reticulum Ca(2+)-ATPase retain their functional Ca2+ binding properties after removal of cytoplasmic fragments by proteinase K?B Juul, H Turc, M L Durand, et al.
FEBS Letters|August 4, 1997
mRNP3 and mRNP4 are phosphorylatable by casein kinase II in Xenopus oocytes, but phosphorylation does not modify RNA-binding affinityS Deschamps, H Jacquemin-Sablon, G Triqueneaux, et al.
The Journal of Biological Chemistry|July 11, 1997
The cytoplasmic loop between putative transmembrane segments 6 and 7 in sarcoplasmic reticulum Ca2+-ATPase binds Ca2+ and is functionally importantP Falson, T Menguy, F Corre, et al.
Pageof 9

Showing results (71-80 of 85) with videos related to

Sort By:
Pageof 9
European Journal of Biochemistry|November 3, 1998
Spectroscopic studies of the interaction of Ca2+-ATPase-peptides with dodecyl maltoside and its brominated analogS Soulié, B de Foresta, J V Møller, et al.
Comptes Rendus De L'Academie Des Sciences. Serie III, Sciences De La Vie|January 1, 1987
[A variety of human autoantibodies recognizes in HeLa cells 2 proteins related to the TFIIIA factor of Xenopus laevis which regularizes the transcription of ribosomal 5S RNA]S Lagaye, J P Barque, V Della Valle, et al.
Biochimie|October 23, 1998
FhuA, an Escherichia coli outer membrane protein with a dual function of transporter and channel which mediates the transport of phage DNAM Bonhivers, L Plançon, A Ghazi, et al.
The Journal of Biological Chemistry|August 1, 1998
The cytoplasmic loop located between transmembrane segments 6 and 7 controls activation by Ca2+ of sarcoplasmic reticulum Ca2+-ATPaseT Menguy, F Corre, L Bouneau, et al.
Annals of the New York Academy of Sciences|May 24, 2003
Involvement of the cytoplasmic loop L6-7 in the entry mechanism for transport of Ca2+ through the sarcoplasmic reticulum Ca2+-ATPaseF Corre, C Jaxel, J Fuentes, et al.
Biochemistry|March 21, 1989
Membrane solubilization by detergent: use of brominated phospholipids to evaluate the detergent-induced changes in Ca2+-ATPase/lipid interactionB de Foresta, M le Maire, S Orlowski, et al.
The Journal of Biological Chemistry|May 16, 2000
The transmembrane domains of hepatitis C virus envelope glycoproteins E1 and E2 play a major role in heterodimerizationA Op De Beeck, R Montserret, S Duvet, et al.
The Journal of Biological Chemistry|August 25, 1995
Do transmembrane segments in proteolyzed sarcoplasmic reticulum Ca(2+)-ATPase retain their functional Ca2+ binding properties after removal of cytoplasmic fragments by proteinase K?B Juul, H Turc, M L Durand, et al.
FEBS Letters|August 4, 1997
mRNP3 and mRNP4 are phosphorylatable by casein kinase II in Xenopus oocytes, but phosphorylation does not modify RNA-binding affinityS Deschamps, H Jacquemin-Sablon, G Triqueneaux, et al.
The Journal of Biological Chemistry|July 11, 1997
The cytoplasmic loop between putative transmembrane segments 6 and 7 in sarcoplasmic reticulum Ca2+-ATPase binds Ca2+ and is functionally importantP Falson, T Menguy, F Corre, et al.
Pageof 9