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K Kurzydlowski

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Basic Research in Cardiology|October 23, 1998
Ultrastructural study of calcium shift in ischemic/reperfused rat heart under treatment with dimethylthiourea, diltiazem and amilorideE Czarnowska, E Karwatowska-Prokopczuk, K Kurzydlowski
The Journal of Biological Chemistry|June 14, 1996
The vmax of the Ca2+-ATPase of cardiac sarcoplasmic reticulum (SERCA2a) is not altered by Ca2+/calmodulin-dependent phosphorylation or by interaction with phospholambanA Odermatt, K Kurzydlowski, D H MacLennan
The Journal of Biological Chemistry|January 28, 1994
Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulumT Toyofuku, K Kurzydlowski, M Tada, et al.
The Journal of Biological Chemistry|September 16, 1994
Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholambanT Toyofuku, K Kurzydlowski, M Tada, et al.
The Journal of Biological Chemistry|July 15, 1992
The nucleotide binding/hinge domain plays a crucial role in determining isoform-specific Ca2+ dependence of organellar Ca(2+)-ATPasesT Toyofuku, K Kurzydlowski, J Lytton, et al.
The Journal of Biological Chemistry|June 13, 1997
Phospholamban inhibitory function is activated by depolymerizationY Kimura, K Kurzydlowski, M Tada, et al.
The Journal of Biological Chemistry|September 6, 1996
Phospholamban regulates the Ca2+-ATPase through intramembrane interactionsY Kimura, K Kurzydlowski, M Tada, et al.
The Journal of Biological Chemistry|February 5, 1993
Identification of regions in the Ca(2+)-ATPase of sarcoplasmic reticulum that affect functional association with phospholambanT Toyofuku, K Kurzydlowski, M Tada, et al.
The Journal of Biological Chemistry|June 11, 1998
Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulumY Kimura, M Asahi, K Kurzydlowski, et al.
The Journal of Biological Chemistry|May 16, 2000
Physical interactions between phospholamban and sarco(endo)plasmic reticulum Ca2+-ATPases are dissociated by elevated Ca2+, but not by phospholamban phosphorylation, vanadate, or thapsigargin, and are enhanced by ATPM Asahi, E McKenna, K Kurzydlowski, et al.
Pageof 2

Showing results (1-10 of 14) with videos related to

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Pageof 2
Basic Research in Cardiology|October 23, 1998
Ultrastructural study of calcium shift in ischemic/reperfused rat heart under treatment with dimethylthiourea, diltiazem and amilorideE Czarnowska, E Karwatowska-Prokopczuk, K Kurzydlowski
The Journal of Biological Chemistry|June 14, 1996
The vmax of the Ca2+-ATPase of cardiac sarcoplasmic reticulum (SERCA2a) is not altered by Ca2+/calmodulin-dependent phosphorylation or by interaction with phospholambanA Odermatt, K Kurzydlowski, D H MacLennan
The Journal of Biological Chemistry|January 28, 1994
Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulumT Toyofuku, K Kurzydlowski, M Tada, et al.
The Journal of Biological Chemistry|September 16, 1994
Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholambanT Toyofuku, K Kurzydlowski, M Tada, et al.
The Journal of Biological Chemistry|July 15, 1992
The nucleotide binding/hinge domain plays a crucial role in determining isoform-specific Ca2+ dependence of organellar Ca(2+)-ATPasesT Toyofuku, K Kurzydlowski, J Lytton, et al.
The Journal of Biological Chemistry|June 13, 1997
Phospholamban inhibitory function is activated by depolymerizationY Kimura, K Kurzydlowski, M Tada, et al.
The Journal of Biological Chemistry|September 6, 1996
Phospholamban regulates the Ca2+-ATPase through intramembrane interactionsY Kimura, K Kurzydlowski, M Tada, et al.
The Journal of Biological Chemistry|February 5, 1993
Identification of regions in the Ca(2+)-ATPase of sarcoplasmic reticulum that affect functional association with phospholambanT Toyofuku, K Kurzydlowski, M Tada, et al.
The Journal of Biological Chemistry|June 11, 1998
Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulumY Kimura, M Asahi, K Kurzydlowski, et al.
The Journal of Biological Chemistry|May 16, 2000
Physical interactions between phospholamban and sarco(endo)plasmic reticulum Ca2+-ATPases are dissociated by elevated Ca2+, but not by phospholamban phosphorylation, vanadate, or thapsigargin, and are enhanced by ATPM Asahi, E McKenna, K Kurzydlowski, et al.
Pageof 2