K. Kurzydlowski

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Interaction sites among phospholamban, sarcolipin, and the sarco(endo)plasmic reticulum Ca(2+)-ATPase.

C. Toyoshima, T. Tsuda, T. Morita, 2008, Biochemical and biophysical research communications.

Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban

Y. Sugita, C. Toyoshima, D. Maclennan, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Phospholamban domain IB forms an interaction site with the loop between transmembrane helices M6 and M7 of sarco(endo)plasmic reticulum Ca2+ ATPases

N. Green, D. Maclennan, M. Asahi, 2001, Proceedings of the National Academy of Sciences of the United States of America.

The nucleotide binding/hinge domain plays a crucial role in determining isoform-specific Ca2+ dependence of organellar Ca(2+)-ATPases.

T. Toyofuku, J. Lytton, D. Maclennan, 1992, The Journal of biological chemistry.

Sarcolipin Regulates the Activity of SERCA1, the Fast-twitch Skeletal Muscle Sarcoplasmic Reticulum Ca2+-ATPase*

A. Odermatt, D. Pette, D. Maclennan, 1998, The Journal of Biological Chemistry.

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 ATP*

D. Maclennan, M. Asahi, M. Tada, 2000, The Journal of Biological Chemistry.

The Vmax of the Ca2+-ATPase of Cardiac Sarcoplasmic Reticulum (SERCA2a) Is Not Altered by Ca2+/Calmodulin-dependent Phosphorylation or by Interaction with Phospholamban*

A. Odermatt, D. Maclennan, K. Kurzydlowski, 1996, The Journal of Biological Chemistry.

Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulum.

T. Toyofuku, D. Maclennan, M. Tada, 1994, The Journal of biological chemistry.

Sarcolipin Inhibits Polymerization of Phospholamban to Induce Superinhibition of Sarco(endo)plasmic Reticulum Ca2+-ATPases (SERCAs)*

D. Maclennan, M. Asahi, M. Tada, 2002, The Journal of Biological Chemistry.

Transmembrane Helix M6 in Sarco(endo)plasmic Reticulum Ca2+-ATPase Forms a Functional Interaction Site with Phospholamban

D. Maclennan, M. Asahi, M. Tada, 1999, The Journal of Biological Chemistry.

Identification of regions in the Ca(2+)-ATPase of sarcoplasmic reticulum that affect functional association with phospholamban.

T. Toyofuku, D. Maclennan, M. Tada, 1993, The Journal of biological chemistry.

Ultrastructural study of calcium shift in ischemic/reperfused rat heart under treatment with dimethylthiourea, diltiazem and amiloride

E. Czarnowska, E. Karwatowska-Prokopczuk, K. Kurzydlowski, 1998, Basic Research in Cardiology.

Phospholamban Regulates the Ca2+-ATPase through Intramembrane Interactions*

D. Maclennan, M. Tada, K. Kurzydlowski, 1996, The Journal of Biological Chemistry.

Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban.

T. Toyofuku, D. Maclennan, M. Tada, 1994, The Journal of biological chemistry.

Phospholamban Inhibitory Function Is Activated by Depolymerization*

D. Maclennan, M. Tada, K. Kurzydlowski, 1997, The Journal of Biological Chemistry.

Phospholamban Domain Ib Mutations Influence Functional Interactions with the Ca2+-ATPase Isoform of Cardiac Sarcoplasmic Reticulum*

D. Maclennan, M. Asahi, M. Tada, 1998, The Journal of Biological Chemistry.

Phospholamban domain I/cytochrome b 5 transmembrane sequence chimeras do not inhibit SERCA2a

D. Maclennan, M. Asahi, M. Tada, 1998, FEBS letters.

Identification of Ser38 as the site in cardiac sarcoplasmic reticulum Ca(2+)-ATPase that is phosphorylated by Ca2+/calmodulin-dependent protein kinase.

T. Toyofuku, D. Maclennan, N Narayanan, 1994, The Journal of biological chemistry.