INVESTIGADORES
MONTICH guillermo Gabriel
artículos
Título:
A novel lipid binding protein is a factor required for MgATP stimulation of the squid nerve Na+/Ca2+ exchanger.
Autor/es:
BERBERIAN G, BOLLO M, MONTICH GG, ROBERTS G, DEGIORGIS JA, DIPOLO R, AND BEAUGE L.
Revista:
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Editorial:
Elsevier
Referencias:
Año: 2009 vol. 1788 p. 1255 - 1262
ISSN:
0005-2736
Resumen:
Here we identify a cytosolic factor essential for MgATP up-regulation of the squid nerve Na+/Ca2+ exchanger.
Mass spectroscopy and Western blot analysis established that this factor is a member of the lipocalin super
family of lipid binding proteins of 132 amino acids in length. We named it Regulatory protein of the squid
nerve sodium calcium exchanger (ReP1-NCXSQ). ReP-1-NCXSQ was cloned, over expressed and purified. Far-
UV circular dichroism and infrared spectra suggest a majority of â-strand in the secondary structure.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
UV circular dichroism and infrared spectra suggest a majority of â-strand in the secondary structure.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
UV circular dichroism and infrared spectra suggest a majority of â-strand in the secondary structure.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
nerve sodium calcium exchanger (ReP1-NCXSQ). ReP-1-NCXSQ was cloned, over expressed and purified. Far-
UV circular dichroism and infrared spectra suggest a majority of â-strand in the secondary structure.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
UV circular dichroism and infrared spectra suggest a majority of â-strand in the secondary structure.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
UV circular dichroism and infrared spectra suggest a majority of â-strand in the secondary structure.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
Moreover, the predicted tertiary structure indicates ten â-sheets and two short á-helices characteristic of
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even more,
the phosphorylated ReP1-NCXSQ is able to stimulate the exchanger in the absence of ATP. In addition to the
identification of a new member of the lipid binding protein family, this work shows, for the first time, the
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
requirement of a lipid binding protein for metabolic regulation of an ion transporting system.
most lipid binding proteins. Functional experiments showed that in order to be active ReP1-NCXSQ must
become phosphorylated in the presence of MgATP by a kinase that is Staurosporin insensitive. Even m