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Systematic Discovery of Short Linear Motifs Decodes Calcineurin Phosphatase Signaling
Molecular Cell, 2020 Short linear motifs (SLiMs) drive dynamic protein-protein interactions essential for signaling, but sequence degeneracy and low binding affinities make them difficult to identify.
Jagoree Roy +2 more
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Calcineurin Subunit Interactions: Mapping the Calcineurin B Binding Domain on Calcineurin A
Biochemistry, 1995Recombinant forms of the A and B subunits of the protein phosphatase calcineurin were produced in Escherichia coli, reconstituted into a heterodimer and purified to homogeneity. The reconstituted heterodimer exhibited properties like that of bovine brain calcineurin.
R, Sikkink +5 more
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Advances in Chronic Kidney Disease, 2006
Calcineurin inhibitors, cyclosporine and tacrolimus, have improved allograft survival in solid organ transplantation. Indeed, they have reduced the incidence of acute rejection episodes of cadaveric allograft recipients. Although marked progression has been made in initial survival rates, long-term kidney graft survival has yet to show such encouraging
David, Williams, Lukas, Haragsim
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Calcineurin inhibitors, cyclosporine and tacrolimus, have improved allograft survival in solid organ transplantation. Indeed, they have reduced the incidence of acute rejection episodes of cadaveric allograft recipients. Although marked progression has been made in initial survival rates, long-term kidney graft survival has yet to show such encouraging
David, Williams, Lukas, Haragsim
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Cell Biochemistry and Biophysics, 1999
Calcineurin is a serine-threonine specific Ca(2+)-calmodulin-activated protein phosphatase that is conserved from yeast to humans. Remarkably, this enzyme is the common target for two novel and structurally unrelated immunosuppressive antifungal drugs, cyclosporin A and FK506.
C S, Hemenway, J, Heitman
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Calcineurin is a serine-threonine specific Ca(2+)-calmodulin-activated protein phosphatase that is conserved from yeast to humans. Remarkably, this enzyme is the common target for two novel and structurally unrelated immunosuppressive antifungal drugs, cyclosporin A and FK506.
C S, Hemenway, J, Heitman
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Interactions of Calcineurin A, Calcineurin B, and Ca2+
Biochemistry, 1999Calcineurin B (CN-B) is the Ca(2+)-binding, regulatory subunit of the phosphatase calcineurin. Point mutations to Ca(2+)-binding sites in CN-B were generated to disable individual Ca(2+)-binding sites and evaluate contributions from each site to calcineurin heterodimer formation.
B, Feng, P M, Stemmer
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The Role of Modulatory Calcineurin-Interacting Proteins in Calcineurin Signaling
Trends in Cardiovascular Medicine, 2003Modulatory calcineurin-interacting proteins (MCIPs), also known as the Down syndrome critical region 1 (DSCR1) and DSCR1-like proteins, are a recently described family of small, structurally related proteins that are preferentially expressed in heart, skeletal muscle, and brain.
Beverly A, Rothermel +2 more
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Calcineurin B protects calcineurin A against denaturation by urea
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2004Calcineurin (CN), a heterodimer composed of a catalytic subunit, calcineurin A (CNA) and regulatory subunit, calcineurin B (CNB), is involved in many cellular processes. We investigated the denaturation of CNA by urea in the presence or absence of CNB and found that CNB protected CNA against urea.
Liya, Hu +3 more
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Selective Targeting of Calcineurin Isoforms by Calcineurin Inhibitors
The FASEB Journal, 2020Background Calcineurin Inhibitors (CNIs) have increased one‐year and five‐year post‐transplantation survival rates to ~90% and ~75%, respectively. While CNIs have dramatically improved the quality of patient care, its side effects are also noteworthy: Long‐term CNI therapy is nephrotoxic and is a growing concern
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