[This corrects the article DOI: 10.18632/oncotarget.25805.].
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| http://dx.doi.org/10.18632/oncotarget.26685 | DOI Listing |
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Drug screening with human SMN2 reporter identifies SMN protein stabilizers to correct SMA pathology.
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Department of Biomedical Sciences, University of Illinois College of Medicine Rockford, Rockford, IL, USA
Spinal muscular atrophy (SMA), the leading genetic cause of infant mortality, is caused by reduced levels of functional survival motor neuron (SMN) protein. To identify therapeutic agents for SMA, we established a versatile SMN2-GFP reporter line by targeting the human gene. We then screened a compound library and identified Z-FA-FMK as a potent candidate.
View Article and Find Full Text PDFCorrection: CAPN1 is a novel binding partner and regulator of the tumor suppressor NF1 in melanoma.
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Molecular Cell Biology Department, Weizmann Institute of Science, Rehovot, Israel.
[This corrects the article DOI: 10.18632/oncotarget.25805.
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Laboratory of Genomics, Department of Animal Genomics and Molecular Biology, National Research Institute of Animal Production, Balice, Poland.
The study is aimed at identifying selection footprints within the genome of Limousin cattle. With the use of Extended Haplotype Homozygosity test, supplemented with correction for variation in recombination rates across the genome, we created map of selection footprints and detected 173 significant (p < 0.01) core haplotypes being potentially under positive selection.
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Department of Pharmacology, UIC Cancer Center, University of Illinois at Chicago, 909 South Wolcott Avenue, Room 5097, Chicago, IL 60612-3725, USA.
Calpains are ubiquitous calcium-regulated cysteine proteases that have been implicated in cytoskeletal organization, cell proliferation, apoptosis, cell motility, and hemostasis. Gene targeting was used to evaluate the physiological function of mouse calpain-1 and establish that its inactivation results in reduced platelet aggregation and clot retraction potentially by causing dephosphorylation of platelet proteins. Here, we report that calpain-1 null (Capn1-/-) platelets accumulate protein tyrosine phosphatase 1B (PTP1B), which correlates with enhanced tyrosine phosphatase activity and dephosphorylation of multiple substrates.
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Division of Cancer Biology and Genetics, Queen's University Cancer Research Institute, Kingston, Ontario, Canada.
Ubiquitous mu- and m-calpain proteases are implicated in development and apoptosis. They are heterodimers consisting of 80-kDa catalytic subunits encoded by capn1 and capn2, respectively, and a common 28-kDa regulatory subunit encoded by capn4. The regulatory subunit is required to maintain stability and activity of mu- and m-calpains; thus, genetic disruption of capn4 was predicted to eliminate both calpain activities.
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