Concomitant imatinib and ibrutinib in a patient with chronic myelogenous leukemia and chronic lymphocytic leukemia.

The availability of kinase and other small-molecule inhibitors to treat hematologic malignancies is increasing. Accordingly, novel regimens that employ these therapeutics are rapidly evolving. Herein we report the safe and effective administration of two targeted kinase inhibitors in a patient with concomitant chronic myelogenous leukemia and chronic lymphocytic leukemia.

Deep sequencing of mitochondrial genomes reveals increased mutation load in Friedreich's ataxia.

Objective: Friedreich's ataxia (FRDA) is an autosomal recessive trinucleotide repeat expansion disorder caused by epigenetic silencing of the frataxin gene (FXN). Current research suggests that damage and variation of mitochondrial DNA (mtDNA) contribute to the molecular pathogenesis of FRDA. We sought to establish the extent of the mutation burden across the mitochondrial genome in FRDA cells and investigate the molecular mechanisms connecting FXN downregulation and the acquisition of mtDNA damage.

A combined method for the determination of myocardial perfusion in experimental animals using microspheres and CMR.

A convenient method is introduced for myocardial perfusion research by combining multislice short-axis cine cardiovascular magnetic resonance (MSA-CMR) and colored microspheres (CM). In canine control-ischemia-reperfusion (n = 11), Cardiac output (CO) was measured using MSA-CMR (COMSA), Phase Contrast CMR (PC-CMR, COPC) and CM (from reference blood samples, COmicro) in 3 experimental periods per animal. COmicro significantly and systematically overestimated COMSA (median deviation: 291 mL/min, p < 0.

Can Förster resonance energy transfer measurements uniquely position troponin residues on the actin filament? A case study in multiple-acceptor FRET.

Straightforward interpretation of Förster resonance energy transfer (FRET) data in terms of the distance from donor-labeled troponon-tropomyosin (TnTm) to acceptor-labeled actin is complicated by the potential for energy transfer to acceptors on neighboring actin monomers (cross-transfer). Calculations indicate that cross-transfer can account for a substantial percentage of the total transfer efficiency. In some cases, this renders isolated FRET data uninterpretable.