Histochemical activity of nucleases was investigated in sensitive and resistant rat tumors at several periods after a single dose of cyclophosphamide and was compared with that in a control group of untreated tumors. Intense increase of nuclease activity(mainly that of acid DNAse) appeared only in the cells of the sensitive tumors at 12 hours, reaching its maximum three days after drug administration. Untreated malignant tumors usually have variable amounts of spontaneous necrosis with high nuclease activity. Not the absolute values of high nuclease activity but only the increase of such activity from the basal level of untreated tumors to that measured at frequent periods after trial treatment may be suggested as an early marker of therapeutically induced tumor cell necrosis. However, more investigation is needed before such a marker might be applied as a test for tumor sensitivity to therapeutic agents.
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http://dx.doi.org/10.1002/1097-0142(19810201)47:3<523::aid-cncr2820470316>3.0.co;2-r | DOI Listing |
Anal Chim Acta
January 2025
Department of Chemistry and Biochemistry, Utah State University, 0300 Old Main Hill, Logan, UT, 84322, USA; Department of Chemistry, University of Louisiana at Lafayette, 300 East St. Mary Blvd, Lafayette, LA, 70504, USA. Electronic address:
A rapid and accurate biosensor for detecting disease biomarkers at point-of-care is essential for early disease diagnosis and preventing pandemics. CRISPR-Cas12a is a promising recognition element for DNA biosensors due to its programmability, specificity, and deoxyribonuclease activity initiated in the presence of a biomarker. The current electrochemical CRISPR-Cas12a-based biosensors utilize the single-stranded DNA (ssDNA) self-assembled on an electrode surface and covalently modified with the redox indicator, usually methylene blue (MB).
View Article and Find Full Text PDFCell Host Microbe
January 2025
Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Copenhagen, Denmark. Electronic address:
Type III CRISPR-Cas executes a multifaceted anti-phage response, activating effectors such as a nuclease or membrane depolarizer. In a recent Cell paper, Baca and Majumder et al. report an accessory effector, Cad1, which deaminates ATP into ITP, causing ITP accumulation and host growth arrest, thereby inhibiting phage propagation.
View Article and Find Full Text PDFNucleic Acids Res
January 2025
CSSB Centre for Structural Systems Biology, Deutsches Elektronen-Synchrotron DESY, Notkestr. 85, 22607 Hamburg, Germany.
Dinucleases of the DEDD superfamily, such as oligoribonuclease, Rexo2 and nanoRNase C, catalyze the essential final step of RNA degradation, the conversion of di- to mononucleotides. The active sites of these enzymes are optimized for substrates that are two nucleotides long, and do not discriminate between RNA and DNA. Here, we identified a novel DEDD subfamily, members of which function as dedicated deoxydinucleases (diDNases) that specifically hydrolyze single-stranded DNA dinucleotides in a sequence-independent manner.
View Article and Find Full Text PDFNucleic Acids Res
January 2025
School of Chemical Sciences, Dublin City University, Glasnevin, Dublin 9, Ireland.
Copper compounds with artificial metallo-nuclease (AMN) activity are mechanistically unique compared to established metallodrugs. Here, we describe the development of a new dinuclear copper AMN, Cu2-BPL-C6 (BPL-C6 = bis-1,10-phenanthroline-carbon-6), prepared using click chemistry that demonstrates site-specific DNA recognition with low micromolar cleavage activity. The BPL-C6 ligand was designed to force two redox-active copper centres-central for enhancing AMN activity-to bind DNA, via two phenanthroline ligands separated by an aliphatic linker.
View Article and Find Full Text PDFNat Commun
January 2025
Interdisciplinary Life Sciences Graduate Programs, University of Texas at Austin, Austin, TX, 78712, USA.
Type II CRISPR endonucleases are widely used programmable genome editing tools. Recently, CRISPR-Cas systems with highly compact nucleases have been discovered, including Cas9d (a type II-D nuclease). Here, we report the cryo-EM structures of a Cas9d nuclease (747 amino acids in length) in multiple functional states, revealing a stepwise process of DNA targeting involving a conformational switch in a REC2 domain insertion.
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