Publications by authors named "T Sabo"
Time-resolved small-angle X-ray experiments (TR-SAXS) are reported here that capture and quantify a previously unknown rapid collapse of the unfolded oligonucleotide as an early step in G4 folding of hybrid 1 and hybrid 2 telomeric G-quadruplex structures. The rapid collapse, initiated by a pH jump, is characterized by an exponential decrease in the radius of gyration from 20.6 to 12.
View Article and Find Full Text PDFThe de novo design of miniprotein inhibitors has recently emerged as a new technology to create proteins that bind with high affinity to specific therapeutic targets. Their size, ease of expression, and apparent high stability makes them excellent candidates for a new class of protein drugs. However, beyond circular dichroism melts and hydrogen/deuterium exchange experiments, little is known about their dynamics, especially at the elevated temperatures they seemingly tolerate quite well.
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- Abrin, a toxic protein from the rosary pea plant, is similar to ricin and both disrupt cellular protein synthesis, leading to cell death and severe lung inflammation when inhaled.
- While both toxins have similar disease progression, postexposure treatments show that mice are more effectively protected against abrin than ricin.
- The study found that abrin causes less overall lung damage compared to ricin, particularly in nonhematopoietic cells, allowing for better tissue integrity and improved results from antibody treatment after exposure.
Ricin toxin isolated from the castor bean () is one of the most potent and lethal molecules known. While the pathophysiology and clinical consequences of ricin poisoning by the parenteral route, i.e.
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