In this task, you're given a paragraph from the research paper and your task is to generate a suitable title for the research paper based on the given paper. Under 100 words is a good title length.

Ex Input:
Redirecting the splicing machinery through the hybridization of high affinity, RNase H-incompetent oligonucleotide analogs such as phosphoramidate morpholino oligonucleotides (PMO) might lead to important clinical applications. Chemical conjugation of PMO to arginine-rich cell penetrating peptides (CPP) such as (R-Ahx-R) 4 (with Ahx standing for 6-aminohexanoic acid) leads to sequencespecific splicing correction in the absence of endosomolytic agents in cell culture at variance with most conventional CPPs. Importantly, (R-Ahx-R) 4 -PMO conjugates are effective in mouse models of various viral infections and Duchenne muscular dystrophy. Unfortunately, active doses in some applications might be close to cytotoxic ones thus presenting challenge for systemic administration of the conjugates in those clinical settings. Structureactivity relationship studies have thus been undertaken to unravel CPP structural features important for the efficient nuclear delivery of the conjugated PMO and limiting steps in their internalization pathway. Affinity for heparin (taken as a model heparan sulfate), hydrophobicity, cellular uptake, intracellular distribution and splicing correction have been monitored. Spacing between the charges, hydrophobicity of the linker between the Arg-groups and Arg-stereochemistry influence splicing correction efficiency. A significant correlation between splicing correction efficiency, affinity for heparin and ability to destabilize model synthetic vesicles has been observed but no correlation with cellular uptake has been found. Efforts will have to focus on endosomal escape since it appears to remain the limiting factor for the delivery of these splice-redirecting ON analogs.

Ex Output:
Delivery of steric block morpholino oligomers by (R-X-R) 4 peptides: structure-activity studies


Ex Input:
Background: The novel corona virus SARS-CoV-2 (COVID-19) can infect healthcare workers. We developed an institutional algorithm to protect operating room team members during the COVID-19 pandemic and rationally conserve personal protective equipment (PPE). Study Design: An interventional platform (operating room, interventional suites, and endoscopy) PPE taskforce was convened by the hospital and medical school leadership and tasked with developing a common algorithm for PPE use, to be used throughout the interventional platform. In conjunction with our infection disease experts, we developed our guidelines based upon potential patterns of spread, risk of exposure and conservation of PPE. A decision tree algorithm describing our institutional guidelines for precautions for operating room team members was created. This algorithm is based on urgency of operation, anticipated viral burden at the surgical site, opportunity for a procedure to aerosolize virus, and likelihood a patient could be infected based on symptoms and testing. Conclusion: Despite COVID-19 being a new threat, we have shown that by developing an easyto-follow decision tree algorithm for the interventional platform teams, we can ensure optimal healthcare worker safety.

Ex Output:
Journal Pre-proof Precautions for Operating Room Team Members during the COVID-19 Pandemic Precautions for Operating Room Team Members during the COVID-19 Pandemic


Ex Input:
In the present study, the human TEB4 is identified as a novel ER (endoplasmic reticulum)-resident ubiquitin ligase. TEB4 has homologues in many species and has a number of remarkable properties. TEB4 contains a conserved RING (really interesting new gene) finger and 13 predicted transmembrane domains. The RING finger of TEB4 and its homologues is situated at the Nterminus and has the unconventional C4HC3 configuration. The N-terminus of TEB4 is located in the cytosol. We show that the isolated TEB4 RING domain catalyses ubiquitin ligation in vitro in a reaction that is ubiquitin Lys 48 -specific and involves UBC7 (ubi-quitin-conjugating enzyme 7). These properties are reminiscent of E3 enzymes, which are involved in ER-associated protein degradation. TEB4 is an ER degradation substrate itself, promoting its own degradation in a RING finger-and proteasome-dependent manner.

Ex Output:

TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum