How to unfold a folded large-bore sheath after Impella-supported percutaneous coronary intervention.

Postepy Kardiol Interwencyjnej

Department of Interventional Cardiology, Institute of Cardiology, Jagiellonian University Medical College, John Paul II Hospital, Krakow, Poland.

Published: March 2025


Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11963049PMC
http://dx.doi.org/10.5114/aic.2025.148007DOI Listing

Publication Analysis

Top Keywords

unfold folded
4
folded large-bore
4
large-bore sheath
4
sheath impella-supported
4
impella-supported percutaneous
4
percutaneous coronary
4
coronary intervention
4
unfold
1
large-bore
1
sheath
1

Similar Publications

In live specimens of the nemertodermatidan Flagellophora apelti Faubel and Dörjes, 1978, a peculiar organ looking like a fascicle of bristles-and so called a broom organ by its discoverer-occupies the front third or so of the body. The animal can extrude the organ to splay the bristles in a fan-like array, each bristle having an adhesive tip. Described first by light histology as a bundle of flagella, this organ can be seen by transmission electron microscopy to be actually a bundle of exceedingly long necks of glands.

View Article and Find Full Text PDF

Potent and selective binders of the key proapoptotic proteins BAK and BAX have not been described. We use computational protein design to generate high affinity binders of BAK and BAX with greater than 100-fold specificity for their target. Both binders activate their targets when at low concentration, driving pore formation, but inhibit membrane permeabilization when in excess.

View Article and Find Full Text PDF

Membrane Interactions Drive Hydrogen-Bond Dynamics in the pH-Low Insertion Peptide (pHLIP).

J Phys Chem Lett

September 2025

Department of Chemistry, University of Texas at Austin, 105 E 24th St. A5300, Austin, Texas 78712, United States.

The pH Low Insertion Peptide (pHLIP), a cell-penetrating peptide, presents an ideal model to study peptide-membrane interactions across a range of conformational states. The folded, solvent-exposed unfolded, and membrane-inserted states of pHLIP have been well-characterized, but the intermediate structures remain poorly understood. Studies have focused on understanding folding and membrane interactions; however, there is a relation between the environment, membrane interactions, and local picosecond dynamics that has not been characterized.

View Article and Find Full Text PDF

The efficiency of enzymatic proteolysis is often attributed to the properties of the enzyme itself, with the substrate typically viewed as a passive participant. In this study, we demonstrate that the conformational state of the substrate critically influences proteolytic efficiency. Using human serum albumin (HSA) as a model substrate, papain as the enzyme, and urea as a controlled denaturing agent, we systematically investigated how substrate conformation might affect proteolysis.

View Article and Find Full Text PDF

Magnesium ions (Mg) play a crucial role in stabilizing various RNA tertiary motifs, such as pseudoknots, G-quadruplexes, kissing loops, and A-minor motifs, to name a few. Despite their importance, the precise location and role of Mg ions in RNA folding are challenging to characterize both experimentally and computationally. In this study, we employ an all-atom structure-based model integrated with the dynamic counterion condensation (DCC) model to investigate the folding and unfolding transitions of apo SAM-II riboswitch RNA at physiological concentrations of Mg.

View Article and Find Full Text PDF