Results 71 to 80 of about 1,451,625 (299)
Surgical Closure of an Aortic Septal Defect [PDF]
Circulation, 1952 Occurring just above the aortic and pulmonic valves, an aortic-pulmonary artery communication gives a left-right shunt which may be indistinguishable by clinical findings from a patent ductus arteriosus. Under some circumstances it is possible to identify the lesion by retrograde aortography.
openaire +2 more sources
Liver organoids: modelling complexity in homeostasis and disease
FEBS Letters, EarlyView.Studying liver in vitro has been challenging because simple 2D cell cultures fail to capture liver's cellular and architectural complexity. To bridge this gap, scientists increasingly use organoids, 3D liver models which better mimic liver composition and function. This review examines recent advances in liver organoid complexity and realism, discusses
Anna M. Dowbaj, Meritxell Huch
wiley +1 more source
Golgi enzymes are retrieved from the plasma membrane to the trans‐Golgi network
FEBS Letters, EarlyView.Golgi enzymes are traditionally considered resident proteins retained within the Golgi apparatus. Here, we demonstrate that a subset transiently reaches the cell surface and is subsequently retrieved to the trans‐Golgi network via retrograde transport. Using a nanobody‐based toolkit, we uncover a dynamic trafficking cycle of several Golgi enzymes.
Dominik P. Buser, Tina Junne
wiley +1 more source
Surgical closure of atrial septal defects
Journal of Thoracic Disease, 2018 Surgical repair of an atrial septal defect (ASD) is a safe and effective operation with little to no morbidity and mortality. In an effort to reduce the trauma of surgery, current approaches focus on less invasive surgical techniques, rather than the intracardiac repair.
Matthew, Liava'a, David, Kalfa
openaire +2 more sources
Emerging experimental and computational methods for studying redox‐regulated structural transitions
FEBS Letters, EarlyView.Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass +2 more
wiley +1 more source
FEBS Letters, EarlyView.Encapsulins are protein nanocompartments that play an important role in iron storage. In the Myxococcus xanthus encapsulin system, two cargo proteins called EncB and EncC contribute to iron mineralization. Here, we show that EncB and EncC generate iron‐containing minerals with distinct chemical compositions, suggesting that the composition of stored ...
Harry B. McDowell +2 more
wiley +1 more source
Transcatheter Closure of Residual Atrial Septal Defects After Surgical Closure
Journal of Interventional Cardiology, 2002 The repair of an ostium secundum atrial septal defects (ASDs) by an open heart operation is a safe procedure associated with low mortality and morbidity. Transcatheter closure of ASDs is a less invasive method of repairing ASDs and may also be the procedure of first choice in residual postsurgical ASD.
Chessa M. +4 more
openaire +2 more sources
Structural and biochemical analysis of a B12 superbinder
FEBS Letters, EarlyView.BtuG proteins are vitamin B12 scavengers in Bacteroides thetaiotaomicron, a dominant human gut bacterium. We present crystal structures of three BtuG homologs bound to cobalamin and its precursor cobinamide, revealing picomolar binding affinities, among the highest known for any natural protein.
Jose M. Martinez Felices +3 more
wiley +1 more source
Transcatheter closure of Ventricular Septal defects in Malta : initial experience [PDF]
, 2005 Ventricular septal defects (VSD) consist of deficiencies of the wall separating the two ventricles. VSDs are the commonest congenital cardiac defects. Small VSDs rarely require intervention, however, larger defects cause ventricular volume overload with ...
Aquilina, Oscar +6 more
core
FEBS Letters, EarlyView.Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav +2 more
wiley +1 more source