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Caregiver Perspectives on the Burden of Disease and Treatment in Uncontrolled Gout
Objective Uncontrolled gout (UG) refers to persistently elevated serum urate (SU) levels >6 mg/dL and ongoing gout symptoms despite use of urate‐lowering therapy (ULT). The objective of this study was to evaluate the burden associated with informal caregiving for individuals with UG.
Angelo Gaffo +6 more
wiley +1 more source
Objective High body mass index (BMI ≥ 27 kg/m2) and aberrant gait biomechanics are primary risk factors for knee osteoarthritis (KOA), yet the specific loading patterns linked to clinical disease features remain unclear. Unsupervised machine learning (ML) was used to identify vertical ground reaction force (vGRF) waveform modes of variation and ...
Ashley N. Buck +10 more
wiley +1 more source
Objective Existing patient‐reported outcome (PRO) measures for systemic sclerosis (SSc) have important limitations, including inadequate coverage of early disease and limited inclusion of diffuse cutaneous (dcSSc) and limited cutaneous (lcSSc) subtypes.
George J. Greene +5 more
wiley +1 more source
BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure
The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain.
Ian G Mills +2 more
exaly +5 more sources
BAR Domain Proteins Regulate Rho GTPase Signaling [PDF]
The Bin-Amphiphysin-Rvs (BAR) domain is a membrane lipid binding domain present in a wide variety of proteins, often proteins with a role in Rho-regulated signaling pathways. BAR domains do not only confer binding to lipid bilayers, they also possess a membrane sculpturing ability and thereby directly control the topology of biomembranes.
Pontus Aspenström
exaly +5 more sources
The BAR‐Domain Family of Proteins: A Case of Bending and Binding? [PDF]
BAR-domains recently took centre stage in science through a report on the crystal structure of this domain in Drosophila Amphiphysin. Though only weakly conserved at the sequence level, the structure of the BAR domain shows striking similarity to the GTPase-binding domain of Arfaptin 2, an effector of Rho- and Arf- GTPases.
Bianca Habermann
exaly +3 more sources
The BAR Domain Superfamily: Membrane-Molding Macromolecules [PDF]
Membrane-shaping proteins of the BAR domain superfamily are determinants of organelle biogenesis, membrane trafficking, cell division, and cell migration. An upsurge of research now reveals new principles of BAR domain-mediated membrane remodeling, enhancing our understanding of membrane curvature-mediated information processing.
Pietro De Camilli +2 more
exaly +3 more sources
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Crystal Structure of the Endophilin-A1 BAR Domain
Journal of Molecular Biology, 2005Endophilin has been implicated in the retrieval of membrane via endocytosis of clathrin-coated vesicles, which is crucial for the maintenance of neurotransmitter exocytosis during stimulation; both exocytosis and endocytosis are regulated by intracellular calcium levels.
Winfried Weissenhorn
exaly +3 more sources
Science, 2004
How do cells make vesicles, a process that requires the bending of membranes? In their Perspective, [Lee and Schekman][1] discuss new findings ([ Peter et al .][2]) that identify a domain called the BAR domain in proteins, such as amphiphysin and endophilin, that induces the curvature of membranes at different points during vesicle formation.
Lee, Marcus C.S., Schekman, Randy
openaire +2 more sources
How do cells make vesicles, a process that requires the bending of membranes? In their Perspective, [Lee and Schekman][1] discuss new findings ([ Peter et al .][2]) that identify a domain called the BAR domain in proteins, such as amphiphysin and endophilin, that induces the curvature of membranes at different points during vesicle formation.
Lee, Marcus C.S., Schekman, Randy
openaire +2 more sources

