Publications by authors named "D Boehringer"

Background: Corneal dystrophies are inherited disorders that can lead to significant visual impairment and often require surgical intervention in advanced stages. Fuchs endothelial corneal dystrophy (FECD) is the most frequently diagnosed type in Western countries and remains a leading global indication for corneal transplantation. In contrast, non-Fuchs dystrophies represent a diverse group of less common entities, each with distinct clinical features, surgical considerations, and regional variations in incidence and management.

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Uropathogenic Escherichia coli strains use filamentous type 1 pili to adhere to and invade uroepithelial cells. The pilus consists of a flexible tip fibrillum, formed by the adhesin FimH and the subunits FimG and FimF. The pilus rod is a helical assembly of up to 3000 copies of the main subunit FimA, terminated by a single copy of the subunit FimI that anchors the rod to the assembly platform FimD in the outer membrane.

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Background: Online appointment scheduling (OAS) increases patient satisfaction and enables more efficient care.

Method: A retrospective study in an ophthalmology practice and an ophthalmology university hospital. Over 20 months, all booked practice-appointments before and after OAS implementation were recorded.

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Background: Ophthalmic pathology at the Eye Center at Medical Center, University of Freiburg, Germany, looks back on a tradition of more than 150 years. Surgical specimens and associated histological diagnoses have been archived since 1945. This study is the first of its size to include 39,256 specimens examined in a single ophthalmic pathology laboratory over 71 years.

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Mycobacteria harbor a proteasome that was acquired by Actinobacteria through horizontal gene transfer and that supports the persistence of the human pathogen Mycobacterium tuberculosis within host macrophages. The core particle of the proteasome (20S CP) associates with ring-shaped activator complexes to degrade protein substrates. One of these is the bacterial proteasome activator Bpa that stimulates the ATP-independent proteasomal degradation of the heat shock repressor HspR.

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