Publications by authors named "F M Boldt"

Objective: To evaluate the prevalence, morphology, and clinical significance of a repeatedly observed yet not examined circumscript osseous defect at the anteroinferior aspect of the femoral head, termed femoral head defect.

Materials And Methods: Retrospective study with approval of the institutional review board. There was informed consent by all individuals.

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Objectives: To evaluate the feasibility of 2D and 3D acetabular coverage assessments based on low-dose biplanar radiographs (BPR) in comparison with CT, and to demonstrate the influence of weight-bearing position (WBP) on anterior and posterior acetabular coverages.

Methods: Fifty patients (21 females, 29 males) underwent standing BPR and supine CT of the pelvis. Using dedicated software, BPR-based calculations of anterior and posterior 2D coverages and anterior, posterior, and global 3D coverages were performed in standardized anterior pelvic plane (APP) and WBP.

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We report a novel synthesis strategy to prepare precision polymers providing exact chain lengths, molecular weights and monomer sequences that allow post modifications by convenient DNA hybridization. Two grafted single strand DNA (ssDNA) side chains serve as a versatile platform for sequence-specific attachment of chromophores, proteins, cell-targeting peptide, and a Y-shape DNA linker. This approach resembles a LEGO®-type incorporation of functionalities to create functional biopolymers of high structure definition under mild conditions.

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CRISPR/Cas9-based approaches have greatly facilitated targeted genomic deletions. Contrary to coding genes however, which can be functionally knocked out by frame-shift mutagenesis, non-coding RNA (ncRNA) gene knockouts have remained challenging. Here we present a universal ncRNA knockout approach guided by epigenetic hallmarks, which enables robust gene silencing even in provisionally annotated gene loci.

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The attachment of two different functionalities in a site-selective fashion represents a great challenge in protein chemistry. We report site specific dual functionalizations of peptides and proteins capitalizing on reactivity differences of cysteines in their free (thiol) and protected, oxidized (disulfide) forms. The dual functionalization of interleukin 2 and EYFP proceeded with no loss of bioactivity in a stepwise fashion applying maleimide and disulfide rebridging allyl-sulfone groups.

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