[High-dose medialis recession in latent nystagmus].

Background: Large muscle recessions reduce anomalous head turn (AHT) in infantile nystagmus syndrome (INS). Their quantitative effect to reduce AHT in fusion maldevelopment nystagmus syndrome (FMNS) is unknown.

Aim Of The Study: To evaluate the reduction of AHT by large medial rectus muscle recession in patients with FMNS.

[Highly dosed Anderson and Kestenbaum operations for anomalous head posture due to nystagmus].

Background: The correction of anomalous head posture associated with infantile nystagmus syndrome (INS) is carried out by the Kestenbaum procedure (KP) combining bilateral horizontal yoke muscle recession with resection of their antagonists or by the Anderson procedure (AP) which is confined to yoke muscle recession alone.

Aim Of The Study: To compare the results of highly dosed AP and KP for anomalous head turn (HT).

Patients And Methods: The AP (2013-2019) and KP (2003-2013) were used as the exclusive procedures during the respective time periods.

High-dose Anderson operation for nystagmus-related anomalous head turn.

Purpose: To evaluate the effectiveness of a high-dose Anderson procedure (AP) to correct infantile nystagmus-related anomalous head turn (HT).

Methods: Twenty-nine consecutive orthotropes with infantile nystagmus with and without associated sensory defect received high-dose AP. HT was measured while the patient tried to read letters at best-corrected visual acuity (BCVA) level at 5 m and 0.

Solution Chemistry of N,N'-Disubstituted Amidines: Identification of Isomers and Evidence for Linear Dimer Formation.

Amidines have found widespread use, but their solution chemistry remains poorly understood. In this work, X-ray crystallographic and detailed 1D and 2D NMR spectroscopic studies have been performed to elucidate the preferred isomers and their interconversion mechanisms. Amidines are shown to exist as a mixture of E-syn and Z-anti isomers in solution and to form dimeric H-bonded aggregates that are also observed in the solid state.

Redox control of iron regulatory protein 2 stability.

Iron regulatory protein 2 (IRP2) is a critical switch for cellular and systemic iron homeostasis. In iron-deficient or hypoxic cells, IRP2 binds to mRNAs containing iron responsive elements (IREs) and regulates their expression. Iron promotes proteasomal degradation of IRP2 via the F-box protein FBXL5.

Iron regulation through the back door: iron-dependent metabolite levels contribute to transcriptional adaptation to iron deprivation in Saccharomyces cerevisiae.

Budding yeast (Saccharomyces cerevisiae) responds to iron deprivation both by Aft1-Aft2-dependent transcriptional activation of genes involved in cellular iron uptake and by Cth1-Cth2-specific degradation of certain mRNAs coding for iron-dependent biosynthetic components. Here, we provide evidence for a novel principle of iron-responsive gene expression. This regulatory mechanism is based on the modulation of transcription through the iron-dependent variation of levels of regulatory metabolites.

Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis.

Biogenesis of iron-sulfur (Fe/S) proteins in eukaryotes is an essential process involving the mitochondrial iron-sulfur cluster (ISC) assembly and export machineries and the cytosolic iron/sulfur protein assembly (CIA) apparatus. To define the integration of Fe/S protein biogenesis into cellular homeostasis, we compared the global transcriptional responses to defects in the three biogenesis systems in Saccharomyces cerevisiae using DNA microarrays. Depletion of a member of the CIA machinery elicited only weak (up to 2-fold) alterations in gene expression with no clear preference for any specific cellular process.

Mechanisms of iron-sulfur protein maturation in mitochondria, cytosol and nucleus of eukaryotes.

Iron-sulfur (Fe/S) clusters are important cofactors of numerous proteins involved in electron transfer, metabolic and regulatory processes. In eukaryotic cells, known Fe/S proteins are located within mitochondria, the nucleus and the cytosol. Over the past years the molecular basis of Fe/S cluster synthesis and incorporation into apoproteins in a living cell has started to become elucidated.

The eukaryotic P loop NTPase Nbp35: an essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery.

Soluble P loop NTPases represent a large protein family and are involved in diverse cellular functions. Here, we functionally characterized the first member of the Mrp/Nbp35 subbranch of this family, the essential Nbp35p of Saccharomyces cerevisiae. The protein resides in the cytosol and nucleus and carries an Fe/S cluster at its N terminus.