Publications by authors named "Besold A"

[Metoposcopy].

Ann Chir Plast Esthet

November 2024

From the oracle of Delphi to magnetic resonance imaging, the anatomist's dissecting gaze has always been accompanied by a connective reading, nourishing subjectivity. The face offered to view has thus been the subject since Aristotle (and probably before without any written record of it being kept) of multiple interpretations, becoming a standard throughout the ages. A whole vocabulary emanates from it: metoposcopy, prosopology, physiognomony, phrenology, organology, morphopsychology, amphibology… which punctuated the beyond of the gaze.

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Article Synopsis
  • Rho GTPases, like Rac and Cdc42, help cells grow and shape themselves by affecting their polarity, which is how they organize inside.
  • In some tiny organisms, like fungi, Cdc42 helps produce reactive oxygen species (ROS) in a way that is different from how it happens in bigger organisms.
  • Researchers found that Cdc42 is necessary for the yeast Candida albicans to create ROS during its growth into a filament shape, and this process is controlled in a unique way that doesn't involve large protein complexes present in more complex organisms.
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Copper is an essential metal for virtually all organisms, yet little is known about the extracellular sources of this micronutrient. In serum, the most abundant extracellular Cu-binding molecule is the multi‑copper oxidase ceruloplasmin (Cp). Cp levels increase during infection and inflammation, and pathogens can be exposed to high Cp at sites of infection.

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Calprotectin is a potent antimicrobial that inhibits the growth of pathogens by tightly binding transition metals such as Mn and Zn, thereby preventing their uptake and utilization by invading microbes. At sites of infection, calprotectin is abundantly released from neutrophils, but calprotectin is also present in non-neutrophil cell types that may be relevant to infections. We show here that in patients infected with the Lyme disease pathogen Borreliella (Borrelia) burgdorferi, calprotectin is produced in neutrophil-free regions of the skin, in both epidermal keratinocytes and in immune cells infiltrating the dermis, including CD68 positive macrophages.

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Phosphate is an essential macronutrient required for cell growth and division. Pho84 is the major high-affinity cell-surface phosphate importer of Saccharomyces cerevisiae and a crucial element in the phosphate homeostatic system of this model yeast. We found that loss of Candida albicans Pho84 attenuated virulence in Drosophila and murine oropharyngeal and disseminated models of invasive infection, and conferred hypersensitivity to neutrophil killing.

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Article Synopsis
  • The fungal pathogen acquires essential metals from the host, but the host uses a defense mechanism called nutritional immunity to withhold these micronutrients.
  • The study highlights the role of calprotectin (CP), a protein that sequesters metals like zinc and copper, as a crucial player in this process by preventing the pathogen from accessing these metals.
  • The research shows that CP induces different stress responses for zinc and copper during infection, with the copper response being more prolonged compared to the short-lived zinc response, indicating dynamic metal pools at the host-pathogen interaction.
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Zinc plays key structural and catalytic roles in biology. Structural zinc sites are often referred to as zinc finger (ZF) sites, and the classical ZF contains a Cys2His2 motif that is involved in coordinating Zn(II). An optimized Cys2His2 ZF, named consensus peptide 1 (CP-1), was identified more than 20 years ago using a limited set of sequenced proteins.

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Copper is an essential micronutrient for both pathogens and the animal hosts they infect. However, copper can also be toxic in cells due to its redox properties and ability to disrupt active sites of metalloproteins, such as Fe-S enzymes. Through these toxic properties, copper is an effective antimicrobial agent and an emerging concept in innate immunity is that the animal host intentionally exploits copper toxicity in antimicrobial weaponry.

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Zinc finger (ZF) proteins make up a large family of metalloproteins that contain discrete domains with amino acid ligands (cysteine and histidine) that serve to coordinate zinc in a tetrahedral geometry. Upon zinc coordination, the domains adopt three-dimensional structure. The most well-studied ZFs are the "classical" ZFs, which use a Cys2His2 motif to bind zinc and adopt an antiparallel β sheet/α helical fold.

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The non-classical zinc finger protein, Neural Zinc Finger Factor-1, contains six Cys2His2Cys domains. All three cysteines and the second histidine directly bind Zn(II). Using a combination of mutagenesis, metal coordination and DNA binding studies, we report that the first histidine is involved in a functionally important hydrogen bonding interaction.

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The ferric uptake regulator (Fur) of Helicobacter pylori is a global regulator that is important for colonization and survival within the gastric mucosa. H. pylori Fur is unique in its ability to activate and repress gene expression in both the iron-bound (Fe-Fur) and apo forms (apo-Fur).

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Neural Zinc Finger Factor-1 (NZF-1) and Myelin Transcription Factor 1 (MyT1) are two homologous nonclassical zinc finger (ZF) proteins that are involved in the development of the central nervous system (CNS). Both NZF-1 and MyT1 contain multiple ZF domains, each of which contains an absolutely conserved Cys2His2Cys motif. All three cysteines and the second histidine have been shown to coordinate Zn(II); however, the role of the first histidine remains unresolved.

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Article Synopsis
  • Zinc finger proteins are structural proteins that use zinc to help them fold and function; they usually bind zinc with cysteine and histidine.
  • While classical zinc finger proteins have a well-defined structure (Cys(2)His(2)), there are thirteen less understood families of 'non-classical' zinc finger proteins.
  • This article specifically examines two types of non-classical zinc finger proteins (Cys(3)His and Cys(2)His(2)Cys), highlighting their unique structures and how they interact with different oligonucleotides despite sharing a similar zinc binding method.
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ZIF268, a member of the classical zinc finger protein family, contains three Cys(2)His(2) zinc binding domains that together recognize the DNA sequence 5'-AGCGTGGGCGT-3'. These domains can be fused to an endonuclease to make a chimeric protein to target and cleave specific DNA sequences. A peptide corresponding to these domains, named ZIF268-3D, has been prepared to determine if the zinc finger domain itself can promote DNA cleavage when a redox active metal ion, Fe(II), is coordinated.

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Neural zinc finger factor 1 (NZF-1) is a nonclassical zinc finger protein involved in neuronal development. NZF-1 contains multiple copies of a unique CCHHC zinc-binding domain that recognize a promoter element in the beta-retinoic acid receptor gene termed beta-retinoic acid receptor element (beta-RARE). Previous studies have established that a two-domain fragment of NZF-1 bound with zinc is sufficient for specific DNA binding.

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In Germany, living organ donation of paired and usually not regenerating organs is restricted by law to related individuals, as well as persons who 'obviously entertain an especially intimate personal relationship'. When this law was adopted in 1997, the intention of the legislator was to guarantee the free will of the donor and to exclude any trade of organs. Since then the transplantation of cadaveric organs has not increased.

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