Publications by authors named "J StrAnskY"

Protein-protein interactions, controlling protein aggregation in the solution phase, are crucial for the formulation of protein therapeutics and the use of proteins in diagnostic applications. Additives in the solution phase are factors that may enhance the protein's conformational stability or induce crystallization. Protein-PEG interactions do not always stabilize the native protein structure.

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Background: Eagle's syndrome (ES) is a term describing a group of symptoms associated with the elongation of the styloid process (SP) of the temporal bone or with ossification of the stylohyoid ligament. Clinically, it manifests through pain in the orofacial and pharyngeal regions, similar to that experienced by patients with temporomandibular joint disease. The presented paper aims to assess the evaluation of the success of surgical treatment and the complications associated with such treatment.

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Although pneumonia presents a relatively common diagnosis, it does not always present with classic clinical symptoms, nor does it follow a regular course without complications. The presented case describes a rare case of aspiration necrotizing pneumonia, which despite intensive therapy, progressed to lung gangrene and required a lung lobectomy. Another peculiarity is that the correct diagnosis was established only after the onset of abdominal pain, surprisingly by a trauma surgeon.

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The resistance of the emerging human pathogen Stenotrophomonas maltophilia to tetracycline antibiotics mainly depends on multidrug efflux pumps and ribosomal protection enzymes. However, the genomes of several strains of this Gram-negative bacterium code for a FAD-dependent monooxygenase (SmTetX) homologous to tetracycline destructases. This protein was recombinantly produced and its structure and function were investigated.

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Article Synopsis
  • The NKR-P1 receptor plays an important role in immune responses and cancer, requiring a detailed understanding of its interactions with the LLT1 ligand.
  • Researchers have mapped the crystal structures of the NKR-P1 and its complex with LLT1, revealing that NKR-P1 forms unexpected homodimers that can bind two LLT1 molecules simultaneously.
  • The study shows that only binding to both interfaces of LLT1 is needed for effective inhibitory signaling, contributing to a model of how these protein interactions facilitate immune synapse formation despite weak ligand-receptor affinities.
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