Elevation of truncated (48 kDa) form of unconventional myosin 1C in blood serum correlates with severe Covid-19.

In Covid-19 and autoimmune patients, there are several similarities revealed in the immune responses (Liu et al., 2021; Woodruff et al., 2020).

Covalent Conjugate of Ser-Pro-Cys Tripeptide with PEGylated Comb-Like Polymer as Novel Killer of Human Tumor Cells.

Recently, we detected a previously unknown Ser-Pro-Cys (SPC) tripeptide in the blood serum of multiple sclerosis patients. Its role as a biomarker of the autoimmune disease was suggested, although its origin and real biological activity remained unclear. Here, we created a biocompatible PEGylated comb-like polymer that was used as a platform for covalent immobilization of the SPC, which provided a possibility to explore the biological activity of this tripeptide.

One-year comparative assessment of retention of arch width increases between modified vacuum-formed and Hawley retainers.

Objectives: To compare the clinical effectiveness of Hawley retainers (HRs) and modified vacuum-formed retainers (mVFRs) with palatal coverage in maintaining transverse expansion during a 12-month retention period.

Materials And Methods: Data were collected from postorthodontic treatment patients who met the inclusion criteria. A total of 35 patients were randomly allocated using a centralized randomization technique into either mVFR (n = 18) or HR group (n = 17).

Isolation and identification in human blood serum of the proteins possessing the ability to bind with 48 kDa form of unconventional myosin 1c and their possible diagnostic and prognostic value.

We firstly identified 48 kDa molecular form of the unconventional myosin 1c (p48/Myo1C), and isolated it from blood serum of multiple sclerosis patients. The amount of p48/Myo1C in human blood serum correlated with some autoimmune, hemato-oncological and neurodegenerative diseases and thus may serve as a potential molecular biomarker. The biological functions of this protein in human blood remain unknown.

The Recombinant Fragment of Human κ-Casein Induces Cell Death by Targeting the Proteins of Mitochondrial Import in Breast Cancer Cells.

Breast cancer is still one of the most common cancers for women. Specified therapeutics are indispensable for optimal treatment. In previous studies, it has been shown that RL2, the recombinant fragment of human κ-Casein, induces cell death in breast cancer cells.