Vivid COVID-19 LAMP is an ultrasensitive, quadruplexed test using LNA-modified primers and a zinc ion and 5-Br-PAPS colorimetric detection system.

Sensitive and rapid point-of-care assays have been crucial in the global response to SARS-CoV-2. Loop-mediated isothermal amplification (LAMP) has emerged as an important diagnostic tool given its simplicity and minimal equipment requirements, although limitations exist regarding sensitivity and the methods used to detect reaction products. We describe the development of Vivid COVID-19 LAMP, which leverages a metallochromic detection system utilizing zinc ions and a zinc sensor, 5-Br-PAPS, to circumvent the limitations of classic detection systems dependent on pH indicators or magnesium chelators.

Independent overexpression of the subunits of translation elongation factor complex eEF1H in human lung cancer.

Background: The constituents of stable multiprotein complexes are known to dissociate from the complex to play independent regulatory roles. The components of translation elongation complex eEF1H (eEF1A, eEF1Bα, eEF1Bβ, eEF1Bγ) were found overexpressed in different cancers. To gain the knowledge about novel cancer-related translational mechanisms we intended to reveal whether eEF1H exists as a single unit or independent subunits in different human cancers.

Akt1 expression and activity at different stages in experimental heart failure.

Loss of function or/and death of cardiomyocytes is one of the major contributing factors in the development of heart failure. Cytosolic Hsp60 can directly interact and regulate activation of some kinases and sequestrate certain proapoptotic molecules to avoid the cardiomyocyte apoptosis. We assumed that Akt1 kinase, a downstream effector of PI3 kinase, can interact with Hsp60.

Hsp90 and its co-chaperone, Sgt1, as autoantigens in dilated cardiomyopathy.

Recently, it has been suggested that some heat shock proteins such as Hsp70 and Hsp60 are involved in autoimmune diseases including cardiospecific ones. In this work we focused on the involvement of another wellknown heat shock protein, Hsp90, and its novel co-chaperone,Sgt1, in dilated cardiomyopathy (DCM). We found that the level of autoantibodies against these two proteins was significantly higher in patients with DCM and ischemic heart disease than in sera of healthy donors.

Molecular chaperone, HSP60, and cytochrome P450 2E1 co-expression in dilated cardiomyopathy.

Physiological stresses (heat, hemodynamics, genetic mutations, oxidative injury and myocardial ischemia) produce pathological states in which protein damage and misfolded protein structures are a common denominator. The specialized proteins family of antistress proteins - molecular chaperons (HSPs) - are responsible for correct protein folding, dissociating protein aggregates and transport of newly synthesized polypeptides to the target organelles for final packaging, degradation or repair. They are inducible at different cell processes such as cell division, apoptosis, signal transduction, cell differentiation and hormonal stimulation.