From Self-Assembly to Drug Delivery: Understanding and Exploring Protein Fibrils.

It is crucial to comprehend protein misfolding and aggregation in the domains of biomedicine, pharmaceuticals, and proteins. Amyloid fibrils are formed when proteins misfold and assemble, resulting in the debilitating illness known as "amyloidosis". This work investigates lysozyme fibrillation with pluronics (F68 and F127).

TB treatment delays and associated risk factors in Dushanbe, Tajikistan, 2019-2021.

Background: In Tajikistan, where there are about 8,000 cases annually, many new cases are being diagnosed with severe disease, indicating a delay in receiving care. We aimed to estimate the proportion with delayed care and the main factors contributing to delayed care.

Methods: Using a retrospective cohort design, we conducted a study that included all people aged over 15 years who were newly diagnosed with pulmonary TB in Dushanbe from 2019 to 2021.

A missense variant effect map for the human tumor-suppressor protein CHK2.

The tumor suppressor CHEK2 encodes the serine/threonine protein kinase CHK2 which, upon DNA damage, is important for pausing the cell cycle, initiating DNA repair, and inducing apoptosis. CHK2 phosphorylation of the tumor suppressor BRCA1 is also important for mitotic spindle assembly and chromosomal stability. Consistent with its cell-cycle checkpoint role, both germline and somatic variants in CHEK2 have been linked to breast and other cancers.

A systematic review of using population-level human mobility data to understand SARS-CoV-2 transmission.

The emergence of SARS-CoV-2 into a highly susceptible global population was primarily driven by human mobility-induced introduction events. Especially in the early stages, understanding mobility was vital to mitigating the pandemic prior to widespread vaccine availability. We conducted a systematic review of studies published from January 1, 2020, to May 9, 2021, that used population-level human mobility data to understand SARS-CoV-2 transmission.

Deciphering the spectroscopic and thermodynamic aspects of binding of biologically important antioxidants with the alkali induced state of human serum albumin.

Protein-ligand interactions are crucial for developing and identifying novel therapeutic targets. In this study, we investigate the interaction of the alkali induced state of human serum albumin (pH 11.2) with three hydroxycinnamic acid derivatives (HCDs), ferulic acid (FA), sinapic acid (SA) and -coumaric acid, which are biologically important antioxidants, and compare the outcomes with the results obtained at physiological pH (7.