Recent Advances in Understanding the Function of the PGIP Gene and the Research of Its Proteins for the Disease Resistance of Plants

Polygalacturonase-inhibiting protein (PGIP) is an important plant biochemical anti-disease factor. PGIP has a leucine-rich repeat structure that can selectively bind and inhibit the activity of endo-polygalacturonase (endo-PG) in fungi, playing a key role in plant disease resistance. The regulation of PGIP in plant disease resistance has been well studied, and the effect of PGIP to increase disease resistance is clear. This review summarizes recent advances in understanding the PGIP protein structure, the PGIP mechanism of plant disease resistance, and anti-disease activity by PGIP gene transfer. This overview should contribute to a better understanding of PGIP function and can help guide resistance breeding of PGIP for anti-disease effects.

suPAR, a Circulating Kidney Disease Factor

Urokinase plasminogen activator receptor (uPAR) is a multifaceted, GPI-anchored three-domain protein. Release of the receptor results in variable levels of soluble uPAR (suPAR) in the blood circulation. suPAR levels have been linked to many disease states. In this mini-review, we discuss suPAR as a key circulating molecule mediating kidney disease with a particular focus on differently spliced isoforms.

Genetic analysis of SARS-CoV-2 and the common golden nucleotides to human gene

BackgroundThe coronavirus disease pandemic began in 2019 in Wuhan, China, and continues into 2021, as new mutant viruses appear and require new solutions and treatments. Methods and ResultsIn this study, by genetic analysis of data from 24 SARS-CoV-2 samples from different countries and their alignment with each other and the Wuhan reference virus as well as the human genome, the disease factor is looked at from another angle. The result is the identification of genetic differences in viruses, and the finding of a unique 17-nucleotide sequence between human genes, viruses, and enzymes that can contribute to the onset and progression of the disease. ConclusionsThe role of this sequence in DNA replication and the production of new proteins and its alignment with the EPPK1 gene that may cause disease and its various symptoms are likely.

Alcohol Induced Liver Cirrhosis and its Treatment

The advent of liver diseases globally contributes to a major burden in terms of mortality rate and disease factor. The liver, which is a major complex organ, plays a vital role in the metabolism of the body. The diseases associated with the consumption of alcohol such as cirrhosis and cancer that can be diagnosed through various pathological and cytopathological methods. This review insights how the normally functioning liver cells become vulnerable and lead to the onset of various fatal disorders if left untreated. The alcohol, unlike other drinks, is directly absorbed from the stomach into the bloodstream and is further metabolized by the hepatocytes. The products of alcohol breakdown, such as aldehyde, are toxic to hepatocytes and thus cause liver injury, in cases of chronic alcohol consumption. This injury to the hepatocytes evolves over time and leads to liver cirrhosis. The only cure for severe liver cirrhosis is a transplant of the liver. On the whole, the widespread consumption of alcohol, its making, and effects on the hepatocytes on chronic consumption, which leads to alcoholic liver diseases reviewed.

Moyamoya disease factor RNF213 is a giant E3 ligase with a dynein-like core and a distinct ubiquitin-transfer mechanism

RNF213 is the major susceptibility factor for Moyamoya disease, a progressive cerebrovascular disorder that often leads to brain stroke in adults and children. Characterization of disease-associated mutations has been complicated by the enormous size of RNF213. Here, we present the cryo-EM structure of mouse RNF213. The structure reveals the intricate fold of the 584 kDa protein, comprising an N-terminal stalk, a dynein-like core with six ATPase units, and a multidomain E3 module. Collaboration with UbcH7, a cysteine-reactive E2, points to an unexplored ubiquitin-transfer mechanism that proceeds in a RING-independent manner. Moreover, we show that pathologic MMD mutations cluster in the composite E3 domain, likely interfering with substrate ubiquitination. In conclusion, the structure of RNF213 uncovers a distinct type of an E3 enzyme, highlighting the growing mechanistic diversity in ubiquitination cascades. Our results also provide the molecular framework for investigating the emerging role of RNF213 in lipid metabolism, hypoxia, and angiogenesis.