Numerous students suffer from academic procrastination; it is a common problem and phenomenon in academic settings. Many previous researchers have analyzed its relationships with other factors, such as self-regulation and academic success. This paper aims to provide a full outline of academic procrastination and explore the current hot spots and trends. Bibliometrix and VOSviewer were used to conduct quantitative analysis. The data was collected from the Web of Science core collection database, which contains 1,240 articles from the years 1938 to 2021. The analysis shows that the publication of articles on academic procrastination has been rapidly increasing since 1993. In terms of the most influential countries and institutions, the United states took a prominent lead among all countries, and the most productive institutions in this area were the University of Washington and University of California, Los Angeles. By analyzing the authors, we see that most authors like working with a few collaborators, leading to main groups of authors, such as Murat Balkis and June J. Pilcher. The most frequently cited author was Esther D. Rothblum. Based on the co-citation journals network, Personality and Individual Differences was the prolific and influential journal referring to the number of citations and articles it received. The VOSviewer tool identified the hot spots of academic procrastination, which were mainly distributed as follows: (a) procrastination, (b) academic procrastination, (c) self-regulation, (d) academic performance, and (e) motivation. Therefore, this paper is helpful for scholars and practitioners to know the trend of academic procrastination research comprehensively.
Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common human enzyme defect that affects more than 500 million people worldwide. Individuals affected with G6PD deficiency may occasionally suffer mild-to-severe chronic hemolytic anemia. Chronic non-spherocytic hemolytic anemia (CNSHA) is a potential result of the Class I G6PD variants. This comparative computational study attempted to correct the defect in variants structure by docking the AG1 molecule to selected Class I G6PD variants [G6PDNashville (Arg393His), G6PDAlhambra (Val394Leu), and G6PDDurham (Lys238Arg)] at the dimer interface and structural NADP+ binding site. It was followed by an analysis of the enzyme conformations before and after binding to the AG1 molecule using the molecular dynamics simulation (MDS) approach, while the severity of CNSHA was determined via root-mean-square deviation (RMSD), root-mean-square fluctuation (RMSF), hydrogen bonds, salt bridges, radius of gyration (Rg), solvent accessible surface area analysis (SASA), and principal component analysis (PCA). The results revealed that G6PDNashville (Arg393His) and G6PDDurham (Lys238Arg) had lost the direct contact with structural NADP+ and salt bridges at Glu419 - Arg427 and Glu206 - Lys407 were disrupted in all selected variants. Furthermore, the AG1 molecule re-stabilized the enzyme structure by restoring the missing interactions. Bioinformatics approaches were also used to conduct a detailed structural analysis of the G6PD enzyme at a molecular level to understand the implications of these variants toward enzyme function. Our findings suggest that despite the lack of treatment for G6PDD to date, AG1 remains a novel molecule that promotes activation in a variety of G6PD variants.