There are 10 known mammalian septin genes, some of which produce multiple splice variants. The current nomenclature for the genes and gene products is very confusing, with several different names having been given to the same gene product and distinct names given to splice variants of the same gene. Moreover, some names are based on those of yeast or Drosophila septins that are not the closest homologues. Therefore, we suggest that the mammalian septin field adopt a common nomenclature system, based on that adopted by the Mouse Genomic Nomenclature Committee and accepted by the Human Genome Organization Gene Nomenclature Committee. The human and mouse septin genes will be named SEPT1–SEPT10 and Sept1–Sept10, respectively. Splice variants will be designated by an underscore followed by a lowercase “v” and a number, e.g., SEPT4_v1

The septins are a conserved family of guanosine-5'-triphosphate (GTP)-binding proteins. In mammals they are involved in a variety of cellular processes, such as cytokinesis, exocytosis, and vesicle trafficking. Specifically, SEPT4 has also been shown to be expressed in both human colorectal cancer and malignant melanoma, as well as being involved in neurodegenerative disorders. However, many of the details of the modes of action of septins in general remain unclear, and little is known of their detailed molecular architecture. Here, we define explicitly and characterize the domains of human SEPT4. Regions corresponding to the N-terminal, GTPase, and C-terminal domains as well as the latter two together were successfully expressed in Escherichia coli in soluble form and purified by affinity and size-exclusion chromatographies. The purified domains were analyzed by circular dichroism spectroscopy, fluorescence spectroscopy, dynamic light scattering, and small-angle X-ray scattering, as well as with bioinformatics tools. Of the three major domains that comprise SEPT4, the N-terminal domain contains little regular secondary structure and may be intrinsically unstructured. The central GTPase domain is a mixed alpha/beta structure, probably based on an open beta sheet. As defined here, it is catalytically active and forms stable homodimers in vitro. The C-terminal domain also forms homodimers and can be divided into two regions, the second of which is alpha-helical and consistent with a coiled-coil structure. These studies should provide a useful basis for future biophysical studies of SEPT4, including the structural basis for their involvement in diseases such as cancer and neurodegenerative disorders.

Huaier (Trametes robiniophila murr) Cancer therapyTotal RNA-and small RNA-sequencing RNA editing events Transcriptional controlRecent advances in cancer therapy integrate most advanced devices and inventions among broad areas of science [1][2][3] . Although a rapid progress in the methodology 4-8 , many tasks remain unsolved for successful control of cancer, and for diseases originated from multiple factors and environmental stresses throughout a life-long time 9 . Recent advancement in technology enabled to cultivate those useful natural herb species in quantity 10-14 , and quality-controlled distribution in the conventional granule forms. In 1970's, Huaier (Tremetes robiniophila Murr) has been recognized widely as anticancer drug in China 12-14 (Chinese administration license No. Z-20000109).Huaier has been introduced with its significant anti-cancer effects without any side effects and/or toxicity [13][14][15][16][17][18][19][20][21][22][23] . The effective ingredient of Huaier was proteoglycan, which consists of 41.53% polysaccharides, 12.93% amino acids and 8.72% water 13,14 . The proteoglycan is the most effective anticancer element among all of the isolated ingredients of Huaier extract, which was confirmed on breast cancer MCF-7 15 , liver cancer H22 16, 17 , MHCC97-H 18 , lung cancer 19 , ovarian cancer 20 , colorectal cancer 21 , and human fibrosarcoma HT1080 cells 22 . More importantly, Huaier has no toxicity or side provided a simple and successful evidence that the rescue of Hippo signalling pathway was a molecular basis of anti-cancer effects of Huaier 4, 5 . However, it was not enough, either, to explain all functions associated to anti-cancer effects, such as 1) immunological alterations both to enhance and also inhibit the excessive reaction, 2) normal tissue reproduction after the specific cell death and elimination of cell debris in cancer lesion, and 3) reduction of (oxidative) stress materials in liver, and 4) recovery from the opportunistic infections during cancer therapy, and etc. Therefore, we initiated clinical research to identify Huaier effects on every biophysiological system and influences each other. The samples used in this approach should be free from the effects of chemotherapeutic agents, especially molecular-targeting anti-cancer drugs, which disrupted largely molecular mechanisms. The present study was thus constructed with a collaboration of cancer patients, not a large in number, but wished to have Huaier treatment.The medical characteristics of the 31 volunteer patients were summarized in Table 1. The mean age is 67 years old, since this research excluded the congenital cancer or tumour. The present study summarizes the results from 92 sample sequencing from 31 patients, including 2 normal controls (patient No. 21 and 26), and 4 with benign tumours (No. 13,14,18,and 20). Normal control No. 21 was the same as No. 25, the opportunistic infection case after 8 months of the end of first research period as No. 21. In order to compare the results with the other volunteer patients...

The findings indicate the potential use of microemulsions for the skin delivery of quercetin, where it exerts antioxidative effects.

We have isolated the gene encoding the largest subunit of RNA polymerase II from Plasmodium falciparum. The RPII gene is expressed in the asexual erythrocytic stages of the parasite as a 9 kb mRNA, and is present as a single copy gene located on chromosome 3. The P. falciparum RPII subunit is the largest (2452 amino acids) eukaryotic RPII subunit, and it contains enlarged variable regions that clearly separate and define five conserved regions of the eukaryotic RPII largest subunits. A distinctive carboxyl-terminal domain contains a short highly conserved heptapeptide repeat domain which is bounded on its 5' side by a highly diverged heptapeptide repeat domain, and is bounded on its 3' side by a long carboxyl-terminal extension.