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http://dx.doi.org/10.1111/j.1749-6632.1997.tb52302.x | DOI Listing |
Chem Asian J
January 2025
China Three Gorges University, Key Laboratory of Inorganic Nonmetallic Crystalline and Energy Conversion Materials, College of Materials and Chemical Engineering, China Three Gorges University, CHINA.
The Keggin clusters are one kind of the most representative molecular structures in the field of metal-oxo clusters. Although the different types of Keggin clusters with various components were reported, the research about γ-Keggin isomer remains less developed. This is ascribed to the difficulty in obtaining the stable pure γ-Keggin cluster for the structural isomerization.
View Article and Find Full Text PDFSci Rep
December 2024
Department of Neurosurgery, The Second Affiliated Hospital, Zhejiang University School of Medicine, Jiefang Road 88th, Hangzhou, 310009, China.
Chronic ischemia in moyamoya disease (MMD) impaired white matter microstructure and neural functional network. However, the coupling between cerebral blood flow (CBF) and functional connectivity and the association between structural and functional network are largely unknown. 38 MMD patients and 20 sex/age-matched healthy controls (HC) were included for T1-weighted imaging, arterial spin labeling imaging, resting-state functional MRI and diffusion tensor imaging.
View Article and Find Full Text PDFJ Fungi (Basel)
December 2024
State Key Laboratory of Mycology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
, an ectomycorrhizal fungus, forms a symbiotic relationship with , a rare and endangered species crucial to desert riparian ecosystems. In this study, endofungal bacteria (EFBs) within the fruiting bodies of were confirmed by a polyphasic approach, including genomic sequencing, real-time quantitative PCR targeting the 16S rRNA gene, full-length and next-generation sequencing (NGS) of the 16S rRNA gene, and culture methods. The genera , , , and were abundant in the EFBs of fruiting bodies associated with three hosts and were consistently present across different developmental stages.
View Article and Find Full Text PDFComput Struct Biotechnol J
December 2024
Department of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, School of Agriculture, Biomedicine and Environment, La Trobe University, Bundoora, Australia.
In bacteria the formation of disulphide bonds is facilitated by a family of enzymes known as the disulphide bond forming (Dsb) proteins, which, despite low sequence homology, belong to the thioredoxin (TRX) superfamily. Among these enzymes is the disulphide bond-forming protein A (DsbA); a periplasmic thiol oxidase responsible for catalysing the oxidative folding of numerous cell envelope and secreted proteins. Pathogenic bacteria often contain diverse Dsb proteins with distinct functionalities commonly associated with pathogenesis.
View Article and Find Full Text PDFHuan Jing Ke Xue
November 2024
College of Resources and Environment, Shanxi Agricultural University, Taigu 030800, China.
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