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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Ligand-receptor binding revealed by the TNF family member TALL-1

Article Abstract:

The tumour necrosis factor (TNF) ligand TALL-1 and its cognate receptors, BCMA, TACI and BAFF-R were identified as members of the tumour necrosis factor superfamily, which are essential factors contributing to B-cell maturation. It was revealed that one disulphide bridge in BAFF-R is critical for determining the binding specificity of the extracellular domain eBAFF-R to TALL-1 instead of APRIL, a closely related ligand of TALL-1, which was confirmed by binding experiments in vitro.

Author: Murphy, Robert C., Kappler, John, Zhang, Rongguang, Liu, Yingfang, Hong, Xia, Martin, Wesley E., Xu, Liangguo, Jiang, Ling, Pan, C.heol-Ho, Shu, Hong-Bing, Dai, Shaodong, Zhang, Gonyi
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2003
Ligand binding (Biochemistry), Tumor necrosis factor, Tumour necrosis factor

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Structure of the replicative helicase of the oncoprotein SV40 large tumor antigen

Article Abstract:

Research describes the X-ray structure of the hexameric large tumor antigen oncoprotein exhibiting DNA helicase activity. The hexamer protein binds both single- and double-stranded DNA. It is organized into two tiers which can rotate and produce an 'iris' effect and distort or melt, at the replication fork, the origin and unwinding DNA.

Author: Zhang, Rongguang, DeCaprio, James A., Li, Dawei, Zhao, Rui, Lilyestrom, Wayne, Gai, Dahai, Fanning, Ellen, Jochimiak, Andzej, Szakonyl, Gerda, Chen, Xiaojiang S.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2003
United States, China, Analysis, Physiological aspects, Polyoma virus, Polyomavirus, Structure-activity relationships (Biochemistry), DNA binding proteins, Tumor antigens, Structure, Tumour antigens, DNA replication

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Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase

Article Abstract:

The exploration of structures of ferredoxin-thioredoxin reductase (FTR) provides a structural framework for understanding the mechanism of disulphide reduction by an iron-sulphur enzyme and unknown interaction networks of both ferredoxin (Fdx) and Trx (thioredoxins).

Author: Eklund, Hans, Dai, Shaodong, Friemann, Rosmarie, Glauser, Dominique A., Bourquin, Florence, Manieri, Wanda, Schurmann, Peter
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
Thioredoxin, Ferredoxins

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Subjects list: Research
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