《Nature》目录要览：2010-12-02出版
时间：2010-12-02 阅读： 我要评论:
Minrong Ai et al.
doi:10.1038/nature09537
Abstract: http://www.nature.com/nature/journal/v468/n7324/abs/nature09537.html
Article: http://www.nature.com/nature/journal/v468/n7324/full/nature09537.html
Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1 pp696 - 700
Parkinson's disease is characterized by loss of a small group of neurons — the dopaminergic neurons in the substantia nigra pars compacta. Mitochondrial stress is thought to cause this loss, but why that would occur in these cells and not others is not clear. Here it is shown that oxidant stress is evoked by normal pacemaking of these cells, explaining their vulnerability. Knocking out DJ-1, a gene associated with early onset Parkinson's disease, resulted in reduced protection from this stress.
Jaime N. Guzman et al.
doi:10.1038/nature09536
Abstract: http://www.nature.com/nature/journal/v468/n7324/abs/nature09536.html
Article: http://www.nature.com/nature/journal/v468/n7324/full/nature09536.html
Lkb1 regulates quiescence and metabolic homeostasis of haematopoietic stem cells pp701 - 704
Haematopoietic stem cells (HSCs) are very sensitive to energetic and oxidative stress, and modulation of the balance between their quiescence and proliferation is needed to respond to metabolic stress while preserving HSCs' long-term regenerative capacity. Here, and in two accompanying studies, it is shown that the tumour suppressor Lkb1 has a crucial role in maintaining energy homeostasis in haematopoietic cells.
Boyi Gan et al.
doi:10.1038/nature09595
Abstract: http://www.nature.com/nature/journal/v468/n7324/abs/nature09595.html
Article: http://www.nature.com/nature/journal/v468/n7324/full/nature09595.html
Structural changes of envelope proteins during alphavirus fusion pp705 - 708
The E1 and E2 glycoproteins of alphaviruses form heterodimers and assemble into spikes on the virus surface, which mediate receptor binding and endocytosis. When the virion encounters acidic pH in the endosome E1 and E2 dissociate and E1 triggers fusion with the endosomal membrane. Two papers now provide the first crystal structures for glycoprotein complexes incorporating E2 at acidic and neutral pH, respectively. Together they provide insight into how fusion activation is controlled in alphaviruses.
Long Li et al.
doi:10.1038/nature09546
Abstract: http://www.nature.com/nature/journal/v468/n7324/abs/nature09546.html
Article: http://www.nature.com/nature/journal/v468/n7324/full/nature09546.html
Glycoprotein organization of Chikungunya virus particles revealed by X- ray crystallography pp709 - 712
The E1 and E2 glycoproteins of alphaviruses form heterodimers and assemble into spikes on the virus surface, which mediate receptor binding and endocytosis. When the virion encounters acidic pH in the endosome E1 and E2 dissociate and E1 triggers fusion with the endosomal membrane. Two papers now provide the first crystal structures for glycoprotein complexes incorporating E2 at acidic and neutral pH, respectively. Together they provide insight into how fusion activation is controlled in alphaviruses.
James E. Voss et al.
doi:10.1038/nature09555
Abstract: http://www.nature.com/nature/journal/v468/n7324/abs/nature09555.html
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