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科学家的学术影响力,不仅要看论文的被引次数,还要看论文的替代计量得分。----许老师傅
日前,来自清华大学的研究人员在《自然》(Nature)杂志上报告称,他们解析了人类葡萄糖转运蛋白 GLUT1 的晶体结构。论文通讯作者是来自清华大学的颜宁(Nieng Yan)。
Nature:颜宁解析转运蛋白GLUT1晶体结构
获得 GLUT1、XylE 和 GlcP 的结构为从结构和机制上了解参与各种生物学过程及与许多生物技术应用相关的这一 MFS 葡萄糖转运家族提供了重要的新见解。此外,新研究结果也为开发出靶向 GLUT1 和其他生理上重要的 MFS 葡萄糖转运蛋白的潜在治疗药物提供了指导准则。
原文检索:
Dong Deng, Chao Xu, Pengcheng Sun, Jianping Wu, Chuangye Yan, Mingxu Hu & Nieng Yan. Crystal structure of the human glucose transporter GLUT1. Nature, 18 May 2014; doi:10.1038/nature13306
http://www.bio360.net/news/show/10207.html
in the 97 percentile (ranked 2,351st) of the 81,250 tracked articles of a similar age in all journals
in the 66 percentile (ranked 244th) of the 740 tracked articles of a similar age in Nature
Nature:人的葡萄糖转运蛋白GLUT1-4在大肠杆菌中的同源蛋白XylE的晶体结构
尤为重要的是,序列比对显示这些残基在GLUT1-4中完全保守,从而第一次揭示出GLUT1-4识别底物的分子基础。利用计算机软件同源建模,研究组搭建了人的GLUT1蛋白的三维结构。这一结构模型由于是以具有高度同源的XylE蛋白的晶体结构为基础,比以往研究报道的结果(如写入第5版Lehninger Principles of Biochemistry教科书的GLUT1跨膜模型)更为准确。根据这个结构模型,研究组进一步研究了GLUT1-4与相关人类疾病相关的突变残基的功能与致病机理。
了解更多:
Crystal structure of a bacterial homologue of glucose transporters GLUT1-4
DOI:10.1038/nature11524
Glucose transporters are essential for metabolism of glucose in cells of diverse organisms from microbes to humans, exemplified by the disease-related human proteins GLUT1, 2, 3 and 4. Despite rigorous efforts, the structural information for GLUT1–4 or their homologues remains largely unknown. Here we report three related crystal structures of XylE, an Escherichia coli homologue of GLUT1–4, in complex with d-xylose, d-glucose and 6-bromo-6-deoxy-d-glucose, at resolutions of 2.8, 2.9 and 2.6 Å, respectively. The structure consists of a typical major facilitator superfamily fold of 12 transmembrane segments and a unique intracellular four-helix domain. XylE was captured in an outward-facing, partly occluded conformation. Most of the important amino acids responsible for recognition of d-xylose or d-glucose are invariant in GLUT1–4, suggesting functional and mechanistic conservations. Structure-based modelling of GLUT1–4 allows mapping and interpretation of disease-related mutations. The structural and biochemical information reported here constitutes an important framework for mechanistic understanding of glucose transporters and sugar porters in general.
http://www.bio360.net/news/show/3385.html
Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel
DOI:10.1038/nature11054
颜宁 清华大学医学院
研究报道了细菌电压门控钠通道NaChBac同源物的晶体结构。电压门控钠(Nav)通道是神经和肌肉快速去极化的必不可少的条件,也是重要的药物靶点。确定Nav通道的结构将揭示离子通道的机制,推动潜在的临床应用。细菌Nav通道家族,举例来说细菌的Na+选择性通道(NaChBac)为结构功能分析提供了一个有用的模型系统。中文报道
in the 94 percentile (ranked 3,441st) of the 68,519 tracked articles of a similar age in all journals
in the 48 percentile (ranked 390th) of the 755 tracked articles of a similar age in Nature
in the 86 percentile (ranked 10,060th) of the 74,120 tracked articles of a similar age in all journals
in the 33 percentile (ranked 672nd) of the 1,010 tracked articles of a similar age in Nature
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