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2篇 您的检索式:作者名="Birgit Kemmerling"
    题名 作者 年代 出处 被引量
1Heat Shock Factors HsfB 1 and HsfB2b Are Involved in the Regulation of Pdf1.2 Expression and Pathogen Resistance in Arabidopsis显示文摘以便估计热的功能的角色在 Arabidopsis 的导致压力的班 B 热吃惊因素,我们调查了 AtHsfB1 和 AtHsfB2b 的 T-DNA 猛烈异种。在异种的 defensin 基因 Pdf1.2a/b 的基础 mRNA 水平的一条起来规定种的作为强壮揭示的两倍猛烈 hsfB1/hsfB2b 植物的 Micorarray 分析。Pdf 表示被 jasmonic 酸处理或感染进一步与 necrotrophic 真菌 Alternaria brassicicola 提高。单个变异的 hsfB2b 和双变异的 hsfB1/B2b 显著地在 A 以后在疾病抵抗被改进。brassicicola 感染。为和 Pdf1.2 的倡导者的 Hsf 的一个直接相互作用没有指示,它缺乏完美的 HSE 一致 Hsf 有约束力的序列。然而,在形成变化近来 HsfA2 依赖的 HSE 绑定在 hsfB1/B2b 植物被检测。这建议 HsfB1/B2b 可以在调整热吃惊反应的用以遮闭之物与班 A-Hsf 交往。Pdf 基因的鉴定作为 Hsf 依赖的否定规定的目标是为在关於生命、不能生活的回答的规定的 Hsf 的互联的第一条证据。Mukesh Kumar Wolfgang Busch Hannah Birke Birgit Kemmerling Thorsten Nurnberger Friedrich Schoffl 2009Molecular Plant2009,2,1:15
2Specifying the role of BAK1-interacting receptor-like kinase 3 in brassinosteroid signaling显示文摘Brassinosteroids(BR) are involved in the control of several developmental processes ranging from root elongation to senescence and adaptation to environmental cues. Thus, BR perception and signaling have to be precisely regulated. One regulator is BRI1-associated kinase 1(BAK1)-interacting receptor-like kinase 3(BIR3). In the absence of BR, BIR3 forms complexes with BR insensitive 1(BRI1) and BAK1.However, the biophysical and energetic requirements for complex formation in the absence of the ligand have yet to be determined. Using computational modeling, we simulated the potential complexes between the cytoplasmic domains of BAK1, BRI1 and BIR3. Our calculations and experimental data confirm the interaction of BIR3 Rewith BAK1 and BRI1, with the BAK1 BIR3 interaction clearly favored. Furthermore, we demonstrate that BIR3 and BRI1 share the same interaction site with BAK1. This suggests a competition between BIR3 and BRI1 for binding to BAK1, which results in preferential binding of BIR3 to BAK1 in the absence of the ligand thereby preventing the active participation of BAK1 in BR signaling. Our model also suggests that BAK1 and BRI1 can interact even while BAK1 is in complex with BIR3 at an additional binding site of BAK1 that does not allow active BR signaling.Ruth Groβeholz Anna Feldman-Salit Friederike Wanke Sarina Schulze Nina Glockner Birgit Kemmerling Klaus Harter Ursula Kummer 2020Journal of Integrative Plant Biology2020,62,4:1
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