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Titlebook: Histidine Phosphorylation; Methods and Protocol Claire E. Eyers Book 2020 Springer Science+Business Media, LLC, part of Springer Nature 202

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发表于 2025-3-21 19:15:20 | 显示全部楼层 |阅读模式
书目名称Histidine Phosphorylation
副标题Methods and Protocol
编辑Claire E. Eyers
视频video
概述Includes cutting-edge methods and protocols.Provides step-by-step detail essential for reproducible results.Contains key notes and implementation advice from the experts
丛书名称Methods in Molecular Biology
图书封面Titlebook: Histidine Phosphorylation; Methods and Protocol Claire E. Eyers Book 2020 Springer Science+Business Media, LLC, part of Springer Nature 202
描述.This. .volume. .details the current understanding of roles and regulation on histidine phosphorylation, describing methods for the characterization of protein phosphorylation on histidine. Chapters guide readers through .in vitro. systems, cell-based systems, comprehensive background review articles on histidine kinases and phosphatases. Written in the highly successful .Methods in Molecular Biology .series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls... Authoritative and cutting-edge, .Histidine Phosphorylation: Methods and Protocols .aims to ensure successful results in the further study of this rapidly growing field. .
出版日期Book 2020
关键词histidine kinase substrates; pHis; phosphorylated proteins; mammalian cell signaling; histidine phosphor
版次1
doihttps://doi.org/10.1007/978-1-4939-9884-5
isbn_softcover978-1-4939-9886-9
isbn_ebook978-1-4939-9884-5Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightSpringer Science+Business Media, LLC, part of Springer Nature 2020
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A High-Throughput Strategy for Recombinant Protein Expression and Solubility Screen in , : A Case ocation of soluble and well-folded recombinant proteins suitable for functional and/or structural studies. Small-scale optimization of conditions for protein production and stability saves time, labor, and costs. Here we describe a protocol for quick protein production and solubility screen using Tis
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A Quantitative Method for the Measurement of Protein Histidine Phosphorylation, activity, even in the presence of other protein kinases, for example, serine/threonine or tyrosine kinases. The method involves the measurement of .P, derived from [γ.P]ATP, incorporation into phosphohistidine in a protein substrate. The method makes use of the differential stabilities of phosphohi
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Determination of Phosphohistidine Stoichiometry in Histidine Kinases by Intact Mass Spectrometry,roteins. We describe a procedure for determining the stoichiometry of histidine phosphorylation on the human histidine kinases NME1 and NME2 by intact mass spectrometry under conditions that retain this acid-labile protein modification. By characterizing these two model histidine protein kinases in
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Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases,, the His residue is phosphorylated in . or . depending on whether the ATP molecule used in the reaction is bound to the same or the neighboring subunit, respectively. The . or . autophosphorylation results from an alternative directionality in the connection between helices α1 and α2 in the HK DHp
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Manipulation of Bacterial Signaling Using Engineered Histidine Kinases,(HK) and subsequent transfer of the phosphate group to its downstream cognate response regulator (RR). The RR then elicits a cellular response, commonly through regulation of transcription. Engineering two-component system signaling networks provides a strategy to study bacterial signaling mechanism
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