Two-Component Signaling Systems, Part C

Inbunden, Engelska, 2010

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Beskrivning

Multicellular organisms must be able to adapt to cellular events to accommodate prevailing conditions. Sensory-response circuits operate by making use of a phosphorylation control mechanism known as the "two-component system." This volume, the third in a three-volume treatment edited by the same group of editors, includes a wide range of methods, including those dealing with the Sln-1 kinase pathway, triazole sensitivity in C. albicans, and histidine kinases in cyanobacteria circadian clock.

Includes time-tested core methods and new innovations applicable to any researcher studing two-component signaling systems or histidine kinases
Methods included are useful to both established researchers and newcomers to the field
Relevant background and reference information given for procedures can be used as a guide to developing protocols in a number of disciplines

Produktinformation

Utgivningsdatum:2010-04-23
Mått:152 x 229 x undefined mm
Vikt:950 g
Format:Inbunden
Språk:Engelska
Serie:Methods in Enzymology
Antal sidor:496
Förlag:Elsevier Science
ISBN:9780123813473

Utforska kategorier

Biokemi inom Naturvetenskap och teknik

Innehållsförteckning

Characterizing cross-talk in vivo: avoiding pitfalls and over-interpretationAlbert Siryaporn and Mark GoulianInference of Direct Residue Contacts in Two-Component SignalingBryan Lunt, Hendrik Szurmant, Andrea Procaccini, James A. Hoch, Terence Hwa and Martin WeigtComputational Modeling of Phosphotransfer Complexes in Two-Component SignalingAlexander Schug, Martin Weigt, James A. Hoch, Jose N. Onuchic, Terence Hwa, Hendrik SzurmantKinetic studies of the yeast His-Asp phosphorelay signaling pathwayAlla O. Kaserer, Babak Andi, Paul F. Cook and Ann H. WestPurification of MBP-EnvZ fusion proteins using an automated systemRicardo Oropeza and Edmundo CalvaMeasurement of Response Regulator Autodephosphorylation Rates Spanning Six Orders of MagnitudeRobert B. Bourret, Stephanie A. Thomas, Stephani C. Page, Rachel L. Creager-Allen, Aaron M. Moore, and Ruth E. SilversmithTransmembrane receptors chimeras to probe Hamp domain functionJürgen U. Linder and Joachim E. SchultzLight-Activated Bacterial LOV-domain Histidine KinasesTong-Seung Tseng, Marcus A. Frederickson, Winslow R. Briggs and Roberto A. BogomolniCharacterization of Bacteriophytochromes from Photosynthetic Bacteria: Histidine Kinase Signaling Triggered by light and redox sensingEric Giraud, Jérôme Lavergne and André VerméglioBiophysical assays for protein interactions in the Wsp sensory system and biofilm formationNabanita De, Marcos V.A.S. Navarro, Qi Wang, Petya V. Krasteva and Holger SondermannHigh throughput screening of bacterial protein localizationJohn N. Werner and Zemer GitaiIn vitro and in vivo analysis of the ArcB/A redox signaling pathwayAdrián F. Alvarez and Dimitris GeorgellisPotassium sensing histidine kinase in Bacillus subtilisDaniel López, Erin Gontang and Roberto KolterTwo Component Systems and Regulation of Developmental Progression in Myxococcus XanthusBongsoo Lee, Andreas Schramm, and Penelope I. HiggsTwo-component signaling to the stress MAP kinase cascade in fission yeastSusumu Morigasaki and Kazuhiro ShiozakiGenetic and Biochemical Analysis of the SLN1 Pathway in Saccharomyces cerevisiaeJan S. FasslerAnalysis of mitogen-activated protein kinase phosphorylation in response to stimulation of histidine kinase signaling pathways in NeurosporaCarol A. Jones and Katherine A. BorkovichBiochemical Characterization of Plant Hormone Cytokinin Receptor Histidine Kinases Using MicroorganismsTakeshi Mizuno and Takafumi YamashinoCharacterization of Pseudo-Response Regulators In PlantsWoe-Yeon Kim, Patrice A. Salomé, Sumire Fujiwara, David E. Somers and C. Robertson McClungReversible Histidine Phosphorylation in Mammalian Cells: A Teeter-Totter Formed by Nucleoside Diphosphate Kinase and Protein Histidine PhosphataseThomas Wieland, Hans-Jörg Hippe, Katrin Ludwig, Xiao-Bo Zhou, Michael Korth and Susanne KlumppHistidine phosphorylation in histones and in other mammalian proteinsPaul G. Besant and P.V. Attwood