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Two-Component Signaling Systems, Part C, Volume 471 [Hardback]

Volume editor (Cornell University, Ithaca, NY, USA), Volume editor (Cornell University, Ithaca, NY, USA), Volume editor (The Salk Institute, La Jolla, CA, USA)
  • Formāts: Hardback, 496 pages, height x width: 229x152 mm, weight: 950 g
  • Sērija : Methods in Enzymology
  • Izdošanas datums: 23-Apr-2010
  • Izdevniecība: Academic Press Inc
  • ISBN-10: 0123813476
  • ISBN-13: 9780123813473
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  • Cena: 171,76 €
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  • Formāts: Hardback, 496 pages, height x width: 229x152 mm, weight: 950 g
  • Sērija : Methods in Enzymology
  • Izdošanas datums: 23-Apr-2010
  • Izdevniecība: Academic Press Inc
  • ISBN-10: 0123813476
  • ISBN-13: 9780123813473
Citas grāmatas par šo tēmu:
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



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 inC. 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

Papildus informācija

The third installment of a three-volume treatment of two-component signaling systems and histidine kinases
Characterizing cross-talk in vivo: avoiding pitfalls and
over-interpretation
Albert Siryaporn and Mark Goulian
Inference of Direct Residue Contacts in Two-Component Signaling
Bryan Lunt, Hendrik Szurmant, Andrea Procaccini, James A. Hoch, Terence Hwa
and Martin Weigt
Computational Modeling of Phosphotransfer Complexes in Two-Component
Signaling
Alexander Schug, Martin Weigt, James A. Hoch, Jose N. Onuchic, Terence Hwa,
Hendrik Szurmant
Kinetic studies of the yeast His-Asp phosphorelay signaling pathway
Alla O. Kaserer, Babak Andi, Paul F. Cook and Ann H. West
Purification of MBP-EnvZ fusion proteins using an automated system
Ricardo Oropeza and Edmundo Calva
Measurement of Response Regulator Autodephosphorylation Rates Spanning Six
Orders of Magnitude
Robert B. Bourret, Stephanie A. Thomas, Stephani C. Page, Rachel L.
Creager-Allen, Aaron M. Moore, and Ruth E. Silversmith
Transmembrane receptors chimeras to probe Hamp domain function
Jürgen U. Linder and Joachim E. Schultz
Light-Activated Bacterial LOV-domain Histidine Kinases
Tong-Seung Tseng, Marcus A. Frederickson, Winslow R. Briggs and Roberto A.
Bogomolni
Characterization of Bacteriophytochromes from Photosynthetic Bacteria:
Histidine Kinase Signaling Triggered by light and redox sensing
Eric Giraud, Jérōme Lavergne and André Verméglio
Biophysical assays for protein interactions in the Wsp sensory system and
biofilm formation
Nabanita De, Marcos V.A.S. Navarro, Qi Wang, Petya V. Krasteva and Holger
Sondermann
High throughput screening of bacterial protein localization
John N. Werner and Zemer Gitai
In vitro and in vivo analysis of the ArcB/A redox signaling pathway
Adriįn F. Alvarez and Dimitris Georgellis
Potassium sensing histidine kinase in Bacillus subtilis
Daniel López, Erin Gontang and Roberto Kolter
Two Component Systems and Regulation of Developmental Progression in
Myxococcus Xanthus
Bongsoo Lee, Andreas Schramm, and Penelope I. Higgs
Two-component signaling to the stress MAP kinase cascade in fission yeast
Susumu Morigasaki and Kazuhiro Shiozaki
Genetic and Biochemical Analysis of the SLN1 Pathway in Saccharomyces
cerevisiae
Jan S. Fassler
Analysis of mitogen-activated protein kinase phosphorylation in response
to stimulation of histidine kinase signaling pathways in Neurospora
Carol A. Jones and Katherine A. Borkovich
Biochemical Characterization of Plant Hormone Cytokinin Receptor Histidine
Kinases Using Microorganisms
Takeshi Mizuno and Takafumi Yamashino
Characterization of Pseudo-Response Regulators In Plants
Woe-Yeon Kim, Patrice A. Salomé, Sumire Fujiwara, David E. Somers and C.
Robertson McClung
Reversible Histidine Phosphorylation in Mammalian Cells: A Teeter-Totter
Formed by Nucleoside Diphosphate Kinase and Protein Histidine Phosphatase
Thomas Wieland, Hans-Jörg Hippe, Katrin Ludwig, Xiao-Bo Zhou, Michael Korth
and Susanne Klumpp
Histidine phosphorylation in histones and in other mammalian proteins
Paul G. Besant and P.V. Attwood