Two-Component Signaling Systems, Part C: Volume 471

Two-Component Signaling Systems, Part C: Volume 471

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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.
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Product details

  • Hardback | 496 pages
  • 157.48 x 231.14 x 30.48mm | 839.14g
  • Academic Press Inc
  • San Diego, United States
  • English
  • 471st edition
  • 0123813476
  • 9780123813473

Table of contents

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 Jurgen 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, Jerome Lavergne and Andre Vermeglio
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 Adrian F. Alvarez and Dimitris Georgellis
Potassium sensing histidine kinase in Bacillus subtilis Daniel Lopez, 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. Salome, 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-Joerg 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
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