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Two-component signaling systems. Part C /

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 th...

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Simon, Melvin I., Crane, Brian R., Crane, Alexandrine
Formato: Electrónico eBook
Idioma:Inglés
Publicado: Amsterdam ; Boston : Elsevier/Academic Press, 2010.
Colección:Methods in enzymology ; v. 471.
Temas:
Acceso en línea:Texto completo
Texto completo

MARC

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245 0 0 |a Two-component signaling systems.  |n Part C /  |c edited by Melvin I. Simon, Brian R. Crane, Alexandrine Crane. 
260 |a Amsterdam ;  |a Boston :  |b Elsevier/Academic Press,  |c 2010. 
300 |a 1 online resource (xlvi, 443 pages, 4 unnumbered pages of plates) :  |b illustrations (some color). 
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490 1 |a Methods in enzymology ;  |v v. 471 
504 |a Includes bibliographical references and indexes. 
520 |a 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 
505 0 |a 1. Characterizing Cross-Talk In Vivo: Avoiding Pitfalls and Overinterpretation / Albert Siryaporn / Mark Goulian -- 2. Inference of Direct Residue Contacts in Two-Component Signaling / Andrea Procaccini / Bryan Lunt / Hendrik Szurmant / James A. Hoch / Terence Hwa / Martin Weigt -- 3.Computational Modeling of Phosphotransfer Complexes in Two-Component Signaling / Hendrik Szurmant / Jose N. Onuchic / Alexander Schug / Martin Weigt / Terence Hwa / James A. Hoch -- 4. Kinetic Studies of the Yeast His-Asp Phosphorelay Signaling Pathway / Ann H. West / Paul F. Cook / Alla O. Kaserer / Babak Andi -- 5. Purification of MBP-EnvZ Fusion Proteins Using an Automated System / Edmundo Calva / Ricardo Oropeza -- 6. Measurement of Response Regulator Autodephosphorylation Rates Spanning Six Orders of Magnitude / Stephani C. Page / Ruth E. Silversmith / Aaron M. Moore / Rachel L. Creager-Allen / Stephanie A. Thomas / Robert B. Bourret -- 7. Transmembrane Receptor Chimeras to Probe HAMP Domain Function / Jurgen U. Linder / Joachim E. Schultz -- 8. Light-Activated Bacterial LOV-Domain Histidine Kinases / Marcus A. Frederickson / Tong-Seung Tseng / Winslow R. Briggs / Roberto A. Bogomolni -- 9. Characterization of Bacteriophytochromes from Photosynthetic Bacteria: Histidine Kinase Signaling Triggered by Light and Redox Sensing Eric Giraud / Jerome Lavergne / Andre Vermeglio -- 10. Biophysical Assays for Protein Interactions in the Wsp Sensory System and Biofilm Formation / Holger Sondermann / Marcos V.A.S. Navarro / Qi Wang / Petya V. Krasteva / Nabanita De -- 11. High-Throughput Screening of Bacterial Protein Localization / Zemer Gitai / John N. Werner -- 12. In Vitro and In Vivo Analysis of the ArcB/A Redox Signaling Pathway / Adrian F. Alvarez / Dimitris Georgellis -- 13. Potassium Sensing Histidine Kinase in Bacillus subtilis / Daniel Lopez / Erin A. Gontang / Roberto Kolter -- 14. Two-Component Systems and Regulation of Developmental Progression in Myxococcus xanthus / Bongsoo Lee / Andreas Schramm / Sakthimala Jagadeesan / Penelope I. Higgs -- 15. Two-Component Signaling to the Stress MAP Kinase Cascade in Fission Yeast / Kazuhiro Shiozaki / Susumu Morigasaki -- 16. Genetic and Biochemical Analysis of the SLN1 Pathway in Saccharomyces cerevisiae / Jan S. Fassler / Ann H. West -- 17. Analysis of Mitogen-Activated Protein Kinase Phosphorylation in Response to Stimulation of Histidine Kinase Signaling Pathways in Neurospora / Carol A. Jones / Katherine A. Borkovich -- 18. Biochemical Characterization of Plant Hormone Cytokinin-Receptor Histidine Kinases Using Microorganisms / Takeshi Mizuno / Takafumi Yamashino -- 19. Characterization of Pseudo-Response Regulators in Plants / Sumire Fujiwara / Patrice A. Salome / Woe-Yeon Kim / C. Robertson McClung / David E. Somers -- 20. Reversible Histidine Phosphorylation in Mammalian Cells: A Teeter-Totter Formed by Nucleoside Diphosphate Kinase and Protein Histidine Phosphatase 1 / Katrin Ludwig / Hans-Jorg Hippe / Thomas Wieland / Xiao-Bo Zhou / Susanne Klumpp / Michael Korth -- 21. Histidine Phosphorylation in Histones and In Other Mammalian Proteins / Paul G. Besant / Paul V. Attwood. 
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650 0 |a Protein kinases. 
650 0 |a Phosphoproteins  |x Physiological effect. 
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653 1 0 |a Eiwitten en enzymen 
700 1 |a Simon, Melvin I. 
700 1 |a Crane, Brian R. 
700 1 |a Crane, Alexandrine. 
776 0 8 |i Print version:  |t Two-component signaling systems. Part C.  |d Amsterdam ; Boston : Elsevier/Academic, 2010  |z 9780123813473  |w (OCoLC)499068500 
830 0 |a Methods in enzymology ;  |v v. 471. 
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