Interacting Protein Domains

1. Front Matter

   Pages I-X

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2. Regulation by Reversible Protein Phosphorylation

   1. Front Matter

      Pages 1-1

      PDF

   2. Control of Cellular Processes by Reversible Protein Phosphorylation

      • Edmond H. Fischer

      Pages 3-8

   3. From Phosphorylase to Phosphorylase Kinase

      • L. N. Johnson

      Pages 9-14

   4. Protein Kinase X: A Novel Human Protein Kinase closely related to the Catalytic Subunit of cAMP-dependent Protein Kinase

      • B. Zimmermann, A. Klink, G. Rappold, F. W. Herberg

      Pages 15-18

   5. Interaction of Protein Kinase A_c from Ascaris suum with Proteins and Peptides: Comparison with the Mammalian Enzyme

      • S. Jung, R. Hoffmann, T. Treptau, P. H. Rodriguez, B. G. Harris, P. F. Cook et al.

      Pages 19-24

3. Methodology

   1. Front Matter

      Pages 25-25

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   2. Interaction Studies Using Biosensors

      • Ariane Maleszka, Friedrich W. Herberg

      Pages 27-36

   3. Advances in Determination of Protein Structure by X-ray Diffraction Methods

      • L. N. Johnson

      Pages 37-44

   4. Spectroscopical studies on the interaction between ww domain and proline-rich peptides

      • Elena Baraldi, Maria Macias, Marko Hyvonen, Hartmut Oschkinat, Matti Saraste

      Pages 45-48

   5. Novel Microscope-Based Approaches for the Investigation of Protein-Protein Interactions in Signal Transduction

      • György Vereb, Christoph K. Meyer, Thomas M. Jovin

      Pages 49-52

   6. Binding studies with SH2 domains from the phosphotyrosine kinase ZAP70 using surface plasmon resonance and scintillation proximity assays

      • D. Whitaker, J. Hartley, P. Rugman, E. Keech, R. Handa, L. Price et al.

      Pages 53-57

   7. Leucine Zipper mediated Homodimerization of Autoantigen L7 analyzed by Electrospray Ionization Mass Spectrometry and Yeast Two Hybrid Interactions

      • Stephan Witte, Frank Neumann, Michael Przybylski, Ulrich Krawinkel

      Pages 59-62

   8. Proteins at Work: Time-Resolved FTIR Studies of Bacteriorhodopsin and the GTP-Binding Protein P21

      • Klaus Gerwert

      Pages 63-72

4. Phospholipid Signaling

   1. Front Matter

      Pages 73-73

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   2. Downstream Signaling from Phosphoinositide 3-Kinase

      • Lewis Cawley

      Pages 75-81

   3. Phosphoinositide-3-Kinase Mediated Activation of JNK by the ßPDGFR

      • M. A. López-Ilasaca, J. S. Gutkind, M. A. Heidaran

      Pages 83-86

   4. Regulation of Phospholipase C isozymes

      • Sue Goo Rhee, Yun Soo Bae

      Pages 87-92

   5. Substrate Binding and Catalytic Mechanism in Phospholipase C from Bacillus cereus

      • Dorthe da Graça Thrige, Jette Raun Byberg Buur, Flemming Steen Jørgensen

      Pages 93-96

   6. Identification of Three Active Site Residues Involved in Substrate Binding by Human 43 kDa-D-myo-Inositol 1,4,5-Trisphosphate 5-Phosphatase

      • David Communi, Christophe Erneux

      Pages 97-100

This is now the fourth time that protein phosphorylation has been the focus of a NATO Advanced Study Institute. The first meeting with the topic "Signal Trans­ duction and Protein Phosphorylation" was held on the island of Spezai, Greece, in September 1986. The second one took place in Chateau La Londe, France, in September 1989 on "Cellular Regulation by Protein Phosphorylation", the third one on " Tyrosine Phosphorylation/Dephosphorylation and Downstream Signaling" was in September 1992 in Maratea, Italy. The titles of these books clearly mirror the developments that have taken place in the last decade. Beginning with the recognition that protein phosphorylation is at the center of signaling -clearly established in 1990 -it became apparent that many cellular processes are regulated by this mode. A new focus then emerged when it was recognized that growth factors are bound to corresponding receptors trigger protein tyrosine phosphorylation which controls cell prolifera­ tion. This was the topic of the third meeting in this series. It is now evident that further progress depends on understanding the three dimensional structure of the proteins involved. It goes without saying, for example, that understanding the location of proteins by adaptor proteins is only possible on the basis of the three dimensional protein structure. Therefore, the fourth meeting in this series concentrated on the protein structure of signaling molecules as well as on the elucidation of the principles of protein domain interactions.

• ATP
• Activation
• Antigen
• FTIR-Spektroskopie
• Proteinphosphorylierung
• Proteinstruktur
• Vivo
• cellular processes
• enzymes
• opioid
• protein phosphorylation
• proteins
• regulation
• translation
• x-ray diffraction

• Institut für Physiologische Chemie Abt. Biochemie Supramolekularer Systeme, Ruhr-Universität Bochum, Bochum, Germany

  Ludwig Heilmeyer

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