By Prof. Dr. Gerhard Krauss(auth.)
Chapter 1 The rules of Gene Expression (pages 1–87):
Chapter 2 The legislation of Enzyme job (pages 89–114):
Chapter three constitution and serve as of sign Pathways (pages 115–149):
Chapter four Signaling via Nuclear Receptors (pages 151–177):
Chapter five G Protein?Coupled sign Transmission Pathways (pages 179–229):
Chapter 6 Intracellular Messenger elements: “Second Messengers” (pages 231–268):
Chapter 7 Ser/Thr?Specific Protein Kinases and Protein Phosphatases (pages 269–309):
Chapter eight sign Transmission through Transmembrane Receptors with Tyrosine?Specific Protein Kinase job (pages 311–354):
Chapter nine sign Transmission through Ras Proteins (pages 355–381):
Chapter 10 Intracellular sign Transduction: The Protein Cascades of the MAP Kinase Pathways (pages 383–393):
Chapter eleven Membrane Receptors with linked Tyrosine Kinase task (pages 395–416):
Chapter 12 different Receptor sessions (pages 417–427):
Chapter thirteen law of the telephone Cycle (pages 429–468):
Chapter 14 Malfunction of Signaling Pathways and Tumorigenesis: Oncogenes and Tumor Suppressor Genes (pages 469–509):
Chapter 15 Apoptosis (pages 511–532):
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Additional info for Biochemistry of Signal Transduction and Regulation, Third Edition
Examples of other trans-activating domains are the glutamine-rich domains of the transcription factor Sp1 and the proline-rich domain of the transcription factor CTF/ NF1, which contains 20 % proline residues. It is assumed that trans-activating domains are structural elements that can adapt to become complementary to a surface of the transcription apparatus in a flexible and rather unspecific manner. Furthermore, parts of the trans-activating domain mediate contacts to the chromatin-remodeling and chromatin-modifying complexes and recruit these to the enhancer or promotor region.
A) The Trp repressor requires Trp in order to bind its affiliated DNA binding element. In the absence of tryptophan, the Trp repressor can not bind to the regulatory sequence and is therefor inactive. Upon an increase in the tryptohan concentration, tryptophan binds to the Trp repressor and transforms it into a binding-proficient form. The DNA bound Trp repressor prevents the transcription of the structural genes, and the biosynthesis of tryptophan is halted. B) structural basis for the activation of the DNA binding of the Trp repressor by tryptohan molecules.
In the Trp-free form, the prerequisite for a strong cooperative binding of the repressor dimer is not fulfilled, since the recognition helices are not positioned optimally for binding to the recognition sequence in the major groove of the DNA. Metal Ions as Effector Molecules Metal ions can serve as effector molecules as well as controlling the DNA-binding activity of regulatory proteins. , 1999). An increase of Ca2+ in the form of a Ca2+ signal (see Chapter 6) leads to a reduced affinity to its DNA element and to an increased expression of the target gene.
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