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Titlebook: Reversible Protein Phosphorylation in Cell Regulation; R. L. Khandelwal,J. H. Wang Book 1993 Springer Science+Business Media Dordrecht 199

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书目名称Reversible Protein Phosphorylation in Cell Regulation
编辑R. L. Khandelwal,J. H. Wang
视频video
丛书名称Developments in Molecular and Cellular Biochemistry
图书封面Titlebook: Reversible Protein Phosphorylation in Cell Regulation;  R. L. Khandelwal,J. H. Wang Book 1993 Springer Science+Business Media Dordrecht 199
出版日期Book 1993
关键词Calcium; Krebs; Nucleotide; biochemistry; cell; mutagen; mutation; phosphorylation; protein; receptor
版次1
doihttps://doi.org/10.1007/978-1-4615-2600-1
isbn_softcover978-1-4613-6113-8
isbn_ebook978-1-4615-2600-1
copyrightSpringer Science+Business Media Dordrecht 1993
The information of publication is updating

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Mutagenesis of the catalytic subunit of rabbit muscle protein phosphatase-1. These results indicate that the catalytic mechanism of ppase-1 is different from that of the protein tyrosine phosphatases which involve a cysteinyl phosphate intermediate. (Mol Cell Biochem . 113–119, 1993)
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The phosphorylation of stathmin by MAP kinasestathmin kinases detected in PC12 cells after stimulation by nerve growth factor (NGF). The results suggest that MAP kinases are the enzymes responsible for increasing the level of phosphorylation of Ser-25, which has been observed previously in PC12 cells following stimulation by NGF. (Mol Cell Biochem . 151–156, 1993)
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Autophosphorylation: a salient feature of protein kinasesffects the functional properties of most protein kinases. Members of the protein kinase family exhibit diversity in the characteristics and functions of autophosphorylation, but certain common themes are emerging. (Mol Cell Biochem . 51–70, 1993)
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Development and characterization of fluorescently-labeled myosin light chain kinase calmodulin-bindies responsible for binding calmodulin. These regions are known as calmodulin-binding domains and in many cases are contained within sequences that are short enough to be synthesized by solid-phase techniques. The ability to chemically-synthesize target enzyme calmodulin-binding domains has permitted
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Expression of cGMP-dependent protein kinase in ,ic cell lines but so far not in prokaryotic cells. Three vectors were constructed for the expression of Iα cGMP kinase in .. Transformation with the pET3a/cgk vector which uses the T7 RNA polymerase/promotor system resulted in efficient accumulation of cGMP kinase. Most of the protein was in an inso
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