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Posttranslational modification of proteins. expanding nature's inventory

Christopher T. Walsh

Publikováno
Englewood : Roberts and Co. Publishers, c2006
Stránkování
xxi, 490 s. : il., tab. ; 27 cm

Jazyk angličtina Země Spojené státy americké

Typ dokumentu monografie

Perzistentní odkaz   https://www.medvik.cz/link/MED00172520
Odkazy

Knihovny.cz ISBN 0-9747077-3-2

More than five percent of the genes in higher eukaryotic genomes encode enzymes that posttranslationally modify proteins, greatly expanding the complexity and diversity of proteomes. This book examines the molecular logic of the major types of covalent modifications of proteins and their biological consequences.

Bibliografie atd.

Obsahuje bibliografie a rejstřík

Obsah

Protein phosphorylation by protein kinases -- Sulfuryl transfers: action of protein sulfotransferases and aryl sulfatases -- Modifications of cysteine and methionine by oxidation-reduction -- Protein methylation -- Protein N-acetylation -- Protein lipidation -- Proteolytic posttranslational modification of proteins -- Ubiquitin and ubiquitin-like protein tags -- Protein glycosylation -- ADP ribosylation of proteins from NAD as donor -- Posttranslational hydroxylation of proteins -- Protein automodification reactions -- Swinging arms for biotin, lipoate, and phosphopantetheine tethering to proteins -- Protein carboxylation and amidation -- Diversification of proteomes.

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