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Endogenous ADP-Ribosylation / edited by Friedrich Koch-Nolte.

Contributor(s): SpringerLink (Online service) | Koch-Nolte, Friedrich, editor literario
Material type: materialTypeLabelE-bookSeries: (Current Topics in Microbiology and Immunology, 0070-217X; 384).Publisher: Cham, Switzerland : Springer, 2015Description: 1 recurso en línea (VIII, 213 páginas) :.ISBN: 9783319107714.Subject: Microbiología médica | Inmunología | FarmacologíaOnline resources: Acceso a este recurso digital (usuarios Universidad Europea de Madrid)Digital Resources
Contents:
The natural history of ADP-ribosyltransferases and the ADP ribosylation system -- Identification and Analysis of ADP-ribosylated Proteins -- Photorhabdus luminescens toxins TccC3 and TccC5: Insecticidal ADP-ribosyltransferases that modify threonine and glutamine -- Reaction mechanism of mono-ADP-ribosyltransferase based on structures of the complex of enzyme and substrate protein -- Regulation of nitrogenase by reversible mono-ADP-ribosylation -- ADP-ribosylation of P2X7: a matter of life and death for regulatory T cells and natural killer T cells -- Pierisins and CARP-1: ADP-ribosylation of DNA by ARTCs in butterflies and shellfish -- Comparative structural analysis of the putative mono-ADP-ribosyltransferases of the ARTD/PARP family -- Function and regulation of the mono-ADP-ribosyltransferase ARTD10 -- Regulation of nucleocytoplasmic transport by ADP-ribosylation: the emerging role of karyopherin-β1 mono-ADP-ribosylation by ARTD15.
Abstract: This volume gathers the latest exciting findings on ADP-ribosylation from renowned experts in the field. It includes ten chapters, organized into the following three thematic sections: Â{u2DC2}Â{u2820} Evolution and detection of endogenous ADP-ribosylation Â{u2DC2}Â{u2820} ADP-ribosylation by the ARTC family of ADP-ribosyltransferases (R-S-E ARTs) ·Â{u2820} ADP-ribosylation by the ARTD family of ADP-ribosyltransferases (H-Y-E ARTs) The book will provide readers a better understanding of ADP-ribosylating toxins and their endogenous relatives. This provides a basis for developing novel toxin-neutralizing drugs and drugs targeting endogenous ADP-ribosyltransferase relatives.
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Holdings
Item type Current library Collection Call number Copy number Status Date due Barcode Item holds
LIBRO-E NO PRÉSTAMO LIBRO-E NO PRÉSTAMO Madrid Digital Acceso Electrónico (UEM) Ciencias de la Salud QP625.A29 E536 2015 EB (Browse shelf(Opens below)) .i11568264 Acceso electrónico eBOOK .i11568264
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The natural history of ADP-ribosyltransferases and the ADP ribosylation system -- Identification and Analysis of ADP-ribosylated Proteins -- Photorhabdus luminescens toxins TccC3 and TccC5: Insecticidal ADP-ribosyltransferases that modify threonine and glutamine -- Reaction mechanism of mono-ADP-ribosyltransferase based on structures of the complex of enzyme and substrate protein -- Regulation of nitrogenase by reversible mono-ADP-ribosylation -- ADP-ribosylation of P2X7: a matter of life and death for regulatory T cells and natural killer T cells -- Pierisins and CARP-1: ADP-ribosylation of DNA by ARTCs in butterflies and shellfish -- Comparative structural analysis of the putative mono-ADP-ribosyltransferases of the ARTD/PARP family -- Function and regulation of the mono-ADP-ribosyltransferase ARTD10 -- Regulation of nucleocytoplasmic transport by ADP-ribosylation: the emerging role of karyopherin-β1 mono-ADP-ribosylation by ARTD15.

This volume gathers the latest exciting findings on ADP-ribosylation from renowned experts in the field. It includes ten chapters, organized into the following three thematic sections: Â{u2DC2}Â{u2820} Evolution and detection of endogenous ADP-ribosylation Â{u2DC2}Â{u2820} ADP-ribosylation by the ARTC family of ADP-ribosyltransferases (R-S-E ARTs) ·Â{u2820} ADP-ribosylation by the ARTD family of ADP-ribosyltransferases (H-Y-E ARTs) The book will provide readers a better understanding of ADP-ribosylating toxins and their endogenous relatives. This provides a basis for developing novel toxin-neutralizing drugs and drugs targeting endogenous ADP-ribosyltransferase relatives.

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