SUMO : methods and protocols /
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| Imprint: | New York, NY : Humana Press : Springer, [2016] ©2016 |
|---|---|
| Description: | 1 online resource (xi, 306 pages) : illustrations (some color) |
| Language: | English |
| Series: | Methods in molecular biology, 1064-3745 ; 1475 Methods in molecular biology (Clifton, N.J.) ; v. 1475. |
| Subject: | |
| Format: | E-Resource Book |
| URL for this record: | http://pi.lib.uchicago.edu/1001/cat/bib/11266528 |
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| 245 | 0 | 0 | |a SUMO : |b methods and protocols / |c edited by Manuel S. Rodriguez. |
| 264 | 1 | |a New York, NY : |b Humana Press : |b Springer, |c [2016] | |
| 264 | 4 | |c ©2016 | |
| 300 | |a 1 online resource (xi, 306 pages) : |b illustrations (some color) | ||
| 336 | |a text |b txt |2 rdacontent | ||
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| 338 | |a online resource |b cr |2 rdacarrier | ||
| 490 | 1 | |a Methods in molecular biology, |x 1064-3745 ; |v 1475 | |
| 504 | |a Includes bibliographical references and index. | ||
| 505 | 0 | 0 | |t Concepts and methodologies to study protein SUMOylation : an overview / |r Michael J. Matunis and Manuel S. Rodríguez -- |t Regulation of chromatin by dynamic SUMO modifications / |r Nicole R. Wilson and Mark Hochstrasser -- |t Reconstitution of the recombinant RanBP2 SUMO E3 ligase complex / |r Tobias Ritterhoff [and others] -- |t Production and purification of recombinant SUMOylated proteins using engineered bacteria / |r Frédérique Brockly, Marc Piechaczyk, and Guillaume Bossis -- |t Fluorescent in vitro assay to investigate paralog- specific SUMO conjugation / |r Nathalie Eisenhardt, Viduth K. Chaugule, and Andrea Pichler -- |t Identification and characterization of SUMO-SIM interactions / |r Koraljka Husnjak, Jan Keiten-Schmitz, and Stefan Müller -- |t Real-time surface plasmon resonance (SPR) for the analysis of interactions between SUMO traps and mono- or polySUMO moieties / |r Wendy Xolalpa, Manuel S. Rodríguez, and Patrick England -- |t Using biotinylated SUMO-traps to analyze SUMOylated proteins / |r Valérie Lang [and others] -- |t In vitro characterization of chain depolymerization activities of SUMO-specific proteases / |r Julia Eckhoff and R. Jürgen Dohmen -- |t Detection of protein SUMOylation in situ by proximity ligation assays / |r Umut Sahin [and others] -- |t In situ SUMOylation and DeSUMOylation assays : fluorescent methods to visualize SUMOylation and DeSUMOylation in permeabilized cells / |r Eri Yuasa and Hisato Saitoh -- |t Analysis of SUMOylated proteins in cells and in vivo using the BioSUMO strategy / |r Lucia Pirone [and others] -- |t Label-free identification and quantification of SUMO target proteins / |r Ivo A. Hendriks and Alfred C.O. Vertegaal -- |t Use of multimeric protein scaffolds for identifying multi-SUMO binding proteins / |r Elisa Aguilar-Martínez and Andrew D. Sharrocks -- |t Isolation of in vivo SUMOylated chromatin-bound proteins / |r Tasneem Bawa-Khalfe -- |t Identification of substrates of protein-group SUMOylation / |r Ivan Psakhye and Stefan Jentsch -- |t Tools to study SUMO conjugation in Caenorhabditis elegans / |r Federico Pelisch and Ronald T. Hay -- |t Purification of SUMO conjugates from Arabidopsis for mass spectrometry analysis / |r Thérèse C. Rytz, Marcus J. Miller, and Richard D. Vierstra -- |t Detection of SUMOylation in plasmodium falciparum / |r Katherine H. Reiter and Michael J. Matunis -- |t Systematic Localization and Identification of SUMOylation Substrates in Knock-In Mice Expressing Affinity-Tagged SUMO1 / |r Marilyn Tirard and Nils Brose. |
| 588 | 0 | |a Online resource; title from PDF title page (SpringerProtocol, viewed August 14, 2016). | |
| 520 | |a This volume explores various methodologies to study biochemical, molecular, and cellular biology aspects of some processes regulated by protein SUMOylation. SUMO: Methods and Protocols is organized into four parts, and starts with an historical overview on protein SUMOylation and a presentation of the methods included in the book. The first part also includes a review on chromatin regulation by dynamic SUMO modifications. The second part focuses on in vitro techniques, including biochemical methods to study mechanistic aspects of protein SUMOylation. The third part includes protocols to be used with cell cultures, which often are the first approaches used in most laboratories. The final part includes methodologies adapted for the analysis in vivo using distinct model organisms. Written in the highly successful Methods in Molecular Biology series format, chapters include a brief introduction to the subject, a list of necessary materials and reagents, a step-by-step reproducible laboratory protocol ending with a Notes section on troubleshooting tips, and tips and strategies to avoid known pitfalls. Unique and cutting-edge, SUMO: Methods and Protocols provides a comprehensive source of protocols for specialists and researchers not familiar with this vital system. | ||
| 650 | 0 | |a Small ubiquitin-related modifiers |v Laboratory manuals. | |
| 650 | 0 | |a Sumoylation |x Methodology. | |
| 650 | 0 | |a Molecular biology |x Methodology. | |
| 650 | 2 | |a Small Ubiquitin-Related Modifier Proteins |x analysis | |
| 650 | 2 | |a Small Ubiquitin-Related Modifier Proteins |x physiology | |
| 650 | 6 | |a Biologie moléculaire |x Méthodologie. | |
| 650 | 7 | |a Biochemistry. |2 bicssc | |
| 650 | 7 | |a Science |x Life Sciences |x Biochemistry. |2 bisacsh | |
| 650 | 7 | |a Small ubiquitin-related modifiers |2 fast | |
| 650 | 7 | |a Molecular biology |x Methodology |2 fast | |
| 655 | 2 | |a Laboratory Manual | |
| 655 | 7 | |a Laboratory manuals |2 fast | |
| 655 | 7 | |a Laboratory manuals. |2 lcgft |0 http://id.loc.gov/authorities/genreForms/gf2014026120 | |
| 655 | 7 | |a Manuels de laboratoire. |2 rvmgf | |
| 700 | 1 | |a Rodriguez, Manuel S., |e editor. | |
| 776 | 0 | 8 | |i Print version: |t SUMO. |d New York : Humana Press, [2016] |z 9781493963560 |w (DLC) 2016945171 |w (OCoLC)948561438 |
| 830 | 0 | |a Methods in molecular biology (Clifton, N.J.) ; |v v. 1475. |x 1064-3745 |0 http://id.loc.gov/authorities/names/n92002874 | |
| 856 | 4 | 0 | |u https://link.springer.com/10.1007/978-1-4939-6358-4 |y Springer Nature |
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