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  Analysis of Sumoylation

Pichler, A. (2008). Analysis of Sumoylation. Methods in Molecular Biology, 446, 131-138.

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 Creators:
Pichler, Andrea1, Author              
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1Department of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243644              

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Free keywords: SUMO; His-SUMO1; Ni2+ pull down; E3-ligase; RanBP2 IR1+M
 Abstract: Reversible attachment of SUMO (small ubiquitin related modifi er) regulates a large number of proteins and plays an important role in processes such as transcriptional regulation, nucleo-cytoplasmic transport, genome integrity, and cell cycle progression. The steady state level of most sumoylated proteins is very low, presumably caused by strictly regulated modifi cation and/or rapid cycles of modifi cation and de-modifi cation. This often causes a detection problem of sumoylation in vivo. One approach to overcome this obstacle is described here and involves enrich ment of sumoylated proteins under denaturing conditions. After sumoylation is veri fied, addressing its functional consequences is the logical next step. This will benefit signifi cantly from the availability of large quantities of modifi ed protein. A protocol for effi cient in vitro sumoylation of target proteins is described here. It makes use of an E3 ligase fragment that functions without target discrimination.

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Language(s): eng - English
 Dates: 2008
 Publication Status: Published in print
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 Rev. Type: Peer
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Title: Methods in Molecular Biology
  Other : Methods Mol. Biol.
Source Genre: Journal
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Publ. Info: US : Springer
Pages: - Volume / Issue: 446 Sequence Number: - Start / End Page: 131 - 138 Identifier: ISSN: 1064-3745
CoNE: https://pure.mpg.de/cone/journals/resource/954927725544