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Anna Shevchenko

Researcher at Max Planck Society

Publications -  76
Citations -  13854

Anna Shevchenko is an academic researcher from Max Planck Society. The author has contributed to research in topics: DNA replication & Proteome. The author has an hindex of 51, co-authored 73 publications receiving 13105 citations. Previous affiliations of Anna Shevchenko include European Bioinformatics Institute.

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A generic protein purification method for protein complex characterization and proteome exploration.

TL;DR: A generic procedure to purify proteins expressed at their natural level under native conditions using a novel tandem affinity purification (TAP) tag and Combined with mass spectrometry, the TAP strategy allows for the identification of proteins interacting with a given target protein.
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Exit from Mitosis Is Triggered by Tem1-Dependent Release of the Protein Phosphatase Cdc14 from Nucleolar RENT Complex

TL;DR: A mutation is identified, net1-1, that bypasses the lethality of tem1 delta and is a key component of a multifunctional complex, denoted RENT (for regulator of nucleolar silencing and telophase), that also contains Cdc14 and the silencing regulator Sir2.
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Cohesin's Binding to Chromosomes Depends on a Separate Complex Consisting of Scc2 and Scc4 Proteins

TL;DR: It is shown that Scc2p forms a complex with a novel protein, Scc4p, which is also necessary for sister cohesion, suggesting that a major role for the SCC2p/SCC4p complex is to facilitate the loading of cohesin complexes onto chromosomes.
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Promotion of NEDD8-CUL1 Conjugate Cleavage by COP9 Signalosome

TL;DR: It is proposed that the broad spectrum of activities previously attributed to CSN subunits—including repression of photomorphogenesis, activation of JUN, and activation of p27 nuclear export—underscores the importance of dynamic cycles of NEDD8 attachment and removal in biological regulation.
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The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4

TL;DR: Eukaryotic Set1Cs are H3 lysine 4 methyltransferases and are related to trxG action through association with Ash2 homologues, thus adding a new specificity and a new subclass of SET domain proteins known to methyl transferases.