Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 407949
Title Proteomic Analysis of Mouse Oocytes Reveals 28 Candidate Factors of the "Reprogrammome"
Author(s) Pfeiffer, M.J.; Siatkowski, M.; Paudel, Y.; Balbach, S.T.; Baeumer, N.; Crosetto, N.; Drexler, H.C.A.; Fuellen, G.; Boiani, M.
Source Journal of Proteome Research 10 (2011)5. - ISSN 1535-3893 - p. 2140 - 2153.
DOI https://doi.org/10.1021/pr100706k
Department(s) Animal Breeding and Genetics
WIAS
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) cell-cycle progression - embryonic stem-cells - b histone acetyltransferase - double-strand breaks - gene-expression - messenger-rna - arginine methyltransferase-1 - dna methyltransferases - mammalian oocytes - protein-synthesis
Abstract The oocyte is the only cell of the body that can reprogram transplanted somatic nuclei and sets the gold standard for all reprogramming methods. Therefore, an in-depth characterization of its proteome holds promise to advance our understanding of reprogramming and germ cell biology. To date, limitations on oocyte numbers and proteomic technology have impeded this task, and the search for reprogramming factors has been conducted in embryonic stem (ES) cells instead. Here, we present the proteome of metaphase II mouse oocytes to a depth of 3699 proteins, which substantially extends the number of proteins identified until now in mouse oocytes and is comparable by size to the proteome of undifferentiated mouse ES cells. Twenty-eight oocyte proteins, also detected in ES cells, match the criteria of our multilevel approach to screen for reprogramming factors, namely nuclear localization, chromatin modification, and catalytic activity. Our oocyte proteome catalog thus advances the definition of the "reprogrammome", the set of molecules--proteins, RNAs, lipids, and small molecules--that enable reprogramming
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