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Anastasia Wyce

Research Profile

Chemicals & Drugs

Living Beings

Saccharomyces cerevisiae

Phenomena

Physiology

Genes & Molecular Sequences

Amino Acid Sequences

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Procedures

Chromatin Immunoprecipitation

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Publications

TOP 3
Anastasia Wyce; Yuchen Bai; Sunil Nagpal; Catherine C Thompson
Research Resource: The androgen receptor modulates expression of genes with critical roles in muscle development and function.
Xiao-Yong Zhang; Maya Varthi; Stephen M Sykes; Charles Phillips; Claude Warzecha; Wenting Zhu; Anastasia Wyce; Alan W Thorne; Shelley L Berger; Steven B McMahon
The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression.
Anastasia Wyce; Tiao Jiang Xiao; Kelly A Whelan; Christine Kosman; Wendy Walter; Dirk Eick; Timothy R Hughes; Nevan J Krogan; Brian D Strahl; Shelley L Berger
H2B ubiquitylation acts as a barrier to Ctk1 nucleosomal recruitment prior to removal by Ubp8 within a SAGA-related complex.

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All Publications

2010: Anastasia Wyce; Yuchen Bai; Sunil Nagpal; Catherine C Thompson
Research Resource: The androgen receptor modulates expression of genes with critical roles in muscle development and function.
Molecular endocrinology (Baltimore, Md.) 2010;24(8):1665-74.
2008: Xiao-Yong Zhang; Maya Varthi; Stephen M Sykes; Charles Phillips; Claude Warzecha; Wenting Zhu; Anastasia Wyce; Alan W Thorne; Shelley L Berger; Steven B McMahon
The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression.
Molecular cell 2008;29(1):102-11.
2007: Anastasia Wyce; Tiao Jiang Xiao; Kelly A Whelan; Christine Kosman; Wendy Walter; Dirk Eick; Timothy R Hughes; Nevan J Krogan; Brian D Strahl; Shelley L Berger
H2B ubiquitylation acts as a barrier to Ctk1 nucleosomal recruitment prior to removal by Ubp8 within a SAGA-related complex.
Molecular cell 2007;27(2):275-88.
2006: Vinod Nayak; Kehao Zhao; Anastasia Wyce; Marc F Schwartz; Wan-Sheng Lo; Shelley L Berger; Ronen Marmorstein
Structure and dimerization of the kinase domain from yeast Snf1, a member of the Snf1/AMPK protein family.
Structure (London, England : 1993) 2006;14(3):477-85.
2005: N C Tolga Emre; Kristin Ingvarsdottir; Anastasia Wyce; Adam Wood; Nevan J Krogan; Karl W Henry; Keqin Li; Ronen Marmorstein; Jack F Greenblatt; Ali Shilatifard; Shelley L Berger
Maintenance of low histone ubiquitylation by Ubp10 correlates with telomere-proximal Sir2 association and gene silencing.
Molecular cell 2005;17(4):585-94.
2005: Kristin Ingvarsdottir; Nevan J Krogan; N C Tolga Emre; Anastasia Wyce; Natalie J Thompson; Andrew Emili; Timothy R Hughes; Jack F Greenblatt; Shelley L Berger
H2B ubiquitin protease Ubp8 and Sgf11 constitute a discrete functional module within the Saccharomyces cerevisiae SAGA complex.
Molecular and cellular biology 2005;25(3):1162-72.
2004: Anastasia Wyce; Karl W Henry; Shelley L Berger
H2B ubiquitylation and de-ubiquitylation in gene activation.
Novartis Foundation symposium 2004;259():63-73; discussion 73-7, 163-9.
2003: Karl W Henry; Anastasia Wyce; Wan-Sheng Lo; Laura J Duggan; N C Tolga Emre; Cheng-Fu Kao; Lorraine Pillus; Ali Shilatifard; Mary Ann Osley; Shelley L Berger
Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8.
Genes & development 2003;17(21):2648-63.
2002: Westley J Friesen; Anastasia Wyce; Sergey Paushkin; Linda Abel; Juri Rappsilber; Matthias Mann; Gideon Dreyfuss
A novel WD repeat protein component of the methylosome binds Sm proteins.
The Journal of biological chemistry 2002;277(10):8243-7.
2001: Westley J Friesen; Sergey Paushkin; Anastasia Wyce; Séverine Massenet; G S Pesiridis; Gregory D Van Duyne; Juri Rappsilber; Matthias Mann; Gideon Dreyfuss
The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins.
Molecular and cellular biology 2001;21(24):8289-300.
2001: Westley J Friesen; Séverine Massenet; Sergey Paushkin; Anastasia Wyce; Gideon Dreyfuss
SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets.
Molecular cell 2001;7(5):1111-7.