A
Alex Vassilev
Researcher at National Institutes of Health
Publications - 29
Citations - 4631
Alex Vassilev is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Chromatin & Origin recognition complex. The author has an hindex of 22, co-authored 28 publications receiving 4341 citations.
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Journal ArticleDOI
DNA damage activates p53 through a phosphorylation–acetylation cascade
Kazuyasu Sakaguchi,Julio E. Herrera,Shin'ichi Saito,Toru Miki,Michael Bustin,Alex Vassilev,Carl W. Anderson,Ettore Appella +7 more
TL;DR: It is suggested that DNA damage enhances p53 activity as a transcription factor in part through carboxy-terminal acetylation that, in turn, is directed by amino- terminal phosphorylation.
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TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm
TL;DR: It is proposed that YAP65 regulates TEAD-dependent transcription in response to mitogenic signals, and YAP 65 also binds Src/Yes protein tyrosine kinases, and the carboxy-terminal acidic activation domain in YAP is the transcriptional activation domain for TEAD transcription factors.
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Overlapping but Distinct Patterns of Histone Acetylation by the Human Coactivators p300 and PCAF within Nucleosomal Substrates
R. Louis Schiltz,Craig A. Mizzen,Alex Vassilev,Richard G. Cook,C. David Allis,Yoshihiro Nakatani +5 more
TL;DR: The core histone residues acetylated in vitro by recombinant p300 and PCAF within mononucleosomes are determined, suggesting that PCAF-associated polypeptides do not alter the substrate specificity.
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HATs off: selective synthetic inhibitors of the histone acetyltransferases p300 and PCAF.
Ontario D. Lau,Ontario D. Lau,Tapas K. Kundu,Raymond E. Soccio,Slimane Ait-Si-Ali,Ehab M. Khalil,Alex Vassilev,Alan P. Wolffe,Yoshihiro Nakatani,Robert G. Roeder,Philip A. Cole,Philip A. Cole +11 more
TL;DR: In this paper, the authors describe the design, synthesis, and application of peptide CoA conjugates as selective HAT inhibitors for the transcriptional coactivators p300 and PCAF.
Journal ArticleDOI
Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase.
Eva Wolf,Alex Vassilev,Yasutaka Makino,Andrej Sali,Yoshihiro Nakatani,Stephen K. Burley,Stephen K. Burley +6 more
TL;DR: The X-ray structure of a canonical GCN5-related N-acetyltransferase (GNAT) bound to coenzyme A (CoA) has been determined at 2.3 A resolution and represents the catalytic core of this large enzyme superfamily.