K
Karen J. Buchkovich
Researcher at Cold Spring Harbor Laboratory
Publications - 17
Citations - 4060
Karen J. Buchkovich is an academic researcher from Cold Spring Harbor Laboratory. The author has contributed to research in topics: Retinoblastoma-like protein 1 & Retinoblastoma protein. The author has an hindex of 11, co-authored 17 publications receiving 4020 citations. Previous affiliations of Karen J. Buchkovich include New York University & Cephalon.
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Journal ArticleDOI
Association between an oncogene and an anti-oncogene: the adenovirus E1A proteins bind to the retinoblastoma gene product.
Peter Whyte,Peter Whyte,Karen J. Buchkovich,Jonathan M. Horowitz,Stephen H. Friend,Stephen H. Friend,Margaret Raybuck,Margaret Raybuck,Robert A. Weinberg,Ed Harlow +9 more
TL;DR: The interaction between E1A and the retinoblastoma gene product is the first demonstration of a physical link between an oncogene and an anti-oncogene.
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The retinoblastoma protein is phosphorylated during specific phases of the cell cycle.
TL;DR: In this paper, the authors look for changes in p105-RB that may regulate its activity during the cell cycle, and generate synchronized cell populations and follow their progression through the cell-cycle.
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Point mutational inactivation of the retinoblastoma antioncogene
Jonathan M. Horowitz,David W. Yandell,Sang Ho Park,Susan Canning,Peter Whyte,Karen J. Buchkovich,Ed Harlow,Robert A. Weinberg,Thaddeus P. Dryja +8 more
TL;DR: A novel, aberrant Rb protein detected in J82 bladder carcinoma cells was not able to form a complex with E1A and was less stable than p105-Rb, which was observed to result from a single point mutation within a splice acceptor sequence in J 82 genomic DNA.
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The retinoblastoma protein is phosphorylated on multiple sites by human cdc2.
TL;DR: Using tryptic phosphopeptide mapping, it is shown that pRB is phosphorylated on multiple serine and threonine residues in vivo and that many of these phosphorylation events can be mimicked in vitro using purified p34cdc2.
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The cellular 107K protein that binds to adenovirus E1A also associates with the large T antigens of SV40 and JC virus
TL;DR: In human cells, the large T antigens of SV40 or JC virus also form complexes with 107K, suggesting that these associations may represent another component of a common mechanism for transformation between adenoviruses and polyoma viruses.