共 66 条
IDENTIFICATION OF CELLULAR PROTEINS THAT CAN INTERACT SPECIFICALLY WITH THE T/E1A-BINDING REGION OF THE RETINOBLASTOMA GENE-PRODUCT
被引:538
作者:

KAELIN, WG
论文数: 0 引用数: 0
h-index: 0
机构: HARVARD UNIV,SCH MED,BOSTON,MA 02115

PALLAS, DC
论文数: 0 引用数: 0
h-index: 0
机构: HARVARD UNIV,SCH MED,BOSTON,MA 02115

DECAPRIO, JA
论文数: 0 引用数: 0
h-index: 0
机构: HARVARD UNIV,SCH MED,BOSTON,MA 02115

KAYE, FJ
论文数: 0 引用数: 0
h-index: 0
机构: HARVARD UNIV,SCH MED,BOSTON,MA 02115

LIVINGSTON, DM
论文数: 0 引用数: 0
h-index: 0
机构: HARVARD UNIV,SCH MED,BOSTON,MA 02115
机构:
[1] HARVARD UNIV,SCH MED,BOSTON,MA 02115
[2] NCI,USN,MED ONCOL BRANCH,BETHESDA,MD 20814
[3] UNIFORMED SERV UNIV HLTH SCI,BETHESDA,MD 20814
来源:
关键词:
D O I:
10.1016/0092-8674(91)90236-R
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
The SV40 T antigen (T)/adenovirus E1A-binding domain of the retinoblastoma gene product (pRB) has been fused to S. japonicum glutathione S-transferase, and the chimera, bound to insoluble glutathione, was used to search for cellular proteins that can interact specifically with pRB. At least seven such proteins were detected in extracts of multiple human tumor cell lines. These proteins failed to bind to a family of pRB fusion proteins that harbor inactivating mutations in the T/E1A-binding domain and to the wild-type fusion protein in the presence of a peptide replica of the pRB-binding domain of T. Therefore, the binding of one or more of these proteins may contribute to the growth-suppressing function of pRB.
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页码:521 / 532
页数:12
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