REGULATION BY THE AUTOPHOSPHORYLATION SITE IN OVEREXPRESSED PP60C-SRC

被引：124

作者：

KMIECIK, TE ^{[1
]}

JOHNSON, PJ ^{[1
]}

SHALLOWAY, D ^{[1
]}

机构：

[1] PENN STATE UNIV,DEPT MOLEC & CELL BIOL,UNIVERSITY PK,PA 16802

来源：

MOLECULAR AND CELLULAR BIOLOGY | 1988年 / 8卷 / 10期

关键词：

D O I：

10.1128/MCB.8.10.4541

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：

引用

页码：4541 / 4546

页数：6

共 26 条

[1]

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[3] FORMS OF PP60V-SRC ISOLATED FROM ROUS-SARCOMA VIRUS-TRANSFORMED CELLS [J].

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KING, CS .

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[6]

COOPER JA, 1987, ONCOGENE RES, V1, P297

[7] ACTIVATION OF THE PP60C-SRC KINASE BY MIDDLE ANTIGEN-T BINDING OR BY DEPHOSPHORYLATION [J].

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[8] RESTRICTION OF THE INVITRO AND INVIVO TYROSINE PROTEIN-KINASE ACTIVITIES OF PP60C-SRC RELATIVE TO PP60V-SRC [J].

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[9] LOCAL MUTAGENESIS OF ROUS-SARCOMA VIRUS - THE MAJOR SITES OF TYROSINE AND SERINE PHOSPHORYLATION OF P60SRC ARE DISPENSABLE FOR TRANSFORMATION [J].

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HANAFUSA, H .

CELL, 1983, 34 (02) :597-607

[10] REPLACEMENT OF INSULIN-RECEPTOR TYROSINE RESIDUES 1162 AND 1163 COMPROMISES INSULIN-STIMULATED KINASE-ACTIVITY AND UPTAKE OF 2-DEOXYGLUCOSE [J].

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EDERY, M ;

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CELL, 1986, 45 (05) :721-732

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