SH2 DOMAINS - ELEMENTS THAT CONTROL PROTEIN INTERACTIONS DURING SIGNAL TRANSDUCTION

被引：38

作者：

HELDIN, CH

机构：

[1] Ludwig Institute for Cancer Research, Biomedical Center, S-751 24 Uppsala

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1991年 / 16卷 / 12期

关键词：

D O I：

10.1016/0968-0004(91)90175-U

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：

[No abstract available]

引用

页码：450 / 452

页数：3

共 17 条

[11] A TYROSINE-PHOSPHORYLATED CARBOXY-TERMINAL PEPTIDE OF THE FIBROBLAST GROWTH-FACTOR RECEPTOR (FLG) IS A BINDING-SITE FOR THE SH2 DOMAIN OF PHOSPHOLIPASE C-GAMMA-1
MOHAMMADI, M
HONEGGER, AM
ROTIN, D
FISCHER, R
BELLOT, F
LI, W
DIONNE, CA
JAYE, M
RUBINSTEIN, M
SCHLESSINGER, J
[J]. MOLECULAR AND CELLULAR BIOLOGY, 1991, 11 (10) : 5068 - 5078
[12] ACTIVATION OF THE PROTOONCOGENE P60C-SRC BY POINT MUTATIONS IN THE SH2 DOMAIN
OBRIEN, MC
FUKUI, Y
HANAFUSA, H
[J]. MOLECULAR AND CELLULAR BIOLOGY, 1990, 10 (06) : 2855 - 2862
[13] BCR SEQUENCES ESSENTIAL FOR TRANSFORMATION BY THE BCR-ABL ONCOGENE BIND TO THE ABL-SH2 REGULATORY DOMAIN IN A NON-PHOSPHOTYROSINE-DEPENDENT MANNER
PENDERGAST, AM
MULLER, AJ
HAVLIK, MH
MARU, Y
WITTE, ON
[J]. CELL, 1991, 66 (01) : 161 - 171
[14] A NONCATALYTIC DOMAIN CONSERVED AMONG CYTOPLASMIC PROTEIN-TYROSINE KINASES MODIFIES THE KINASE FUNCTION AND TRANSFORMING ACTIVITY OF FUJINAMI SARCOMA-VIRUS P130GAG-FPS
SADOWSKI, I
STONE, JC
PAWSON, T
[J]. MOLECULAR AND CELLULAR BIOLOGY, 1986, 6 (12) : 4396 - 4408
[15] A PROTEIN-TYROSINE PHOSPHATASE WITH SEQUENCE SIMILARITY TO THE SH2 DOMAIN OF THE PROTEIN-TYROSINE KINASES
SHEN, SH
BASTIEN, L
POSNER, BI
CHRETIEN, P
[J]. NATURE, 1991, 352 (6337) : 736 - 739
[16] CLONING OF PI3 KINASE ASSOCIATED P85 UTILIZING A NOVEL METHOD FOR EXPRESSION CLONING OF TARGET PROTEINS FOR RECEPTOR TYROSINE KINASES
SKOLNIK, EY
MARGOLIS, B
MOHAMMADI, M
LOWENSTEIN, E
FISCHER, R
DREPPS, A
ULLRICH, A
SCHLESSINGER, J
[J]. CELL, 1991, 65 (01) : 83 - 90
[17] SIGNAL TRANSDUCTION BY RECEPTORS WITH TYROSINE KINASE-ACTIVITY
ULLRICH, A
SCHLESSINGER, J
[J]. CELL, 1990, 61 (02) : 203 - 212

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