标题
Receptor tyrosine kinases with intracellular pseudokinase domains
作者
关键词
-
出版物
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 41, Issue 4, Pages 1029-1036
出版商
Portland Press Ltd.
发表日期
2013-07-18
DOI
10.1042/bst20130104
参考文献
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注意:仅列出部分参考文献,下载原文获取全部文献信息。- Oncogenic ERBB3 Mutations in Human Cancers
- (2013) Bijay S. Jaiswal et al. CANCER CELL
- Assessing the range of kinase autoinhibition mechanisms in the insulin receptor family
- (2012) Stephen C. Artim et al. BIOCHEMICAL JOURNAL
- The complex world of WNT receptor signalling
- (2012) Christof Niehrs NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Ror1 Is a Pseudokinase That Is Crucial for Met-Driven Tumorigenesis
- (2011) A. Gentile et al. CANCER RESEARCH
- Overcoming resistance to tyrosine kinase inhibitors: Lessons learned from cancer cells treated with EGFR antagonists
- (2011) Brent N. Rexer et al. CELL CYCLE
- Rapid Phospho-Turnover by Receptor Tyrosine Kinases Impacts Downstream Signaling and Drug Binding
- (2011) Laura B. Kleiman et al. MOLECULAR CELL
- Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms
- (2011) Natalia Jura et al. MOLECULAR CELL
- A Raf-induced allosteric transition of KSR stimulates phosphorylation of MEK
- (2011) Damian F. Brennan et al. NATURE
- The pseudokinase domain of JAK2 is a dual-specificity protein kinase that negatively regulates cytokine signaling
- (2011) Daniela Ungureanu et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Mutation that blocks ATP binding creates a pseudokinase stabilizing the scaffolding function of kinase suppressor of Ras, CRAF and BRAF
- (2011) J. Hu et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Cell Signaling by Receptor Tyrosine Kinases
- (2010) Mark A. Lemmon et al. CELL
- Kinases as targets in the treatment of solid tumors
- (2010) Georgios Giamas et al. CELLULAR SIGNALLING
- Pseudokinases-remnants of evolution or key allosteric regulators?
- (2010) Elton Zeqiraj et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- Development trends for human monoclonal antibody therapeutics
- (2010) Aaron L. Nelson et al. NATURE REVIEWS DRUG DISCOVERY
- Targeting non-malignant disorders with tyrosine kinase inhibitors
- (2010) Friedrich Grimminger et al. NATURE REVIEWS DRUG DISCOVERY
- COSMIC: mining complete cancer genomes in the Catalogue of Somatic Mutations in Cancer
- (2010) S. A. Forbes et al. NUCLEIC ACIDS RESEARCH
- ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation
- (2010) Fumin Shi et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Ror2 Receptor Requires Tyrosine Kinase Activity to Mediate Wnt5A Signaling
- (2009) Amanda Mikels et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3
- (2009) N. Jura et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- ROP2 from Toxoplasma gondii: A Virulence Factor with a Protein-Kinase Fold and No Enzymatic Activity
- (2009) Gilles Labesse et al. STRUCTURE
- Structure of the Pseudokinase VRK3 Reveals a Degraded Catalytic Site, a Highly Conserved Kinase Fold, and a Putative Regulatory Binding Site
- (2009) Eric D. Scheeff et al. STRUCTURE
- ATP and MO25α Regulate the Conformational State of the STRADα Pseudokinase and Activation of the LKB1 Tumour Suppressor
- (2009) Elton Zeqiraj et al. PLOS BIOLOGY
- CASK Functions as a Mg2+-Independent Neurexin Kinase
- (2008) Konark Mukherjee et al. CELL
- Acquired resistance to tyrosine kinase inhibitors during cancer therapy
- (2008) Jeffrey A Engelman et al. CURRENT OPINION IN GENETICS & DEVELOPMENT
- Src family kinases are required for WNT5 signaling through the Derailed/RYK receptor in the Drosophila embryonic central nervous system
- (2008) R. R. Wouda et al. DEVELOPMENT
- The Deleted in Brachydactyly B Domain of ROR2 Is Required for Receptor Activation by Recruitment of Src
- (2008) Shiva Akbarzadeh et al. PLoS One
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