Title |
p21-Activated Kinase 1 (Pak1) Phosphorylates BAD Directly at Serine 111 In Vitro and Indirectly through Raf-1 at Serine 112
|
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Published in |
PLOS ONE, November 2011
|
DOI | 10.1371/journal.pone.0027637 |
Pubmed ID | |
Authors |
Diana Z. Ye, Shenghao Jin, Ya Zhuo, Jeffrey Field |
Abstract |
Cell survival depends on the balance between protective and apoptotic signals. When the balance of signals tips towards apoptosis, cells undergo programmed cell death. This balance has profound implications in diseases including cancer. Oncogenes and tumor suppressors are mutated to promote cell survival during tumor development, and many chemotherapeutic drugs kill tumor cells by stimulating apoptosis. BAD is a pro-apoptotic member of the Bcl-2 family of proteins, which can be phosphorylated on numerous sites to modulate binding to Bcl-2 and 14-3-3 proteins and inhibit its pro-apoptotic activities. One of the critical phosphorylation sites is the serine 112 (S112), which can be phosphorylated by several kinases including Pak1. |
X Demographics
Geographical breakdown
Country | Count | As % |
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Unknown | 1 | 100% |
Demographic breakdown
Type | Count | As % |
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Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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United Kingdom | 1 | 3% |
Denmark | 1 | 3% |
Germany | 1 | 3% |
Unknown | 35 | 92% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 11 | 29% |
Researcher | 9 | 24% |
Student > Bachelor | 4 | 11% |
Student > Postgraduate | 3 | 8% |
Student > Doctoral Student | 3 | 8% |
Other | 5 | 13% |
Unknown | 3 | 8% |
Readers by discipline | Count | As % |
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Agricultural and Biological Sciences | 16 | 42% |
Biochemistry, Genetics and Molecular Biology | 8 | 21% |
Medicine and Dentistry | 3 | 8% |
Environmental Science | 2 | 5% |
Unspecified | 1 | 3% |
Other | 5 | 13% |
Unknown | 3 | 8% |