Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Philip E. Ryan"'
Autor:
Mariya S Liyasova, Ke Ma, Donna Voeller, Philip E Ryan, Jinqiu Chen, Rachel E Klevit, Stanley Lipkowitz
Publikováno v:
PLoS ONE, Vol 14, Iss 5, p e0216967 (2019)
Many receptor tyrosine kinases (RTKs, such as EGFR, MET) are negatively regulated by ubiquitination and degradation mediated by Cbl proteins, a family of RING finger (RF) ubiquitin ligases (E3s). Loss of Cbl protein function is associated with malign
Externí odkaz:
https://doaj.org/article/96dd9dd4f7ff4a2bbd1769476308f672
Autor:
Silvano Rakeem Daniels, Mariya Liyasova, Stephen C Kales, Marion M Nau, Philip E Ryan, Jeffrey E Green, Stanley Lipkowitz
Publikováno v:
PLoS ONE, Vol 14, Iss 7, p e0219143 (2019)
Receptor Tyrosine Kinase (RTK) signaling is essential for normal biological processes and disruption of this regulation can lead to tumor initiation and progression. Cbl proteins (Cbl, Cbl-b and Cbl-c) are a family of RING finger (RF) ubiquitin ligas
Externí odkaz:
https://doaj.org/article/79cd95f3885c45088a69cbd78b042ecb
Autor:
Philip E Ryan, Stephen C Kales, Rajgopal Yadavalli, Marion M Nau, Han Zhang, Stanley Lipkowitz
Publikováno v:
PLoS ONE, Vol 7, Iss 11, p e49428 (2012)
Cbl proteins (Cbl, Cbl-b and Cbl-c) are ubiquitin ligases that are critical regulators of tyrosine kinase signaling. In this study we identify a new Cbl-c interacting protein, Hydrogen peroxide Induced Construct 5 (Hic-5). The two proteins interact t
Externí odkaz:
https://doaj.org/article/28f9f8d7a876472da8f17bea2af14911
Autor:
Philip E. Ryan, Mariya S. Liyasova, Stanley Lipkowitz, Marion M. Nau, Jeffrey Green, Stephen C. Kales, Silvano Rakeem Daniels
Publikováno v:
PLoS ONE
PLoS ONE, Vol 14, Iss 7, p e0219143 (2019)
PLoS ONE, Vol 14, Iss 7, p e0219143 (2019)
Receptor Tyrosine Kinase (RTK) signaling is essential for normal biological processes and disruption of this regulation can lead to tumor initiation and progression. Cbl proteins (Cbl, Cbl-b and Cbl-c) are a family of RING finger (RF) ubiquitin ligas
Autor:
Donna Voeller, Rachel E. Klevit, Ke Ma, Mariya S. Liyasova, Jinqiu Chen, Philip E. Ryan, Stanley Lipkowitz
Publikováno v:
PLoS ONE
PLoS ONE, Vol 14, Iss 5, p e0216967 (2019)
PLoS ONE, Vol 14, Iss 5, p e0216967 (2019)
Many receptor tyrosine kinases (RTKs, such as EGFR, MET) are negatively regulated by ubiquitination and degradation mediated by Cbl proteins, a family of RING finger (RF) ubiquitin ligases (E3s). Loss of Cbl protein function is associated with malign
Publikováno v:
Biochemistry and Molecular Biology Education. 45:13-24
Translational science is an emerging field that holds great promise to accelerate the development of novel medical interventions. As the field grows, so does the demand for highly trained biomedical scientists to fill the positions that are being cre
Publikováno v:
Journal of Biological Chemistry. 285:23687-23698
Cbl proteins are ubiquitin ligases (E3s) that play a significant role in regulating tyrosine kinase signaling. There are three mammalian family members: Cbl, Cbl-b, and Cbl-c. All have a highly conserved N-terminal tyrosine kinase binding domain, a c
Publikováno v:
Trends in Biochemical Sciences. 31:79-88
Cbl proteins are regulators of signal transduction through many pathways and, consequently, regulate cell function and development. They are ubiquitin ligases that ubiquitinate and target many signaling molecules for degradation. The Cbl proteins the
Autor:
Ralph W deVere White, Hsing Jien Kung, Xu Bao Shi, Pierre Yves Desprez, Philip E. Ryan, Ruth Louise Vinall, Colin A. Baron, Jeffrey P. Gregg, Clifford G. Tepper
Publikováno v:
The Prostate. 65:375-389
BACKGROUND. Tumor suppressor p53 mutations are associated with the transition of prostate cancer to metastatic, hormone-refractory disease and stable expression of p53 gain-of-function (p53 GOF ) alleles support growth of LNCaP in androgen-depleted m
Publikováno v:
Cancer Research. 76:4542-4542
Ubiquitin ligases (E3s) are critical component of ubiquitination. In collaboration with ubiquitin-conjugating enzymes (E2s), E3s confer specificity to the ubiquitination process and direct the conjugation of ubiquitin to one or more lysines on the ta