Zobrazeno 1 - 10
of 57
pro vyhledávání: '"Marion M. Nau"'
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
Publikováno v:
PLoS ONE, Vol 9, Iss 1, p e87116 (2014)
The Cbl proteins (Cbl, Cbl-b, and Cbl-c) are a highly conserved family of RING finger ubiquitin ligases (E3s) that function as negative regulators of tyrosine kinases in a wide variety of signal transduction pathways. In this study, we identify a new
Externí odkaz:
https://doaj.org/article/6a03ab554f364d1982b7553d1cc0a240
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:
Silvano R. Daniels, Stephen C. Kales, Mariya Liyasova, Marion M. Nau, Phil E. Ryan, Jeffrey E. Green, Stanley Lipkowitz
Publikováno v:
Cancer Research. 78:555-555
Receptor Tyrosine Kinase (RTK) signaling, which is essential for cellular growth and proliferation, can lead to malignant transformation and tumorigenesis when aberrantly activated. Cbl proteins (Cbl, Cbl-b, and Cbl-c) are a conserved family of RING
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:
Stan Lipkowitz, Marion M. Nau
Publikováno v:
Gene. 308:103-113
The genomic organization of cbl genes from a variety of mammalian and non-mammalian species was determined by a combination of cloning and database searches. Humans and mice have three cbl genes (c-cbl, 1 cblb, and cblc) which show remarkable conserv
Autor:
Kristie Gehlhaus, Natasha J. Caplen, Jason J. Pitt, Jennifer L Dine, Magdalena Grandin, Sirisha Chakka, Stanley Lipkowitz, Sireesha V. Garimella, Marion M. Nau
Publikováno v:
Breast Cancer Research : BCR
Introduction Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) binds to its receptors, TRAIL-receptor 1 (TRAIL-R1) and TRAIL-receptor 2 (TRAIL-R2), leading to apoptosis by activation of caspase-8 and the downstream executioner caspases,
Autor:
Mauricio Cuello, Marion M. Nau, Alessandra Magnifico, Allan M. Weissman, Yaffa R. Rubinstein, Yosef Yarden, Stan Lipkowitz, Seth A. Ettenberg
Publikováno v:
Journal of Biological Chemistry. 276:27677-27684
Cbl proteins function as ubiquitin protein ligases for the activated epidermal growth factor receptor and, thus, negatively regulate its activity. Here we show that Cbl-b is ubiquitinated and degraded upon activation of the receptor. Epidermal growth