Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Maria A. Burnatowska-Hledin"'
Autor:
Bryan Kunkler, Daniel Salamango, Zachary J DeBruine, Caitlin Ploch, Shirley Dean, David Grossens, Michael P Hledin, Gabriel A Marquez, Julie Madden, Abigayle Schnell, Michael Short, Maria A Burnatowska-Hledin
Publikováno v:
PLoS ONE, Vol 13, Iss 5, p e0196760 (2018)
Angiogenesis is essential for cancer metastasis, thus the discovery and characterization of molecules that inhibit this process is important. Thalidomide is a teratogenic drug which is known to inhibit angiogenesis and effectively inhibit cancer meta
Externí odkaz:
https://doaj.org/article/92b4baccab6f43ce954b1cbeeaedde7e
Publikováno v:
The FASEB Journal. 32
Autor:
Shirley E. Bradley Dean, Zachary J. DeBruine, Steven P. Lewis, Richard Garrett, Stephanie Harrier, Maria A. Burnatowska-Hledin, Angelica N. Willis, Joe A. Habbouche, Megan Ludwig, Brian T. Kempers, Aaron D. Sayfie
Publikováno v:
Cell and tissue research. 368(1)
VACM-1/CUL5 is a member of the cullin family of proteins involved in the E3 ligase-dependent degradation of diverse proteins that regulate cellular proliferation. The ability of VACM-1/CUL5 to inhibit cellular growth is affected by its posttranslatio
Autor:
Gary L. Dewey, Bradley T. Andresen, Isabelle P. Le, Shirley E. Bradley Dean, Joseph L. Stodola, Inara B. Lazdins, Pete Haak, Maria A. Burnatowska-Hledin, Travis R. Ruch, Alyssa E. Johnson, James H. Resau, Ashleigh Sartor, Christopher C. Barney
Publikováno v:
Cell and Tissue Research. 349:527-539
VACM-1, a cul5 gene product, when overexpressed in vitro, has an antiproliferative effect. In vivo, VACM-1/cul5 is present in tissues involved in the regulation of water balance. Neither proteins targeted for VACM-1/cul5-specific degradation nor fact
Autor:
Angelica N. Willis, Steven P. Lewis, James H. Resau, Alyssa E. Johnson, Maria A. Burnatowska-Hledin
Publikováno v:
APMIS. 119:421-430
VACM-1, a cul-5 gene product, functions via an E3 ligase complex and when overexpressed, has an antiproliferative effect in many cell types. Overexpression of VACM-/cul5 cDNA mutated at the PKA-specific phosphorylation site at Ser730 reversed this ph
Autor:
Alyssa E. Johnson, Michael P. Hledin, Steven P. Lewis, Justin Lubbers, Danelle R. Graves, Emily Harper, Maria A. Burnatowska-Hledin, Gabriel Márquez
Publikováno v:
Cell Biology and Toxicology. 27:95-105
Vasopressin-activated calcium-mobilizing (VACM-1) protein is a cul-5 gene product that forms complexes with a subclass of ubiquitin E3 ligases involved in proteasomal protein degradation. The expression of VACM-1 cDNA in the T47D breast cancer cell l
Autor:
Anne Caitlin Short, Rachel Vankempen, Michael D. Seymour, Michael Short, Maria A. Burnatowska-Hledin
Publikováno v:
Biochemistry and Molecular Biology Education. 38:242-246
Practical instruction of proteomics concepts was provided using high-performance liquid chromatography coupled with a mass selective detection system (HPLC-MS) for the analysis of simulated protein digests. The samples were prepared from selected dip
Publikováno v:
Molecular and Cellular Biochemistry. 301:13-20
Vasopressin-activated calcium mobilizing receptor (VACM-1)/cullin 5 (cul 5) inhibits growth when expressed in T47D breast cancer cells by a mechanism that involves a decrease in MAPK phosphorylation and a decrease in the early growth response element
Autor:
R. Wilcox, Inara B. Lazdins, A.E. Zeneberg, Ashleigh Sartor, J.B. Kossoris, P. Zhao, Maria A. Burnatowska-Hledin, R. Shearer
Publikováno v:
Biochemical and Biophysical Research Communications. 343:1086-1093
We have sequenced a 4.9 kb clone (KLB22) which shares 99% sequence homology with the rabbit vasopressin-activated calcium mobilizing (VACM-1) protein. The 5′ terminus sequence of KLB22 cDNA (nucleotides 1–1961) is continuous and overlapping with
Publikováno v:
International review of cell and molecular biology. 313
Vasopressin-activated calcium-mobilizing (VACM-1)/cul5 is the least conserved member of a cullin protein family involved in the formation of E3-specific ligase complexes that are responsible for delivering the ubiquitin protein to their target substr