Cargando…
Designing a HER2/neu promoter to drive α1,3galactosyltransferase expression for targeted anti-αGal antibody-mediated tumor cell killing
INTRODUCTION: Our goal was to specifically render tumor cells susceptible to natural cytolytic anti-αGal antibodies by using a murine α1,3galactosyltransferase (mαGalT) transgene driven by a designed form of HER2/neu promoter (pNeu), the transcription of which is frequently observed to be above basa...
Autores principales: | Lanteri, Marion, Ollier, Laurence, Giordanengo, Valérie, Lefebvre, Jean-Claude |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2005
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1175063/ https://www.ncbi.nlm.nih.gov/pubmed/15987454 http://dx.doi.org/10.1186/bcr1034 |
Ejemplares similares
-
Characteristics of α-Gal epitope, anti-Gal antibody, α1,3 galactosyltransferase and its clinical exploitation (Review)
por: HUAI, GUOLI, et al.
Publicado: (2016) -
Alpha-Gal Syndrome: Involvement of Amblyomma americanum α-D-Galactosidase and β-1,4 Galactosyltransferase Enzymes in α-Gal Metabolism
por: Sharma, Surendra Raj, et al.
Publicado: (2021) -
Screening and purification of NanB sialidase from Pasteurella multocida with activity in hydrolyzing sialic acid Neu5Acα(2–6)Gal and Neu5Acα(2–3)Gal
por: Nugroho, Christian Marco Hadi, et al.
Publicado: (2022) -
Distribution of Bacterial α1,3-Galactosyltransferase Genes in the Human Gut Microbiome
por: Montassier, Emmanuel, et al.
Publicado: (2020) -
Alpha 1,3-Galactosyltransferase Deficiency in Pigs Increases Sialyltransferase Activities That Potentially Raise Non-Gal Xenoantigenicity
por: Park, Jong-Yi, et al.
Publicado: (2011)