In JoVE (1)
Other Publications (1)
Articles by Adam Benjamin in JoVE
En praktisk og Novel metode for å utvinne genomisk DNA fra Blodprøverør Kits for Plasma Protein Preservation Jon Waters1, Vishal Dhere1, Adam Benjamin1, Arvind Sekar1, Archana Kumar1, Sampath Prahalad2, David T. Okou1, Subra Kugathasan1 1Division of Gastroenterology, Hepatology and Nutrition, Department of Pediatrics, Emory University School of Medicine and Children's Health Care of Atlanta, 2Division of Rheumatology, Department of Pediatrics, Emory University School of Medicine and Children's Health Care of Atlanta Vi beskriver en ny metode for å isolere genomisk DNA fra blod samles for plasma / serologi. Etter plasma-samlingen, er den kompakterte blod vanligvis kassert. Vår nye fremgangsmåte representerer en betydelig forbedring i forhold til eksisterende metoder og gjør DNA tilgjengelig og plasma fra en enkelt kilde, uten å be om ytterligere blod.
Other articles by Adam Benjamin on PubMed
Fusion Tyrosine Kinase NPM-ALK Deregulates MSH2 and Suppresses DNA Mismatch Repair Function Novel Insights into a Potent Oncoprotein The American Journal of Pathology. Jul, 2011 | Pubmed ID: 21703420 The fusion tyrosine kinase NPM-ALK is central to the pathogenesis of ALK-positive anaplastic large cell lymphoma (ALK(+)ALCL). We recently identified that MSH2, a key DNA mismatch repair (MMR) protein integral to the suppression of tumorigenesis, is an NPM-ALK-interacting protein. In this study, we found in vitro evidence that enforced expression of NPM-ALK in HEK293 cells suppressed MMR function. Correlating with these findings, six of nine ALK(+)ALCL tumors displayed evidence of microsatellite instability, as opposed to none of the eight normal DNA control samples (P = 0.007, Student's t-test). Using co-immunoprecipitation, we found that increasing levels of NPM-ALK expression in HEK293 cells resulted in decreased levels of MSH6 bound to MSH2, whereas MSH2Â·NPM-ALK binding was increased. The NPM-ALKÂ·MSH2 interaction was dependent on the activation/autophosphorylation of NPM-ALK, and the Y191 residue of NPM-ALK was a crucial site for this interaction and NPM-ALK-mediated MMR suppression. MSH2 was found to be tyrosine phosphorylated in the presence of NPM-ALK. Finally, NPM-ALK impeded the expected DNA damage-induced translocation of MSH2 out of the cytoplasm. To conclude, our data support a model in which the suppression of MMR by NPM-ALK is attributed to its ability to interfere with normal MSH2 biochemistry and function.