Publications by authors named "Groeneger A"
A rapid single-tube multiplex polymerase chain reaction assay for the seven most prevalent alpha-thalassemia deletions and alphaalphaalpha(anti 3.7) alpha-globin gene triplication.
Hemoglobin
January 2010
alpha-Globin gene triplications may exacerbate the alpha chain and beta chain imbalance in beta-thalassemia (beta-thal) and may compensate for the effect of alpha-globin gene deletion in alpha-thal. Identification of an alpha-globin gene triplication is, therefore, valuable in predicting the clinical phenotype of the thalassemias. To be able to detect alpha-globin gene triplications, we have modified an existing multiplex polymerase chain reaction (PCR) assay for the seven most prevalent alpha-globin gene deletions by incorporating two triplication-specific primers and concurrently substituting one of the original primers by a newly designed primer.
View Article and Find Full Text PDFcDNA-AFLP is a genome-wide expression analysis technology that does not require any prior knowledge of gene sequences. This PCR-based technique combines a high sensitivity with a high specificity, allowing detection of rarely expressed genes and distinguishing between homologous genes. In this report, we validated quantitative expression data of 110 cDNA-AFLP fragments in yeast with DNA microarrays and GeneChip data.
View Article and Find Full Text PDFArticle Synopsis
- HIV integrase (IN) is crucial for the integration of viral DNA into host DNA, involving three functional domains: catalytic, DNA binding, and N-terminal regions.
- Mutant proteins D116I (which binds DNA but lacks an active site) and C delta 73 (which has an active site but does not bind DNA) cannot function individually but can work together, indicating that IN operates as an oligomer with distinct roles for different subunits.
- Three classes of mutants based on these domains can complement each other's functions, particularly when N- and C-terminal regions are combined in one molecule for optimal efficiency.
Mutational analysis of the integrase protein of human immunodeficiency virus type 2.
Proc Natl Acad Sci U S A
October 1992
Article Synopsis
- Purified integrase (IN) protein plays a critical role in nicking and integrating viral DNA into target DNA, with a study conducted on 43 site-directed mutants of HIV-2 IN to assess its functional activities.
- Three specific mutations (Asp-64-->Val, Asp-116-->Ile, Glu-152-->Leu) were found to nearly eliminate IN function, while 25 other mutations showed no impact.
- Certain mutations affected specific functions differently, highlighting the importance of the zinc finger-like motif at the amino terminus and indicating that Asn-120 is key in determining integration-site preference.