Comparison of next generation sequencing (NGS) - (SNPs) and capillary electrophoresis (CE) - (STRs) in the genetic analysis of human remains.

A pilot study was performed using two different DNA technology platforms conducted by two laboratories to analyze DNA extracted from 83-year-old, human male skeletal remains from 16 individuals, of which there are no other viable means to identify these war victims. The workflow of the more recent developed ForenSeq Kintelligence Kit and next generation sequencing was compared to that of the standard capillary electrophoresis - short tandem repeat (STR) method (Power Plex ESX17 and Y23 Systems). The findings indicate that greater amount of useful genetic data can be gained with the Kintelligence system across the range of samples under study and particularly for samples in which partial or no STR profiles are obtained.

A global analysis of Y-chromosomal haplotype diversity for 23 STR loci.

In a worldwide collaborative effort, 19,630 Y-chromosomes were sampled from 129 different populations in 51 countries. These chromosomes were typed for 23 short-tandem repeat (STR) loci (DYS19, DYS389I, DYS389II, DYS390, DYS391, DYS392, DYS393, DYS385ab, DYS437, DYS438, DYS439, DYS448, DYS456, DYS458, DYS635, GATAH4, DYS481, DYS533, DYS549, DYS570, DYS576, and DYS643) and using the PowerPlex Y23 System (PPY23, Promega Corporation, Madison, WI). Locus-specific allelic spectra of these markers were determined and a consistently high level of allelic diversity was observed.

Genetic population study of 11 Y chromosome STR loci in Greece.

Statistical properties of eleven Y chromosome Short Tandem Repeat (STR) markers were analyzed (DYS391, DYS389I, DYS439, DYS389II, DYS438, DYS437, DYS19, DYS392, DYS393, DYS390 and DYS385) in a Greek population sample. The 200 subjects where distributed across Greece, from various Peripheries. 182 distinct haplotypes were found.

Identification of the retinol-binding protein (RBP) interaction site and functional state of RBPs for the membrane receptor.

This laboratory has advanced a model whereby retinol is transported around the body bound to retinol-binding protein (RBP), is transferred across the membrane of cells by a specific receptor/transporter, and is picked up from the membrane by an intracellular homolog, cellular retinol-binding protein (CRBP). This process involves a number of protein-protein interactions, and we hypothesized that conformational changes were an integral part of the retinol transfer mechanism. Previously we identified the potential interaction site on RBP for its membrane receptor.