Conjuring SNPs to detect associations

Reviver submitted, created time 1 year 5 months (www.nature.com)

"Human genome-wide association studies pose a challenge in identifying significant disease associations from nearly half a million statistical tests. A new report describes an especially promising approach, recently applied to the Wellcome Trust Case Control Consortium data sets, that uses the correlated structure of genomic variation to impute genotypes at missing sites and to test association with both observed and imputed SNPs.'

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Allelic association studies of genome wide association data can reveal errors in marker position assignments

DanyC submitted, created time 1 year 6 months (www.biomedcentral.com)

“Background Genome wide association (GWA) studies provide the opportunity to develop new kinds of analysis. Analysing pairs of markers from separate regions might lead to the detection of allelic association which might indicate an interaction between nearby genes. Method 396,591 markers typed in 541 subjects were studied. 7.8*10^10 pairs of markers were screened and those showing initial evidence for allelic association were subjected to more thorough investigation along with 10 flanking markers on either side. Results No evidence was detected for interaction

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Oxidative protein said catch me if you can!

angelfish submitted, created time 1 year 10 months (www.jcb.org)

“The intermembrane space (IMS) of mitochondria, the compartment that phylogenetically originated from the periplasm of bacteria, contains machinery to catalyze the oxidative folding of protein.This machinery introduces disulfide bonds into newly imported precursor proteins, thereby locking them in a folded conformation. Because folded proteins cannot traverse the translocase of the outer membrane, this stably traps the proteins in the mitochondria

1 comment | Blog It | Email It | Keywords: amyloid precursor protein scaffold protein protein association Gab-2 protein protein construct protein network protein-DNA interactions

HIV relation protein news:structural basis for viral late-domain binding to Alix

nomad submitted, created time 1 year 10 months (www.nature.com)

The modular protein Alix is a central node in endosomal-lysosomal trafficking and the budding of human immunodeficiency virus (HIV)-1. The Gag p6 protein of HIV-1 contains a LYPxnLxxL motif that is required for Alix-mediated budding and binds a region of Alix spanning residues 360–702. The structure of this fragment of Alix has the shape of the letter 'V' and is termed the V domain. The V domain has a topologically complex arrangement of 11 -helices, with connecting loops that cross three times between the two arms of the V

Submit comment | Blog It | Email It | Keywords: Alix HIV Gag p6 Alix V domain Protein design protein structure and function HIV infection protein association protein folding

WATER MEDIATION IN PROTEIN FOLDING AND MOLECULAR RECOGNITION