Disorders of hemoglobin

Protein misfolding and deposition underlie an increasing number of debili-tating human disorders. Alzheimer’s disease is pathologically characterized by the presence of numerous insoluble amyloid plaques in the brain, com-posed primarily of the 42 amino acid humanb-amyloid peptide (Ab42). Disease-linked mutations in Ab42 occur in or near a central hydrophobic cluster comprising residues 17–21.

11p dell39 27-03-2013 37 5   Download

Oculopharyngeal muscular dystrophy (OPMD) is an autosomal dominant disease that usually manifests itself within the fifth decade. The most prom-inent symptoms are progressive ptosis, dysphagia, and proximal limb mus-cle weakness. The disorder is caused by trinucleotide (GCG) expansions in the N-terminal part of the poly(A)-binding protein 1 (PABPN1) that result in the extension of a 10-alanine segment by up to seven more alanines.

10p inspiron33 23-03-2013 49 4   Download

Lithium is a therapeutic agent commonly used to treat bipolar disorder and its beneficial effects are thought to be due to a combination of activa-tion of the Wnt⁄b-catenin pathway via inhibition of glycogen synthase kin-ase-3b and depletion of the inositol pool via inhibition of the inositol monophosphatase-1.

17p galaxyss3 19-03-2013 24 3   Download

The potent immunomodulatory, anti-inflammatory and procoagulant properties of protein no. 4 secreted from the rat seminal vesicle epithelium (SV-IV) have previously been found to be modulated by a supramolecular monomer–trimer equilibrium.

12p media19 05-03-2013 39 3   Download

Coagulation factor XI (FXI) is the zymogen of a serine protease that, when converted to its active form, contributes to blood coagulation through proteolytic activation of factor IX. FXI deficiency is typically an autosomal recessive disorder, characterized by bleeding symptoms mainly associated with injury or surgery.

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Conformational diseases constitute a group of heterologous disorders in which a constituent host protein undergoes changes in conformation, lead-ing to aggregation and deposition. To understand the molecular mecha-nisms of the process of amyloid fibril formation, numerousin vitro and in vivo studies, including model and pathologically relevant proteins, have been performed.

20p cosis54 05-01-2013 34 2   Download