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This article presents information related to a study conducted by researchers W.L Chung and colleagues published in the "Journal of Biological Chemistry," that focuses on matters related to cytoplasmic targeting signals in transmembrane invariant. According to the study protein targeting mechanisms in flagellated protozoan parasites have received considerable interest because of a huge bias in these organisms toward the glycosylphosphatidylinositol anchor as a mechanism for the membrane attachment of cell surface macromolecules.

The article cites a study which states that a disintegrin and metalloprotease 23 (ADAM23) is a cell-surface glycoprotein expressed by central nervous system neurons. Researcher A.P. Goldsmith and colleagues, Cambridge University, explained that several members of the ADAM family of proteins have been implicated in biological processes ranging from fertilization to myoblast fusion and neural cell fate determination. Goldsmith and colleagues published their study in the "Journal of Neuroscience Research."

This article cites a study which states that scientists from England have reported that EpsinR is an adaptor for the SNARE protein Vti1b. As a more direct assay for epsinR function, researchers isolated clathrin-coated vesicle from control and siRNA-treated cells and then looked for differences in cargo content, wrote researcher J. Hirst and colleagues, Cambridge University. In clathrin-depleted cells, both coat and cargo proteins are greatly reduced in this preparation. Hirst and colleagues published their study in "Molecular Biology of the Cell."

The article presents information on a study from England which reports that the heparin binding properties of heparin cofactor II (HCII) suggest an antithrombin (AT)-like activation mechanism. The serpin HCII is a glycosaminoglycan-activated inhibitor of thrombin that circulates at a high concentration in the blood. The antithrombotic effect of heparin, however, is due primarily to the specific interaction of a fraction of heparin chains with the related serpin AT. What currently prevents selective therapeutic activation of HCII is the lack of knowledge of the determinants of glycosaminoglycan binding specificity.

The article reports that increased transcription factor expression identifies reactive progenitor cells. According to recent research from England published in the journal "Molecular and Cellular Neuroscience," the increased expression in the central nervous system (CNS) of two transcription factors identifies reactive oligodendrocyte progenitor cells (OPCs) responding to demyelination. Within the adult CNS, a quiescent population of OPCs become activated in response to demyelination and give rise to remyelinating oligodendrocytes.

The article cites a study by researcher P.R.M. Siljander and colleagues, published in a 2004 issue of "Journal of Biological Chemistry," which reports that the activation state of integrin determines the selectivity for novel recognition sites in fibrillar collagens. Sequence alignment was used to investigate the occurrence of related motifs in other human fibrillar collagens, and located a conserved array of novel GER motifs within their triple helical domains. Researchers compared the integrin binding properties of synthetic triple helical peptides containing examples of such sequences or the previously identified motifs.

The article focuses on a study related to the association of metaplastic facilitation and ultrastructural changes in synaptic properties with long-term modulation of the lamprey locomotor network. The study was conducted by researcher S. Bevan and colleagues at the Cambridge University and published in the journal "Journal of Neuroscience." The neuropeptide substance P evokes a long-term protein synthesis-dependent increase in the cycle frequency of locomotor network activity in the lamprey. Substance P potentiates low-frequency-evoked EPSPs from excitatory network interneurons. Long term changes in synaptic properties are often associated with changes in synaptic organization. Substance P thus has long-term effects on synaptic organization and function.

Discusses research done on a novel bacteria exit duct for proteins and drugs by Vassilis Koronakis, published in a 2003 issue of "FEBS Letters."

Discusses research being done on pentraxins serum amyloid P component and C-reactive protein, with reference to a study by J. Andrew Aquilina and Carol V. Robinson, published in the 2003 issue of "Biochemical Journal."

The article reports a study related to wild-type spectrin domains which have the same stability but very different kinetic properties. According to researchers in England, the study of proteins with the same architecture, but different sequence has proven to be a valuable tool in the protein folding field. As a prelude to studies on the folding mechanism of spectrin domains they present the kinetic characterisation of the wild-type forms of the 15th, 16th, and 17th domains of chicken brain alpha-spectrin. They show that the proteins all behave in a two-state manner, with different kinetic properties, said K.A. Scott and colleagues, Cambridge University.

The article cites a study by researchers V. Vellani and colleagues, which reports that functional bradykinin (BK) B1 receptors are expressed in nociceptive neurones and are upregulated by the neurotrophin glial cell line derived neurotrophic factor (GDNF). The researchers show that specific B1 receptor activation causes translocation of the e isoform of protein kinase C (PKC-epsilon) to the membrane of a small fraction of freshly isolated sensory neurons from rats and mice. Vellani and colleagues published their study in the "Journal of Physiology."