OPCML (opioid binding protein/cell adhesion molecule-like)

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OPCML (opioid binding protein/cell adhesion molecule-like)

OPCML consisted of one half beta-sheets and one fourth alpha-helices. Hydropathy analysis suggested that hydrophobic and hydrophilic regions were evenly distributed along the sequence, but the NH2and COOH-termini were hydrophobic. Hydrophobic moments and Fourier-transform amphipathic analyses further suggest that residues 23-30 and 83-93 were amphipathic beta-sheets. Structural elements include...

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Regulation of acute and chronic opioid receptor functions by OBCAM, a cell adhesion-like molecule.

Opioid receptors were one of the first class of cell surface receptors to be identified using in vitro binding assays with brain tissue, but for many years efforts to purify and clone them were unsuccessful because of their sensitivity to detergents, their heterogeneity, and the lack of a simple biochemical assay for their function (Loh and Smith 1990). Several laboratories, including the autho...

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Dileucine and PDZ-binding motifs mediate synaptic adhesion-like molecule 1 (SALM1) trafficking in hippocampal neurons.

Synaptic adhesion-like molecules (SALMs) are a family of cell adhesion molecules involved in neurite outgrowth and synapse formation. Of the five family members, only SALM1, -2, and -3 contain a cytoplasmic C-terminal PDZ-binding motif. We have found that SALM1 is unique among the SALMs because deletion of its PDZ-binding motif (SALM1ΔPDZ) blocks its surface expression in heterologous cells. Wh...

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Binding properties of a cell adhesion molecule from neural tissue.

We have previously identified and purified a cell surface glycoprotein from retina and brain, called neural cell adhesion molecule or N-CAM, that appears to be involved in neural cell--cell adhesion, the fasciculation of neurites, and the formation of normal tissue patterns in the retina. The present studies reveal that artificial vesicles containing lipid and purified N-CAM bind to different c...

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Reovirus binding determinants in junctional adhesion molecule-A.

Junctional adhesion molecule-A (JAM-A) serves as a serotype-independent receptor for mammalian orthoreoviruses (reoviruses). The membrane-distal immunoglobulin-like D1 domain of JAM-A is required for homodimerization and binding to reovirus attachment protein sigma1. We employed a structure-guided mutational analysis of the JAM-A dimer interface to identify determinants of reovirus binding. We ...

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ژورنال

عنوان ژورنال: Atlas of Genetics and Cytogenetics in Oncology and Haematology

سال: 2011

ISSN: 1768-3262

DOI: 10.4267/2042/44641