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Protein phosphorylation remains as a black box in signal
Protein phosphorylation remains as a black box in signal

... Nagoya University Graduate School of Medicine Protein phosphorylation is a major post-translational modification in eukaryotic cells that plays a critical role in various cellular processes. More than 500 protein kinases are encoded in the human genome and are classified into 7 major groups based on ...
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... internalize and to cluster in clathrin coated pits Tyr → Cys mutation in cytosolic domain, which is within Tyr-X-X-φ motif and unable to bind μ2 of AP2 heterotetramer complex general sorting signal motifs should be used as a CLUE, not a fact ...
Effect of protein aggregation and protein structure on magnetite
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... Magnetococcus marinus MC-1 has been shown to control the size of magnetite crystals in in vitro experiments, thereby demonstrating its potential as a candidate protein for the production of magnetite nanoparticles possibly useful in medical and other applications. However, the importance of the stru ...
Helices From Readily in Biological Structures
Helices From Readily in Biological Structures

... grouped into families, in which in family member has an amino acid sequences and a three-dimensional conformation that closely resembles that of other family members. For example the serine protease which is a family of protein involve in cleavage of protein. Chymotrypsin and elastase are very simil ...
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3.3 Cell Membrane

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ABSTRACT - University of Colorado
ABSTRACT - University of Colorado

... To reduce the likelihood of cross-linking, phenylalanine (F) was substituted for tyrosine at the same sites. We examined aggregate formation and neurotoxic effects of these constructs in a rat dopaminergic cell line (N27 cells) by transient transfection. Results showed that expression of Y39C or Y12 ...
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... A. Analyzing genome data using computers B. Figuring out a protein structure from X-ray crystallography C. Calculating the tree of life D. Detecting homologs using primary sequence similarity E. Detecting homologs using secondary sequence similarity 2. ATP, GTP, NAD, NADP, FMN, and FAD are example o ...
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G protein–coupled receptor



G protein–coupled receptors (GPCRs), also known as seven-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptor, and G protein–linked receptors (GPLR), constitute a large protein family of receptors that sense molecules outside the cell and activate inside signal transduction pathways and, ultimately, cellular responses. Coupling with G proteins, they are called seven-transmembrane receptors because they pass through the cell membrane seven times.G protein–coupled receptors are found only in eukaryotes, including yeast, choanoflagellates, and animals. The ligands that bind and activate these receptors include light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters, and vary in size from small molecules to peptides to large proteins. G protein–coupled receptors are involved in many diseases, and are also the target of approximately 40% of all modern medicinal drugs. Two of the United States's top five selling drugs (Hydrocodone and Lisinopril) act by targeting a G protein–coupled receptor. The 2012 Nobel Prize in Chemistry was awarded to Brian Kobilka and Robert Lefkowitz for their work that was ""crucial for understanding how G protein–coupled receptors function."". There have been at least seven other Nobel Prizes awarded for some aspect of G protein–mediated signaling.There are two principal signal transduction pathways involving the G protein–coupled receptors: the cAMP signal pathway and the phosphatidylinositol signal pathway. When a ligand binds to the GPCR it causes a conformational change in the GPCR, which allows it to act as a guanine nucleotide exchange factor (GEF). The GPCR can then activate an associated G protein by exchanging its bound GDP for a GTP. The G protein's α subunit, together with the bound GTP, can then dissociate from the β and γ subunits to further affect intracellular signaling proteins or target functional proteins directly depending on the α subunit type (Gαs, Gαi/o, Gαq/11, Gα12/13).
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