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Citations Search

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J. Neuroendocrinol. 19, 309-319. Inhibition of vasopressin V1b receptor translation by upstream open reading frames in the 5'-untranslated region. 2007

Rabadan-Diehl, C., Martínez, A., Volpi, S., Subburaju, S. and Aguilera, G.

Notes: The authors studied the rat VP V1b receptor (V1bR) gene including the 826 base 5´ UTR, which has five ORFs upstream (uORF) of the V1bR protein start codon, to examine the effect of the upstream peptides on V1bR translation. The V1bR gene was cloned into the pALTER®-MAX Vector, and substitution mutations were created in the uORF translation initiation codons with the Altered Sites® II in vitro Mutagenesis System. One microgram of the linearized pALTER®- V1bR construct was transcribed using the Riboprobe® System and translated using Wheat Germ Extract with or without 35S-methionine. The unlabeled protein was analyzed by Western blot. The radiolabeled protein was spun through a 3% sucrose cushion, precipitated and separated by SDS-PAGE. For a possible membrane-targeted protein, the uORF1 was transcribed in vitro and then translated using Rabbit Reticulocyte Lysate, Canine Pancreatic Microsomal Membanes and 35S-methionine. The proteins were spun through a 3% sucrose cushion and then run on a 15% SDS-PAGE gel to determine membrane presence. (3749)

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FEBS J. 273, 5612-5624. Aberrant interchain disulfide bridge of tissue-nonspecific alkaline phosphatase with an Arg433-->Cys substitution associated with severe hypophosphatasia. 2006

Nasu, M., Ito, M., Ishida, Y., Numa, N., Komaru, K., Nomura, S. and Oda, K.

Notes: The wildtype tissue-nonspecific alkaline phosphatase (TNSALP) gene was cloned into the pALTER®-MAX Vector, and codons for specific arginines were mutated using the Altered Sites® II Mammalian in vitro Mutagenesis System. The mutant constructs were subcloned and used for either transient or stable transfection experiments. (3747)

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Cancer Res. 66, 324–330. The role of 17beta-hydroxysteroid dehydrogenases in modulating the activity of 2-methoxyestradiol in breast cancer cells. 2006

Newman, S.P., Ireson, C.R., Tutill, H.J., Day, J.M., Parsons, M.F., Leese, M.P., Potter, B.V., Reed, M.J. and Purohit, A.

Notes: To study the estrogen conversion pathway and drugs that could potentially moderate the activity of the pathway, full-length 17β-HSD type 2 cDNA was cloned and full-length 7β-HSD type 1 cDNA was subcloned into the pALTER®-MAX Vector. MCF-7 cells, which have low 17β-HSD types 1 and 2 activities, and MDA-MB-231 cells, which have high oxidative 17β-HSD type 2 activity, were seeded at 20% confluency and transfected 24 hours later with the 17β-HSD type 1 or 2 pALTER®-MAX constructs or empty pALTER®-MAX. Compounds used for metabolism studies were added on day 3, and the cells and medium were extracted on day 5 for analysis by HPLC. The 17β-HSD enzyme activity was assayed 72 hours post-transfection. (3554)

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FEBS Lett. 272, 1704–1717. Novel aggregate formation of a frame-shift mutant protein of tissue-nonspecific alkaline phosphatase is ascribed to three cysteine residues in the C-terminal extension. Retarded secretion and proteasomal degradation. 2005

Komaru, K., Ishida, Y., Amaya, Y., Goseki-Sone, M., Orimo, H. and Oda, K.

Notes: To examine further the phenotype of a known tissue-nonspecific alkaline phosphatase (TNSALP) frameshift mutant, the cDNAs for wildtype TNSALP and TNSALP (1559delT) were subcloned into pALTER®-MAX Vector. Three cysteine residues were replaced with serines using the Altered Sites® II Mammalian Mutagenesis System. The substitution mutations were confirmed by DNA sequencing and the plasmids transfected into CHO cells. The size of the TNSALP (1559delT) product was compared to wildtype TNSALP using the TNT® T7 Coupled Reticulocyte Lysate System and [35S]methionine ⁄ cysteine with or without Canine Pancreatic Microsomal Membranes. The proteins were analyzed using SDS-PAGE and fluorography. (3519)

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J. Biol. Chem. 274, 34728-34734. A conserved seven amino acid stretch important for murine mitochondrial glycerol-3-phosphate acyltransferase activity: Significance of arginine 318 in catalysis. 1999

Dircks, L.K., Ke, J., Sul, H.S.

Notes: The Altered Sites® II Mammalian in vitro Mutagenesis System was used to produce and express 14 different mutant templates from within the pALTER®-MAX Mammalian Expression Vector. Thirteen of the mutants were simple codon changes accomplished with oligonucleotides as short as a 22-mer and as long as a 63-mer. A 21bp deletion was accomplished with a 36-mer. The mutants were expressed in a COS-1 cell derivative. (1235)

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J. Biol. Chem. 274, 17184-17192. Phosphorylation of serine 256 by protein kinase B disrupts transactivation by FKHR and mediates effects of insulin on insulin-like growth factor-binding protein-1 promoter activity through a conserved insulin response sequence. 1999

Guo, S., Rena, G., Cichy, S., He, X., Cohen, P., Unterman, T.

Notes: The pALTER®-MAX Vector was used to create mutations causing three separate amino acid substitutions on the FKHR cDNA. The Reverse Transcriptase System was used for RT-PCR. (1088)

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J. Biol. Chem. 273, 35273-35281. Cbl-mediated negative regulation of the Syk tyrosine kinase. A critical role for Cbl phosphotyrosine-binding domain binding to Syk phosphotyrosine 323. 1998

Lupher, M.L. Jr., Rao, N., Lill, N.L., Andoniou, C.E., Miyake, S., Clark, E.A., Druker, B., Band, H.

Notes: Altered-Sites® II Mammalian Mutagenesis System was used to make mutants of cbl and syk subcloned in the pALTER®-Max Vector. (0753)

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J. Biol. Chem. 273, 8323-8331. Fyn, Yes and Syk phosphorylation sites in c-Cbl map to the same tyrosine residues that become phosphorylated in activated T cells. 1998

Feshchenko, E.A., Langdon, W.Y., Tsygankov, A.Y.

Notes: The Altered Sites® II Mammalian in vitro Mutagenesis System was used to create 14 different mutant constructs of cDNA cloned into the pALTER®-MAX Mammalian Expression Vector. Up to five mutations were made in the same template. The constructs were expressed in Jurkat cells, COS-7 cells and a derivative of Jurkat's called JCaM1.6 and analyzed for phosphorylation. (1153)

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J. Biol. Chem. 272, 33140-33144. The Cbl Phosphotyrosine-binding Domain Selects a D(N/D)XpY Motif and Binds to the Tyr292 Negative Regulatory Phosphorylation Site of ZAP-70. 1997

Lupher, M.L. Jr, Songyang, Z., Shoelson, S.E., Cantley, L.C. , Band, H.

Notes: The Altered Sites® II Mammalian Mutagenesis System was used to make tyrosine to phenylalanine mutations in the ZAP-70 protein using the pALTER®-Max Vector. The mutants were transiently transfected into COS-7 cells with three other vectors expressing the Cbl protooncogene, Lck and CD8-x chimeric receptor. Lysates from the cells were assayed for phosphorylation of the ZAP-70 protein. (0754)

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