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J. Med. Genet. 33, 721-725. BRCA1 mutations in a selected series of breast/ovarian cancer patients. 1996

Garvin, A. M. , Spycher, M. , Haner, M. , Torhorst, J. , Muller, H. , Herrmann, R. , Rochlitz, C. , Weber, W. , Scott, R. J.

Notes: PTT was used to rapidly screen the BRCA1 gene. Transcription and translation was performed on five overlapping fragments (amplified by PCR) of the entire coding region of the BRCA1 cDNA or genomic DNA using the TNT® T7 Coupled Reticulocyte Lysate System. (1144)

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Nat. Genet. 13, 238-240. BRCA2 mutations in primary breast and ovarian cancers. 1996

Lancaster, J.M., Wooster, R., Mangion, J., Phelan, C.M., Cochran, C., Gumbs, C., Seal, S., Barfoot, R., Collins, N., Bignell, G., Patel, S., Hamoudi, R., Larsson, C., Wiseman, R.W., Berchuck, A., Iglehart, J.D., Marks, J.R., Ashworth, A., Stratton, M.R., Futreal, P.A.

Notes: The protein truncation test was performed on PCR products from the BRCA2 gene. The PCR products were used in the TNT® T7 Coupled Reticulocyte Lysate System to express the protein, and the protein was analyzed by SDS-PAGE. (0834)

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Bone 18, 125-132. Characterization and cloning of the E11 antigen, a marker expressed by rat osteoblasts and osteocytes. 1996

Wetterwald, A., Hoffstetter, W., Cecchini, M.G., Lanske, B., Wagner, C., Fleisch, H. and Atkinson, M.

Notes: The E11 cDNA was transcribed and translated in vitro using the TNT® T3 Coupled Reticulocyte Lysate System in the presence of [35S]methionine. The protein was immunoprecipitated with mAb E11 and with a control IgG1 antibody. When the membrane was reacted with the mAb E11, the appropriate molecular weight bands were seen, verifying that the cDNA codes for E11. (1778)

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J. Biol. Chem. 271(17), 10282-10290. Characterization of AMP-activated protein kinase beta and gamma subunits.  Assembly of the heterotrimeric complex in vitro. 1996

Woods, A., Cheung, P.C., Smith, F.C., Davison, M.D., Scott, J., Beri, R.K. and Carling, D.

Notes: [35S]methionine-labeled AMPK (AMP activated protein kinase) subunits were cotranslated in vitro using the TNT® Coupled Reticulocyte Lysate System. The proteins were co-immunoprecipitated and shown to associate in vitro. The results indicate that a ternary complex is formed between the alpha, beta and gamma subunits rather than a mixture of dimers. When the lysates were programmed without beta, the alpha and gamma did not co-immunoprecipitate. (1779)

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J. Biol. Chem. 271, 24817-24843. Cloning and characterization of islet cell antigen-related protein-tyrosine phosphatase (PTP), a novel receptor-like PTP and autoantigen in insulin-dependent diabetes. 1996

Cui, L., Yu, W.P., DeAizpurua, H.J., Schmidli, R.S. and Pallen, C.J.

Notes: The IAR PTP protein (1015 residues) and the B11 protein (820 residues) were synthesized in the presence or absence of the Canine Microsomal Membranes. The predicted protein sequences contain one transmembrane domain. Proteinase K digestion in the presence or absence of Triton X-100 demonstrated the protection of a fragment consistent with the single membrane spanning domain. (1616)

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Proc. Natl. Acad. Sci. USA 93, 5925-5930. Cloning of a novel receptor expressed in rat prostate and ovary. 1996

Kuiper, G.G., Enmark, E., Pelto Huikko, M., Nilsson, S., Gustafsson, J.A.

Notes: cDNAs were synthesized from rat prostate total RNA using primers to the most conserved regions of the DNA-binding domain and ligand-binding domain of the nuclear receptor family. Protein was synthesized from one clone using the TNT® Coupled Reticulocyte Lysate System and incubated with [3H]-labeled estradiol (E2) and various competitors. Only estrogens competed effectively with E2; therefore, the protein is probably an estrogen receptor. (0858)

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Biochemistry 35, 10422-10435. Cofactor A is a molecular chaperone required for beta-tubulin folding: functional and structural characterization. 1996

Melki, R., Rommelaere, H., Leguy, R., Vandekerckhove, J. and Ampe, C.

Notes: [35S]methionine-labeled cofactor A was produced using the TNT® T7 Coupled Reticulocyte Lysate System. The protein interacts with beta-tubulin monomer on a Superose® 6 gel-filtration column. In addition, Cofactor A binds native or quasinative beta-tubulin in folding buffer. (1785)

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Proc. Natl. Acad. Sci. USA 93, 10685-10690. Conformational change and enhanced stabilization of the vitamin D receptor by the 1,25-dihydroxyvitamin D3 analog KH1060. 1996

van den Bemd, G. C. , Pols, H. A. , Birkenhager, J. C. , van Leeuwen, J. P.

Notes: The VDR protein was translated in the TNT® Coupled Reticulocyte Lysate System in the presence of [35S]methionine. The protein was incubated with various concentrations of hormones (1,25-(OH)2 vitamin D3, OCT, KH1060, all-trans retinoic acid, progesterone, 17β-estradiol, thyroid hormone, and 9-cis retinoic acid) and then exposed to trypsin, chymotrypsin and proteinase K. (0215)

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J. Med. Genet. 33, 274-280. Correlation between the development of extracolonic manifestations in FAP patients and mutations beyond codon 1403 in the APC gene. 1996

Dobbie, Z. , Spycher, M. , Mary, J. L. , Haner, M. , Guldenschuh, I. , Hurliman, R. , Amman, R. , Roth, J. , Muller, H. , Scott, R. J.

Notes: PCR was performed using primers to introduce a T7 promoter and a translation initiation sequence into PCR products used as templates in TNT® Coupled Reticulocyte Lysate System reactions. Truncation mutations were detected in 12/26 FAP patients; however, 33% of confirmed protein truncations in APC were not detected using the protein truncation test (PTT). (1238)

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J. Virol. 70, 3876-3886. Coxsackie B3 virus protein 2B contains a cationic amphipathic helix that is required for viral RNA replication. 1996

van Kuppeveld, F.J., Galama, J.M., Zoll, J., van den Hurk, P.J. and Melchers, W.J.

Notes: Mutations were generated in the amphipathic helix of CBV3 protein 2B. RNA transcripts of CBV3 protein 2B were synthesized and translated in TNT® T7 Coupled Reticulocyte Lysate System supplemented with 20% HeLa cell initation factors, to see if mutations affected polyprotein synthesis and processing. None of the mutations affected polyprotein processing. (1918)

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J. Mol. Neurosci. 7, 203-215. CR16, a novel proline-rich protein expressed in rat brain neurons, binds to SH3 domains and is a MAP kinase substrate. 1996

Weiler, M.C., Smith, J.L. and Masters, J.N.

Notes: The TNT® Coupled Reticulocyte Lysate System was used to produce [35S]methionine-labeled CR16 protein. The labeled protein was incubated with a GST-fusion of SH3 immobilized on glutathione agarose and a directed interaction was determined. (1534)

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Biochemistry 35, 3614-3618. Cryptic initiation at the human D4 receptor reveals a functional role for the amino terminus. 1996

Schoots, O., Sanyal, S., Guan, H.C., Jovanovic, V., Van Tol, H.H.

Notes: The TNT® Coupled Reticulocyte Lysate System used an alternative initiation codon when translating 5´ deletion mutants of the human D4 receptor. This result suggests that an amino-terminal truncated D4 receptor might exist in vivo and that the amino terminus may stabilize the active state of the receptor. (0415)

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J. Biol. Chem. 271, 11209-11213. D4-GDI, a substrate of CPP32, is proteolyzed during Fas-induced apoptosis. 1996

Na, S., Chuang, T.H., Cunningham, A., Turi, T.G., Hanke, J.H., Bokoch, G.M. and Danley, D.E.

Notes: Wild type and mutant D4-GDI were expressed in the TNT® T7 Coupled Reticulocyte Lysate System and labeled with [35S]methionine. The protein was then incubated with bacterially expressed CPP32, the apoptosis protease. The wild type protein was cleaved into a fragment of the same size as that seen in vivo, but an Asp19 to Asn mutation in D4-GDI blocked the cleavage event. (2041)

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J. Biol. Chem. 271, 16703-16711. Determination of the structure of the N-terminal splice region of the cyclic AMP-specific phosphodiesterase RD1 (RNPDE4A1) by 1H NMR and identification of the membrane association domain using chimeric constructs 1996

Smith, J., Scotland, G., Beattie, J., Trayer, I., Houslay, M.

Notes: Chimeric in-frame fusion proteins of the N-terminal portion of different mutants of RD1 and the N-terminal region of CAT were produced using the TNT® SP6 Coupled Reticulocyte Lysate System. The chimeric protein was added to COS cell membranes and checked for membrane association. This work, coupled with structural studies, allowed for the identification of the N-terminal splice region that confers membrane targeting upon RD1. (1787)

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Mol. Cell. Biol. 16, 745-752. Extensive alternative splicing and dual promoter usage generate Tcf-1 protein isoforms with differential transcription control properties. 1996

Van de Wetering, M., Castrop, J., Korinek, V. and Clevers, H.

Notes: TCF-1 proteins were produced using the TNT® SP6 Coupled Reticulocyte Lysate System. TCF-1 proteins were used in gel retardation assays, which showed that the extended TCF-1 N-terminus does not reconstitute an intramolecular DNA-binding inhibition domain. (1817)

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Am. J. Hum. Genet. 58, 441-450. Founding BRCA1 mutations in hereditary breast and ovarian cancer in southern Sweden. 1996

Johannsson, O., Ostermeyer, E.A., Hakansson, S., Friedman, L.S., Johansson, U., Sellberg, G., Brondum Nielsen, K., Sele, V., Olsson, H., King, M.C., Borg, A.

Notes: Nine germline mutations in BRCA1 were identified by use of the SSCP and heteroduplex analysis (HA) and by the PTT of exon 11 of BRCA1. PTT was performed using the TNT® T7 Coupled Reticulocyte Lysate System. Six of the truncation mutations were detected by PTT including two cases that were not detected by HA. (0984)

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Eur. J. Hum. Genet. 4, 143-152. Four novel dystrophin point mutations: detection by protein truncation test and transcript analysis in lymphocytes from Duchenne muscular dystrophy patients. 1996

Tuffery, S., Bareil, C., Demaille, J., Claustres, M.

Notes: The combination of RT-PCR and PTT were used to detect novel mutations in 4/6 DMD patients. The PTT analysis was performed using the TNT® T7 Coupled Reticulocyte Lysate System. (0243)

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J. Biol. Chem. 271, 8843-8850. Functional characterization of DNA-binding domains of the subunits of the heterodimeric aryl hydrocarbon receptor complex imputing novel and canonical basic helix-loop-helix protein-DNA interactions. 1996

Bacsi, S. and Hankinson, O.

Notes: AHR and ARNT, as well as their mutant derivatives, were expressed in the TNT® T7 Coupled Reticulocyte Lysate System in the presence or the absence of [35S]methionine. The radiolabeled AHR and ARNT were mixed with equimolar amounts of mutant ARNT and AHR, respectively. Immunoprecipitation was performed, and all AHR mutants dimerized with ARNT as efficiently as wild type AHR. (1758)

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Plant Cell 8, 1041-1059. GT-2: in vivo transcriptional activation activity and definition of novel twin DNA binding domains with reciprocal target sequence selectivity. 1996

Ni, M. , Dehesh, K. , Tepperman, J. M. , Quail, P. H.

Notes: C-terminal and N-terminal GT-2 deletion mutant proteins as well as site-directed GT-2 mutant proteins were synthesized from PCR templates using the TNT® T7 Coupled Reticulocyte Lysate System. Polypeptide segments in the N-terminal and C-terminal domains of GT-2 were analyzed for differential DNA binding to GT-box target sites. (0609)

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FEBS Lett. 390, 253-257. Heteromeric channel formation and Ca(2+)-free media reduce the toxic effect of the weaver Kir 3.2 allele. 1996

Tucker, S.J., Pessia, M., Moorhouse, A.J., Gribble, F., Ashcroft, F.M., Maylie, J., Adelman, J.P.

Notes: In vitro translated Kir protein was produced from the TNT® Coupled Reticulocyte Lysate System and used to verify antibody detection and specificity in Western blots. (0242)

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J. Biol. Chem. 271, 13786-13795. Identification of a murine TEF-1-related gene expressed after mitogenic stimulation of quiescent fibroblasts and during myogenic differentiation. 1996

Klebanow, E.R., Poon, D., Zhou, S. and Weil, P.A.

Notes: [35S]labeled FR-19B (FGF-regulated 19B) protein was transcribed using the T7 RNA polymerase and translated in the TNT® Coupled Reticulocyte Lysate System. A gel shift assay was performed with these proteins and double-stranded oligo from the SV40 enhancer. The results indicate that FR-19B specifically binds to the GT-IIC motif. (1804)

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Oncogene 12, 1971-1980. In vivo association of ATFa with JNK/SAP kinase activities. 1996

Bocco, J.L., Bahr, A., Goetz, J., Hauss, C., Kallunki, T., Kedinger, C. and Chatton, B.

Notes: SAPK proteins were synthesized using the TNT® T3 Coupled Reticulocyte Lysate System. These proteins were incubated with GST-cJun or GST-ATFa fusion proteins. The results demonstrate that the SAPKs interact with ATFa and c-Jun in vitro. (1749)

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Br. J. Cancer 74, 1104-1108. Infrequent alterations of the APC and MCC genes in gastric cancers from British patients. 1996

Sud, R., Talbot, I.C., Delhanty, J.D.

Notes: SSCP and heteroduplex analysis were used to screen exons of APC from gastric cancer lines; in addition, protein truncation test (PTT) was used to screen the MCR (mutation cluster region) of exon 15. The template was produced by PCR of genomic MCR DNA and used in the TNT® Coupled Reticulocyte Lysate System in the presence of 35S methionine. (0309)

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J. Biol. Chem. 271, 15187-15193. Investigation of myotonic dystrophy kinase isoform translocation and membrane association. 1996

Waring , J.D., Haq, R., Tamai, K., Sabourin, L.A., Ikeda, J.-E. and Korneluk, R.G.

Notes: The MyoD kinase was translated using the TNT® Coupled Reticulocyte Lysate System in the presence or absence of the microsomes. No change in mobility was noted for the MyoD kinase but the a-factor control did get glycosylated. The MyoD kinase did not gain protection from proteinase K but the a-factor was fully protected. (1604)

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Hum. Genet. 98, 528-533. Multiple products in the protein truncation test due to alternative splicing in the adenomatous polyposis coli (APC) gene. 1996

Bala, S., Kraus, C., Wijnen, J., Meera Khan, P. and Ballhausen, W.G.

Notes: The protein truncation test (PTT) was used to identify translational stops in transcripts of the APC (adenomatous polyposis coli) gene from familial adenomatous polyposis patients. Overlapping sets of oligonucleotide primers were used to amplify specific regions of APC cDNAs. These gene fragments were expressed in the TNT® T7 Coupled Reticulocyte System. (1454)

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