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GST pull-down assays were carried out with 0.5–2.2 μM of GST-fused proteins [65]. Co-precipitates were resolved on SDS-PAGE and analyzed by Western blot with antibodies described in the Results section. Unfolded and partially denatured Cox11 were generated by incubating recombinant and native Cox11 overnight with 5.6 and 7 M guanidine hydrochloride and urea, respectively. The Cox11 conformers were then diluted ~20-fold in CHAPS-binding buffer containing GST-LD. Immunoprecipitation assays with 5 μg of antibody and Western blots (~ 200–400 ng/ml of antibody) were performed exactly as described previously [13]."}

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{"project":"craft-ca-core-dev","denotations":[{"id":"T8218","span":{"begin":0,"end":5},"obj":"CHEBI:1418"},{"id":"T8219","span":{"begin":18,"end":25},"obj":"UBERON:0000966"},{"id":"T8220","span":{"begin":36,"end":46},"obj":"GO:0010467"},{"id":"T8221","span":{"begin":248,"end":251},"obj":"CHEBI:8984"},{"id":"T8222","span":{"begin":291,"end":301},"obj":"GO:0042571"},{"id":"T8223","span":{"begin":336,"end":344},"obj":"GO:0043335"},{"id":"T8224","span":{"begin":369,"end":374},"obj":"PR:000005770"},{"id":"T8225","span":{"begin":427,"end":432},"obj":"PR:000005770"},{"id":"T8226","span":{"begin":488,"end":492},"obj":"CHEBI:16199"},{"id":"T8227","span":{"begin":512,"end":517},"obj":"PR:000005770"},{"id":"T8228","span":{"begin":559,"end":564},"obj":"CHEBI:1418"},{"id":"T8229","span":{"begin":639,"end":647},"obj":"GO:0042571"},{"id":"T8230","span":{"begin":686,"end":694},"obj":"GO:0042571"}],"text":"CHAPS-solubilized retinal extracts, expression, and purification of GST-fused constructs were prepared as previously described [65]. GST pull-down assays were carried out with 0.5–2.2 μM of GST-fused proteins [65]. Co-precipitates were resolved on SDS-PAGE and analyzed by Western blot with antibodies described in the Results section. Unfolded and partially denatured Cox11 were generated by incubating recombinant and native Cox11 overnight with 5.6 and 7 M guanidine hydrochloride and urea, respectively. The Cox11 conformers were then diluted ~20-fold in CHAPS-binding buffer containing GST-LD. Immunoprecipitation assays with 5 μg of antibody and Western blots (~ 200–400 ng/ml of antibody) were performed exactly as described previously [13]."}

{"project":"2_test","denotations":[{"id":"17069463-10736720-85858876","span":{"begin":128,"end":130},"obj":"10736720"},{"id":"17069463-10736720-85858877","span":{"begin":210,"end":212},"obj":"10736720"},{"id":"17069463-11553612-85858878","span":{"begin":744,"end":746},"obj":"11553612"},{"id":"T88246","span":{"begin":128,"end":130},"obj":"10736720"},{"id":"T42365","span":{"begin":210,"end":212},"obj":"10736720"},{"id":"T65437","span":{"begin":744,"end":746},"obj":"11553612"}],"text":"CHAPS-solubilized retinal extracts, expression, and purification of GST-fused constructs were prepared as previously described [65]. GST pull-down assays were carried out with 0.5–2.2 μM of GST-fused proteins [65]. Co-precipitates were resolved on SDS-PAGE and analyzed by Western blot with antibodies described in the Results section. Unfolded and partially denatured Cox11 were generated by incubating recombinant and native Cox11 overnight with 5.6 and 7 M guanidine hydrochloride and urea, respectively. The Cox11 conformers were then diluted ~20-fold in CHAPS-binding buffer containing GST-LD. Immunoprecipitation assays with 5 μg of antibody and Western blots (~ 200–400 ng/ml of antibody) were performed exactly as described previously [13]."}