Search Results - "Kudlicki, W"

The past, present and future of cell-free protein synthesis by KATZEN, Federico, CHANG, Geoffrey, KUDLICKI, Wieslaw

“…Recent technical advances have revitalized cell-free expression systems to meet the increasing demands for protein synthesis. Cell-free systems offer several…”
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Membrane protein expression: no cells required by Katzen, Federico, Peterson, Todd C, Kudlicki, Wieslaw

“…Structural and functional studies of membrane proteins have been severely hampered by difficulties in producing sufficient quantities of properly folded…”
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Activation and release of enzymatically inactive, full-length rhodanese that is bound to ribosomes as peptidyl-tRNA by KUDLICKI, W, ODOM, O. W, KRAMER, G, HARDESTY, B

“…Synthesis of rhodanese in a cell-free coupled transcription/translation system derived from Escherichia coli leads to an accumulation of full-length rhodanese…”
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In vitro engineering using synthetic tRNAs with altered anticodons including four-nucleotide anticodons by Kramer, G, Kudlicki, W, Hardesty, B

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In vitro engineering using acyl-derivatized tRNAs by Odom, O W, Kudlicki, W, Hardesty, B

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Inhibition of the release factor-dependent termination reaction on ribosomes by DnaJ and the N-terminal peptide of rhodanese by Kudlicki, W, Odom, O W, Merrill, G, Kramer, G, Hardesty, B

“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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The Importance of the N-terminal Segment for DnaJ-mediated Folding of Rhodanese While Bound to Ribosomes as Peptidyl-tRNA by Kudlicki, Wieslaw, Odom, O.W., Kramer, Gisela, Hardesty, Boyd, Merrill, Gerald A., Horowitz, Paul M.

“…Two lines of evidence indicate the importance of the N-terminal portion of rhodanese for correct folding of the nascent ribosome-bound polypeptide. A mutant…”
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Development of a chaperone-deficient system by fractionation of a prokaryotic coupled transcription/translation system by Kudlicki, W, Mouat, M, Walterscheid, J P, Kramer, G, Hardesty, B

“…A coupled transcription/translation system from Escherichia coli has been developed that is very active for protein synthesis but deficient in chaperone…”
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Cotranslational folding of nascent proteins on Escherichia coli ribosomes by Hardesty, B, Kudlicki, W, Odom, O W, Zhang, T, McCarthy, D, Kramer, G

“…Evidence is presented for cotranslational folding of rhodanese or ricin during its synthesis on Escherichia coli ribosomes. During transcription-translation,…”
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Identification of spectrin-related peptides associated with the reticulocyte heme-controlled alpha subunit of eukaryotic translational initiation factor 2 kinase and of Mr 95,000 peptide that appears to be the catalytic subunit by Kudlicki, W, Fullilove, S, Read, R, Kramer, G, Hardesty, B

“…An isolation procedure for the reticulocyte heme-controlled alpha subunit of eukaryotic translational initiation factor 2 (eIF-2 alpha) kinase is described…”
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The NH2-terminal sequence of the alpha and gamma subunits of eukaryotic initiation factor 2 and the phosphorylation site for the heme-regulated eIF-2 alpha kinase by Wettenhall, R E, Kudlicki, W, Kramer, G, Hardesty, B

“…Rabbit reticulocyte eukaryotic initiation factor 2 was phosphorylated with the heme-regulated alpha subunit of eukaryotic initiation factor 2 kinase, and then…”
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The 90-kDa component of reticulocyte heme-regulated eIF-2 alpha (initiation factor 2 alpha-subunit) kinase is derived from the beta subunit of spectrin by KUDLICKI, W, FULLILOVE, S, KRAMER, G, HARDESTY, B

“…Antibodies from three different lines of monoclonal hybridomas crossreact with both the beta subunit of spectrin and the 90-kDa peptide present in highly…”
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A type 1 phosphoprotein phosphatase active with phosphorylated Mr = 68,000 initiation factor 2 kinase by Szyszka, R, Kudlicki, W, Kramer, G, Hardesty, B, Galabru, J, Hovanessian, A

“…A type 1 protein phosphatase from reticulocytes is shown to efficiently dephosphorylate the Mr = 68,000 phosphopeptide of the double-stranded RNA-dependent…”
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Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF-Tu flexing by Kudlicki, W, Coffman, A, Kramer, G, Hardesty, B

“…The translation elongation factor (EF) Tu has chaperone-like capacity to promote renaturation of denatured rhodanese. This renaturation activity is greatly…”
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From Gene to HSQC in under Five Hours:  High-Throughput NMR Proteomics by Keppetipola, Shiranthi, Kudlicki, Wieslaw, Nguyen, Bao D, Meng, Xi, Donovan, Kevin J, Shaka, A. J

“…A simple, rapid, in vitro cell-free protein expression system, Expressway NMR, is introduced and used to express the small ubiquitin-related modifier protein…”
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Association of the heme-controlled eIF-2 alpha kinase with spectrin-derived peptides by Kramer, G, Kudlicki, W, Fullilove, S, Hardesty, B

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On the role of cyclic AMP-independent protein kinases in the modification of yeast ribosomal proteins in vivo by Kudlicki, W, Szyszka, R, Grankowski, N, Gasior, E

“…Two proteins of yeast 40S ribosome subunit and four proteins of the 60S ribosome subunit were labelled in vivo with [32P]orthophosphate. Five of these proteins…”
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Ribosome-associated protein kinase from Saccharomyces cerevisiae by Grankowski, N., Kudlicki, W., Gasior, E.

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Ribosomal protein as substrate for a GTP dependent protein kinase from yeast by Kudlicki, W, Grankowski, N, Gasior, E

“…A protein kinase specific for casein and acidic ribosomal proteins was isolated and partly characterized. It was found that the enzyme utilizes GTP and ATP as…”
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Proteins of yeast ribosomal subunits: number and general properties by Grankowski, N, Kudlicki, W, Paleń, E, Gasior, E

“…1. Saccharomyces cerevisiae at the early stationary phase of growth accumulate 80 S ribosomes, easily dissociating into subunits, which retain full activity in…”
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