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Hardesty Boyd
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http://hub.abes.fr/acs/periodical/bichaw/1980/volume_19/issue_4/101021bi00545a028/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1983/volume_22/issue_24/101021bi00293a034/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1987/volume_26/issue_21/101021bi00395a003/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/1989/volume_28/issue_4/101021bi00430a001/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1984/volume_23/issue_21/101021bi00316a037/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1991/volume_30/issue_42/101021bi00106a028/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1993/volume_32/issue_31/101021bi00082a015/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_44/101021bi00044a003/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1983/volume_22/issue_1/101021bi00270a012/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1991/volume_30/issue_19/101021bi00233a026/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1972/volume_11/issue_10/101021bi00760a028/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1992/volume_31/issue_8/101021bi00123a023/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1980/volume_19/issue_26/101021bi00567a001/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/1990/volume_29/issue_48/101021bi00500a004/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1992/volume_31/issue_50/101021bi00165a004/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1993/volume_32/issue_13/101021bi00064a022/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/1981/volume_20/issue_18/101021bi00521a033/authorship/5
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GroEL and GroES increase the specific enzymic activity of newly-synthesized rhodanese if present during in vitro transcription/translation
Fluorescence studies on the interaction of inhibitor 2 and okadaic acid with the catalytic subunit of type 1 phosphoprotein phosphatases
Folding of an Enzyme into an Active Conformation While Bound as Peptidyl-tRNA to the Ribosome
Partial purification and characterization of a 90000-dalton peptide involved in activation of the eIF-2.alpha. protein kinase of the hemin-controlled translational repressor
The phosphorylation state of the reticulocyte 90-kDa heat shock protein affects its ability to increase phosphorylation of peptide initiation factor 2 .alpha. subunit by the heme-sensitive kinase
In vitro protein engineering using synthetic tRNAAla with different anticodons
Comparison of ribosomal entry and acceptor transfer ribonucleic acid binding sites on Escherichia coli 70S ribosomes. Fluorescence energy transfer measurements from Phe-tRNAPhe to the 3' end of 16S ribonucleic acid
Movement of tRNA but not the nascent peptide during peptide bond formation on ribosomes
The 90-kilodalton peptide of the heme-regulated eIF-2.alpha. kinase has sequence homology with the 90-kilodalton heat shock protein
Binding of S21 to the 50S subunit and the effect of the 50S subunit on nonradiative energy transfer between the 3' end of 16S RNA and S21
Evidence for RNA in the peptidyl transferase center of Escherichia coli ribosomes as indicated by fluorescence
Distances between 3' ends of ribosomal ribonucleic acids reassembled into Escherichia coli ribosomes
Binding of aminoacyl transfer ribonucleic acid synthetases to ribosomes from rabbit reticulocytes
Fluorescence study of the topology of messenger RNA bound to the 30S ribosomal subunit of Escherichia coli
Localization of the elongation factor EF-Tu binding site on Escherichia coli ribosomes
Fluorescence characterization of the environment encountered by nascent polyalanine and polyserine as they exit Escherichia coli ribosomes during translation
Position of transfer ribonucleic acid on Escherichia coli ribosomes. Distance from the 3' end of 16S ribonucleic acid to three points on phenylalanine-accepting transfer ribonucleic acid in the donor site of 70S ribosomes
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