Search Results - "Marcus, John P."

A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels by Marcus, John P., Green, Jodie L., Goulter, Ken C., Manners, John M.

“…Summary A new family of antimicrobial peptides has been discovered in Macadamia integrifolia. The first member of this new family to be purified from nut…”
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Peptide Fragments From Plant Vicilins Expressed in Escherichia Coli Exhibit Antimicrobial Activity In Vitro by Marcus, John P, Goulter , Ken C, Manners, John M

“…Peptide fragments that exhibit antimicrobial activity in vitro have been shown to be produced by cleavage from the hydrophilic region near the N terminus of…”
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Enhanced quantitative resistance to Leptosphaeria maculans conferred by expression of a novel antimicrobial peptide in canola (Brassica napus L.) by Kazan, Kemal, Rusu, Anca, Marcus, John P, Goulter, Ken C, Manners, John M

“…The novel antimicrobial peptide MiAMP1, originally isolated from the seeds of Macadamia integrifolia, was constitutively expressed in transgenic tobacco and…”
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MiAMP1, a novel protein from Macadamia integrifolia adopts a Greek key beta-barrel fold unique amongst plant antimicrobial proteins by McManus, A.M, Nielsen, K.J, Marcus, J.P, Harrison, S.J, Green, J.L, Manners, J.M, Craik, D.J

“…MiAMP1 is a recently discovered 76 amino acid residue, highly basic protein from the nut kernel of Macadamia integrifolia which possesses no sequence homology…”
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MiAMP1, a novel protein from Macadamia integrifolia adopts a greek key β-barrel fold unique amongst plant antimicrobial proteins 1 1Edited by P. E. Wright by McManus, Ailsa M., Nielsen, Katherine J., Marcus, John P., Harrison, Stuart J., Green, Jodie L., Manners, John M., Craik, David J.

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Threonine formation via the coupled activity of 2-amino-3-ketobutyrate coenzyme A lyase and threonine dehydrogenase by MARCUS, J. P, DEKKER, E. E

“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Purification and characterization of a plant antimicrobial peptide expressed in Escherichia coli by Harrison, S J, McManus, A M, Marcus, J P, Goulter, K C, Green, J L, Nielsen, K J, Craik, D J, Maclean, D J, Manners, J M

“…MiAMP1 is a low-molecular-weight, cysteine-rich, antimicrobial peptide isolated from the nut kernel of Macadamia integrifolia. A DNA sequence encoding MiAMP1…”
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Purification and Characterization of a Plant Antimicrobial Peptide Expressed inEscherichia coli by Harrison, Stuart J., McManus, Ailsa M., Marcus, John P., Goulter, Ken C., Green, Jodie L., Nielsen, Katherine J., Craik, David J., Maclean, Donald J., Manners, John M.

“…MiAMP1 is a low-molecular-weight, cysteine-rich, antimicrobial peptide isolated from the nut kernel ofMacadamia integrifolia.A DNA sequence encodingMiAMP1 with…”
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Purification, characterisation and cDNA cloning of an antimicrobial peptide from Macadamia integrifolia by Marcus, J.P, Goulter, K.C, Green, J.L, Harrison, S.J, Manners, J.M

“…An antimicrobial peptide with no significant amino acid sequence similarity to previously described peptides has been isolated from the nut kernels of…”
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Identification of a Second Active Site Residue in Escherichia coli L-Threonine Dehydrogenase: Methylation of Histidine-90 with Methyl p-Nitrobenzenesulfonate by Marcus, J.P., Dekker, E.E.

“…Incubation of L-threonine dehydrogenase from Escherichia coli with methyl p-nitrobenzenesulfonate results in a time- and concentration-dependent loss of…”
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pH-dependent decarboxylation of 2-amino-3-ketobutyrate, the unstable intermediate in the threonine dehydrogenase-initiated pathway for threonine utilization by Marcus, J P, Dekker, E E

“…2-Amino-3-ketobutyrate can be readily formed enzymatically by the action of L-threonine dehydrogenase. A convenient assay for determining the half-life of this…”
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Identity and some properties of the L-threonine aldolase activity manifested by pure 2-amino-3-ketobutyrate ligase of Escherichia coli by Marcus, J P, Dekker, E E

“…2-Amino-3-ketobutyrate ligase catalyzes the reversible, pyridoxal 5'-phosphate-dependent condensation of glycine with acetyl CoA forming the unstable…”
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