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Immunohistochemistry and Biosynthesis of N‐Acetylaspartylglutamate in Spinal Sensory Ganglia
Abstract: N‐Acetylaspartylglutamate (NAAG) is a nervous system‐specific dipeptide which has been implicated in chemical neurotransmission. Antisera were prepared against NAAG in order to study itsExpand
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Quantification and localization of phosphorylated myosin I isoforms in Acanthamoeba castellanii
The actin-activated Mg(2+)-ATPase activities of the three myosin I isoforms in Acanthamoeba castellanii are significantly expressed only after phosphorylation of a single site in the myosin I heavyExpand
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Murine aspartoacylase: cloning, expression and comparison with the human enzyme.
Canavan disease is caused by mutations in aspartoacylase, the enzyme that degrades N-acetylaspartate (NAA) into acetate and aspartate. Murine aspartoacylase (mASPA) was cloned using sequenceExpand
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Substrate specificity of Acanthamoeba myosin I heavy chain kinase as determined with synthetic peptides.
Phosphorylation of a single threonine (myosin IA) or serine (myosins IB and IC) in the heavy chains of the Acanthamoeba myosin I isozymes is required for expression of their actin-activatedExpand
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Conformational behavior of fragments of adrenocorticotropin and their antisense peptides determined by NMR spectroscopy and CD spectropolarimetry
An ‘antisense’ peptide (‘HTCA’), whose sequence was generated by reading the antisense RNA sequence corresponding to ACTH(1–24) was shown to bind ACTH(1–24) with a K d of 0.3 nM in a solid‐matrixExpand
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Activation of ganglionic tyrosine hydroxylase by peptides of the secretin-glucagon family: Structure-function studies
The hydroxylation of tyrosine to dopa is the rate-limiting reaction in catecholamine biosynthesis. It has been previously reported that secretin, vasoactive intestinal peptide and peptide histidineExpand
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