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A J Ganzhorn

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Recent Articles
1.
Ganzhorn A, Hoflack J, Pelton P, Strasser F, Chanal M, Piettre S
Bioorg Med Chem . 1998 Dec; 6(10):1865-74. PMID: 9839016
alpha-Hydroxyphosphonates are moderately potent (Ki = 6-600 microM) inhibitors of the enzyme myo-inositol monophosphatase (McLeod et al., Med. Chem. Res. 1992, 2, 96). Hydroxy-[4-(5,6,7,8-tetrahydronaphtyl-1-oxy)phenyl]methyl phosphonate (3) was resynthesized and its...
2.
Bolkenius F, Ganzhorn A
Gen Pharmacol . 1998 Nov; 31(5):655-9. PMID: 9809459
1. Peptidylglycine alpha-amidating mono-oxygenase (PAM) is a bifunctional key enzyme in the bioactivation of neuropeptides. Its biosynthesis, distribution, functional role, and pharmacological manipulation are discussed. 2. PAM biosynthesis from a...
3.
Piettre S, Andre C, Chanal M, Ducep J, Lesur B, Piriou F, et al.
J Med Chem . 1998 Jan; 40(26):4208-21. PMID: 9435892
The first successful preparation of mono- and disubstituted 3,7-dihydroxytropolone involves a four-step synthetic scheme. Thus, bromination of 3,7-dihydroxytropolone (8) followed by permethylation of the resultant products furnished gram quantities of...
4.
Bolkenius F, Ganzhorn A, Chanal M, Danzin C
Biochem Pharmacol . 1997 Jun; 53(11):1695-702. PMID: 9264322
Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3) catalyses the rate-limiting step in the post-translational activation of substance P, among other neuropeptides, from its glycine-extended precursor. Comparative kinetic studies were performed, using...
5.
Ganzhorn A, Lepage P, Pelton P, Strasser F, Vincendon P, Rondeau J
Biochemistry . 1996 Aug; 35(33):10957-66. PMID: 8718889
The role of lysine residues in the catalytic mechanism of myo-inositol monophosphatase (EC 3.1.3.25) was investigated. The enzyme was completely inactivated by amidination with ethyl acetimidate or reductive methylation with...
6.
Saudek V, Vincendon P, Do Q, Atkinson R, SKLENAR V, Pelton P, et al.
Eur J Biochem . 1996 Aug; 240(1):288-91. PMID: 8925839
The interaction of Li+ with myo-inositol monophosphatase was studied by 7Li-NMR spectroscopy. Li+ binding to the enzyme induces a downfield shift and broadening of the 7Li-NMR signal. Changes of the...
7.
Strasser F, Pelton P, Ganzhorn A
Biochem J . 1995 Apr; 307 ( Pt 2):585-93. PMID: 7733900
Activation and inhibition of recombinant bovine myo-inositol monophosphatase by metal ions was studied with two substrates, D,L-inositol 1-phosphate and 4-nitrophenyl phosphate. Mg2+ and Co2+ are essential activators of both reactions....
8.
Huggins J, Ganzhorn A, Saudek V, Pelton J, Atkinson R
Eur J Biochem . 1994 Apr; 221(1):581-93. PMID: 8168546
The structure of cGMP-dependent protein kinase I alpha-(546-576)-peptide amide (peptide-546) and its effects on cGMP-dependent protein kinase I alpha (G-kinase) have been studied. By primary sequence analysis and analogy to...
9.
Ganzhorn A, Vincendon P, Pelton J
Biochim Biophys Acta . 1993 Feb; 1161(2-3):303-10. PMID: 8381671
Structural aspects of myo-inositol monophosphatase were examined by spectroscopic techniques and empirical prediction methods. The enzyme belongs to the alpha/beta class of proteins, with approx. 33% alpha-helix and 29% beta-sheet,...
10.
Pelton P, Ganzhorn A
J Biol Chem . 1992 Mar; 267(9):5916-20. PMID: 1313422
The pH dependence of myo-inositol monophosphatase may indicate a role for histidine residues in the catalytic mechanism (Ganzhorn, A. J., and Chanal, M.-C. (1990) Biochemistry 29, 6065-6071). This possibility was...