Zobrazeno 1 - 10 of 17 pro vyhledávání: '"H. M. Verheij"'
1
NMR Studies of Fusarium solani pisi Cutinase in Complex with Phosphonate Inhibitors
Autor: H. M. Verheij, Henri A. M. Pepermans, M. L. M. Mannesse, A. Groenewegen, M. R. Egmond, Cornelis W. Hilbers, Jeanine J. Prompers, B. Van Noorloos
Publikováno v: Biochemistry, 38(19), 5982-5994. American Chemical Society
The backbone dynamics of Fusarium solani pisi cutinase in complex with a phosphonate inhibitor has been studied by a variety of nuclear magnetic resonance experiments to probe internal motions on different time scales. The results have been compared
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01a5d053db0e026ef7ac3b116a8cb6d1
https://doi.org/10.1021/bi990039k
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2
Crystal structure of cutinase covalently inhibited by a triglyceride analogue
Autor: S, Longhi, M, Mannesse, H M, Verheij, G H, De Haas, M, Egmond, E, Knoops-Mouthuy, C, Cambillau
Publikováno v: Protein science : a publication of the Protein Society. 6(2)
Cutinase from Fusarium solani is a lipolytic enzyme that hydrolyses triglycerides efficiently. All the inhibited forms of lipolytic enzymes described so far are based on the use of small organophosphate and organophosphonate inhibitors, which bear li
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b7fd989376cabc2d1f0c74008b107dd3
https://pubmed.ncbi.nlm.nih.gov/9041628
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3
Incorporation of an unnatural amino acid in the active site of porcine pancreatic phospholipase A2. Substitution of histidine by 1,2,4-triazole-3-alanine yields an enzyme with high activity at acidic pH
Autor: S H, Beiboer, B, van den Berg, N, Dekker, R C, Cox, H M, Verheij
Publikováno v: Protein engineering. 9(4)
The effect of the substitution of the active site histidine 48 by the unnatural 1,2,4-triazole-3-alanine (TAA) amino acid analogue in porcine pancreas phospholipase A2 (PLA2) was studied. TAA was introduced biosynthetically using a his-auxotrophic Es
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5915441cbc7e2cdf3bc749fda1cffc18
https://pubmed.ncbi.nlm.nih.gov/8738210
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4
Targeting of porcine pancreatic phospholipase A2 to human platelets: introduction of an RGD sequence by genetic engineering
Autor: A C, Bekkers, H, van der Vuurst, G, van Willigen, J W, Akkerman, H M, Verheij
Publikováno v: Thrombosis and haemostasis. 74(4)
The possibility to induce specific disruption of activated platelets by binding of porcine pancreatic phospholipase A2 (PLA2) was tested by constructing a set of PLA2-mutants containing an Arg-Gly-Asp (RGD) sequence. One mutant was made with RGD as p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::03b7057fd8ef5f60abd665036b2ddfc8
https://pubmed.ncbi.nlm.nih.gov/8560426
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7
Regulation and role of phospholipases in host-bacteria interaction
Autor: P, Elsbach, J, Weiss, G, Wright, S, Forst, C J, van den Bergh, H M, Verheij
Publikováno v: Progress in clinical and biological research. 349
Deacylating phospholipases play essential roles in numerous biological events, requiring tight control of hydrolytic activity. Most cells, unless stimulated or perturbed, exhibit little phospholipid turnover. Activation of phospholipases A (PLA) is u
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bbbf14fe1adc418f4d29f1b747dea5d6
https://pubmed.ncbi.nlm.nih.gov/2204927
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10
Lipoprotein nature of the colicin A lysis protein: effect of amino acid substitutions at the site of modification and processing
Autor: Claude Lazdunski, Daniel Baty, Danièle Cavard, S P Howard, H M Verheij
Publikováno v: Journal of Bacteriology. 169:2187-2194
The colicin A lysis protein (Cal) is required for the release of colicin A to the medium by producing bacteria. This protein is produced in a precursor form that contains a cysteine at the cleavage site (-Leu-Ala-Ala-Cys). The precursor must be modif
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b40790a188e4e6a16f94640eb9789121
https://doi.org/10.1128/jb.169.5.2187-2194.1987
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