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Brummer lipase is an evolutionary conserved fat storage regulator in Drosophila.
TLDR
A screen to identify nutritionally regulated genes that control energy storage in the model organism Drosophila identified the brummer (bmm) gene, a homolog of human adipocyte triglyceride lipase (ATGL) and their evolutionary conservation suggests Brummer/ATGL family members to be implicated in human obesity. Expand
6,8-Difluoro-4-methylumbiliferyl phosphate: a fluorogenic substrate for protein tyrosine phosphatases.
TLDR
The measured kinetic and inhibitor constants for DIFMUP cleavage were comparable with those of the widely used but less discriminative and practicable substrates, para-nitrophenylphosphate and phosphotyrosine-containing peptides, respectively. Expand
Identification of binding proteins for cholesterol absorption inhibitors as components of the intestinal cholesterol transporter
TLDR
It is suggested that an integral membrane protein of M r 145 kDa is (a component of) the cholesterol absorption system in the brush border membrane of small intestinal enterocytes. Expand
Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: comparison with non-lipolytic and lipolytic carboxylesterases.
TLDR
Results indicate that human HSL, together with other lipolytic carboxylesterases, are active on short chain esters and hydrolyze water insoluble trioctanoin, vinyl laurate and olive oil, whereas the action of EST2, AFEST, protein RV1399C and non-lipolyticCarboxylesTERases is restricted to solutions of short chain substrates. Expand
Sensitive assay for hormone-sensitive lipase using NBD-labeled monoacylglycerol to detect low activities in rat adipocytes Published, JLR Papers in Press, January 1, 2005. DOI
TLDR
A convenient assay procedure based on NBD-MAG should facilitate the search for small molecule HSL inhibitors and provide an efficient substrate for rat adipocyte and human recombinant HSL. Expand
Use of an inhibitor to identify members of the hormone-sensitive lipase family.
TLDR
Surface-enhanced laser desorption ionization time-of-flight mass spectrometry analysis of a trypsin digest of AFEST treated with the inhibitor or not treated showed the occurrence of an increase in the molecular masses of the "GESAGG"-containing peptide, which indicates that a covalent enzyme-inhibitor complex has been formed. Expand
Might the kinetic behavior of hormone-sensitive lipase reflect the absence of the lid domain?
TLDR
The preincubation of the recombinant HSL with a serine esterase inhibitor in 1:100 molar excess leads to complete HSL inhibition within 15 min, indicating that the catalytic serine of HSL is highly reactive and that it is readily accessible. Expand
The molecular mechanism of human hormone-sensitive lipase inhibition by substituted 3-phenyl-5-alkoxy-1,3,4-oxadiazol-2-ones.
TLDR
A kinetic model is proposed to describe the inhibition of HSL by compound 7600 in the aqueous phase as well as its partial reactivation at the lipid-water interface. Expand
Continuous monitoring of cholesterol oleate hydrolysis by hormone-sensitive lipase and other cholesterol esterases Published, JLR Papers in Press, February 16, 2005. DOI 10.1194/jlr.M400509-JLR200
TLDR
A specific cholesterol esterase assay is developed using cholesterol oleate dispersed in phosphatidylcholine and gum arabic by sonication to continuously monitor the hydrolysis of CO by HSL, and the activity of HSL on CO is ∼4- to 5-fold higher than on long-chain TAGs. Expand
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