Discovery of Phenyl Acetic Acid Substituted Quinolines as Novel Liver X Receptor Agonists for the Treatment of Atherosclerosis

Autor: Liang Chen, Ponnal Nambi, Qiang-Yuan Liu, Rayomand J Unwalla, Valerie Clerin, Michael D Basso, Mathias Färnegårdh, Irene Feingold, Dawn A. Savio, James Carl Keith, Christopher P. Miller, Jay Wrobel, Anita R Halpern, Farooq Azam, Anna Wilhelmsson, Annika Goos-Nilsson, Robert R. Singhaus, Christine Resmini, Christine Huselton, Baihua Hu, Michael D. Collini, Elaine M. Quinet, Tomas Bonn, Cristofer Enroth

Publikováno v: Journal of Medicinal Chemistry. 49:6151-6154

A structure-based approach was used to optimize our new class of quinoline LXR modulators leading to phenyl acetic acid substituted quinolines 15 and 16. Both compounds displayed good binding affinity for LXRbeta and LXRalpha and were potent activato

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::848e63d4bc070abcc49582c768ac1f2a
https://doi.org/10.1021/jm0609566

Functional analysis of the M.HpyAIV DNA methyltransferase of Helicobacter pylori

Autor: Margareta Krabbe, Britta Björkholm, Cecilia Jernberg, Anna Skoglund, Lars Engstrand, Cristofer Enroth, Christina Nilsson, Katja Schirwitz, Anders F. Andersson

Publikováno v: Journal of bacteriology. 189(24)

A large number of genes encoding restriction-modification (R-M) systems are found in the genome of the human pathogen Helicobacter pylori . R-M genes comprise approximately 10% of the strain-specific genes, but the relevance of having such an abundan

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c93b944854e919f2dab84fe53b3e0388
https://pubmed.ncbi.nlm.nih.gov/17921292

Studies of the mechanism of phenol hydroxylase: effect of mutation of proline 364 to serine

Autor: Ylva Lindqvist, David P. Ballou, Vincent Massey, Cristofer Enroth, Dong Xu

Publikováno v: Biochemistry. 41(46)

An active site residue in phenol hydroxylase (PHHY), Pro364, was mutated to serine to investigate its role in enzymatic catalysis. In the presence of phenol, the reaction between the reduced flavin of P364S and oxygen is very fast, but only 13% of th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::163a0ae5501c4a50af839905f903b334
https://pubmed.ncbi.nlm.nih.gov/12427024

Crystallization and preliminary crystallographic data of the PAS domain of the NifL protein from Azotobacter vinelandii

Autor: Cristofer Enroth, Jacques Vervoort, Paul A. Tucker, Jörg Hendle, Marco H. Hefti

Publikováno v: Acta Crystallographica Section D-Biological Crystallography 57 (2001) 12
Acta Crystallographica Section D-Biological Crystallography, 57(12), 1895-1896

The Azotobacter vinelandii NifL protein is a redox-sensing flavoprotein which inhibits the activity of the nitrogen-specific transcriptional activator NifA. The N-terminal PAS domain has been overexpressed in Escherichia coli and crystallized by the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a8fffe07e7dad256e7b7666f60ef352
https://research.wur.nl/en/publications/crystallization-and-preliminary-crystallographic-data-of-the-pas-

The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis

Autor: Cristofer Enroth, Halina Y. Neujahr, Ylva Lindqvist, Gunter Schneider

Publikováno v: Structure (London, England : 1993). 6(5)

Background: The synthesis of phenolic compounds as by-products of industrial reactions poses a serious threat to the environment. Understanding the enzymatic reactions involved in the degradation and detoxification of these compounds is therefore of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::577b0405e2e6ea625fc84aa375ced9e9
https://pubmed.ncbi.nlm.nih.gov/9634698