Wsol V - Search Results

1

Purification and characterization of akr1b10 from human liver: role in carbonyl reduction of xenobiotics.

Martin HJ, Breyer-Pfaff U, Wsol V, Venz S, Block S, Maser E. Martin HJ, et al. Among authors: wsol v. Drug Metab Dispos. 2006 Mar;34(3):464-70. doi: 10.1124/dmd.105.007971. Epub 2005 Dec 28. Drug Metab Dispos. 2006. PMID: 16381663

2

11Beta-hydroxysteroid dehydrogenase type 1: purification from human liver and characterization as carbonyl reductase of xenobiotics.

Maser E, Wsol V, Martin HJ. Maser E, et al. Among authors: wsol v. Mol Cell Endocrinol. 2006 Mar 27;248(1-2):34-7. doi: 10.1016/j.mce.2005.10.019. Epub 2005 Dec 15. Mol Cell Endocrinol. 2006. PMID: 16343739

3

Partial purification and characterization of a new human membrane-bound carbonyl reductase playing a role in the deactivation of the anticancer drug oracin.

Skarydová L, Skarka A, Novotná R, Zivná L, Martin HJ, Wsól V, Maser E. Skarydová L, et al. Among authors: wsol v. Toxicology. 2009 Oct 1;264(1-2):52-60. doi: 10.1016/j.tox.2009.07.013. Epub 2009 Jul 25. Toxicology. 2009. PMID: 19635524

4

Human carbonyl reductases.

Malátková P, Maser E, Wsól V. Malátková P, et al. Among authors: wsol v. Curr Drug Metab. 2010 Oct;11(8):639-58. doi: 10.2174/138920010794233530. Curr Drug Metab. 2010. PMID: 20942781 Review.

5

Proteasome inhibitors MG-132 and bortezomib induce AKR1C1, AKR1C3, AKR1B1, and AKR1B10 in human colon cancer cell lines SW-480 and HT-29.

Ebert B, Kisiela M, Wsól V, Maser E. Ebert B, et al. Among authors: wsol v. Chem Biol Interact. 2011 May 30;191(1-3):239-49. doi: 10.1016/j.cbi.2010.12.026. Epub 2011 Jan 6. Chem Biol Interact. 2011. PMID: 21215737

6

Studies on reduction of S-nitrosoglutathione by human carbonyl reductases 1 and 3.

Staab CA, Hartmanová T, El-Hawari Y, Ebert B, Kisiela M, Wsol V, Martin HJ, Maser E. Staab CA, et al. Among authors: wsol v. Chem Biol Interact. 2011 May 30;191(1-3):95-103. doi: 10.1016/j.cbi.2011.01.016. Epub 2011 Jan 21. Chem Biol Interact. 2011. PMID: 21256830

7

Stereochemical aspects of carbonyl reduction of the original anticancer drug oracin by mouse liver microsomes and purified 11beta-hydroxysteroid dehydrogenase type 1.

Wsól V, Szotáková B, Skálová L, Maser E. Wsól V, et al. Chem Biol Interact. 2003 Feb 1;143-144:459-68. doi: 10.1016/s0009-2797(02)00221-1. Chem Biol Interact. 2003. PMID: 12604232

8

Aldo-keto reductases (AKR) from the AKR1C subfamily catalyze the carbonyl reduction of the novel anticancer drug oracin in man.

Wsol V, Szotakova B, Martin HJ, Maser E. Wsol V, et al. Toxicology. 2007 Sep 5;238(2-3):111-8. doi: 10.1016/j.tox.2007.05.021. Epub 2007 May 26. Toxicology. 2007. PMID: 17618725

9

Structural basis for substrate specificity in human monomeric carbonyl reductases.

Pilka ES, Niesen FH, Lee WH, El-Hawari Y, Dunford JE, Kochan G, Wsol V, Martin HJ, Maser E, Oppermann U. Pilka ES, et al. Among authors: wsol v. PLoS One. 2009 Oct 20;4(10):e7113. doi: 10.1371/journal.pone.0007113. PLoS One. 2009. PMID: 19841672 Free PMC article.

10

The novel anticancer drug oracin: different stereospecificity and cooperativity for carbonyl reduction by purified human liver 11beta-hydroxysteroid dehydrogenase type 1.

Wsól V, Szotáková B, Skálová L, Maser E. Wsól V, et al. Toxicology. 2004 May 3;197(3):253-61. doi: 10.1016/j.tox.2004.01.009. Toxicology. 2004. PMID: 15033547

Save citations to file

Email citations

Send citations to clipboard

Add to Collections

Add to My Bibliography

Create a file for external citation management software

Your saved search

Your RSS Feed

My Custom Filters

Publication date

Text availability

Article attribute

Article type

Article Language

Species

Sex

Age

Other

100 results

Search Page

Filters