A Combinatorial Approach Defines Specificities of Members of the Caspase Family and Granzyme B
- N. Thornberry, T. Rano, D. Nicholson
- BiologyJournal of Biological Chemistry
- 18 July 1997
A novel method employing a positional scanning substrate combinatorial library to rigorously define individual specificities of caspase and granzyme B proteases divides these proteases into three distinct groups and suggests that several have redundant functions.
Inhibition of Human Caspases by Peptide-based and Macromolecular Inhibitors*
- M. Garcia-Calvo, E. Peterson, B. Leiting, R. Ruel, D. Nicholson, N. Thornberry
- Biology, ChemistryJournal of Biological Chemistry
- 4 December 1998
The results obtained with peptide-based inhibitors are in accord with those predicted from the substrate specificity studies described earlier, and the cowpox serpin CrmA is a potent and selective inhibitor of Group I and most Group III caspases, suggesting that this virus facilitates infection through inhibition of both apoptosis and the host inflammatory response.
The target of ezetimibe is Niemann-Pick C1-Like 1 (NPC1L1).
- M. Garcia-Calvo, J. Lisnock, N. Thornberry
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 7 June 2005
A binding assay is developed and shown that labeled ezetimibe glucuronide binds specifically to a single site in brush border membranes and to human embryonic kidney 293 cells expressing NPC1L1, which unequivocally establish NPC1 L1 as the direct target of ezETimibe and should facilitate efforts to identify the molecular mechanism of cholesterol transport.
Purification and characterization of three inhibitors of voltage-dependent K+ channels from Leiurus quinquestriatus var. hebraeus venom.
- M. L. García, M. Garcia-Calvo, P. Hidalgo, A. Lee, R. Mackinnon
- Biology, ChemistryBiochemistry
- 7 June 1994
Three new toxins from the venom of the scorpion Leiurus quinquestriatus var. hebraeus have been identified on the basis of their ability to block the Shaker K+ channel. These toxins have been…
Tremorgenic indole alkaloids potently inhibit smooth muscle high-conductance calcium-activated potassium channels.
- H. Knaus, O. McManus, A. Smith
- Biology, ChemistryBiochemistry
- 17 May 1994
Indole diterpenes are the most potent nonpeptidyl inhibitors of maxi-K channels identified to date, although tremorgenicity may be unrelated to channel block.
Purification, characterization, and biosynthesis of margatoxin, a component of Centruroides margaritatus venom that selectively inhibits voltage-dependent potassium channels.
- M. Garcia-Calvo, R. Leonard, M. L. García
- BiologyJournal of Biological Chemistry
- 5 September 1993
Biochemical characterization of cholesteryl ester transfer protein inhibitors
- M. Ranalletta, K. Bierilo, T. Fisher
- Biology, ChemistryJournal of Lipid Research
- 1 September 2010
The biochemical characterization of anacetrapib, a potent inhibitor of CETP, was described and dalcetrapib was found to covalently label both human and mouse plasma proteins, indicating that these inhibitors promote the formation of a complex between CETP and HDL, resulting in inhibition of CETp activity.
Primary sequence and immunological characterization of beta-subunit of high conductance Ca(2+)-activated K+ channel from smooth muscle.
- H. Knaus, K. Folander, R. Swanson
- BiologyJournal of Biological Chemistry
- 24 June 1994
The data demonstrate that, in vivo, the high conductance Ca(2+)-activated K+ channel exists as a multimer containing both alpha- andbeta-subunits, and this cDNA represents the first beta-subunit of a potassium channel cloned to date.
Subunit composition of the high conductance calcium-activated potassium channel from smooth muscle, a representative of the mSlo and slowpoke family of potassium channels.
- H. Knaus, M. Garcia-Calvo, G. Kaczorowski, M. L. García
- BiologyJournal of Biological Chemistry
- 11 February 1994
Purification and catalytic properties of human caspase family members
- M. Garcia-Calvo, E. Peterson, N. Thornberry
- BiologyCell Death and Differentiation
- 1 April 1999
To better understand the catalytic properties of caspase family of cysteine proteases, and to facilitate the identification of selective inhibitors, ten homologues of human origin are systematically purified and biochemically characterized.
...
...