Lecaille F - Search Results

1

Probing cathepsin K activity with a selective substrate spanning its active site.

Lecaille F, Weidauer E, Juliano MA, Brömme D, Lalmanach G. Lecaille F, et al. Biochem J. 2003 Oct 15;375(Pt 2):307-12. doi: 10.1042/BJ20030468. Biochem J. 2003. PMID: 12837132 Free PMC article.

2

Inhibition of trypanosomal cysteine proteinases by their propeptides.

Lalmanach G, Lecaille F, Chagas JR, Authié E, Scharfstein J, Juliano MA, Gauthier F. Lalmanach G, et al. Among authors: lecaille f. J Biol Chem. 1998 Sep 25;273(39):25112-6. doi: 10.1074/jbc.273.39.25112. J Biol Chem. 1998. PMID: 9737969 Free article.

3

Revisiting the S2 specificity of papain by structural analogs of Phe.

Lecaille F, Serveau C, Gauthier F, Lalmanach G. Lecaille F, et al. FEBS Lett. 1999 Feb 26;445(2-3):311-4. doi: 10.1016/s0014-5793(99)00143-x. FEBS Lett. 1999. PMID: 10094479 Free article.

4

Subsite specificity of trypanosomal cathepsin L-like cysteine proteases. Probing the S2 pocket with phenylalanine-derived amino acids.

Lecaille F, Authié E, Moreau T, Serveau C, Gauthier F, Lalmanach G. Lecaille F, et al. Eur J Biochem. 2001 May;268(9):2733-41. doi: 10.1046/j.1432-1327.2001.02172.x. Eur J Biochem. 2001. PMID: 11322895 Free article.

5

Reversible inhibition of cathepsin L-like proteases by 4-mer pseudopeptides.

Lecaille F, Cotton J, McKerrow JH, Ferrer-Di Martino M, Boll-Bataillé E, Gauthier F, Lalmanach G. Lecaille F, et al. FEBS Lett. 2001 Nov 2;507(3):362-6. doi: 10.1016/s0014-5793(01)03008-3. FEBS Lett. 2001. PMID: 11696372 Free article.

The peptides share the framework: Cha-X1-X2-Pro (Cha=cyclohexyl-alanine, X1 and X2 were phenylalanyl analogs), based on a previous report [Lecaille, F., Authie, E., Moreau, T., Serveau, C., Gauthier, F. and Lalmanach, G. (2001) Eur. ...

The peptides share the framework: Cha-X1-X2-Pro (Cha=cyclohexyl-alanine, X1 and X2 were phenylalanyl analogs), based on a previous report [ …

6

Selective inhibition of the collagenolytic activity of human cathepsin K by altering its S2 subsite specificity.

Lecaille F, Choe Y, Brandt W, Li Z, Craik CS, Brömme D. Lecaille F, et al. Biochemistry. 2002 Jul 2;41(26):8447-54. doi: 10.1021/bi025638x. Biochemistry. 2002. PMID: 12081494

7

Congopain from Trypanosoma congolense: drug target and vaccine candidate.

Lalmanach G, Boulangé A, Serveau C, Lecaille F, Scharfstein J, Gauthier F, Authié E. Lalmanach G, et al. Among authors: lecaille f. Biol Chem. 2002 May;383(5):739-49. doi: 10.1515/BC.2002.077. Biol Chem. 2002. PMID: 12108538 Review.

8

Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design.

Lecaille F, Kaleta J, Brömme D. Lecaille F, et al. Chem Rev. 2002 Dec;102(12):4459-88. doi: 10.1021/cr0101656. Chem Rev. 2002. PMID: 12475197 Review. No abstract available.

9

Procongopain from Trypanosoma congolense is processed at basic pH: an unusual feature among cathepsin L-like cysteine proteases.

Serveau C, Boulangé A, Lecaille F, Gauthier F, Authié E, Lalmanach G. Serveau C, et al. Among authors: lecaille f. Biol Chem. 2003 Jun;384(6):921-7. doi: 10.1515/BC.2003.103. Biol Chem. 2003. PMID: 12887059

10

Cathepsin K: a cysteine protease with unique kinin-degrading properties.

Godat E, Lecaille F, Desmazes C, Duchêne S, Weidauer E, Saftig P, Brömme D, Vandier C, Lalmanach G. Godat E, et al. Among authors: lecaille f. Biochem J. 2004 Nov 1;383(Pt. 3):501-6. doi: 10.1042/BJ20040864. Biochem J. 2004. PMID: 15265002 Free PMC article.

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