Literature for inhibitor I29.001: cathepsin L propeptide

(Topics flags: S Structure, E Expression. To select only the references relevant to a single topic, click the link above. See explanation.)

2018
1. Cardenas-Guerra,R.E., Martinez-Castillo,M., Ortega-Lopez,J., Shibayama,M. and Arroyo,R.
   Dataset of cathepsin L-like CP inhibition of Naegleria fowleri and Acanthamoeba castellanii by ppTvCP4r from Trichomonas vaginalis
   Data Brief (2018) 18, 404-408. PubMed  Europe PubMed DOI  PMC  EPMC
2. Kwon,C.W., Yang,H., Yeo,S., Park,K.M., Jeong,A.J., Lee,K.W., Ye,S.K. and Chang,P.S.
   Molecular cloning and anti-invasive activity of cathepsin L propeptide-like protein from Calotropis procera R. Br. against cancer cells
   J Enzyme Inhib Med Chem (2018) 33, 657-664. PubMed  Europe PubMed DOI
2001
3. [YEAR:25-4-2001]Alves,L.C., St Hilaire,P.M., Meldal,M., Sanderson,S.J., Mottram,J.C., Coombs,G.H., Juliano,L. and Juliano,M.A.
   Identification of peptides inhibitory to recombinant cysteine proteinase, CPB, of Leishmania mexicana
   Mol Biochem Parasitol (25-4-2001) 114, 81-88. PubMed  Europe PubMed DOI
2000
4. Guay,J., Falgueyret,J.P., Ducret,A., Percival,M.D. and Mancini,J.A.
   Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides
   Eur J Biochem (2000) 267, 6311-6318. PubMed  Europe PubMed DOI
5. [YEAR:10-3-2000]Guo,Y.L., Kurz,U., Schultz,J.E., Lim,C.C., Wiederanders,B. and Schilling,K.
   The alpha1/2 helical backbone of the prodomains defines the intrinsic inhibitory specificity in the cathepsin L-like cysteine protease subfamily
   FEBS Lett (10-3-2000) 469, 203-207. PubMed  Europe PubMed DOI
1999
6. [YEAR:25-1-1999]Roche,L., Tort,J. and Dalton,J.P.
   The propeptide of Fasciola hepatica cathepsin L is a potent and selective inhibitor of the mature enzyme
   Mol Biochem Parasitol (25-1-1999) 98, 271-277. PubMed  Europe PubMed DOI
1998
7. [YEAR:1-9-1998]Groves,M.R., Coulombe,R., Jenkins,J. and Cygler,M.
   Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes
   Proteins (1-9-1998) 32, 504-514. PubMed  Europe PubMed DOI
1997
8. Cygler,M. and Mort,J.S.
   Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity
   Biochimie (1997) 79, 645-652. PubMed  Europe PubMed DOI
1996
9. Carmona,E., Dufour,E., Plouffe,C., Takebe,S., Mason,P., Mort,J.S. and Menard,R.
   Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases
   Biochemistry (1996) 35, 8149-8157. PubMed  Europe PubMed DOI
10. Coulombe,R., Grochulski,P., Sivaraman,J., Menard,R., Mort,J.S. and Cygler,M.
    Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
    EMBO J (1996) 15, 5492-5503. PubMed  Europe PubMed  PMC  EPMC  E  S
11. Volkel,H., Kurz,U., Linder,J., Klumpp,S., Gnau,V., Jung,G. and Schultz,J.E.
    Cathepsin L is an intracellular and extracellular protease in Paramecium tetraurelia. Purification, cloning, sequencing and specific inhibition by its expressed propeptide
    Eur J Biochem (1996) 238, 198-206. PubMed  Europe PubMed