Literature for peptidase C01.013: cathepsin X
(References are filtered for relevance to Inhibitor. To remove the filter click here. See explanation.)
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Fonovic,U.P., Knez,D., Hrast,M., Zidar,N., Proj,M., Gobec,S. and Kos,J.
Structure-activity relationships of triazole-benzodioxine inhibitors of cathepsin X
Eur J Med Chem193, 112218-112218. PubMed Europe PubMed DOI I -
Mountford,S.J., Anderson,B.M., Xu,B., Tay,E.S.V., Szabo,M., Hoang,M.L., Diao,J., Aurelio,L., Campden,R.I., Lindstrom,E., Sloan,E.K., Yates,R.M., Bunnett,N.W., Thompson,P.E. and Edgington-Mitchell,L.E.
Application of a sulfoxonium ylide electrophile to generate cathepsin X-selective activity-based probes
ACS Chem Biol15, 718-727. PubMed Europe PubMed DOI I -
Fonovic,U.P., Mitrovic,A., Knez,D., Jakos,T., Pislar,A., Brus,B., Doljak,B., Stojan,J., Zakelj,S., Trontelj,J., Gobec,S. and Kos,J.
Identification and characterization of the novel reversible and selective cathepsin X inhibitors
Sci Rep7, 11459-11459. PubMed Europe PubMed DOI I -
Pislar,A., Bozic,B., Zidar,N. and Kos,J.
Inhibition of cathepsin X reduces the strength of microglial-mediated neuroinflammation
Neuropharmacology114, 88-100. PubMed Europe PubMed DOI I -
Pecar Fonovic,U., Jevnikar,Z., Rojnik,M., Doljak,B., Fonovic,M., Jamnik,P. and Kos,J.
Profilin 1 as a target for cathepsin X activity in tumor cells
PLoS ONE8, e53918-e53918. PubMed Europe PubMed DOI I -
Skvarc,M., Stubljar,D., Kopitar,A.N., Jeverica,S., Tepes,B., Kos,J. and Ihan,A.
Inhibition of cathepsin X enzyme influences the immune response of THP-1 cells and dendritic cells infected with Helicobacter pylori
Radiol Oncol47, 258-265. PubMed Europe PubMed DOI I -
Menard,R., Therrien,C., Lachance,P., Sulea,T., Qo,H., Alvarez-Hernandez,A.D. and Roush,W.R.
Cathepsins X and B display distinct activity profiles that can be exploited for inhibitor design
Biol Chem382, 839-845. PubMed Europe PubMed DOI I -
[YEAR:6-3-2001]Therrien,C., Lachance,P., Sulea,T., Purisima,E.O., Qi,H., Ziomek,E., Alvarez-Hernandez,A., Roush,W.R. and Menard,R.
Cathepsins X and B can be differentiated through their respective mono- and dipeptidyl carboxypeptidase activities
Biochemistry40, 2702-2711. PubMed Europe PubMed DOI I -
Klemencic,I., Carmona,A.K., Cezari,M.H.S., Juliano,M.A., Juliano,L., Guncar,G., Turk,D., Krizaj,I., Turk,V. and Turk,B.
Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase
Eur J Biochem267, 5404-5412. PubMed Europe PubMed DOI I
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