Literature for TLCK (S01.151 inhibitor)

Summary Literature Inhibits

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

    2014
  1. Reuther,C., Ganjam,G.K., Dolga,A.M. and Culmsee,C.
    The serine protease inhibitor TLCK attenuates intrinsic death pathways in neurons upstream of mitochondrial demise
    Apoptosis (2014) 19, 1545-1558. PubMed  Europe PubMed DOI  I
  2. 2009
  3. Ha,K.H., Byun,M.S., Choi,J., Jeong,J., Lee,K.J. and Jue,D.M.
    N-Tosyl-l-phenylalanine chloromethyl ketone inhibits NF-kappaB activation by blocking specific cysteine residues of IkappaB kinase beta and p65/RelA
    Biochemistry (2009) 48, 7271-7278. PubMed  Europe PubMed DOI  I
  4. 2008
  5. Frydrych,I. and Mlejnek,P.
    Serine protease inhibitors N-alpha-tosyl-L-lysinyl-chloromethylketone (TLCK) and N-tosyl-l-phenylalaninyl-chloromethylketone (TPCK) are potent inhibitors of activated caspase proteases
    J Cell Biochem (2008) 103, 1646-1656. PubMed  Europe PubMed DOI  I
  6. 1996
  7. Stoppler,H., Stoppler,M.C., Adduci,A., Koval,D. and Schlegel,R.
    The serine protease inhibitors TLCK and TPCK react with the RB-binding core of HPV-18 E7 protein and abolish its RB-binding capability
    Virology (1996) 217, 542-553. PubMed  Europe PubMed DOI  I
  8. 1990
  9. [YEAR:15-5-1990]Greco,N.J., Tenner,T.E., Jr., Tandon,N.N. and Jamieson,G.A.
    PPACK-thrombin inhibits thrombin-induced platelet aggregation and cytoplasmic acidification but does not inhibit platelet shape change
    Blood (15-5-1990) 75, 1989-1990. PubMed  Europe PubMed  I
  10. 1984
  11. [YEAR:23-7-1984]Gilles,A.M. and Keil,B.
    Evidence for an active-center cysteine in the SH-proteinase alpha-clostripain through use of N-tosyl-L-lysine chloromethyl ketone
    FEBS Lett (23-7-1984) 173, 58-62. PubMed  Europe PubMed  I
  12. 1983
  13. Malthouse,J.P.G., Mackenzie,N.E., Boyd,A.S.F. and Scott,A.I.
    Detection of a tetrahedral adduct in a trypsin-chloromethyl ketone specific inhibitor complex by 13C NMR
    J Am Chem Soc (1983) 105, 1685-1686.  I
  14. 1976
  15. Poulos,T.L., Alden,R.A., Freer,S.T., Birktoft,J.J. and Kraut,J.
    Polypeptide halomethyl ketones bind to serine proteases as analogs of the tetrahedral intermediate. X-ray crystallographic comparison of lysine- and phenylalanine-polypeptide chloromethyl ketone-inhibited subtilisin
    J Biol Chem (1976) 251, 1097-1103. PubMed  Europe PubMed  S  I
  16. 1971
  17. Porter,W.H., Cunningham,L.W. and Mitchell,W.M.
    Studies on the active site of clostripain. The specific inactivation by the chloromethyl ketone derived from alpha-N-tosyl-L-lysine
    J Biol Chem (1971) 246, 7675-7682. PubMed  Europe PubMed  I
  18. 1969
  19. Smith,R.L. and Shaw,E.
    Pseudotrypsin. A modified bovine trypsin produced by limited autodigestion
    J Biol Chem (1969) 244, 4704-4712. PubMed  Europe PubMed  I
  20. Wolthers,B.C.
    Kinetics of inhibition of papain by TLCK and TPCK in the presence of BAEE as substrate
    FEBS Lett (1969) 2, 143-145. PubMed  Europe PubMed  I
  21. 1968
  22. [YEAR:20-3-1968]Whitaker,J.R. and Perez-Villase nor,J.
    Chemical modification of papain. I. Reaction with the chloromethyl ketones of phenylalanine and lysine and with phenylmethyl-sulfonyl fluoride
    Arch Biochem Biophys (20-3-1968) 124, 70-78. PubMed  Europe PubMed  I
  23. 1967
  24. [YEAR:10-4-1967]Kafatos,F.C., Law,J.H. and Tartakoff,A.M.
    Cocoonase. II. Substrate specificity, inhibitors, and classification of the enzyme
    J Biol Chem (10-4-1967) 242, 1488-1494. PubMed  Europe PubMed  I
  25. 1965
  26. [YEAR:21-12-1965]Petra,P.H., Cohen,W. and Shaw,E.N.
    Isolation and characterization of the alkylated histidine from TLCK inhibited trypsin
    Biochem Biophys Res Commun (21-12-1965) 21, 612-618. PubMed  Europe PubMed  I
  27. Shaw,E., Mares-Guia,M. and Cohen,W.
    Evidence for an active-center histidine in trypsin through use of a specific reagent, 1-chloro-3-tosylamido-7-amino-2-heptanone, the chloromethyl ketone derived from Nalpha-tosyl-L-lysine
    Biochemistry (1965) 4, 2219-2224.  I