Literature for inhibitor I57.001: staphostatin B

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

2013
1. Yokoi,K.J., Kuzuwa,S., Kondo,M., Yamakawa,A., Taketo,A. and Kodaira,K.
   Inactivation of the serine proteinase operon (proMCD) of Staphylococcus warneri M: serine proteinase and cysteine proteases are involved in the autolysis
   Gene512, 240-246. PubMed  Europe PubMed DOI
2012
2. Bhaskar,A., Upgade,A. and Kavitha,P.
   Characterization of keratitis disease causing 56k cysteine protease encoding gene from Serratia marcescens
   J Proteomics Bioinformatics5, 226-229. DOI
2011
3. Kantyka,T., Shaw,L.N. and Potempa,J.
   Papain-like proteases of Staphylococcus aureus
   Adv Exp Med Biol712, 1-14. PubMed  Europe PubMed DOI  V
2010
4. Nickerson,N., Ip,J., Passos,D.T. and McGavin,M.J.
   Comparison of staphopain A (ScpA) and B (SspB) precursor activation mechanisms reveals unique secretion kinetics of proSspB (staphopain B), and a different interaction with its cognate staphostatin, SspC
   Mol Microbiol75, 161-177. PubMed  Europe PubMed DOI
2007
5. Dubin,G., Wladyka,B., Stec-Niemczyk,J., Chmiel,D., Zdzalik,M., Dubin,A. and Potempa,J.
   The staphostatin family of cysteine protease inhibitors in the genus Staphylococcus as an example of parallel evolution of protease and inhibitor specificity
   Biol Chem388, 227-235. PubMed  Europe PubMed DOI
2006
6. Potempa,J., Travis,J., Golonka,E. and Shaw,L.
   Poison-antidote systems in bacteria: the co-evolution of functional counterparts
   Cell Mol Biol (Noisy-le-grand)52, 18-22. PubMed  Europe PubMed DOI  V
2005
7. [YEAR:11-1-2005]Filipek,R., Potempa,J. and Bochtler,M.
   A comparison of staphostatin B with standard mechanism serine protease inhibitors
   J Biol Chem280, 14669-14674. PubMed  Europe PubMed DOI  S
8. Potempa,J., Golonka,E., Filipek,R. and Shaw,L.N.
   Fighting an enemy within: cytoplasmic inhibitors of bacterial cysteine proteases
   Mol Microbiol57, 605-610. PubMed  Europe PubMed DOI
9. Shaw,L.N., Golonka,E., Szmyd,G., Foster,S.J., Travis,J. and Potempa,J.
   Cytoplasmic control of premature activation of a secreted protease zymogen: deletion of staphostatin B (SspC) in Staphylococcus aureus 8325-4 yields a profound pleiotropic phenotype
   J Bacteriol187, 1751-1762. PubMed  Europe PubMed DOI
2003
10. Dubin,G.
    Defense against own arms: staphylococcal cysteine proteases and their inhibitors
    Acta Biochim Pol50, 715-724. PubMed  Europe PubMed DOI
11. [YEAR:17-10-2003]Filipek,R., Rzychon,M., Oleksy,A., Gruca,M., Dubin,A., Potempa,J. and Bochtler,M.
    The staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease
    J Biol Chem278, 40959-40966. PubMed  Europe PubMed DOI  S
12. Rzychon,M., Sabat,A., Kosowska,K., Potempa,J. and Dubin,A.
    Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases
    Mol Microbiol49, 1051-1066. PubMed  Europe PubMed DOI
13. Rzychon,M., Filipek,R., Sabat,A., Kosowska,K., Dubin,A., Potempa,J. and Bochtler,M.
    Staphostatins resemble lipocalins, not cystatins in fold
    Protein Sci12, 2252-2256. PubMed  Europe PubMed DOI  S
2002
14. [YEAR:1-11-2002]Massimi,I., Park,E., Rice,K., Muller-Esterl,W., Sauder,D. and McGavin,M.J.
    Identification of a novel maturation mechanism and restricted substrate specificity for the SspB cysteine protease of Staphylococcus aureus
    J Biol Chem277, 41770-41777. PubMed  Europe PubMed DOI