Literature for peptidase C01.116: ervatamin C

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

2013
1. Dutta,S., Dattagupta,J.K. and Biswas,S.
   Enhancement of proteolytic activity of a thermostable papain-like protease by structure-based rational design
   PLoS ONE8, e62619-e62619. PubMed  Europe PubMed DOI  E
2011
2. Dutta,S., Choudhury,D., Dattagupta,J.K. and Biswas,S.
   C-terminal extension of a plant cysteine protease modulates proteolytic activity through a partial inhibitory mechanism
   FEBS J278, 3012-3024. PubMed  Europe PubMed DOI
2010
3. Dutta,S., Ghosh,R., Dattagupta,J.K. and Biswas,S.
   Heterologous expression of a thermostable plant cysteine protease in Escherichia coli both in soluble and insoluble forms
   Process Biochem45, 1307-1312. DOI  E
2008
4. Ghosh,R., Chakraborty,S., Chakrabarti,C., Dattagupta,J.K. and Biswas,S.
   Structural insights into the substrate specificity and activity of ervatamins, the papain-like cysteine proteases from a tropical plant, Ervatamia coronaria
   FEBS J275, 421-434. PubMed  Europe PubMed DOI  S
2007
5. Ghosh,R., Dattagupta,J.K. and Biswas,S.
   A thermostable cysteine protease precursor from a tropical plant contains an unusual C-terminal propeptide: cDNA cloning, sequence comparison and molecular modeling studies
   Biochem Biophys Res Commun362, 965-970. PubMed  Europe PubMed DOI
2004
6. [YEAR:17-2-2004]Thakurta,P.G., Biswas,S., Chakrabarti,C., Sundd,M., Jagannadham,M.V. and Dattagupta,J.K.
   Structural basis of the unusual stability and substrate specificity of ervatamin C, a plant cysteine protease from Ervatamia coronaria
   Biochemistry43, 1532-1540. PubMed  Europe PubMed DOI  S
2003
7. [YEAR:8-10-2003]Patel,B.K. and Jagannadham,M.V.
   A high cysteine containing thiol proteinase from the latex of Ervatamia heyneana: purification and comparison with ervatamin B and C from Ervatamia coronaria
   J Agric Food Chem51, 6326-6334. PubMed  Europe PubMed DOI
2000
8. Sundd,M., Kundu,S. and Jagannadham,M.V.
   Alcohol-induced conformational transitions in ervatamin C. An alpha-helix to beta-sheet switchover
   J Protein Chem19, 169-176. PubMed  Europe PubMed DOI
1999
9. Chakrabarti,C., Biswas,S., Kundu,S., Sundd,M., Jagannadham,M.V. and Dattagupta,J.K.
   Crystallization and preliminary X-ray analysis of ervatamin B and C, two thiol proteases from Ervatamia coronaria
   Acta Crystallogr D Biol Crystallogr55, 1074-1075. PubMed  Europe PubMed DOI
10. [YEAR:2-11-1999]Kundu,S., Sundd,M. and Jagannadham,M.V.
    Structural characterization of a highly stable cysteine protease ervatamin C
    Biochem Biophys Res Commun264, 635-642. PubMed  Europe PubMed DOI
1998
11. Sundd,M., Kundu,S., Pal,G.P. and Medicherla,J.V.
    Purification and characterization of a highly stable cysteine protease from the latex of Ervatamia coronaria
    Biosci Biotechnol Biochem62, 1947-1955. PubMed  Europe PubMed DOI
1943
12. Jaffe,W.G.
    A new vegetable proteolytic enzyme of the papain class
    Rev Brasil Biol3, 149-157.