Literature for peptidase C01.099: ervatamin B

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

2017
1. Uday,P., Maheshwari,M., Sharanappa,P., Nafeesa,Z., Kameshwar,V.H., Priya,B.S. and Nanjunda Swamy,S.
   Exploring hemostatic and thrombolytic potential of heynein - a cysteine protease from Ervatamia heyneana latex
   J Ethnopharmacol199, 316-322. PubMed  Europe PubMed DOI
2015
2. Singh,M.K., Usha,R., Hithayshree,K.R. and Bindhu,O.S.
   Hemostatic potential of latex proteases from Tabernaemontana divaricata (L.) R. Br. ex. Roem. and Schult. and Artocarpus altilis (Parkinson ex. F.A. Zorn) Forsberg
   J Thromb Thrombolysis39, 43-49. PubMed  Europe PubMed DOI
2011
3. Prasanna Kumari,N.K. and Jagannadham,M.V.
   SDS induced molten globule state of heynein; a new thiol protease: evidence of domains and their sequential unfolding
   Colloids Surf B Biointerfaces82, 609-615. PubMed  Europe PubMed DOI
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
2003
5. [YEAR:1-6-2003]Biswas,S., Chakrabarti,C., Kundu,S., Jagannadham,M.V. and Dattagupta,J.K.
   Proposed amino acid sequence and the 1.63 A X-ray crystal structure of a plant cysteine protease, ervatamin B: some insights into the structural basis of its stability and substrate specificity
   Proteins51, 489-497. PubMed  Europe PubMed DOI  S
6. [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
2002
7. [YEAR:31-3-2002]Kundu,S., Sundd,M. and Jagannadham,M.V.
   Alcohol and temperature induced conformational transitions in ervatamin B: sequential unfolding of domains
   J Biochem Mol Biol35, 155-164. PubMed  Europe PubMed
8. [YEAR:31-3-2002]Sundd,M., Kundu,S. and Jagannadham,M.V.
   Acid and chemical induced conformational changes of ervatamin B. Presence of partially structured multiple intermediates
   J Biochem Mol Biol35, 143-154. PubMed  Europe PubMed
2000
9. Kundu,S., Sundd,M. and Jagannadham,M.V.
   Purification and characterization of a stable cysteine protease ervatamin B, with two disulfide bridges, from the latex of Ervatamia coronaria
   J Agric Food Chem48, 171-179. PubMed  Europe PubMed DOI
1999
10. 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
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.