Fig. 1. Multiple amino acid sequence alignment of C. procera cysteine peptidases. Sequence alignment was performed with C. procera cysteine peptidases (CpCP A-E), (SnuCalCp 01–20), procerain B, procerain and papain. The highly conserved cysteine residues that participate in the disulfide bond formation are highlighted in gray and the conserved residues involved in the active site are indicated by vertical black arrows.Published as part of Freitas, Cleverson D.T., Silva, Rafaela O., Ramos, Márcio V., Porfírio, Camila T.M.N., Farias, Davi F., Sousa, Jeanlex S., Oliveira, João P.B., Souza, Pedro F.N., Dias, Lucas P. & Grangeiro, Thalles B., 2020, Identification, characterization, and antifungal activity of cysteine peptidases from Calotropis p...
<p>Amino acid sequence alignment of <i>P. aeruginosa</i> and <i>B. phytofirmans</i> Tse1 (A) and Tsi...
<p>(A) Structure-based alignment of the amino acid sequences of serine proteases from <i>Pseudoalter...
Asclepain f is a papain-like protease previously isolated and characterized from latex of Asclepias ...
Freitas, Cleverson D.T., Silva, Rafaela O., Ramos, Márcio V., Porfírio, Camila T.M.N., Farias, Davi ...
Fig. 2. Three-dimensional models of cysteine peptidases from Calotropis procera (CpCP A, CpCP C and ...
Fig. 4. Antifungal activity of three cysteine peptidases (CpCP1, CpCP2 and CpCP3) from Calotropis pr...
Fig. 3. Effect of pH, temperature and substrate concentration on the proteolytic activity of CpCP1, ...
Fig. 6. Membrane permeabilization induced by cysteine peptidases from Calotropis procera latex in sp...
Fig. 5. Atomic force microscopic images of Fusarium oxysporum spores treated with the three cysteine...
Fig. 7. Detection of ROS in spores of F. oxysporum after treatment with latex peptidases (CpCP1, CpC...
The latex of Calotropis procera is a rich source of proteolytic activity. This latex is known to con...
Calotropis procera R. Br., a traditional medicinal plant in India, is a promising source of commerci...
Calotropis procera R. Br., a traditional medicinal plant in India, is a promising source of com-merc...
AbstractThe latex of Calotropis procera is a rich source of proteolytic activity. This latex is know...
<p>Predicted amino acid sequences of a papain, NTCP23 (CysP1), CysP2, CysP4, CysP5, NTCP6 (CysP6), C...
<p>Amino acid sequence alignment of <i>P. aeruginosa</i> and <i>B. phytofirmans</i> Tse1 (A) and Tsi...
<p>(A) Structure-based alignment of the amino acid sequences of serine proteases from <i>Pseudoalter...
Asclepain f is a papain-like protease previously isolated and characterized from latex of Asclepias ...
Freitas, Cleverson D.T., Silva, Rafaela O., Ramos, Márcio V., Porfírio, Camila T.M.N., Farias, Davi ...
Fig. 2. Three-dimensional models of cysteine peptidases from Calotropis procera (CpCP A, CpCP C and ...
Fig. 4. Antifungal activity of three cysteine peptidases (CpCP1, CpCP2 and CpCP3) from Calotropis pr...
Fig. 3. Effect of pH, temperature and substrate concentration on the proteolytic activity of CpCP1, ...
Fig. 6. Membrane permeabilization induced by cysteine peptidases from Calotropis procera latex in sp...
Fig. 5. Atomic force microscopic images of Fusarium oxysporum spores treated with the three cysteine...
Fig. 7. Detection of ROS in spores of F. oxysporum after treatment with latex peptidases (CpCP1, CpC...
The latex of Calotropis procera is a rich source of proteolytic activity. This latex is known to con...
Calotropis procera R. Br., a traditional medicinal plant in India, is a promising source of commerci...
Calotropis procera R. Br., a traditional medicinal plant in India, is a promising source of com-merc...
AbstractThe latex of Calotropis procera is a rich source of proteolytic activity. This latex is know...
<p>Predicted amino acid sequences of a papain, NTCP23 (CysP1), CysP2, CysP4, CysP5, NTCP6 (CysP6), C...
<p>Amino acid sequence alignment of <i>P. aeruginosa</i> and <i>B. phytofirmans</i> Tse1 (A) and Tsi...
<p>(A) Structure-based alignment of the amino acid sequences of serine proteases from <i>Pseudoalter...
Asclepain f is a papain-like protease previously isolated and characterized from latex of Asclepias ...