Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Neeta Asthana"'
Publikováno v:
Journal of Biological Chemistry. 279:55042-55050
Melittin, a naturally occurring antimicrobial peptide, exhibits strong lytic activity against both eukaryotic and prokaryotic cells. Despite a tremendous amount of work done, very little is known about the amino acid sequence, which regulates its tox
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2d10040e3db11a4ebf2dee327f5aa51e
https://doi.org/10.1074/jbc.m408881200
https://doi.org/10.1074/jbc.m408881200
Autor:
Sarfuddin Azmi, Saurabh Srivastava, Achchhe Lal Vishwakarma, Richa Verma, Brijesh K. Pandey, Raghvendra M. Srivastava, Neeta Asthana, Jimut Kanti Ghosh, Aqeel Ahmad
Publikováno v:
Biochemistry. 49(36)
Melittin is a good model antimicrobial peptide to understand the basis of its lytic activities against bacteria and mammalian cells. Novel analogues of melittin were designed by substituting the leucine residue(s) at the "d" and "a" positions of its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29be988f9fe33527102a2b011799e748
https://pubmed.ncbi.nlm.nih.gov/20695504
https://pubmed.ncbi.nlm.nih.gov/20695504
Autor:
Aqeel Ahmad, Jimut Kanti Ghosh, Sharada Prasad Yadav, Richa Verma, Brijesh K. Pandey, Dharamsheela Singh, Raj Kamal Tripathi, Neeta Asthana
Publikováno v:
Biochimica et biophysica acta. 1788(2)
Hemolysin E (HlyE), a pore-forming protein-toxin and a potential virulence factor of Escherichia coli , exhibits cytotoxic activity to mammalian cells. However, very little is known about how the different individual segments contribute in the toxic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71a1df4ee0e8a96077437ac9a15e3a81
https://pubmed.ncbi.nlm.nih.gov/19111524
https://pubmed.ncbi.nlm.nih.gov/19111524
Autor:
Swati Prakash Srivastava, Aqeel Ahmad, Jimut Kanti Ghosh, Kalyan Mitra, Sharada Prasad Yadav, Neeta Asthana
Publikováno v:
The Journal of biological chemistry. 281(31)
The toxicity of naturally occurring or designed antimicrobial peptides is a major barrier for converting them into drugs. To synthesize antimicrobial peptides with reduced toxicity, several amphipathic peptides were designed based on the leucine zipp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b357ebe2bf2a7ade01171ddf5ef25ca2
https://pubmed.ncbi.nlm.nih.gov/16717087
https://pubmed.ncbi.nlm.nih.gov/16717087
Publikováno v:
The Journal of biological chemistry. 279(53)
Melittin, a naturally occurring antimicrobial peptide, exhibits strong lytic activity against both eukaryotic and prokaryotic cells. Despite a tremendous amount of work done, very little is known about the amino acid sequence, which regulates its tox
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a2b029c1ec7b95b35184fc5a1cc23de8
https://pubmed.ncbi.nlm.nih.gov/15475354
https://pubmed.ncbi.nlm.nih.gov/15475354
Autor:
Raghvendra M. Srivastava, Neeta Asthana, Brijesh K. Pandey, Jimut Kanti Ghosh, Sarfuddin Azmi, Aqeel Ahmad, Vikas Yadav
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. (11):2411-2420
Although BMAP-28 is a potent cathelicidin-derived bovine antimicrobial peptide, its cytotoxic activity against the human and other mammalian cells is of concern for converting it into a novel antimicrobial drug. We have identified a short leucine and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ded4dd1029cca1cf7643c994e275f9dc