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Solution structure of the anticancer p28 peptide in biomimetic medium

open access: yesJournal of Peptide Science, 2021
The p28 peptide derived from Pseudomonas aeruginosa azurin shows an anticancer activity after binding to p53 protein and is currently in Phase I of clinical trials. We have studied its structure in water and in a biomimetic media and show that the peptide is unstructured in water but when studied in a biomimetic medium assumes a structure very similar ...
Francesca Cantini   +2 more
exaly   +7 more sources
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Anticancer Actions of Azurin and Its Derived Peptide p28

Protein Journal, 2020
Cancers are a great threat to humans. In cancer therapy, surgical removal of the tumor combined with radiotherapy and chemotherapy is the most routine treatment procedure and usually the most effective. However, radiotherapy and chemotherapy drugs that kill cancer cells efficiently also kill normal cells, thus exhibiting large side effects.
Zhengding Su, Yongqi Huang, Meng Gao
exaly   +3 more sources

Cellular Source of the Poxviral N1R/p28 Gene Family

Virus Genes, 2004
Full-length poxvirus N1R/p28 orthologous proteins feature a prominent C-terminal RING zinc-finger motif. The RING moiety is conspicuously mutated in a number of vaccinia virus strains relative to variola virus. This, together with empirical data, suggests that N1R/p28 proteins promote virulence by suppressing apoptosis. Poxvirus N1R/p28 orthologues are
Robert Nicholls   +2 more
exaly   +3 more sources

Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle

open access: yesMolecular Cell, 2017
The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP ...
Ying Lu, Yuanchen Dong, Shuobing Chen
exaly   +2 more sources

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