Azurin interaction with the lipid raft components ganglioside GM-1 and caveolin-1 increases membrane fluidity and sensitivity to anti-cancer drugs-Reference-Cited by-同舟云学术

Azurin interaction with the lipid raft components ganglioside GM-1 and caveolin-1 increases membrane fluidity and sensitivity to anti-cancer drugs

Published:2018-07-03 Issue:13 Volume:17 Page:1649-1666
ISSN:1538-4101
Container-title:Cell Cycle
language:en
Short-container-title:Cell Cycle

Author:

Bernardes Nuno¹^ORCID,Garizo Ana Rita¹^ORCID,Pinto Sandra N.²^ORCID,Caniço Bernardo¹,Perdigão Catarina¹^ORCID,Fernandes Fábio²³^ORCID,Fialho Arsenio M.¹⁴^ORCID

Affiliation:

1. iBB-Institute for Bioengineering and Biosciences, Biological Sciences Research Group, Lisbon, Portugal

2. Centro de Química-Física Molecular and Institute of Nanoscience and Nanotechnology, Instituto Superior Técnico, Lisbon, Portugal

3. UCIBIO, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Caparica, Portugal

4. Department of Bioengineering, Instituto Superior Técnico, University of Lisbon, Lisbon, Portugal

Funder

Fundação para a Ciência e a Tecnologia

Publisher

Informa UK Limited

Subject

Cell Biology,Developmental Biology,Molecular Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/15384101.2018.1489178

Reference48 articles.

1. Bacterial redox protein azurin, tumor suppressor protein p53, and regression of cancer

2. Noncationic Peptides Obtained From Azurin Preferentially Enter Cancer Cells

3. A cell penetrating peptide derived from azurin inhibits angiogenesis and tumor growth by inhibiting phosphorylation of VEGFR-2, FAK and Akt

4. A peptide fragment of azurin induces a p53-mediated cell cycle arrest in human breast cancer cells

5. Modulation of membrane properties of lung cancer cells by azurin enhances the sensitivity to EGFR-targeted therapy and decreased β1 integrin-mediated adhesion

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