scholarly journals Synthesis and Biological Activities of Aplyronine A Analogues toward the Development of Antitumor Protein–Protein Interaction Inducers between Actin and Tubulin: Conjugation of the C1–C9 Macrolactone Part and the C24–C34 Side Chain

ACS Omega ◽  
2019 ◽  
Vol 4 (5) ◽  
pp. 8598-8613 ◽  
Author(s):  
Kentaro Futaki ◽  
Momoko Takahashi ◽  
Kenta Tanabe ◽  
Akari Fujieda ◽  
Hideo Kigoshi ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Biological Activities ◽  
Side Chain ◽  
Protein Protein Interaction ◽  
Aplyronine A

scholarly journals Proximal Protein Interaction Landscape of RAS Paralogs

Cancers ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 3326 ◽  
Author(s):  
Benoît Béganton ◽  
Etienne Coyaud ◽  
Estelle M. N. Laurent ◽  
Alain Mangé ◽  
Julien Jacquemetton ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Protein Interactions ◽  
Biological Activities ◽  
Mammalian Species ◽  
Variable Region ◽  
Specific Protein ◽  
Protein Networks ◽  
Ras Proteins ◽  
Wild Type ◽  
Protein Protein Interaction

RAS proteins (KRAS, NRAS and HRAS) are frequently activated in different cancer types (e.g., non-small cell lung cancer, colorectal cancer, melanoma and bladder cancer). For many years, their activities were considered redundant due to their high degree of sequence homology (80% identity) and their shared upstream and downstream protein partners. However, the high conservation of the Hyper-Variable-Region across mammalian species, the preferential activation of different RAS proteins in specific tumor types and the specific post-translational modifications and plasma membrane-localization of each paralog suggest they could ensure discrete functions. To gain insights into RAS proteins specificities, we explored their proximal protein–protein interaction landscapes using the proximity-dependent biotin identification technology (BioID) in Flp-In T-REx 293 cell lines stably transfected and inducibly expressing wild type KRAS4B, NRAS or HRAS. We identified more than 800 high-confidence proximal interactors, allowing us to propose an unprecedented comparative analysis of wild type RAS paralogs protein networks. These data bring novel information on poorly characterized RAS functions, e.g., its putative involvement in metabolic pathways, and on shared as well as paralog-specific protein networks that could partially explain the complexity of RAS functions. These networks of protein interactions open numerous avenues to better understand RAS paralogs biological activities.

scholarly journals Analysis of the aplyronine A-induced protein–protein interaction between actin and tubulin by surface plasmon resonance

2016 ◽  
Vol 24 (12) ◽  
pp. 2809-2814 ◽  
Author(s):  
Yuichiro Hirayama ◽  
Kota Yamagishi ◽  
Tomohiro Suzuki ◽  
Hirokazu Kawagishi ◽  
Masaki Kita ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Protein Interaction ◽  
Plasmon Resonance ◽  
Protein Protein Interaction ◽  
Aplyronine A

Peptide and small molecule inhibitors of the Keap1–Nrf2 protein–protein interaction

2015 ◽  
Vol 43 (4) ◽  
pp. 674-679 ◽  
Author(s):  
Geoff Wells
Keyword(s):  
Small Molecule ◽  
Protein Interaction ◽  
Small Molecule Inhibitors ◽  
Biological Activities ◽  
Cancer Chemoprevention ◽  
Antioxidant Response ◽  
Related Factor ◽  
Promoter Regions ◽  
Protein Protein Interaction ◽  
Antioxidant Response Elements

The transcription factor nuclear factor erythroid-2-related factor 2 (Nrf2) up-regulates the expression of a range of cytoprotective enzymes with antioxidant response elements in their promoter regions and thus can protect cells against oxidative damage. Increasing Nrf2 activity has been proposed as a therapeutic intervention in a range of chronic neurodegenerative conditions and cancer chemoprevention. One of the main mechanisms by which Nrf2 is negatively regulated involves an interaction with the ubiquitination facilitator protein, Kelch-like ECH-associated protein 1 (Keap1) that facilitates degradation of Nrf2. Inhibition of this process underlies the mode of action of a broad group of compounds that increase Nrf2 activity. A number of natural products, including the isothiocyanate sulforaphane, up-regulate Nrf2 by interacting with Keap1 in a covalent manner to stall its activity. Recently, a number of peptide and small molecule inhibitors of the protein-protein interaction (PPI) between Keap1 and Nrf2 have been described. These classes of compound have contrasting modes of action at the molecular level and there is emerging evidence that their biological activities have similarities and differences. This review describes the various classes of PPI inhibitor that have been described in the literature and the biological evaluations that have been performed.

Development of a novel inducer of protein–protein interactions based on aplyronine A

2018 ◽  
Vol 54 (68) ◽  
pp. 9537-9540 ◽  
Author(s):  
Takayuki Ohyoshi ◽  
Atsuhiro Takano ◽  
Mayu Namiki ◽  
Tomotaka Ogura ◽  
Yuto Miyazaki ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Biological Activities ◽  
Side Chain ◽  
Protein Protein Interactions ◽  
Swinholide A ◽  
Aplyronine A

An aplyronine A–swinholide A hybrid, consisting of the macrolactone part of aplyronine A and the side chain part of swinholide A, was designed, synthesized, and evaluated for biological activities.

An efficient transient assays system using Agrobacterium-mediated transformation of onion (Allium cepa) epidermal cells

2020 ◽  
Vol 80 (03) ◽  
Author(s):  
Yu-Miao Zhang ◽  
Jun Wang ◽  
Tao Wu
Keyword(s):  
Subcellular Localization ◽  
Protein Interaction ◽  
Protein Interactions ◽  
Epidermal Cells ◽  
Cyclin Dependent Kinase ◽  
Protein Subcellular Localization ◽  
Protein Protein Interactions ◽  
Efficient System ◽  
Protein Protein Interaction ◽  
Onion Epidermal Cells

In this study, the Agrobacterium infection medium, infection duration, detergent, and cell density were optimized. The sorghum-based infection medium (SbIM), 10-20 min infection time, addition of 0.01% Silwet L-77, and Agrobacterium optical density at 600 nm (OD600), improved the competence of onion epidermal cells to support Agrobacterium infection at >90% efficiency. Cyclin-dependent kinase D-2 (CDKD-2) and cytochrome c-type biogenesis protein (CYCH), protein-protein interactions were localized. The optimized procedure is a quick and efficient system for examining protein subcellular localization and protein-protein interaction.

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