Structural Diversity and Role of Phytochemicals against P38-α Mitogen-activated Protein Kinase and Epidermal Growth Factor Receptor Kinase Domain: A Privileged Computational Approach

نویسندگان

چکیده

Computational databases and tools in recent times have been proved to provide an essential aid for anticancer studies the field of oncology. Molecular docking facilitate structural diversity plant-derived phytomolecules having properties against receptor proteins involved cancer signaling pathways. The current study involves investigation phytocompounds-agasthisflavone, anacardic acid, zoapatanolide A, a purified product plant extract Amarogopinois546 were subjected on p38-α MAPK EGFR Kinase domain. effectiveness this was evaluated by comparing interactions standard drug, doxorubicin molecules. is analyzed compound estimated with lowest binding energy considered highest affinity towards active site proteins. isolated displayed least score large number hydrogen bonds hydrophobic P38α MAP kinase comparison This preliminary result can strongly be supported carrying out experimental evaluation near future.

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Activation of p38 Mitogen-Activated Protein Kinase Promotes Epidermal Growth Factor Receptor Internalization

Endocytic trafficking plays an important role in the regulation of the epidermal growth factor receptor (EGFR). To address if cellular kinases regulate EGFR internalization, we used anisomycin, a potent activator of kinase cascades in mammalian cells, especially the stress-activated mitogen-activated protein (MAP) kinase subtypes. Here, we report that activation of p38 MAP kinase by anisomycin ...

متن کامل

Mitogen-activated protein kinase stimulation by a tyrosine kinase-negative epidermal growth factor receptor.

Mutation of the epidermal growth factor receptor (EGF-R) within the ATP binding subdomain results in a receptor that lacks tyrosine kinase activity and is defective in signal transduction. However, this kinase-negative EGF-R is able to activate MAP kinase (Campos-Gonzalez, R., and Glenny, J. R. (1992) J. Biol. Chem. 267, 14535-14538). This observation suggests that signal initiation by the EGF-...

متن کامل

Dual mitogen-activated protein kinase and epidermal growth factor receptor inhibition in biliary and pancreatic cancer.

This study aimed to develop rational combinations of targeted agents against biliary and pancreatic cancers. To this end, we compared the global gene expression profile of biliary cancer cell lines with different degrees of sensibility to the epidermal growth factor receptor tyrosine kinase inhibitors gefitinib and erlotinib using the Affymetrix U133A microarray platform. A set of 32 genes, inc...

متن کامل

Role of p38 mitogen-activated protein kinase in cardiac remodelling.

BACKGROUND AND PURPOSE Mitogen-activated protein kinases (MAPK) are centrally involved in several mechanisms important for heart failure such as apoptosis, activation of inflammatory responses and cell proliferation. We therefore evaluated the effect of the selective p38 MAPK inhibitor SB 239063 on progression of left ventricular remodelling after myocardial infarction (MI) in rats. EXPERIMEN...

متن کامل

Role of phosphoinositide 3-kinase in activation of ras and mitogen-activated protein kinase by epidermal growth factor.

The paradigm for activation of Ras and extracellular signal-regulated kinase (ERK)/mitogen-activated protein (MAP) kinase by extracellular stimuli via tyrosine kinases, Shc, Grb2, and Sos does not encompass an obvious role for phosphoinositide (PI) 3-kinase, and yet inhibitors of this lipid kinase family have been shown to block the ERK/MAP kinase signalling pathway under certain circumstances....

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Journal of Pure and Applied Microbiology

سال: 2021

ISSN: ['2581-690X', '0973-7510']

DOI: https://doi.org/10.22207/jpam.15.4.48