Autophagy and Metabolism: Potential Target for Cancer Therapy presents updates on autophagy in cancer metabolism and how it can be used to develop new, more efficient treatments. Written by experts in the field, the book presents recent research and explains how to translate it to the clinical setting. Sections discuss tumor cell metabolism and autophagy as therapeutic targets, autophagy regulation in cancer, signaling pathways in metabolic dysregulation in solid tumors, metabolic stress and cell death pathways, and the role of the tumor microenvironment. In addition, topics cover combined targeting autophagy, metabolism for cancer therapy, and the autophagy effect on immune cell metabolism. This will be a valuable resource for researchers, oncologists, graduate students, and members of the biomedical field who are interested in learning more about the interaction between autophagy and cancer metabolism.

HIV-1 Proteases (PR) are an enzyme which cleaves the long HIV polyprotein into small functional peptide fragment. These small fragments again terminate into mature HIV. Inhibition of cleavage of poly protein into small peptide fragment could prevent regeneration of HIV. Computational docking between HIV-1 PR and derivatives of Cyclic Urea Inhibitors (CUIs) has provide us clue to design drug against AIDS. Computational approaches were used to dock ligand (CUIs) with HIV-1 PR to stop cleavage. CUIs are seven-member ring structure of cyclic urea compound. It incorporates the hydrogen-bonding equivalents of an enzyme-bound water molecule into a low molecular weight. Our result suggest that some of derivatives of CUIs binds with HIV-1 PR, which can be stop the fuction of HIV-1 PR(cleavage of long protein chain into small peptide fragment).Evaluation of docking results was performed based on steric complementarity. This can be called the best fitting of ligand to the enzyme pocket. The following three factors are primarily involved to influence binding conformation between ligand and a protein.These are binding energy, hydrogen bonding, and hydrophobic interaction.