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"In two volumes, this book elucidates the crucial mechanisms that control the dynamics of phosphoinositide conversion. Volume II extends into the role of phosphoinositides in membrane organization and vesicular traffic. Endocytosis and exocytosis are modulated by phosphoinositides, which determine the fate and activity of integral membrane proteins. Phosphatidylinositol(4,5)-bisphosphate is a prominent flag in the plasma membrane, while phosphatidylinositol-3-phosphate decorates early endosomes. The Golgi apparatus is rich in phosphatidylinositol-4-phosphate, stressed cells increase phosphatidylinositol(3,5)-bisphosphate, and the nucleus has a phosphoinositide metabolism of its own. Phosphoinositide-dependent signaling cascades and the spatial organization of distinct phosphoinositide species are required in organelle function, fission and fusion, membrane channel regulation, cytoskeletal rearrangements, adhesion processes, and thus orchestrate complex cellular responses including growth, proliferation, differentiation, cell motility, and cell polarization."

""Reflecting the major advances that have been made in the field over the past decade, this book provides an overview of current models of biological systems. The focus is on simple quantitative models, highlighting their role in enhancing our understanding of the strategies of gene regulation and dynamics of information transfer along signalling pathways, as well as in unravelling the interplay between function and evolution. The chapters are self-contained, each describing key methods for studying the quantitative aspects of life through the use of physical models. They focus, in particular, on connecting the dynamics of proteins and DNA with strategic decisions on the larger scale of a living cell, using E. coli and phage lambda as key examples. Encompassing fields such as quantitative molecular biology, systems biology and biophysics, this book will be a valuable tool for students from both biological and physical science backgrounds"--"

"This book will provide a detailed review of existing knowledge on the functional characterization of biological networks. In 15 chapters authored by an international group of prolific systems biology and bioinformatics researchers, it will organize, conceptualize, and summarize the existing core of research results and computational methods on understanding biological function from a network perspective."

"Ester asam lemak kelapa sawit sukrosa dapat disintesis melalui reaksi esterifikasi enzimatis menggunakan lipase Candida rugosa. Pada penelitian ini, digunakan pelarut isoamil alkohol dan isobutanol. Reaksi esterifikasi menggunakan lipase Candida rugosa E.C.3.1.1.3 bebas maupun terimobilisasi pada nanopartikel Fe3O4-kitosan. Imobilisasi lipase Candida rugosa pada nanopartikel Fe3O4-kitosan menggunakan metode ikat silang dengan glutaraldehida sebagai agen pengikat silang. Terhadap hasil imobilisasi dilakukan uji aktivitas dan persen loading. Pada peggunaan enzim 200 ppm didapatkan persen loading imobilisasi lipase sebesar 31,4% dengan aktivitas hidrolisis lipase terimobilisasi sebesar 3,470 U/mL, aktivitas spesifik 0,991 U/mg, serta efisiensi imobilisasi sebesar 23,25 %. Sementara itu, pada penggunaan 350 ppm enzim didapatkan persen loading imobilisasi lipase sebesar 64,4 % dengan aktivitas hidrolisis lipase terimobilisasi sebesar 2,245 U/mL, aktivitas spesifik 0,64 U/mg, serta efisiensi imobilisasi sebesar 14,88%. Kondisi rasio substrat optimum diperoleh pada rasio 1 : 90 (sukrosa : asam lemak). Hasil uji emulsifer menunjukkan hasil positif. Pelarut terbaik untuk sintesis ester -sukrosa dengan lipase terimobilisasi adalah isobutanol.

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Palm oil fatty acid-sucrose can be synthesized via enzymatic esterification using Candida rugosa lipase. The solvents used in this study were isoamyl alcohol and isobutanol. Esterification reaction was carried out enzymatically using free lipase and immobilized Candida rugosa lipase E.C. 3.1.1.3 on Fe3O4-chitosan nanoparticles. The immobilized lipase were examined to determine the loading percentage and the hydrolytic activity. The loading percentage obtained while using 200 ppm lipase for immobilization was 31,4%, with hydrolytic activity of immobilized lipase was 3,47 U/mL, the specific activity of 0,99 U/mg and the immobilization efficiency of 23,25%. Meanwhile by using 350 ppm lipase the loading percentage obtained was 64,4% with hydrolytic activity of 2,25 U/mL, the specific activity of 0,64 U/mg and the immobilization efficiency of 14,8 %. From this optimization study of esterification, the highest conversion came from sugar and fatty acid ratio 1 : 90. The esterification product gave positive test on emulsifier test. The best solvent to synthesize ester-sucrose using immobilized lipase is isobutanol."