Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

The coordinated action of the different cytoskeletal polymers--microtubules, actin filaments and neurofilaments-- is essential for the establishment, remodeling and maintenance of neuronal architecture throughout the neuron lifetime. Neurons are among the most polarized cells, with a long thin axon and multiple thicker and shorter dendrites. Achieving this complex morphology, and the precise and accurate formation of an intricate network of synaptic contacts is critical for the proper transmission and reception of signals in the brain. Neuronal polarization precedes axon outgrowth and the subsequent differentiation of short neurites into dendrites, as part of the neuronal differentiation program that involves both intrinsic and extrinsic signals that converge at the cytoskeletal level. Growth cones, which are sensory and locomotor structures located at the tip of growing axons, are key elements in the transduction of extracellular cues into cytoskeletal changes, guiding axons to their right destinations. Neuronal migration, another crucial process during brain development, occurs in close coordination with neuronal differentiation. Migration involves as well an extensive rearrangement of neuronal cell shape that relies on cytoskeleton reorganization. Further processes, such as dendritic spine formation and growth, establishment of synaptic contacts or synaptic plasticity in mature neurons also depend on cytoskeletal dynamics. Fine-tune regulation of neuronal cytoskeleton is therefore crucial for the maintenance of neuronal integrity and functionality. Mutations in genes that code for cytoskeletal proteins often have deleterious effects in neurons, such as abnormal migration or differentiation, deficient axonal transport of organelles and synaptic vesicles, or impaired synaptic signaling. Several human Nervous System disorders, including neurodevelopmental, psychiatric, and neurodegenerative diseases, have been linked to cytoskeletal dysfunction. Cytoskeletal reorganization is also crucial to regulate nerve cell repair following Nervous System injury. Many of the pathways that control cell-intrinsic axon regeneration lead to axon cytoskeletal remodeling. Moreover, most extracellular cues that inhibit regeneration of damaged axons in Central Nervous System following traumatic injury or neurodegeneration, are known to modulate cytoskeletal dynamics and organization. Based on these findings, regulators of cytoskeleton dynamics have emerged as promising therapeutic targets in several brain disorders and in the context of regeneration of injured axons. Hence, remodeling of neuronal cytoskeleton underlies all the dramatic morphological changes that occur in developing and adult neurons. Understanding the specific molecular mechanisms that control cytoskeleton rearrangements in neurons is far from complete. This Frontiers Research Topic gathers a selection of articles focused on the diverse and key roles of cytoskeleton in neuronal biology.

neuronal cytoskeleton --- astrocyte cytoskeleton --- microtubules (MTs) --- actin cytoskeleton --- tau --- neuron

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Lignans are a class of natural products found mainly in plants. They have a wide variety of structures and exhibit a range of potent biological activities. Lignans are also well-known components of a number of widely eaten foods and are frequently studied for their dietary impact. Owing to these factors, lignans have been extensively studied by scientists from a large number of disciplines. This collection of research and review articles describes topics ranging in scope from the recent isolation and structural elucidation of new lignans, strategies towards the chemical synthesis of lignans, assessment of their biological activities and potential for further therapeutic development. Research showing the impact of lignans in the food and agricultural industries is also presented.

taste-active compound --- heilaohu --- 9-norlignans --- antioxidant activity --- drug-like --- human health --- chemometrics --- lignan --- bitterness --- red-flowered Chinese magnolia vine --- antioxidant --- ruminant --- secoisolariciresinol diglucoside --- quantification --- intermolecular interactions --- cattle --- anti-inflammatory activity --- acyl-Claisen --- LOX --- seed --- food groups --- microtubules --- anti-proliferative --- acetylcholinesterase inhibitors --- flax --- arylnaphthalene lignan --- epiboly --- aryldihydronaphthalene lignan --- multiple bioactive components --- enterolignan --- total synthesis --- genetic --- synthesis --- cultivated --- cell cycle --- chronic diseases --- national databases --- oxidation --- chemical components --- molecular dynamics --- COX --- lignans --- hydroxycinnamic acid --- chemical structures --- Chinese magnolia vine --- stereoselective synthesis --- sPLA2 --- Bursera fagaroides --- in silico studies --- antibacterial activity --- semisynthesis --- dibenzyl butyrolactones --- flavonoid glycoside --- lignan glycoside --- chemical characterization --- hydroxymatairesinol --- podophyllotoxin --- Lespedeza cuneata --- Bursera --- oak ageing --- Schisandrae Chinensis Fructus --- F-actin --- cultivar --- UHPLC-MS/MS --- bioactivity --- podophyllotoxin-type lignans --- harmonized databases --- graph theory --- antioxidants --- health promotion --- simultaneous quantitation --- natural products --- dietary intake --- cell migration --- Lignan --- chemical space --- diet --- Lauraceae --- pharmacokinetic --- cytotoxicity --- tujia ethnomedicine --- flavonolignans --- flavonol --- adipocyte and osteoblast differentiation --- Burseraceae --- environment --- dietary lignans --- phytochemical analysis --- Schisandra chinensis --- animal health --- neolignans --- Schisandra rubriflora --- cancer --- norlignans --- wild

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

This book is an embodiment of a series of articles that were published as part of a Special Issue of Biomolecules. It is dedicated to exploring the role of intrinsically disordered proteins (IDPs) in various chronic diseases. The main goal of the articles is to describe recent progress in elucidating the mechanisms by which IDPs cause various human diseases, such as cancer, cardiovascular disease, amyloidosis, neurodegenerative diseases, diabetes, and genetic diseases, to name a few. Contributed by leading investigators in the field, this compendium serves as a valuable resource for researchers, clinicians as well as postdoctoral fellows and graduate students

IDP --- fuzzy interactions --- protein complementation assays --- split-GFP reassembly --- kinetics --- membraneless organelles --- optical tweezer --- liquid–liquid phase separation --- protein diffusion --- depletion interaction --- entropic force --- low-complexity sequences --- intrinsically disordered proteins --- PAGE4 --- conformational plasticity --- order–disorder transition --- phosphorylation --- intrinsic disordered protein --- extremely fuzzy complex --- protein interaction --- binding mechanism --- tumor protein p53 --- mouse double minute 2 --- mouse double minute 4 --- Kinase-inducible domain interacting domain --- phosphomimetics --- nuclear magnetic resonance --- transient secondary structure --- COR15A --- Late embryogenesis abundant --- Trifluoroethanol --- Nuclear magnetic resonance --- intrinsically disordered regions --- functional segments --- disease-related proteins --- protein-protein interaction --- subcellular location --- glucocorticoid receptor --- intrinsically disordered --- transactivation activity --- gene regulation --- coactivators --- microtubule associated protein --- tau --- intrinsically disordered protein --- dynamic configuration --- free energy landscape --- microtubules --- electrostatics --- diffusion --- protein structure prediction --- molecular modelling --- molecular dynamics --- tau–microtubule association --- conformational ensemble --- replica exchange molecular dynamics --- drug design --- n/a --- liquid-liquid phase separation --- order-disorder transition --- tau-microtubule association