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Molecular chaperones or heat-shock proteins (HSPs) play essential roles in safeguarding structural stability and preventing misfolding and aggregation of proteins, and maintaining the proteome functionality in the cell. For over two decades until the present time, new functions have been discovered and several molecular mechanisms have been elucidated for many chaperones, while the field is being continuously challenged by new open questions. Probably as a consequence of the increasing research on the molecular bases of neurodegenerative diseases, and the realisation that many such disorders are linked to protein misfolding processes, unleashing the roles and mechanisms of chaperones in the context of neurodegeneration has become a prime scientific goal. This e-book contains a diversity of reviews, perspective and original research articles highlighting the importance and potential of this emerging subject.
molecular chaperone --- therapeutics --- neurodegenerative disease --- heat-shock response --- protein misfolding --- neuroprotection --- neurodegeneration --- heat-shock protein --- proteostasis --- amyloid protein
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Molecular chaperones or heat-shock proteins (HSPs) play essential roles in safeguarding structural stability and preventing misfolding and aggregation of proteins, and maintaining the proteome functionality in the cell. For over two decades until the present time, new functions have been discovered and several molecular mechanisms have been elucidated for many chaperones, while the field is being continuously challenged by new open questions. Probably as a consequence of the increasing research on the molecular bases of neurodegenerative diseases, and the realisation that many such disorders are linked to protein misfolding processes, unleashing the roles and mechanisms of chaperones in the context of neurodegeneration has become a prime scientific goal. This e-book contains a diversity of reviews, perspective and original research articles highlighting the importance and potential of this emerging subject.
molecular chaperone --- therapeutics --- neurodegenerative disease --- heat-shock response --- protein misfolding --- neuroprotection --- neurodegeneration --- heat-shock protein --- proteostasis --- amyloid protein
Choose an application
Molecular chaperones or heat-shock proteins (HSPs) play essential roles in safeguarding structural stability and preventing misfolding and aggregation of proteins, and maintaining the proteome functionality in the cell. For over two decades until the present time, new functions have been discovered and several molecular mechanisms have been elucidated for many chaperones, while the field is being continuously challenged by new open questions. Probably as a consequence of the increasing research on the molecular bases of neurodegenerative diseases, and the realisation that many such disorders are linked to protein misfolding processes, unleashing the roles and mechanisms of chaperones in the context of neurodegeneration has become a prime scientific goal. This e-book contains a diversity of reviews, perspective and original research articles highlighting the importance and potential of this emerging subject.
molecular chaperone --- therapeutics --- neurodegenerative disease --- heat-shock response --- protein misfolding --- neuroprotection --- neurodegeneration --- heat-shock protein --- proteostasis --- amyloid protein
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The plant-derived polyphenol curcumin has been used in promoting health and combating disease for thousands of years. Its therapeutic effects have been successfully utilized in Ayurvedic and Traditional Chinese Medicine in order to treat inflammatory diseases. Current results from modern biomolecular research reveal the modulatory effects of curcumin on a variety of signal transduction pathways associated with inflammation and cancer. In this context, curcumin's antioxidant, anti-inflammatory, anti-tumorigenic, and even anti-metastatic activities are discussed. On the cellular level, the reduced activity of several transcription factors (such as NFkB or AP-1) and the suppression of inflammatory cytokines, matrix degrading enzymes, metastasis related genes and even microRNAs are reported. On functional levels, these molecular effects translate into reduced proliferative, invasive, and metastatic capacity, as well as induced tumor cell apoptosis. All these effects have been observed not only in vitro but also in animal models. In combination with anti-neoplastic drugs like Taxol, kinase inhibitors, and radiation therapy, curcumin potentiates the drugs' therapeutic power and can protect against undesired side effects. Natural plant-derived compounds like curcumin have one significant advantage: They do not usually cause side effects. This feature qualifies curcumin for primary prevention in healthy persons with a predisposition to cancer, arteriosclerosis, or chronic inflammatory diseases. Nonetheless, curcumin is considered safe, although potential toxic effects stemming from high dosages, long-term intake, and pharmacological interactions with other compounds have yet to be assessed. This Special Issue examines in detail and updates current research on the molecular targets, protective effects, and modes of action of natural plant-derived compounds and their roles in the prevention and treatment of human diseases.
minerals --- cancer treatment --- chitosan --- n/a --- neurodegeneration --- antioxidant activity --- senescence --- tumor proliferation --- nanoparticles --- antimicrobial agents --- oxidative metabolites --- drug discovery --- Akt/mTOR signaling --- micronutrients --- ulcerative colitis --- transmission electron microscopy --- metabolic reprogramming --- curcumin --- death receptor --- chaperone-mediated autophagy --- wound healing --- brain ischemia --- autophagy --- Alzheimer’s disease --- genes --- transthyretin --- inflammatory bowel disease --- cellular pathway --- centrifugal partition chromatography --- nutrition --- amyloid --- Curcuma longa --- protein aggregation --- supportive care --- IL-17 --- senolytics --- complementary medicine --- macronutrients --- structure activity relationship --- gastroprotection --- Zingiberaceae --- anti-inflamation --- TLC bioautography --- microbiota --- glioblastoma multiforme --- amyloidosis --- SHMT2 --- antioxidants --- silica --- apoptosis --- reflux esophagitis --- gastric ulcer --- TLC-MS --- anti-cancer --- anticancer --- ImageJ --- anti-tumor --- delivery system --- wound --- Helicobacter pylori --- direct protein binding --- protein misfolding --- tumor growth --- diet --- Crohn’s disease --- hydrostatic counter-current chromatography --- ageing --- renal cell cancer --- gastric cancer --- amino-acids --- STAT3 --- mechanism of action --- inflamm-aging --- mitophagy --- necrotizing enterocolitis --- cell cycling --- vitamins --- turmeric tuber --- cancer --- tau protein --- Alzheimer's disease --- Crohn's disease
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It is now clearly established that some proteins or protein regions are devoid of any stable secondary and/or tertiary structure under physiological conditions, but still possess fundamental biological functions. These intrinsically disordered proteins (IDPs) or regions (IDRs) have peculiar features due to their plasticity such as the capacity to bind their biological targets with high specificity and low affinity, and the possibility of interaction with numerous partners. A correlation between intrinsic disorder and various human diseases such as cancer, diabetes, amyloidoses and neurodegenerative diseases is now evident, highlighting the great importance of the topic. In this volume, we have collected recent high-quality research about IDPs and human diseases. We have selected nine papers which deal with a wide range of topics, from neurodegenerative disease to cancer, from IDR-mediated interactions to bioinformatics tools, all related to IDP peculiar features. Recent advances in the IDPs/IDRs issue are here presented, contributing to the progress of knowledge of the intrinsic disorder field in human disease.
alpha-synuclein --- NMR --- secondary structure propensity --- pre-structured motifs (PreSMos) --- intrinsically disordered protein --- ubiquitin-proteasome system --- intrinsically disordered proteins --- protein misfolding --- molecular recognition features --- cancer --- neurodegenerative diseases --- protein degradation --- EPR spectroscopy --- isothermal titration calorimetry --- protein-ligand interaction --- site-directed spin labeling --- protein structural dynamics --- WASp interacting protein --- protein–protein interactions --- actin --- cytoskeleton remodeling --- SH3 domain --- proline-rich motif --- single nucleotide variants --- interface core and rim --- human disease --- intrinsically disordered regions --- linear motifs --- gene duplications --- de novo --- evolutionary origin --- circular dichroism --- flexibility --- fluorescence --- importin --- isothermal titration calorimetry (ITC) --- molecular docking --- nuclear magnetic resonance (NMR) --- nuclear protein 1 (NPR1) --- peptide --- Methyl-CpG-binding protein 2 (MeCP2) --- Rett syndrome --- intrinsically disordered protein (IDP) --- protein stability --- protein-DNA interaction --- proteostasis --- ubiquitin independent degradation --- NADH-26S proteasome --- n/a --- protein-protein interactions
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It is now clearly established that some proteins or protein regions are devoid of any stable secondary and/or tertiary structure under physiological conditions, but still possess fundamental biological functions. These intrinsically disordered proteins (IDPs) or regions (IDRs) have peculiar features due to their plasticity such as the capacity to bind their biological targets with high specificity and low affinity, and the possibility of interaction with numerous partners. A correlation between intrinsic disorder and various human diseases such as cancer, diabetes, amyloidoses and neurodegenerative diseases is now evident, highlighting the great importance of the topic. In this volume, we have collected recent high-quality research about IDPs and human diseases. We have selected nine papers which deal with a wide range of topics, from neurodegenerative disease to cancer, from IDR-mediated interactions to bioinformatics tools, all related to IDP peculiar features. Recent advances in the IDPs/IDRs issue are here presented, contributing to the progress of knowledge of the intrinsic disorder field in human disease.
Research & information: general --- Biology, life sciences --- alpha-synuclein --- NMR --- secondary structure propensity --- pre-structured motifs (PreSMos) --- intrinsically disordered protein --- ubiquitin-proteasome system --- intrinsically disordered proteins --- protein misfolding --- molecular recognition features --- cancer --- neurodegenerative diseases --- protein degradation --- EPR spectroscopy --- isothermal titration calorimetry --- protein-ligand interaction --- site-directed spin labeling --- protein structural dynamics --- WASp interacting protein --- protein-protein interactions --- actin --- cytoskeleton remodeling --- SH3 domain --- proline-rich motif --- single nucleotide variants --- interface core and rim --- human disease --- intrinsically disordered regions --- linear motifs --- gene duplications --- de novo --- evolutionary origin --- circular dichroism --- flexibility --- fluorescence --- importin --- isothermal titration calorimetry (ITC) --- molecular docking --- nuclear magnetic resonance (NMR) --- nuclear protein 1 (NPR1) --- peptide --- Methyl-CpG-binding protein 2 (MeCP2) --- Rett syndrome --- intrinsically disordered protein (IDP) --- protein stability --- protein-DNA interaction --- proteostasis --- ubiquitin independent degradation --- NADH-26S proteasome
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