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Dual Specificity Phosphatases: From Molecular Mechanisms to Biological Function

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ISBN: 9783039216888 9783039216895 Year: Pages: 240 DOI: 10.3390/books978-3-03921-689-5 Language: English
Publisher: MDPI - Multidisciplinary Digital Publishing Institute
Subject: Science (General) --- Biology
Added to DOAB on : 2019-12-09 11:49:16
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Abstract

Dual specificity phosphatases (DUSPs) constitute a heterogeneous group of protein tyrosine phosphatases with the ability to dephosphorylate Ser/Thr and Tyr residues from proteins, as well as from other non-proteinaceous substrates including signaling lipids. DUSPs include, among others, MAP kinase (MAPK) phosphatases (MKPs) and small-size atypical DUSPs. MKPs are enzymes specialized in regulating the activity and subcellular location of MAPKs, whereas the function of small-size atypical DUSPs seems to be more diverse. DUSPs have emerged as key players in the regulation of cell growth, differentiation, stress response, and apoptosis. DUSPs regulate essential physiological processes, including immunity, neurobiology and metabolic homeostasis, and have been implicated in tumorigenesis, pathological inflammation and metabolic disorders. Accordingly, alterations in the expression or function of MKPs and small-size atypical DUSPs have consequences essential to human disease, making these enzymes potential biological markers and therapeutic targets. This Special Issue covers recent advances in the molecular mechanisms and biological functions of MKPs and small-size atypical DUSPs, and their relevance in human disease.

Lipopolysaccharides (LPSs)

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ISBN: 9783039282562 9783039282579 Year: Pages: 390 DOI: 10.3390/books978-3-03928-257-9 Language: English
Publisher: MDPI - Multidisciplinary Digital Publishing Institute
Subject: Medicine (General) --- Allergy and Immunology
Added to DOAB on : 2020-04-07 23:07:08
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Abstract

The cytoplasm of Gram-negative bacteria is bound by three layers: an inner membrane, a layer of peptidoglycan, and an outer membrane. The outer membrane is an asymmetric lipidic bilayer, with phospholipids on its inner surface and lipopolysaccharides (LPSs) on the outside, with the latter being the major component of the outer leaflet and covering nearly three-quarters of the total outer cell surface. All LPSs possess the same general chemical architecture independently of bacterial activity (pathogenic, symbiotic, commensal), ecological niche (human, animal, soil, plant, water), or growth conditions. Endotoxins are large amphiphilic molecules consisting of a hydrophilic polysaccharide component and a covalently bound hydrophobic and highly conserved lipid component, termed lipid A (the endotoxin subunit). The polysaccharide component can be divided into two subdomains: the internal and conserved core region as well as the more external and highly variable O-specific chain, also referred to as the O-antigen due to its immunogenic properties. LPSs are endotoxins, one of the most potent class of activators of the mammalian immune system; they can be released from cell surfaces of bacteria during multiplication, lysis, and death. LPS can act through its biological center (lipid A component) on various cell types, of which macrophages and monocytes are the most important.

Keywords

aspirin --- hepcidin --- P65 (nuclear factor-?B) --- IL-6/JAK2/STAT3 pathway --- lipopolysaccharide (LPS) --- nitric oxide (NO) --- iron regulatory protein 1 (IRP1) --- Megalobrama amblycephala --- lipopolysaccharide induced TNF? factor --- lipopolysaccharide stimulation --- innate immune --- Aeromonas --- genomics --- inner core oligosaccharide --- outer core oligosaccharide --- lipopolysaccharide --- lipopolysaccharide --- Erwinia amylovora --- NMR --- ESI FT-ICR --- structural determination --- Bordetellae --- Bordetella holmesii --- endotoxin --- lipid A --- structure --- mass spectrometry --- genomic --- Edwardsiella tarda --- core oligosaccharide --- MALDI-TOF MS --- ESI MSn --- NMR --- genomic --- LPS tolerance --- hypothalamic inflammation --- insulin resistance --- pJNK --- fibroblast --- keratocyte --- cornea --- lipopolysaccharide --- bacteria --- chemokine --- adhesion molecule --- collagen --- tear fluid --- serum resistance --- complement --- Salmonella --- lipopolysaccharide --- sialic acid --- reptile-associated salmonellosis --- sepsis --- time response --- inflammation --- oxidative stress --- endotoxaemia --- mouse --- rat --- lipopolysaccharide --- double-stranded RNA --- epithelial cell --- dendritic cell --- allergic respiratory disorder --- hygiene hypothesis --- rhinovirus --- respiratory syncytial virus --- toll-like receptor --- LPS --- lipopolysaccharide --- heptosyltransferase --- protein dynamics --- glycosyltransferase --- GT-B --- inhibitor design --- lipopolysaccharide --- Coxiella burnetii --- Q fever --- phagosome --- virenose --- Plesiomonas shigelloides --- O-antigen --- lipopolysaccharide --- O-acetylation --- d-galactan I --- HR-MAS --- NMR spectroscopy --- endotoxin --- lipopolysaccharide --- Low Endotoxin Recovery --- phase transitions --- polysorbate --- LPS aggregates --- Small Angle X-ray Scattering --- MAT --- LAL and LER --- anti-conjugate serum --- core oligosaccharide --- lipopolysaccharide --- NMR spectroscopy --- ESI MS --- Proteus penneri

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