name	title	fuMetaTitel	body	fuDCcreator	fuDCcreatorLinks	fuDCpublisher	fuDCpublisherLocation	fuDCSizeOrDuration	fuDCdateYear	fuDCdateMonth	fuDCdateDay	fuDCsubject	fuDCrelationPartOf	fuDCrelation	fuDClanguage	fuDCsource	fuDCcontributor	fuDCtype	fuDCformat	fuDCidentifier	fuDCcoverage	fuDCrights	fuDCdescriptionDE	fuDCdescriptionEN	fuDCIdentifierBibliographicCitation	fuBild	fuDCBibtex	fuLinksZumThema
KA980	Tick-borne encephalitis virus replication, intracellular trafficking, and pathogenicity in human intestinal Caco-2 cell monolayers			"Yu, C.; Achazi, K.; Moller, L.; Schulzke, J. D.; Niedrig, M.; Bucker, R."		PLoS One			2014			"*Pinocytosis; *Virus Replication; Biological Transport; Caco-2 Cells; Cytoskeleton/virology; Encephalitis Viruses, Tick-Borne/metabolism/*pathogenicity/*physiology; Humans; Intestines/*cytology/ultrastructure/*virology; Intracellular Space/*virology; Virulence; Virus Internalization"				https://doi.org/10.1371/journal.pone.0096957		journalArticle		1932-6203 (Electronic) 1932-6203 (Linking)				Tick-borne encephalitis virus (TBEV) is one of the most important vector-borne viruses in Europe and Asia. Its transmission mainly occurs by the bite of an infected tick. However, consuming milk products from infected livestock animals caused TBEV cases. To better understand TBEV transmission via the alimentary route, we studied viral infection of human intestinal epithelial cells. Caco-2 cells were used to investigate pathological effects of TBEV infection. TBEV-infected Caco-2 monolayers showed morphological changes including cytoskeleton rearrangements and cytoplasmic vacuolization. Ultrastructural analysis revealed dilatation of the rough endoplasmic reticulum and further enlargement to TBEV containing caverns. Caco-2 monolayers maintained an intact epithelial barrier with stable transepithelial electrical resistance (TER) during early stage of infection. Concomitantly, viruses were detected in the basolateral medium, implying a transcytosis pathway. When Caco-2 cells were pre-treated with inhibitors of cellular pathways of endocytosis TBEV cell entry was efficiently blocked, suggesting that actin filaments (Cytochalasin) and microtubules (Nocodazole) are important for PI3K-dependent (LY294002) virus endocytosis. Moreover, experimental fluid uptake assay showed increased intracellular accumulation of FITC-dextran containing vesicles. Immunofluorescence microscopy revealed co-localization of TBEV with early endosome antigen-1 (EEA1) as well as with sorting nexin-5 (SNX5), pointing to macropinocytosis as trafficking mechanism. In the late phase of infection, further evidence was found for translocation of virus via the paracellular pathway. Five days after infection TER was slightly decreased. Epithelial barrier integrity was impaired due to increased epithelial apoptosis, leading to passive viral translocation. These findings illuminate pathomechanisms in TBEV infection of human intestinal epithelial cells and viral transmission via the alimentary route.				
KA981	Enzymatically cross-linked hyperbranched polyglycerol hydrogels as scaffolds for living cells			"Wu, C.; Strehmel, C.; Achazi, K.; Chiappisi, L.; Dernedde, J.; Lensen, M. C.; Gradzielski, M.; Ansorge-Schumacher, M. B.; Haag, R."		Biomacromolecules			2014	11	10	"Animals; Cell Line; Cell Survival/drug effects/physiology; Cross-Linking Reagents/*chemistry/pharmacology; Fibroblasts/drug effects/physiology; Glycerol/*chemistry/pharmacology; Hydrogels/*chemistry/pharmacology; Mice; Polymers/*chemistry/pharmacology; Tissue Scaffolds/*chemistry"				https://doi.org/10.1021/bm500705x		journalArticle		1526-4602 (Electronic) 1525-7797 (Linking)				Although several strategies are now available to enzymatically cross-link linear polymers to hydrogels for biomedical use, little progress has been reported on the use of dendritic polymers for the same purpose. Herein, we demonstrate that horseradish peroxidase (HRP) successfully catalyzes the oxidative cross-linking of a hyperbranched polyglycerol (hPG) functionalized with phenol groups to hydrogels. The tunable cross-linking results in adjustable hydrogel properties. Because the obtained materials are cytocompatible, they have great potential for encapsulating living cells for regenerative therapy. The gel formation can be triggered by glucose and controlled well under various environmental conditions.				
KA982	Multivalent anchored and crosslinked hyperbranched polyglycerol monolayers as antifouling coating for titanium oxide surfaces			"Wei, Q.; Krysiak, S.; Achazi, K.; Becherer, T.; Noeske, P. M.; Paulus, F.; Liebe, H.; Grunwald, I.; Dernedde, J.; Hartwig, A.; Hugel, T.; Haag, R."		Colloids and Surfaces B-Biointerfaces			2014	10	1	"Animals; Antifouling; Glycerol/*chemistry; Hyperbranched polyglycerol; Mice; Microscopy, Atomic Force; Multivalent anchoring monolayers; NIH 3T3 Cells; Photoelectron Spectroscopy; Polymers/*chemistry; Protein resistance; Surface modification; Surface Properties; Titanium/*chemistry"				https://doi.org/10.1016/j.colsurfb.2014.08.001		journalArticle		1873-4367 (Electronic) 0927-7765 (Linking)				A set of new catecholic monolayer coatings was developed to improve the antifouling performance of TiO2 surfaces. To solve the problem of the weak charge-transfer interaction between a single catechol anchor and TiO2, multiple catechol groups were combined with hyperbranched polyglycerol (hPG) which is a distinct dendritic scaffold that exposes its multivalent anchor groups on the surface. Thus, multivalent catecholic hPGs can be easily prepared for surface modification. The immobilization of the compounds was monitored by quartz crystal microbalance with dissipation monitoring. Surface properties of the coatings were analyzed by water contact angle, X-ray photoelectron spectroscopy, and atomic force microscopy. The antifouling ability and stability were investigated by protein adsorption and cell adhesion. By increasing the number of catechol groups on the hPG scaffold, the stability and surface coverage could be significantly enhanced. Moreover, the inner-layer crosslinking of the coatings by grafting and initiating vinyl groups clearly improved their long-term stability. As a result, hPG with a catecholic functional degree of 10% (hPG-Cat10) and hPG with both catecholic and vinylic functional degree of 5% (hPG-Cat5-V5) were identified as the best catecholic hPGs to prepare bioinert and stable monolayer coatings on TiO2.				
KA983	Mussel-inspired dendritic polymers as universal multifunctional coatings			"Wei, Q.; Achazi, K.; Liebe, H.; Schulz, A.; Noeske, P. L.; Grunwald, I.; Haag, R."		Angewandte Chemie			2014	10	20	"Animals; bioinspired materials; Bivalvia/*chemistry; dendrimers; Human Umbilical Vein Endothelial Cells; Humans; Microscopy, Atomic Force; Microscopy, Electron, Scanning; multifunctionalization; polymers; Polymers/*chemistry; Proteins/*chemistry; surface chemistry"				https://doi.org/10.1002/anie.201407113		journalArticle		1521-3773 (Electronic) 1433-7851 (Linking)				A rapid and universal approach for multifunctional material coatings was developed based on a mussel-inspired dendritic polymer. This new kind of polymer mimics not only the functional groups of mussel foot proteins (mfps) but also their molecular weight and molecular structure. The large number of catechol and amine groups set the basis for heteromultivalent anchoring and crosslinking. The molecular weight reaches 10 kDa, which is similar to the most adhesive mussel foot protein mfp-5. Also, the dendritic structure exposes its functional groups on the surface like the folded proteins. As a result, a very stable coating can be prepared on virtually any type of material surface within 10 min by a simple dip-coating method, which is as fast as the formation of mussel byssal threads in nature.				
KA984	Synthesis of amphiphilic dendronized polymers to study their self-assembly and transport behavior			"Kumari, M.; Singh, A. K.; Kumar, S.; Achazi, K.; Gupta, S.; Haag, R.; Sharma, S. K."		Polymers for Advanced Technologies			2014	11		"acid; cell compatible amphiphiles; copolymers; dendronized polymers; drug-delivery; novozym 435; peg; polyglycerol; progress"				https://doi.org/10.1002/pat.3293		journalArticle		1042-7147				Herein, we report on the synthesis of PEG-1000-diethyl ester and 2-azido-propane-1,3-diol-based copolymers utilizing Novozym 435 (Candida antarctica lipase) using a biocatalytic method. The linear base copolymer was then functionalized with polyglycerol-based regular [G1.0] and [G2.0] dendrons and C-12/C-14 hydrophobic alkyl chains via an efficient Click approach. The resulting amphiphilic dendronized polymers form well-defined micelles in aqueous solutions. The transport behavior of these polymers was studied by using Nile red as a fluorescent model dye. The cytotoxicity profiles of a few representative polymers were evaluated, and the effect of hydrophobic alkyl chain length as well as the hydrophilic polyglycerol dendron's generation on the biocompatibility of polymeric systems was studied. Copyright (c) 2014 John Wiley & Sons, Ltd.				
KA985	Fabrication of thermoresponsive nanogels by thermo-nanoprecipitation and encapsulation of bioactives			"Giulbudagian, M.; Asadian-Birjand, M.; Steinhilber, D.; Achazi, K.; Molina, M.; Calderon, M."		Polymer Chemistry			2014			"delivery; derivatives; polyglycidol; release; ring-opening polymerization"				https://doi.org/10.1039/c4py01186d		journalArticle		1759-9954				A synthetic method for thermoresponsive, glycerol based nanogels has been developed. The nanogels were synthesized by nanoprecipitation of the orthogonally functionalized macromonomers and their gelation in water. The crosslinking points were generated by strain promoted azide-alkyne cycloaddition which enabled the in situ encapsulation of Doxorubicin HCl. The mild and surfactant free reaction conditions make these nanogels ideal candidates for biomedical applications.				
KA986	pH-responsive dendritic core-multishell nanocarriers			"Fleige, E.; Achazi, K.; Schaletzki, K.; Triemer, T.; Haag, R."		Journal of controlled release : official journal of the Controlled Release Society			2014	7	10	"Antineoplastic Agents/*administration & dosage/pharmacology; Cell Line, Tumor; Delayed-Action Preparations/*chemistry; Doxorubicin; Doxorubicin/*administration & dosage/pharmacology; Drug delivery; Dynamic light scattering; Fluorescent Dyes/administration & dosage; Humans; Hydrogen-Ion Concentration; Imines/chemistry; Light; Nanostructures/*chemistry; Neoplasms/drug therapy; Nile red; Oxazines/administration & dosage; Real time cell analysis; Scattering, Radiation; Transport capacity"				https://doi.org/10.1016/j.jconrel.2014.04.019		journalArticle		1873-4995 (Electronic) 0168-3659 (Linking)				In this paper we describe novel pH-responsive core-multishell (CMS) nanocarrier (pH-CMS), obtained by introducing an aromatic imine linker between the shell and the core. At a pH of 5 and lower the used imine linker was rapidly cleaved as demonstrated by NMR studies. The CMS nanocarriers were loaded with the dye Nile red (NR) and the anticancer drug doxorubicin (DOX), respectively. The transport capacities were determined using UV/Vis spectroscopy, and the sizes of the loaded and unloaded CMS nanocarriers were investigated using dynamic light scattering (DLS). We could show that CMS nanocarriers efficiently transported NR in supramolecular aggregates, while DOX was transported in a unimolecular fashion. After cellular uptake the DOX-loaded pH-responsive nanocarriers showed higher toxicities than the stable CMS nanocarriers. This is due to a more efficient DOX release caused by the cleavage of the pH-labile imine bond at lower pH within the intracellular compartments.				
KA987	Tick-Borne Encephalitis Viruses			"Donoso-Mantke, Oliver; Escadafal, Camille; Sanchini, rea; Domingo, Cristina; Hagedorn, Peter; Patel, Pranav; Achazi, Katharina; Huether, Antje; Niedrig, Matthias"		Manual of Security Sensitive Microbes and Toxins			2014							https://doi.org/10.1201/b16752-22		bookSection										
KA988	Tick-borne encephalitis virus triggers inositol-requiring enzyme 1 (IRE1) and transcription factor 6 (ATF6) pathways of unfolded protein response			"Yu, C.; Achazi, K.; Niedrig, M."		Virus Research			2013	12	26	"*Host-Pathogen Interactions; *Unfolded Protein Response; *Virus Replication; Activating Transcription Factor 6/*metabolism; Animals; Atf6; Cell Line; Chlorocebus aethiops; Encephalitis Viruses, Tick-Borne/*physiology; Endoribonucleases/*metabolism; ER stress; Flavivirus; Humans; Protein Serine-Threonine Kinases/*metabolism; Signal Transduction; Tick-borne encephalitis virus; Virus replication; Xbp1"				https://doi.org/10.1016/j.virusres.2013.https://doi.org/10.012		journalArticle		1872-7492 (Electronic) 0168-1702 (Linking)				Tick-borne encephalitis (TBE) is a serious human neurological disease caused by TBE virus (TBEV). However, the mechanisms of TBEV-caused pathogenesis remain unclear. The endoplasmic reticulum (ER) stress response, also defined as the unfolded protein response (UPR), is an important conserved molecular signaling pathway that modulates many biological functions including innate immunity and viral pathogenesis. Here, we investigated the effects of the two UPR signaling pathways upon TBEV infection in Vero E6 cells. We showed that the amount of heat shock protein 72 (Hsp72) increased in the course of TBEV infection. We then confirmed that TBEV infection activates the IRE1 pathway, leading to RNA and protein expression of the spliced X box binding protein 1 (sXBP1). Furthermore, we observed the translocation of ATF6 during TBEV infection and expression of cleaved transcription factor 6 (ATF6) which suggest activation of ATF6 pathway. Finally, we examined whether inhibition of the IRE1 pathway has an effect on TBEV infection. Cell treatment with 3,5-Dibromosalicylaldehyde (IRE1 inhibitor) and tauroursodeoxycholic acid (TUDCA) showed that TBEV replication was significantly limited. These findings provide the first evidence that TBEV infection activates the two UPR signaling pathways. Moreover, inhibition of TBEV replication by UPR inhibitors may provide a novel therapeutic strategy against TBE.				
KA989	Bioluminescence assay for the highly sensitive detection of botulinum neurotoxin A activity			"Stevens, G. B.; Silver, D. A.; Zgaga-Griesz, A.; Bessler, W. G.; Vashist, S. K.; Patel, P.; Achazi, K.; Strotmeier, J.; Worbs, S.; Dorner, M. B.; Dorner, B. G.; Pauly, D.; Rummel, A.; Urban, G. A.; Krueger, M."		Analyst			2013	10	21	"Animals; Botulinum Toxins, Type A/*analysis/*chemistry; Clostridium botulinum/chemistry; Humans; Luminescent Measurements/*methods; Mice; Mice, Inbred BALB C; Protein Structure, Secondary"				https://doi.org/10.1039/c3an00525a		journalArticle		1364-5528 (Electronic) 0003-2654 (Linking)				This article describes a novel bioluminescence assay for detecting the proteolytic activity of Botulinum NeuroToxins (BoNT) in complex matrices. The assay is capable of detecting traces of BoNT in blood samples as well as in food drinks. The assay was responsive to BoNT/A subtypes 1 to 5, and serotype E3 in buffered solutions. It was responsive to filtered Clostridium botulinum supernatants and BoNT/A1 in complex with neurotoxin associated proteins in bouillon and milk (3.8% fat) down to 400 fM after 4 h RT incubation and in bouillon at concentrations down to 120 fM after 21 h RT incubation. In combination with an immunocapture/enrichment step it could detect BoNT/A1 in citrated plasma at concentrations down to 30 fM (1.2 mouse LD50 per mL). The simplicity of the assay, combined with a demonstrated ability to lyophilize the reagents, demonstrates its usefulness for detection of BoNT in non-specialised analytical laboratories.