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Article ; Online: Antithrombin deficiency: no sugar, no diagnosis!

Bianchini, Elsa P

2022 Volume 140, Issue 2, Page(s) 83–85

MeSH term(s)	Antithrombin III ; Antithrombin III Deficiency/complications ; Antithrombin III Deficiency/diagnosis ; Antithrombin III Deficiency/genetics ; Antithrombins ; Glycosylation ; Humans ; Sugars ; Thrombophilia
Chemical Substances	Antithrombins ; SERPINC1 protein, human ; Sugars ; Antithrombin III (9000-94-6)
Language	English
Publishing date	2022-07-12
Publishing country	United States
Document type	Editorial ; Comment
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood.2022016677
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Article: Serpins in Hemostasis as Therapeutic Targets for Bleeding or Thrombotic Disorders.

Bianchini, Elsa P / Auditeau, Claire / Razanakolona, Mahita / Vasse, Marc / Borgel, Delphine

Frontiers in cardiovascular medicine

2021 Volume 7, Page(s) 622778

Abstract: Bleeding and thrombotic disorders result from imbalances in coagulation or fibrinolysis, respectively. Inhibitors from the serine protease inhibitor (serpin) family have a key role in regulating these physiological events, and thus stand out as potential ...

Abstract	Bleeding and thrombotic disorders result from imbalances in coagulation or fibrinolysis, respectively. Inhibitors from the serine protease inhibitor (serpin) family have a key role in regulating these physiological events, and thus stand out as potential therapeutic targets for modulating fibrin clot formation or dismantling. Here, we review the diversity of serpin-targeting strategies in the area of hemostasis, and detail the suggested use of modified serpins and serpin inhibitors (ranging from small-molecule drugs to antibodies) to treat or prevent bleeding or thrombosis.
Language	English
Publishing date	2021-01-07
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2781496-8
ISSN	2297-055X
ISSN	2297-055X
DOI	10.3389/fcvm.2020.622778
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Article ; Online: N-Glycosylation Deficiency Reduces the Activation of Protein C and Disrupts Endothelial Barrier Integrity.

Pascreau, Tiffany / Saller, François / Bianchini, Elsa P / Lasne, Dominique / Bruneel, Arnaud / Reperant, Christelle / Foulquier, François / Denis, Cécile V / De Lonlay, Pascale / Borgel, Delphine

Thrombosis and haemostasis

2022 Volume 122, Issue 9, Page(s) 1469–1478

Abstract: Phosphomannomutase 2 (PMM2) deficiency is the most prevalent congenital disorder of glycosylation. It is associated with coagulopathy, including protein C deficiency. Since all components of the anticoagulant and cytoprotective protein C system are ... ...

Abstract	Phosphomannomutase 2 (PMM2) deficiency is the most prevalent congenital disorder of glycosylation. It is associated with coagulopathy, including protein C deficiency. Since all components of the anticoagulant and cytoprotective protein C system are glycosylated, we sought to investigate the impact of an
MeSH term(s)	Congenital Disorders of Glycosylation ; Endothelium ; Glycosylation ; Humans ; Phosphotransferases (Phosphomutases)/deficiency ; Protein C ; Thrombin
Chemical Substances	Protein C ; Thrombin (EC 3.4.21.5) ; Phosphotransferases (Phosphomutases) (EC 5.4.2.-)
Language	English
Publishing date	2022-06-19
Publishing country	Germany
Document type	Journal Article
ZDB-ID	518294-3
ISSN	2567-689X ; 0340-6245
ISSN (online)	2567-689X
ISSN	0340-6245
DOI	10.1055/s-0042-1744378
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Article: N-Glycosylation Deficiency Reduces the Activation of Protein C and Disrupts Endothelial Barrier Integrity

Pascreau, Tiffany / Saller, François / Bianchini, Elsa P. / Lasne, Dominique / Bruneel, Arnaud / Reperant, Christelle / Foulquier, François / Denis, Cécile V. / De Lonlay, Pascale / Borgel, Delphine

Thrombosis and Haemostasis

2022 Volume 122, Issue 09, Page(s) 1469–1478

Abstract	Phosphomannomutase 2 (PMM2) deficiency is the most prevalent congenital disorder of glycosylation. It is associated with coagulopathy, including protein C deficiency. Since all components of the anticoagulant and cytoprotective protein C system are glycosylated, we sought to investigate the impact of an N -glycosylation deficiency on this system as a whole. To this end, we developed a PMM2 knockdown model in the brain endothelial cell line hCMEC/D3. The resulting PMM2 low cells were less able to generate activated protein C (APC), due to lower surface expression of thrombomodulin and endothelial protein C receptor. The low protein levels were due to downregulated transcription of the corresponding genes ( THBD and PROCR, respectively), which itself was related to downregulation of transcription regulators Krüppel-like factors 2 and 4 and forkhead box C2. PMM2 knockdown was also associated with impaired integrity of the endothelial cell monolayer—partly due to an alteration in the structure of VE-cadherin in adherens junctions. The expression of protease-activated receptor 1 (involved in the cytoprotective effects of APC on the endothelium) was not affected by PMM2 knockdown. Thrombin stimulation induced hyperpermeability in PMM2 low cells. However, pretreatment of cells with APC before thrombin simulation was still associated with a barrier-protecting effect. Taken as a whole, our results show that the partial loss of PMM2 in hCMEC/D3 cells is associated with impaired activation of protein C and a relative increase in barrier permeability.
Keywords	protein C ; phosphomannomutase 2 ; endothelial ; -glycosylation
Language	English
Publishing date	2022-06-19
Publisher	Georg Thieme Verlag KG
Publishing place	Stuttgart ; New York
Document type	Article
ZDB-ID	518294-3
ISSN	2567-689X ; 0340-6245
ISSN (online)	2567-689X
ISSN	0340-6245
DOI	10.1055/s-0042-1744378
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Article ; Online: The Proteolytic Inactivation of Protein Z-Dependent Protease Inhibitor by Neutrophil Elastase Might Promote the Procoagulant Activity of Neutrophil Extracellular Traps in Sepsis.

Bianchini, Elsa P / Razanakolona, Mahita / Helms, Julie / Zouiti, Fouzia / Couteau-Chardon, Amélie / Marin-Esteban, Viviana / Chaisemartin, Luc de / De-Carvalho, Allan / Bironien, Roselyne / Chollet-Martin, Sylvie / Denis, Cécile V / Diehl, Jean-Luc / Vasse, Marc / Meziani, Ferhat / Borgel, Delphine

Thrombosis and haemostasis

2021 Volume 122, Issue 4, Page(s) 506–516

Abstract: Septic shock is the archetypal clinical setting in which extensive crosstalk between inflammation and coagulation dysregulates the latter. The main anticoagulant systems are systematically impaired, depleted, and/or downregulated. Protein Z-dependent ... ...

Abstract	Septic shock is the archetypal clinical setting in which extensive crosstalk between inflammation and coagulation dysregulates the latter. The main anticoagulant systems are systematically impaired, depleted, and/or downregulated. Protein Z-dependent protease inhibitor (ZPI) is an anticoagulant serpin that not only targets coagulation factors Xa and XIa but also acts as an acute phase reactant whose plasma concentration rises in inflammatory settings. The objective of the present study was to assess the plasma ZPI antigen level in a cohort of patients suffering from septic shock with or without overt-disseminated intravascular coagulation (DIC). The plasma ZPI antigen level was approximately 2.5-fold higher in the patient group (
MeSH term(s)	Anticoagulants/pharmacology ; Blood Proteins ; Disseminated Intravascular Coagulation/metabolism ; Extracellular Traps/metabolism ; Humans ; Leukocyte Elastase/metabolism ; Protease Inhibitors/metabolism ; Proteolysis ; Sepsis/metabolism ; Serpins/metabolism ; Shock, Septic/metabolism
Chemical Substances	Anticoagulants ; Blood Proteins ; Protease Inhibitors ; Serpins ; plasma protein Z ; Leukocyte Elastase (EC 3.4.21.37)
Language	English
Publishing date	2021-07-28
Publishing country	Germany
Document type	Journal Article
ZDB-ID	518294-3
ISSN	2567-689X ; 0340-6245
ISSN (online)	2567-689X
ISSN	0340-6245
DOI	10.1055/a-1530-3980
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Article: Inactivated antithrombins as fondaparinux antidotes: a promising alternative to haemostatic agents as assessed in vitro in a thrombin-generation assay.

Bourti, Yasmine / Fazavana, Judicael / Armand, Marine / Saller, François / Lasne, Dominique / Borgel, Delphine / Bianchini, Elsa P

Thrombosis and haemostasis

2016 Volume 116, Issue 3, Page(s) 452–460

Abstract: In the absence of specific antidote to fondaparinux, two modified forms of antithrombin (AT), one recombinant inactive (ri-AT) and the other chemically inactivated (chi-AT), were designed to antagonise AT-mediated anticoagulants, e. g. heparins or ... ...

Abstract	In the absence of specific antidote to fondaparinux, two modified forms of antithrombin (AT), one recombinant inactive (ri-AT) and the other chemically inactivated (chi-AT), were designed to antagonise AT-mediated anticoagulants, e. g. heparins or fondaparinux. These inactive ATs were previously proven to effectively neutralise anticoagulant activity associated with heparin derivatives in vitro and in vivo, as assessed by direct measurement of anti-FXa activity. This study was undertaken to evaluate in vitro the effectivity of inactive ATs to reverse anticoagulation by heparin derivatives and to compare them with non-specific fondaparinux reversal agents, like recombinant-activated factor VII (rFVIIa) or activated prothrombin-complex concentrate (aPCC), in a thrombin-generation assay (TGA). Addition of fondaparinux (3 µg/ml) to normal plasma inhibited thrombin generation by prolonging lag time (LT) as much as 244 % and lowering endogenous thrombin potential (ETP) to 17 % of their control (normal plasma) values. Fondaparinux-anticoagulant activity was reversed by ri-AT and chi-AT, as reflected by the corrections of LT up to 117 % and 114 % of its control value, and ETP recovery to 78 % and 63 %, respectively. Unlike ri-AT that had no effect on thrombin generation in normal plasma, chi-AT retained anticoagulant activity that minimises its reversal capacity. However, both ATs were more effective than rFVIIa or aPCC at neutralising fondaparinux and, unlike non-specific antidotes, inactive ATs specifically reversed AT-mediated anticoagulant activities, as suggested by their absence of procoagulant activity in anticoagulant-free plasma.
Language	English
Publishing date	2016-08-30
Publishing country	Germany
Document type	Journal Article
ZDB-ID	518294-3
ISSN	0340-6245
ISSN	0340-6245
DOI	10.1160/TH15-12-0927
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Article ; Online: Development of a recombinant antithrombin variant as a potent antidote to fondaparinux and other heparin derivatives.

Bianchini, Elsa P / Fazavana, Judicael / Picard, Veronique / Borgel, Delphine

Blood

2010 Volume 117, Issue 6, Page(s) 2054–2060

Abstract: Heparin derivative-based therapy has evolved from unfractionated heparin (UFH) to low-molecular-weight heparins (LMWHs) and now fondaparinux, a synthetic pentasaccharide. Contrary to UFH or LMWHs, fondaparinux is not neutralized by protamine sulfate, and ...

Abstract	Heparin derivative-based therapy has evolved from unfractionated heparin (UFH) to low-molecular-weight heparins (LMWHs) and now fondaparinux, a synthetic pentasaccharide. Contrary to UFH or LMWHs, fondaparinux is not neutralized by protamine sulfate, and no antidote is available to counteract bleeding disorders associated with overdosing. To make the use of fondaparinux safer, we developed an antithrombin (AT) variant as a potent antidote to heparin derivatives. This variant (AT-N135Q-Pro394) combines 2 mutations: substitution of Asn135 by a Gln to remove a glycosylation site and increase affinity for heparins, and the insertion of a Pro between Arg393 and Ser394 to abolish its anticoagulant activity. As expected, AT-N135Q-Pro394 anticoagulant activity was almost abolished, and it exhibited a 3-fold increase in fondaparinux affinity. AT-N135Q-Pro394 was shown to reverse fondaparinux overdosing in vitro in a dose-dependent manner through a competitive process with plasma AT for fondaparinux binding. This antidote effect was also observed in vivo: administration of AT-N135Q-Pro394 in 2.5-fold molar excess versus plasma AT neutralized 86% of the anti-Xa activity within 5 minutes in mice treated with fondaparinux. These results clearly demonstrate that AT-N135Q-Pro394 can reverse the anticoagulant activity of fondaparinux and thus could be used as an antidote for this drug.
MeSH term(s)	Amino Acid Substitution ; Animals ; Anticoagulants/antagonists & inhibitors ; Anticoagulants/toxicity ; Antidotes/pharmacology ; Antithrombin Proteins/genetics ; Antithrombin Proteins/pharmacology ; Antithrombins/pharmacology ; Drug Design ; Female ; Fondaparinux ; HEK293 Cells ; Hemorrhage/chemically induced ; Hemorrhage/drug therapy ; Heparin Antagonists/pharmacology ; Humans ; Mice ; Polysaccharides/antagonists & inhibitors ; Polysaccharides/toxicity ; Recombinant Proteins/genetics ; Recombinant Proteins/pharmacology
Chemical Substances	Anticoagulants ; Antidotes ; Antithrombin Proteins ; Antithrombins ; Heparin Antagonists ; Polysaccharides ; Recombinant Proteins ; Fondaparinux (J177FOW5JL)
Language	English
Publishing date	2010-11-03
Publishing country	United States
Document type	Evaluation Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Validation Study
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood-2010-06-288522
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Article ; Online: Inactivated antithombin as anticoagulant reversal in a rat model of cardiopulmonary bypass: a potent and potentially safer alternative to protamine.

Bianchini, Elsa P / Sebestyen, Alexandre / Abache, Toufik / Bourti, Yasmine / Fontayne, Alexandre / Richard, Vincent / Tamion, Fabienne / Plantier, Jean-Luc / Doguet, Fabien / Borgel, Delphine

British journal of haematology

2018 Volume 180, Issue 5, Page(s) 715–720

Abstract: Heparin anticoagulation followed by protamine reversal is commonly used in cardiopulmonary bypass (CPB). As an alternative to protamine, a recombinant inactive antithrombin (riAT) was designed as an antidote to heparin and was previously shown to be as ... ...

Abstract	Heparin anticoagulation followed by protamine reversal is commonly used in cardiopulmonary bypass (CPB). As an alternative to protamine, a recombinant inactive antithrombin (riAT) was designed as an antidote to heparin and was previously shown to be as potent as protamine in-vitro. In the present study, riAT was assessed for its ability to neutralize heparin after CPB in a rat model. After 60 min of CPB under heparin, rats received 5 mg/kg protamine, 37.5 mg/kg riAT or phosphate buffered saline (PBS) as placebo. Residual anticoagulant activity was assessed using the activated partial thromboplastin time assay before, and 10-30 min after reversion. Haemodynamic monitoring was performed and plasma histamine concentration was also measured. In this model, riAT appeared to be as efficient as protamine in neutralizing heparin. Ten minutes after injection, riAT and protamine both decreased heparin activity, to 1.8 ± 1.3 and 4.5 ± 1.4 u/ml, respectively (23.1 ± 5.1 u/ml in placebo group). Furthermore, evolution of mean carotid arterial pressure, heart rate and plasma histamine levels was comparable in rats treated with PBS or riAT, while protamine exhibited haemodynamic side effects and increased histamine plasma concentration. Thus, riAT could represent an advantage over protamine in CPB because it efficiently reverses heparin activity without negative effects on haemodynamic parameters and plasma histamine level.
MeSH term(s)	Animals ; Anticoagulants/pharmacology ; Antithrombins/pharmacology ; Cardiopulmonary Bypass ; Hemodynamics/drug effects ; Heparin/pharmacology ; Heparin Antagonists/pharmacology ; Histamine/metabolism ; Male ; Protamines/pharmacology ; Rats, Wistar
Chemical Substances	Anticoagulants ; Antithrombins ; Heparin Antagonists ; Protamines ; Histamine (820484N8I3) ; Heparin (9005-49-6)
Language	English
Publishing date	2018-01-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80077-6
ISSN	1365-2141 ; 0007-1048
ISSN (online)	1365-2141
ISSN	0007-1048
DOI	10.1111/bjh.15091
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Article: The Proteolytic Inactivation of Protein Z-Dependent Protease Inhibitor by Neutrophil Elastase Might Promote the Procoagulant Activity of Neutrophil Extracellular Traps in Sepsis

Bianchini, Elsa P. / Razanakolona, Mahita / Helms, Julie / Zouiti, Fouzia / Couteau-Chardon, Amélie / Marin-Esteban, Viviana / Chaisemartin, Luc de / De-Carvalho, Allan / Bironien, Roselyne / Chollet-Martin, Sylvie / Denis, Cécile V. / Diehl, Jean-Luc / Vasse, Marc / Meziani, Ferhat / Borgel, Delphine

Thrombosis and Haemostasis

2021 Volume 122, Issue 04, Page(s) 506–516

Abstract	Septic shock is the archetypal clinical setting in which extensive crosstalk between inflammation and coagulation dysregulates the latter. The main anticoagulant systems are systematically impaired, depleted, and/or downregulated. Protein Z-dependent protease inhibitor (ZPI) is an anticoagulant serpin that not only targets coagulation factors Xa and XIa but also acts as an acute phase reactant whose plasma concentration rises in inflammatory settings. The objective of the present study was to assess the plasma ZPI antigen level in a cohort of patients suffering from septic shock with or without overt-disseminated intravascular coagulation (DIC). The plasma ZPI antigen level was approximately 2.5-fold higher in the patient group ( n = 100; 38 with DIC and 62 without) than in healthy controls ( n = 31). The elevation's magnitude did not appear to depend on the presence/absence of DIC. Furthermore, Western blots revealed the presence of cleaved ZPI in plasma from patients with severe sepsis, independently of the DIC status. In vitro, ZPI was proteolytically inactivated by purified neutrophil elastase (NE) and by NE on the surface of neutrophil extracellular traps (NETs). The electrophoretic pattern of ZPI after NE-catalyzed proteolysis was very similar to that resulting from the clotting process—suggesting that the cleaved ZPI observed in severe sepsis plasma is devoid of anticoagulant activity. Taken as a whole, our results (1) suggest that NE is involved in ZPI inactivation during sepsis, and (2) reveal a novel putative mechanism for the procoagulant activity of NETs in immunothrombosis.
Keywords	ZPI ; SERPINA10 ; elastase ; NETs ; sepsis ; inflammation
Language	English
Publishing date	2021-06-16
Publisher	Georg Thieme Verlag KG
Publishing place	Stuttgart ; New York
Document type	Article
ZDB-ID	518294-3
ISSN	2567-689X ; 0340-6245
ISSN (online)	2567-689X
ISSN	0340-6245
DOI	10.1055/a-1530-3980
Database	Thieme publisher's database

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Article ; Online: Auto-associative heparin nanoassemblies: a biomimetic platform against the heparan sulfate-dependent viruses HSV-1, HSV-2, HPV-16 and RSV.

Lembo, David / Donalisio, Manuela / Laine, Claire / Cagno, Valeria / Civra, Andrea / Bianchini, Elsa P / Zeghbib, Narimane / Bouchemal, Kawthar

European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V

2014 Volume 88, Issue 1, Page(s) 275–282

Abstract: A new, simple and green method was developed for the manufacturing of heparin nanoassemblies active against the heparan sulfate-dependent viruses HSV-1, HSV-2, HPV-16 and RSV. These nanoassemblies were obtained by the auto-association of O-palmitoyl- ... ...

Abstract	A new, simple and green method was developed for the manufacturing of heparin nanoassemblies active against the heparan sulfate-dependent viruses HSV-1, HSV-2, HPV-16 and RSV. These nanoassemblies were obtained by the auto-association of O-palmitoyl-heparin and α-cyclodextrin in water. The synthesized O-palmitoyl-heparin derivatives mixed with α-cyclodextrin resulted in the formation of crystalline hexagonal nanoassemblies as observed by transmission electron microscopy. The nanoassembly mean hydrodynamic diameters were modulated from 340 to 659 nm depending on the type and the initial concentration of O-palmitoyl-heparin or α-cyclodextrin. The antiviral activity of the nanoassemblies was not affected by the concentration of the components. However, the method of the synthesis of O-palmitoyl-heparin affected the antiviral activity of the formulations. We showed that reduced antiviral activity is correlated with lower sulfation degree and anticoagulant activity.
MeSH term(s)	Animals ; Anticoagulants/chemistry ; Antiviral Agents/chemistry ; Biomimetics/methods ; Cell Line, Tumor ; Cell Survival ; Cercopithecus aethiops ; Crystallization ; HEK293 Cells ; Heparin/chemistry ; Herpesvirus 1, Human/drug effects ; Herpesvirus 2, Human/drug effects ; Human papillomavirus 16/drug effects ; Humans ; Hydrodynamics ; Microscopy, Electron, Transmission ; Nanoparticles/chemistry ; Nanotechnology ; Respiratory Syncytial Viruses/drug effects ; Swine ; Vero Cells ; Water/chemistry ; alpha-Cyclodextrins/chemistry
Chemical Substances	Anticoagulants ; Antiviral Agents ; alpha-Cyclodextrins ; Water (059QF0KO0R) ; Heparin (9005-49-6) ; alpha-cyclodextrin (Z1LH97KTRM)
Language	English
Publishing date	2014-09
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1065368-5
ISSN	1873-3441 ; 0939-6411
ISSN (online)	1873-3441
ISSN	0939-6411
DOI	10.1016/j.ejpb.2014.05.007
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