LIVIVO - Search results -

Search results

Result 1 - 10 of total 21

Search options

Article ; Online: HRMAS-NMR and simulation study of the self-assembly of surfactants on carbon nanotubes.

Singh, Raman Preet / Kaur, Taranpreet

Physical chemistry chemical physics : PCCP

2023 Volume 25, Issue 18, Page(s) 12900–12913

Abstract: Polyethoxylated surfactants, such as those of the Tween and Pluronic series, are commonly used to disperse carbon nanotubes (CNTs) and other nanoparticles. However, the current understanding of the nature of interactions between these surfactants and ... ...

Abstract	Polyethoxylated surfactants, such as those of the Tween and Pluronic series, are commonly used to disperse carbon nanotubes (CNTs) and other nanoparticles. However, the current understanding of the nature of interactions between these surfactants and CNTs is limited. The nature of the interactions between surfactants (Tween-80 [T80] and Pluronic F68 [PF68]) and CNTs was investigated using high-resolution magic angle spinning nuclear magnetic resonance (HRMAS-NMR) and coarse-grained molecular dynamics (MD) simulations. HRMAS-NMR revealed that T80 molecules interact with single-walled CNTs (SWCNTs) and multi-walled CNTs (MWCNTs)
Language	English
Publishing date	2023-05-10
Publishing country	England
Document type	Journal Article
ZDB-ID	1476244-4
ISSN	1463-9084 ; 1463-9076
ISSN (online)	1463-9084
ISSN	1463-9076
DOI	10.1039/d2cp03762a
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Article: Evaluation of the Effect of Vitamin D Levels During the Last Trimester of Pregnancy on Fetomaternal Outcomes in Patients With Preeclampsia.

Saini, Shweta / Kumari, Kalpana / Rai, Priyanka / Kaur, Taranpreet / Raj, Manish

Cureus

2023 Volume 15, Issue 11, Page(s) e49145

Abstract: Introduction Preeclampsia is a multisystem disorder with hypertension after 20 weeks of gestation. Among many predictors of preeclampsia, vitamin D being one of them is under many studies for establishing a correlation between levels of vitamin D and ... ...

Abstract	Introduction Preeclampsia is a multisystem disorder with hypertension after 20 weeks of gestation. Among many predictors of preeclampsia, vitamin D being one of them is under many studies for establishing a correlation between levels of vitamin D and preeclampsia. Objective To observe a relation between vitamin D levels and preeclampsia and assess related fetomaternal outcomes. Method It is an observational study at the tertiary care center. One hundred twenty patients, out of which 60 were taken as cases with BP>140/90, and 60 were taken as controls with normal BP in a tertiary care center from January 1, 2020, to June 30, 2021. All investigations were sent, and the mode of delivery and the fetomaternal outcome were assessed. Results Compared to normal pregnant patients, preeclamptic patients have significantly lower levels of vitamin D with a p-value of <0.001, which is significant. Conclusion There is a relationship between vitamin D levels and preeclampsia. However, the effects of supplementation of vitamin D on fetomaternal outcomes need further studies.
Language	English
Publishing date	2023-11-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	2747273-5
ISSN	2168-8184
ISSN	2168-8184
DOI	10.7759/cureus.49145
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Methods for characterizing the material properties of biomolecular condensates.

Alshareedah, Ibraheem / Kaur, Taranpreet / Banerjee, Priya R

Methods in enzymology

2020 Volume 646, Page(s) 143–183

Abstract: Biomolecular condensates are membrane-less sub-cellular compartments that perform a plethora of important functions in signaling and storage. The material properties of biomolecular condensates such as viscosity, surface tension, viscoelasticity, and ... ...

Abstract	Biomolecular condensates are membrane-less sub-cellular compartments that perform a plethora of important functions in signaling and storage. The material properties of biomolecular condensates such as viscosity, surface tension, viscoelasticity, and macromolecular diffusion play important roles in regulating their biological functions. Aberrations in these properties have been implicated in various neurodegenerative disorders and certain types of cancer. Unraveling the molecular driving forces that control the fluid structure and dynamics of biomolecular condensates across different length- and time-scales necessitates the application of innovative biophysical methodologies. In this chapter, we discuss major experimental techniques that are widely used to study the material states and dynamics of biomolecular condensates as well as their practical and conceptual limitations. We end this chapter with a discussion on more advanced tools that are currently emerging to address the complex fluid dynamics of these condensates.
MeSH term(s)	Diffusion ; Macromolecular Substances ; Viscosity
Chemical Substances	Macromolecular Substances
Language	English
Publishing date	2020-07-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1557-7988
ISSN (online)	1557-7988
DOI	10.1016/bs.mie.2020.06.009
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: FUS oncofusion protein condensates recruit mSWI/SNF chromatin remodeler via heterotypic interactions between prion-like domains.

Davis, Richoo B / Kaur, Taranpreet / Moosa, Mahdi Muhammad / Banerjee, Priya R

Protein science : a publication of the Protein Society

2021 Volume 30, Issue 7, Page(s) 1454–1466

Abstract: Fusion transcription factors generated by genomic translocations are common drivers of several types of cancers including sarcomas and leukemias. Oncofusions of the FET (FUS, EWSR1, and TAF15) family proteins result from the fusion of the prion-like ... ...

Abstract	Fusion transcription factors generated by genomic translocations are common drivers of several types of cancers including sarcomas and leukemias. Oncofusions of the FET (FUS, EWSR1, and TAF15) family proteins result from the fusion of the prion-like domain (PLD) of FET proteins to the DNA-binding domain (DBD) of certain transcription regulators and are implicated in aberrant transcriptional programs through interactions with chromatin remodelers. Here, we show that FUS-DDIT3, a FET oncofusion protein, undergoes PLD-mediated phase separation into liquid-like condensates. Nuclear FUS-DDIT3 condensates can recruit essential components of the global transcriptional machinery such as the chromatin remodeler SWI/SNF. The recruitment of mammalian SWI/SNF (mSWI/SNF) is driven by heterotypic PLD-PLD interactions between FUS-DDIT3 and core subunits of SWI/SNF, such as the catalytic component BRG1. Further experiments with single-molecule correlative force-fluorescence microscopy support a model wherein the fusion protein forms condensates on DNA surface and enrich BRG1 to activate transcription by ectopic chromatin remodeling. Similar PLD-driven co-condensation of mSWI/SNF with transcription factors can be employed by other oncogenic fusion proteins with a generic PLD-DBD domain architecture for global transcriptional reprogramming.
MeSH term(s)	Cell Line ; Chromosomal Proteins, Non-Histone/chemistry ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; Humans ; Microscopy, Fluorescence ; Oncogene Proteins, Fusion/chemistry ; Oncogene Proteins, Fusion/genetics ; Oncogene Proteins, Fusion/metabolism ; Prions/chemistry ; Prions/genetics ; Prions/metabolism ; Protein Domains ; RNA-Binding Protein FUS/chemistry ; RNA-Binding Protein FUS/genetics ; RNA-Binding Protein FUS/metabolism ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Chromosomal Proteins, Non-Histone ; FUS protein, human ; Oncogene Proteins, Fusion ; Prions ; RNA-Binding Protein FUS ; SWI-SNF-B chromatin-remodeling complex ; Transcription Factors
Language	English
Publishing date	2021-06-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.4127
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 3407: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 1: Show issues

Order via subito

Details ▾

Article: Characterization and toxicity of a phosphate-binding exobiopolymer produced by Acinetobacter haemolyticus MG606.

Kaur, Taranpreet / Ghosh, Moushumi

Journal of water and health

2017 Volume 15, Issue 1, Page(s) 103–111

Abstract: A novel, phosphate-binding exobiopolymer (EBP) produced by Acinetobacter haemolyticus MG606 was characterized and its biocompatibility evaluated in RAW 264.7 cells and in mice. EBP was identified as a 50 kDa heteropolysaccharide composed of pentose and ... ...

Abstract	A novel, phosphate-binding exobiopolymer (EBP) produced by Acinetobacter haemolyticus MG606 was characterized and its biocompatibility evaluated in RAW 264.7 cells and in mice. EBP was identified as a 50 kDa heteropolysaccharide composed of pentose and hexose sugars. EBP exhibited cytotoxicity, stimulation of free radical production and loss of mitochondrial and lysosomal integrity in RAW 264.7 cells at 500 μg/mL concentration while lower concentrations exhibited no significant (p > 0.05) effect on these parameters. EBP exhibited dose-dependent mortality, body weight reduction, hypothermia and clinical signs of toxicity in mice following intraperitoneal administration. The LD
MeSH term(s)	Acinetobacter/chemistry ; Acinetobacter/metabolism ; Animals ; Biopolymers/analysis ; Biopolymers/toxicity ; Female ; Injections, Intraperitoneal ; Mice ; Phosphates/metabolism ; RAW 264.7 Cells ; Toxicity Tests
Chemical Substances	Biopolymers ; Phosphates
Language	English
Publishing date	2017-02
Publishing country	England
Document type	Journal Article
ZDB-ID	2123845-5
ISSN	1996-7829 ; 1477-8920
ISSN (online)	1996-7829
ISSN	1477-8920
DOI	10.2166/wh.2016.176
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Bonn / Germany

Z 7513: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Sequence-encoded and composition-dependent protein-RNA interactions control multiphasic condensate morphologies.

Kaur, Taranpreet / Raju, Muralikrishna / Alshareedah, Ibraheem / Davis, Richoo B / Potoyan, Davit A / Banerjee, Priya R

Nature communications

2021 Volume 12, Issue 1, Page(s) 872

Abstract: Multivalent protein-protein and protein-RNA interactions are the drivers of biological phase separation. Biomolecular condensates typically contain a dense network of multiple proteins and RNAs, and their competing molecular interactions play key roles ... ...

Abstract	Multivalent protein-protein and protein-RNA interactions are the drivers of biological phase separation. Biomolecular condensates typically contain a dense network of multiple proteins and RNAs, and their competing molecular interactions play key roles in regulating the condensate composition and structure. Employing a ternary system comprising of a prion-like polypeptide (PLP), arginine-rich polypeptide (RRP), and RNA, we show that competition between the PLP and RNA for a single shared partner, the RRP, leads to RNA-induced demixing of PLP-RRP condensates into stable coexisting phases-homotypic PLP condensates and heterotypic RRP-RNA condensates. The morphology of these biphasic condensates (non-engulfing/ partial engulfing/ complete engulfing) is determined by the RNA-to-RRP stoichiometry and the hierarchy of intermolecular interactions, providing a glimpse of the broad range of multiphasic patterns that are accessible to these condensates. Our findings provide a minimal set of physical rules that govern the composition and spatial organization of multicomponent and multiphasic biomolecular condensates.
MeSH term(s)	Amino Acid Sequence ; Arginine/metabolism ; Base Sequence ; Peptides/metabolism ; Prions/metabolism ; RNA/metabolism ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/metabolism ; Surface Tension
Chemical Substances	Peptides ; Prions ; RNA-Binding Proteins ; RNA (63231-63-0) ; Arginine (94ZLA3W45F)
Language	English
Publishing date	2021-02-08
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-21089-4
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Acinetobacter haemolyticus MG606 produces a novel, phosphate binding exobiopolymer.

Kaur, Taranpreet / Ghosh, Moushumi

Carbohydrate polymers

2015 Volume 132, Page(s) 72–79

Abstract: The present study evaluated an extracellular, novel biopolymer produced by Acinetobacter haemolyticus MG606 for its physicochemical properties and phosphate binding mechanism. The exobiopolymer (EBP) was characterized to be majorly polysaccharide in ... ...

Abstract	The present study evaluated an extracellular, novel biopolymer produced by Acinetobacter haemolyticus MG606 for its physicochemical properties and phosphate binding mechanism. The exobiopolymer (EBP) was characterized to be majorly polysaccharide in nature consisting of 48.9 kDa heteropolysaccharide composed of galactose, glucose, xylose, lyxose, allose, ribose, arabinose, mannose and fructose. Maximum phosphate binding efficiency of 25mg phosphate/g of EBP was described by Langmuir isotherm and further, the physicochemical and spectroscopic studies revealed that phosphate appeared to bind predominantly with the polysaccharide fraction, and to a relatively lesser extent to protein fraction of EBP. The electrostatic interactions with amino groups and ligand exchange with hydroxyl groups of EBP were found to be primary basis for phosphate binding mechanism. The results of this study implicate the feasibility of the EBP for commercial bioremediation processes.
MeSH term(s)	Acinetobacter/chemistry ; Acinetobacter/metabolism ; Biodegradation, Environmental ; Environmental Pollutants/isolation & purification ; Environmental Pollutants/metabolism ; Phosphates/isolation & purification ; Phosphates/metabolism ; Polysaccharides/chemistry ; Polysaccharides/metabolism
Chemical Substances	Environmental Pollutants ; Phosphates ; Polysaccharides
Language	English
Publishing date	2015-11-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1501516-6
ISSN	1879-1344 ; 0144-8617
ISSN (online)	1879-1344
ISSN	0144-8617
DOI	10.1016/j.carbpol.2015.06.002
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: Characterization and upregulation of bifunctional phosphoglucomutase/phosphomannomutase enzyme in an exobiopolymer overproducing strain of Acinetobacter haemolyticus.

Kaur, Taranpreet / Ghosh, Moushumi

Microbiological research

2015 Volume 181, Page(s) 8–14

Abstract: Several members of the Acinetobacter spp. produce exobiopolymer (EBP) of considerable biotechnological interest. In a previous study, we reported phosphate removal capacity of EBP produced by Acinetobacter haemolyticus. Insertional mutagenesis was ... ...

Abstract	Several members of the Acinetobacter spp. produce exobiopolymer (EBP) of considerable biotechnological interest. In a previous study, we reported phosphate removal capacity of EBP produced by Acinetobacter haemolyticus. Insertional mutagenesis was attempted to develop EBP-overproducing strains of A. haemolyticus and mutant MG606 was isolated. In order to understand the underlying mechanism of overproduction, the EBP overproducing mutant MG606 was analyzed and compared with the wild type counterpart for its key EBP synthetic enzymes. The EBP produced by MG606 mutant was 650 mg/L compared to 220 mg/L in its wild type counterpart. Significantly high (p<0.05) levels of phosphoglucomutase/phosphomannomutase (PGM/PMM) in MG606 mutant was noted, whereas activities of other enzymes responsible for EBP synthesis showed no significant change (p>0.05). The up-regulation of PGM/PMM expression in mutant was further confirmed by real time reverse transcriptase (RT)-PCR of PGM/PMM transcripts. The optimal conditions for PGM/PMM activity were found to be 35 °C and pH 7.5; PGM/PMM activity was inhibited by ions such as lithium, zinc, nickel. Further, incubation of cells with a PGM inhibitor (lithium) resulted in a concentration-dependent decrease in EBP production further confirming the role of PGM/PMM overexpression in enhanced EBP production by the mutant. Overall the results of our study indicate a key role of PGM/PMM in enhanced EBP production, as evident from enhanced enzyme activity, increased PGM/PMM transcripts and reduction in EBP synthesis by a PGM inhibitor. We envisage a potential exploitation of the insights so obtained to effectively engineer strains of Acinetobacter for overproducing phosphate binding EBP.
MeSH term(s)	Acinetobacter/drug effects ; Acinetobacter/enzymology ; Acinetobacter/genetics ; Electrophoresis, Polyacrylamide Gel ; Mutagenesis, Insertional ; Phosphoglucomutase/chemistry ; Phosphoglucomutase/genetics ; Phosphoglucomutase/metabolism ; Phosphotransferases (Phosphomutases)/chemistry ; Phosphotransferases (Phosphomutases)/genetics ; Phosphotransferases (Phosphomutases)/metabolism ; RNA-Directed DNA Polymerase ; Real-Time Polymerase Chain Reaction ; Substrate Specificity ; Transcriptional Activation ; Up-Regulation
Chemical Substances	RNA-Directed DNA Polymerase (EC 2.7.7.49) ; Phosphotransferases (Phosphomutases) (EC 5.4.2.-) ; Phosphoglucomutase (EC 5.4.2.2) ; phosphomannomutase (EC 5.4.2.8)
Language	English
Publishing date	2015-12
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1189614-0
ISSN	1618-0623 ; 0944-5013
ISSN (online)	1618-0623
ISSN	0944-5013
DOI	10.1016/j.micres.2015.08.003
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Ud II Zs.7: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article: Characterization and upregulation of bifunctional phosphoglucomutase/phosphomannomutase enzyme in an exobiopolymer overproducing strain of Acinetobacter haemolyticus

Kaur, Taranpreet / Moushumi Ghosh

Microbiological research. 2015 Dec., v. 181

2015

Abstract	Several members of the Acinetobacter spp. produce exobiopolymer (EBP) of considerable biotechnological interest. In a previous study, we reported phosphate removal capacity of EBP produced by Acinetobacter haemolyticus. Insertional mutagenesis was attempted to develop EBP-overproducing strains of A. haemolyticus and mutant MG606 was isolated. In order to understand the underlying mechanism of overproduction, the EBP overproducing mutant MG606 was analyzed and compared with the wild type counterpart for its key EBP synthetic enzymes. The EBP produced by MG606 mutant was 650mg/L compared to 220mg/L in its wild type counterpart. Significantly high (p<0.05) levels of phosphoglucomutase/phosphomannomutase (PGM/PMM) in MG606 mutant was noted, whereas activities of other enzymes responsible for EBP synthesis showed no significant change (p>0.05). The up-regulation of PGM/PMM expression in mutant was further confirmed by real time reverse transcriptase (RT)-PCR of PGM/PMM transcripts. The optimal conditions for PGM/PMM activity were found to be 35Â°C and pH 7.5; PGM/PMM activity was inhibited by ions such as lithium, zinc, nickel. Further, incubation of cells with a PGM inhibitor (lithium) resulted in a concentration-dependent decrease in EBP production further confirming the role of PGM/PMM overexpression in enhanced EBP production by the mutant. Overall the results of our study indicate a key role of PGM/PMM in enhanced EBP production, as evident from enhanced enzyme activity, increased PGM/PMM transcripts and reduction in EBP synthesis by a PGM inhibitor. We envisage a potential exploitation of the insights so obtained to effectively engineer strains of Acinetobacter for overproducing phosphate binding EBP.
Keywords	Acinetobacter haemolyticus ; enzyme activity ; gene expression regulation ; gene overexpression ; insertional mutagenesis ; ions ; lithium ; mutants ; nickel ; pH ; phosphates ; phosphoglucomutase ; phosphomannomutase ; RNA-directed DNA polymerase ; zinc
Language	English
Dates of publication	2015-12
Size	p. 8-14.
Publishing place	Elsevier GmbH
Document type	Article
ZDB-ID	1189614-0
ISSN	1618-0623 ; 0944-5013
ISSN (online)	1618-0623
ISSN	0944-5013
DOI	10.1016/j.micres.2015.08.003
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 1148: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article: Acinetobacter haemolyticus MG606 produces a novel, phosphate binding exobiopolymer

Kaur, Taranpreet / Moushumi Ghosh

Carbohydrate polymers. 2015 Nov. 05, v. 132

2015

Abstract	The present study evaluated an extracellular, novel biopolymer produced by Acinetobacter haemolyticus MG606 for its physicochemical properties and phosphate binding mechanism. The exobiopolymer (EBP) was characterized to be majorly polysaccharide in nature consisting of 48.9kDa heteropolysaccharide composed of galactose, glucose, xylose, lyxose, allose, ribose, arabinose, mannose and fructose. Maximum phosphate binding efficiency of 25mg phosphate/g of EBP was described by Langmuir isotherm and further, the physicochemical and spectroscopic studies revealed that phosphate appeared to bind predominantly with the polysaccharide fraction, and to a relatively lesser extent to protein fraction of EBP. The electrostatic interactions with amino groups and ligand exchange with hydroxyl groups of EBP were found to be primary basis for phosphate binding mechanism. The results of this study implicate the feasibility of the EBP for commercial bioremediation processes.
Keywords	Acinetobacter haemolyticus ; allose ; arabinose ; biopolymers ; bioremediation ; electrostatic interactions ; fructose ; galactose ; glucose ; ligands ; mannose ; phosphates ; polysaccharides ; ribose ; sorption isotherms ; spectral analysis ; xylose
Language	English
Dates of publication	2015-1105
Size	p. 72-79.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	1501516-6
ISSN	1879-1344 ; 0144-8617
ISSN (online)	1879-1344
ISSN	0144-8617
DOI	10.1016/j.carbpol.2015.06.002
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

To top

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

Order via subito