LIVIVO - Search results -

Search results

Result 1 - 10 of total 59

Search options

Article ; Online: Plant biotechnology: Green for Good V 2019.

Kopecny, David / Vlcko, Tomas

2020 Volume 57, Page(s) 1–3

Abstract: The Green for Good (G4G) conferences bring together plant science researchers mainly from Europe, as well as guests from overseas. As with previous G4G conferences, the 5th event (G4G V) was held at Palacký University Olomouc, Czech Republic, organized ... ...

Abstract	The Green for Good (G4G) conferences bring together plant science researchers mainly from Europe, as well as guests from overseas. As with previous G4G conferences, the 5th event (G4G V) was held at Palacký University Olomouc, Czech Republic, organized by the Centre of Region Haná for Biotechnological and Agricultural Research and the European Federation of Biotechnology. The meeting focused on trends in plant biotechnology, genetics and biochemistry to identify the basis for solving the global challenge of providing food for an ever-growing population. The invited speakers provided insights into plant genomics, gene-editing, plant molecular farming and application of nanomaterials. This conference meeting report summarizes key lectures given by a variety of excellent speakers.
MeSH term(s)	Agriculture ; Biotechnology ; Europe ; Gene Editing ; Humans ; Plants/genetics ; Research Personnel
Language	English
Publishing date	2020-02-01
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2400836-9
ISSN	1876-4347 ; 1871-6784
ISSN (online)	1876-4347
ISSN	1871-6784
DOI	10.1016/j.nbt.2020.01.004
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

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.

Details ▾
- Full text online
- Order with fees

Article: Plant biotechnology: Green for Good V 2019

Kopecny, David / Vlcko, Tomas

New biotechnology. 2020 July 25, v. 57

2020

Abstract	The Green for Good (G4G) conferences bring together plant science researchers mainly from Europe, as well as guests from overseas. As with previous G4G conferences, the 5th event (G4G V) was held at Palacký University Olomouc, Czech Republic, organized by the Centre of Region Haná for Biotechnological and Agricultural Research and the European Federation of Biotechnology. The meeting focused on trends in plant biotechnology, genetics and biochemistry to identify the basis for solving the global challenge of providing food for an ever-growing population. The invited speakers provided insights into plant genomics, gene-editing, plant molecular farming and application of nanomaterials. This conference meeting report summarizes key lectures given by a variety of excellent speakers.
Keywords	biochemistry ; gene editing ; genomics ; molecular farming ; nanomaterials ; Czech Republic
Language	English
Dates of publication	2020-0725
Size	p. 1-3.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	2400836-9
ISSN	1876-4347 ; 1871-6784
ISSN (online)	1876-4347
ISSN	1871-6784
DOI	10.1016/j.nbt.2020.01.004
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

Article ; Online: Biochemical and structural basis of polyamine, lysine and ornithine acetylation catalyzed by spermine/spermidine N‐acetyl transferase in moss and maize

Bělíček, Jakub / Ľuptáková, Eva / Kopečný, David / Frömmel, Jan / Vigouroux, Armelle / Ćavar Zeljković, Sanja / Jagic, Franjo / Briozzo, Pierre / Kopečný, David Jaroslav / Tarkowski, Petr / Nisler, Jaroslav / De Diego, Nuria / Moréra, Solange / Kopečná, Martina

The Plant Journal. 2023 May, v. 114, no. 3 p.482-498

2023

Abstract: Polyamines such as spermidine and spermine are essential regulators of cell growth, differentiation, maintenance of ion balance and abiotic stress tolerance. Their levels are controlled by the spermidine/spermine N¹‐acetyltransferase (SSAT) via ... ...

Abstract	Polyamines such as spermidine and spermine are essential regulators of cell growth, differentiation, maintenance of ion balance and abiotic stress tolerance. Their levels are controlled by the spermidine/spermine N¹‐acetyltransferase (SSAT) via acetylation to promote either their degradation or export outside the cell as shown in mammals. Plant genomes contain at least one gene coding for SSAT (also named NATA for N‐AcetylTransferase Activity). Combining kinetics, HPLC‐MS and crystallography, we show that three plant SSATs, one from the lower plant moss Physcomitrium patens and two from the higher plant Zea mays, acetylate various aliphatic polyamines and two amino acids lysine (Lys) and ornithine (Orn). Thus, plant SSATs exhibit a broad substrate specificity, unlike more specific human SSATs (hSSATs) as hSSAT1 targets polyamines, whereas hSSAT2 acetylates Lys and thiaLys. The crystal structures of two PpSSAT ternary complexes, one with Lys and CoA, the other with acetyl‐CoA and polyethylene glycol (mimicking spermine), reveal a different binding mode for polyamine versus amino acid substrates accompanied by structural rearrangements of both the coenzyme and the enzyme. Two arginine residues, unique among plant SSATs, hold the carboxyl group of amino acid substrates. The most abundant acetylated compound accumulated in moss was N⁶‐acetyl‐Lys, whereas N⁵‐acetyl‐Orn, known to be toxic for aphids, was found in maize. Both plant species contain very low levels of acetylated polyamines. The present study provides a detailed biochemical and structural basis of plant SSAT enzymes that can acetylate a wide range of substrates and likely play various roles in planta.
Keywords	Physcomitrium ; Zea mays ; abiotic stress ; acetyl coenzyme A ; acetylation ; acetyltransferases ; arginine ; cell growth ; corn ; crystallography ; exports ; genes ; humans ; lysine ; mosses and liverworts ; ornithine ; polyethylene glycol ; spermidine ; spermine ; stress tolerance ; substrate specificity ; toxicity
Language	English
Dates of publication	2023-05
Size	p. 482-498.
Publishing place	John Wiley & Sons, Ltd
Document type	Article ; Online
Note	JOURNAL ARTICLE
ZDB-ID	1088037-9
ISSN	1365-313X ; 0960-7412
ISSN (online)	1365-313X
ISSN	0960-7412
DOI	10.1111/tpj.16148
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 6071: 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 ; Online: Biochemical and structural basis of polyamine, lysine and ornithine acetylation catalyzed by spermine/spermidine N-acetyl transferase in moss and maize.

The Plant journal : for cell and molecular biology

2023 Volume 114, Issue 3, Page(s) 482–498

Abstract	Polyamines such as spermidine and spermine are essential regulators of cell growth, differentiation, maintenance of ion balance and abiotic stress tolerance. Their levels are controlled by the spermidine/spermine N
MeSH term(s)	Animals ; Humans ; Polyamines/metabolism ; Spermidine ; Spermine/metabolism ; Zea mays/metabolism ; Lysine/metabolism ; Ornithine/metabolism ; Acetylation ; Acetyltransferases/genetics ; Acetyltransferases/metabolism ; Catalysis ; Mammals/metabolism
Chemical Substances	Polyamines ; Spermidine (U87FK77H25) ; Spermine (2FZ7Y3VOQX) ; Lysine (K3Z4F929H6) ; Ornithine (E524N2IXA3) ; Acetyltransferases (EC 2.3.1.-)
Language	English
Publishing date	2023-03-16
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1088037-9
ISSN	1365-313X ; 0960-7412
ISSN (online)	1365-313X
ISSN	0960-7412
DOI	10.1111/tpj.16148
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 6071: 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 ; Online: Amino acid conjugation of oxIAA is a secondary metabolic regulation involved in auxin homeostasis.

Brunoni, Federica / Pěnčík, Aleš / Žukauskaitė, Asta / Ament, Anita / Kopečná, Martina / Collani, Silvio / Kopečný, David / Novák, Ondřej

The New phytologist

2023 Volume 238, Issue 6, Page(s) 2264–2270

MeSH term(s)	Amino Acids/metabolism ; Arabidopsis Proteins/metabolism ; Arabidopsis/metabolism ; Homeostasis ; Indoleacetic Acids/metabolism ; Gene Expression Regulation, Plant
Chemical Substances	Amino Acids ; Arabidopsis Proteins ; Indoleacetic Acids
Language	English
Publishing date	2023-03-31
Publishing country	England
Document type	Letter ; Research Support, Non-U.S. Gov't
ZDB-ID	208885-x
ISSN	1469-8137 ; 0028-646X
ISSN (online)	1469-8137
ISSN	0028-646X
DOI	10.1111/nph.18887
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 868: 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 ; Online: Plant nucleoside N-ribohydrolases: riboside binding and role in nitrogen storage mobilization.

Ľuptáková, Eva / Vigouroux, Armelle / Končitíková, Radka / Kopečná, Martina / Zalabák, David / Novák, Ondřej / Salcedo Sarmiento, Sara / Ćavar Zeljković, Sanja / Kopečný, David Jaroslav / von Schwartzenberg, Klaus / Strnad, Miroslav / Spíchal, Lukáš / De Diego, Nuria / Kopečný, David / Moréra, Solange

The Plant journal : for cell and molecular biology

2023 Volume 117, Issue 5, Page(s) 1432–1452

Abstract: Cells save their energy during nitrogen starvation by selective autophagy of ribosomes and degradation of RNA to ribonucleotides and nucleosides. Nucleosides are hydrolyzed by nucleoside N-ribohydrolases (nucleosidases, NRHs). Subclass I of NRHs ... ...

Abstract	Cells save their energy during nitrogen starvation by selective autophagy of ribosomes and degradation of RNA to ribonucleotides and nucleosides. Nucleosides are hydrolyzed by nucleoside N-ribohydrolases (nucleosidases, NRHs). Subclass I of NRHs preferentially hydrolyzes the purine ribosides while subclass II is more active towards uridine and xanthosine. Here, we performed a crystallographic and kinetic study to shed light on nucleoside preferences among plant NRHs followed by in vivo metabolomic and phenotyping analyses to reveal the consequences of enhanced nucleoside breakdown. We report the crystal structure of Zea mays NRH2b (subclass II) and NRH3 (subclass I) in complexes with the substrate analog forodesine. Purine and pyrimidine catabolism are inseparable because nucleobase binding in the active site of ZmNRH is mediated via a water network and is thus unspecific. Dexamethasone-inducible ZmNRH overexpressor lines of Arabidopsis thaliana, as well as double nrh knockout lines of moss Physcomitrium patents, reveal a fine control of adenosine in contrast to other ribosides. ZmNRH overexpressor lines display an accelerated early vegetative phase including faster root and rosette growth upon nitrogen starvation or osmotic stress. Moreover, the lines enter the bolting and flowering phase much earlier. We observe changes in the pathways related to nitrogen-containing compounds such as β-alanine and several polyamines, which allow plants to reprogram their metabolism to escape stress. Taken together, crop plant breeding targeting enhanced NRH-mediated nitrogen recycling could therefore be a strategy to enhance plant growth tolerance and productivity under adverse growth conditions.
MeSH term(s)	Nucleosides/metabolism ; Nitrogen/metabolism ; Plant Breeding ; Plants/metabolism ; Uridine/metabolism ; Arabidopsis/genetics
Chemical Substances	Nucleosides ; Nitrogen (N762921K75) ; Uridine (WHI7HQ7H85)
Language	English
Publishing date	2023-12-04
Publishing country	England
Document type	Journal Article
ZDB-ID	1088037-9
ISSN	1365-313X ; 0960-7412
ISSN (online)	1365-313X
ISSN	0960-7412
DOI	10.1111/tpj.16572
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 6071: 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: Long-Lasting Stable Expression of Human LL-37 Antimicrobial Peptide in Transgenic Barley Plants.

Mirzaee, Malihe / Holásková, Edita / Mičúchová, Alžbeta / Kopečný, David J / Osmani, Zhila / Frébort, Ivo

Antibiotics (Basel, Switzerland)

2021 Volume 10, Issue 8

Abstract: Antimicrobial peptides play a crucial role in the innate immune system of multicellular organisms. LL-37 is the only known member of the human cathelicidin family. As well as possessing antibacterial properties, it is actively involved in various ... ...

Abstract	Antimicrobial peptides play a crucial role in the innate immune system of multicellular organisms. LL-37 is the only known member of the human cathelicidin family. As well as possessing antibacterial properties, it is actively involved in various physiological responses in eukaryotic cells. Accordingly, there is considerable interest in large-scale, low-cost, and microbial endotoxin-free production of LL-37 recombinant peptides for pharmaceutical applications. As a heterologous expression biofactory, we have previously obtained homologous barley (
Language	English
Publishing date	2021-07-23
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2681345-2
ISSN	2079-6382
ISSN	2079-6382
DOI	10.3390/antibiotics10080898
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Characterization of five CHASE-containing histidine kinase receptors from Populus × canadensis cv. Robusta sensing isoprenoid and aromatic cytokinins

Jaworek, Pavel / Tarkowski, Petr / Hluska, Tomáš / Kouřil, Štěpán / Vrobel, Ondřej / Nisler, Jaroslav / Kopečný, David

Planta. 2020 Jan., v. 251, no. 1

2020

Abstract: MAIN CONCLUSION: Five poplar CHASE-containing histidine kinase receptors bind cytokinins and display kinase activities. Both endogenous isoprenoid and aromatic cytokinins bind to the receptors in live cell assays. Cytokinins are phytohormones that play ... ...

Abstract	MAIN CONCLUSION: Five poplar CHASE-containing histidine kinase receptors bind cytokinins and display kinase activities. Both endogenous isoprenoid and aromatic cytokinins bind to the receptors in live cell assays. Cytokinins are phytohormones that play key roles in various developmental processes in plants. The poplar species Populus × canadensis, cv. Robusta, is the first organism found to contain aromatic cytokinins. Here, we report the functional characterization of five CHASE-containing histidine kinases from P. × canadensis: PcHK2, PcHK3a, PcHK3b, PcHK4a and PcHK4b. A qPCR analysis revealed high transcript levels of all PcHKs other than PcHK4b across multiple poplar organs. The ligand specificity was determined using a live cell Escherichia coli assay and we provide evidence based on UHPLC-MS/MS data that ribosides can be true ligands. PcHK2 exhibited higher sensitivity to iP-type cytokinins than the other receptors, while PcHK3a and PcHK3b bound these cytokinins much more weakly, because they possess two isoleucine residues that clash with the cytokinin base and destabilize its binding. All receptors display kinase activity but their activation ratios in the presence/absence of cytokinin differ significantly. PcHK4a displays over 400-fold higher kinase activity in the presence of cytokinin, suggesting involvement in strong responses to changes in cytokinin levels. trans-Zeatin was both the most abundant cytokinin in poplar and that with the highest variation in abundance, which is consistent with its strong binding to all five HKs and activation of cytokinin signaling via A-type response regulators. The aromatic cytokinins’ biological significance remains unclear, their levels vary diurnally, seasonally, and annually. PcHK3 and PcHK4 display the strongest binding at pH 7.5 and 5.5, respectively, in line with their putative membrane localization in the endoplasmic reticulum and plasma membrane.
Keywords	Escherichia coli ; Populus canadensis ; cytokinins ; endoplasmic reticulum ; enzyme activity ; histidine kinase ; isoleucine ; isoprenoids ; ligands ; pH ; plant hormones ; plasma membrane ; quantitative polymerase chain reaction ; receptors ; tandem mass spectrometry
Language	English
Dates of publication	2020-01
Size	p. 1.
Publishing place	Springer Berlin Heidelberg
Document type	Article
ZDB-ID	208909-9
ISSN	1432-2048 ; 0032-0935 ; 1866-2749
ISSN (online)	1432-2048
ISSN	0032-0935 ; 1866-2749
DOI	10.1007/s00425-019-03297-x
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 46/303: 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: Serum albumin as a primary non-covalent binding protein for nitro-oleic acid

Hernychova, Lenka / Alexandri, Eleni / Tzakos, Andreas G. / Zatloukalová, Martina / Primikyri, Alexandra / Gerothanassis, Ioannis P. / Uhrik, Lukas / Šebela, Marek / Kopečný, David / Jedinák, Lukáš / Vacek, Jan

International journal of biological macromolecules. 2022 Apr. 01, v. 203

2022

Abstract: This work explores the interaction of 9/10-nitro-oleic acid (NO₂-OA) with human serum albumin (HSA). The molecular mechanism of the biological action of NO₂-OA is to our knowledge based on a reversible covalent reaction–Michael addition of nucleophilic ... ...

Abstract	This work explores the interaction of 9/10-nitro-oleic acid (NO₂-OA) with human serum albumin (HSA). The molecular mechanism of the biological action of NO₂-OA is to our knowledge based on a reversible covalent reaction–Michael addition of nucleophilic amino acid residues of proteins. Since HSA is an important fatty acid transporter, a key question is whether NO₂-OA can bind covalently or non-covalently to HSA, similarly to oleic acid (OA), which can interact with the FA1-FA7 binding sites of the HSA molecule. ¹H NMR studies and competition analysis with OA and the drugs ibuprofen and warfarin were used to investigate a potential non-covalent binding mode. NO₂-OA/HSA binding was confirmed to compete with warfarin for FA-7 with significantly higher affinity. NO₂-OA competes with ibuprofen for FA-3 and FA-6, however, in contrast to the situation with warfarin, the binding affinities are not significantly different. The described interactions are based exclusively on non-covalent binding. No covalent binding of NO₂-OA to HSA was detected by MS/MS. More detailed studies based on MALDI-TOF-MS and Ellman's assay indicated that HSA can be covalently modified in the presence of NO₂-OA to a very limited extent. It was also shown that NO₂-OA has a higher affinity to HSA than that of OA.
Keywords	Lewis bases ; amino acids ; chemical bonding ; fatty acid transport proteins ; human serum albumin ; ibuprofen ; oleic acid ; warfarin
Language	English
Dates of publication	2022-0401
Size	p. 116-129.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2022.01.050
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.B 2374: 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 ; Online: Oxidation of imidazole- and pyrazole-derived aldehydes by plant aldehyde dehydrogenases from the family 2 and 10.

Frömmel, Jan / Končitíková, Radka / Kopečný, David / Soural, Miroslav / Šebela, Marek

Chemico-biological interactions

2019 Volume 304, Page(s) 194–201

Abstract: Plant cytosolic aldehyde dehydrogenases from family 2 (ALDH2s, EC 1.2.1.3) are non-specific enzymes and participate for example in the metabolism of acetaldehyde or biosynthesis of phenylpropanoids. Plant aminoaldehyde dehydrogenases (AMADHs, ALDH10 ... ...

Abstract	Plant cytosolic aldehyde dehydrogenases from family 2 (ALDH2s, EC 1.2.1.3) are non-specific enzymes and participate for example in the metabolism of acetaldehyde or biosynthesis of phenylpropanoids. Plant aminoaldehyde dehydrogenases (AMADHs, ALDH10 family, EC 1.2.1.19) are broadly specific and play an important role in polyamine degradation or production of osmoprotectants. We have tested imidazole and pyrazole carbaldehydes and their alkyl-, allyl-, benzyl-, phenyl-, pyrimidinyl- or thienyl-derivatives as possible substrates of plant ALDH2 and ALDH10 enzymes. Imidazole represents a building block of histidine, histamine as well as certain alkaloids. It also appears in synthetic pharmaceuticals such as imidazole antifungals. Biological compounds containing pyrazole are rare (e.g. pyrazole-1-alanine and pyrazofurin antibiotics) but the ring is often found as a constituent of many synthetic drugs and pesticides. The aim was to evaluate whether aldehyde compounds based on azole heterocycles are oxidized by the enzymes, which would further support their expected role as detoxifying aldehyde scavengers. The analyzed imidazole and pyrazole carbaldehydes were only slowly converted by ALDH10s but well oxidized by cytosolic maize ALDH2 isoforms (particularly by ALDH2C1). In the latter case, the respective K
MeSH term(s)	Aldehyde Dehydrogenase/metabolism ; Aldehydes/chemistry ; Aldehydes/metabolism ; Imidazoles/chemistry ; Imidazoles/metabolism ; Solanum lycopersicum/enzymology ; Molecular Structure ; Oxidation-Reduction ; Pisum sativum/enzymology ; Pyrazoles/chemistry ; Pyrazoles/metabolism ; Zea mays/enzymology
Chemical Substances	Aldehydes ; Imidazoles ; Pyrazoles ; pyrazole (3QD5KJZ7ZJ) ; imidazole (7GBN705NH1) ; Aldehyde Dehydrogenase (EC 1.2.1.3)
Language	English
Publishing date	2019-02-13
Publishing country	Ireland
Document type	Journal Article
ZDB-ID	218799-1
ISSN	1872-7786 ; 0009-2797
ISSN (online)	1872-7786
ISSN	0009-2797
DOI	10.1016/j.cbi.2019.02.008
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 686: Show issues

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

Order via subito

Details ▾

To top

Full text online

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 Bonn / Germany

Order via subito

Inter-library loan at ZB MED

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

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

Full text online

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

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

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 Cologne/Königswinter

Order via subito