LIVIVO - Search results -

Search results

Result 1 - 10 of total 19

Article: Phosphorylation and

Cantrelle, François-Xavier / Loyens, Anne / Trivelli, Xavier / Reimann, Oliver / Despres, Clément / Gandhi, Neha S / Hackenberger, Christian P R / Landrieu, Isabelle / Smet-Nocca, Caroline

Frontiers in molecular neuroscience

2021 Volume 14, Page(s) 661368

Abstract: Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains. In recent years, other ... ...

Abstract	Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains. In recent years, other posttranslational modifications (PTMs) have been highlighted in the regulation of Tau (dys)functions. Among these PTMs, the
Language	English
Publishing date	2021-06-17
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2452967-9
ISSN	1662-5099
ISSN	1662-5099
DOI	10.3389/fnmol.2021.661368
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 ; Online: Semi-synthesis of a tag-free O-GlcNAcylated tau protein by sequential chemoselective ligation.

Schwagerus, Sergej / Reimann, Oliver / Despres, Clement / Smet-Nocca, Caroline / Hackenberger, Christian P R

Journal of peptide science : an official publication of the European Peptide Society

2016 Volume 22, Issue 5, Page(s) 327–333

Abstract: In this paper, the first semi-synthesis of the Alzheimer-relevant tau protein carrying an O-GlcNAcylation is demonstrated by using sequential chemoselective ligation. The 52-amino acid C-terminus of tau was obtained by native chemical ligation between ... ...

Abstract	In this paper, the first semi-synthesis of the Alzheimer-relevant tau protein carrying an O-GlcNAcylation is demonstrated by using sequential chemoselective ligation. The 52-amino acid C-terminus of tau was obtained by native chemical ligation between two synthetic peptide fragments, one carrying the O-GlcNAc moiety on Ser400, which has recently been demonstrated to inhibit tau phosphorylation and to hinder tau oligomerization, and the other equipped with a photocleavable biotin handle. After desulfurization to deliver a native alanine at the ligation junction, the N-terminal cysteine was unmasked, and the peptide was further used for expressed protein ligation to generate the full-length tau protein, which was purified by a photocleavable biotin tag. We thus provide a synthetic route to obtain a homogenous tag-free O-GlcNAcylated tau protein that can further help to elucidate the significance of posttranslational modification on the tau protein and pave the way for evaluating possible drug targets in Alzheimer's disease. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.
MeSH term(s)	Acetylglucosamine/chemistry ; Alzheimer Disease/metabolism ; Chemistry Techniques, Synthetic ; Humans ; Molecular Structure ; Peptides/chemistry ; Protein Processing, Post-Translational ; Serine/chemistry ; tau Proteins/chemical synthesis ; tau Proteins/chemistry
Chemical Substances	Peptides ; tau Proteins ; Serine (452VLY9402) ; Acetylglucosamine (V956696549)
Language	English
Publishing date	2016-05
Publishing country	England
Document type	Journal Article
ZDB-ID	1234416-3
ISSN	1099-1387 ; 1075-2617
ISSN (online)	1099-1387
ISSN	1075-2617
DOI	10.1002/psc.2870
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 6200: 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: The Study of Posttranslational Modifications of Tau Protein by Nuclear Magnetic Resonance Spectroscopy: Phosphorylation of Tau Protein by ERK2 Recombinant Kinase and Rat Brain Extract, and Acetylation by Recombinant Creb-Binding Protein.

Qi, Haoling / Despres, Clément / Prabakaran, Sudhakaran / Cantrelle, François-Xavier / Chambraud, Béatrice / Gunawardena, Jeremy / Lippens, Guy / Smet-Nocca, Caroline / Landrieu, Isabelle

Methods in molecular biology (Clifton, N.J.)

2017 Volume 1523, Page(s) 179–213

Abstract: Nuclear magnetic resonance (NMR) spectroscopy can be used as an analytical tool to investigate posttranslational modifications of protein. NMR is a valuable tool to map the interaction regions of protein partners. Here, we present protocols that have ... ...

Abstract	Nuclear magnetic resonance (NMR) spectroscopy can be used as an analytical tool to investigate posttranslational modifications of protein. NMR is a valuable tool to map the interaction regions of protein partners. Here, we present protocols that have been developed in the course of our studies of the neuronal Tau protein. Tau is found aggregated in the neurons of Alzheimer's disease patients. Development of the disease is accompanied by increased, abnormal phosphorylation and acetylation of Tau. We have used NMR to investigate how these posttranslational modifications of Tau affect the interactions with its partners. We present here detailed protocols of in vitro phosphorylation of Tau by recombinant kinase, ERK2, or kinase activity of rat brain extracts, and acetylation by recombinant Creb-binding protein (CBP) acetyltransferase. The analytical characterization of the modified Tau by NMR spectroscopy is additionally described.
Language	English
Publishing date	2017
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-6598-4_11
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

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 ▾
- Full text online
- Order with fees

Article: Dendrogenin A synergizes with Cytarabine to Kill Acute Myeloid Leukemia Cells In Vitro and In Vivo.

Serhan, Nizar / Mouchel, Pierre-Luc / Medina, Philippe de / Segala, Gregory / Mougel, Aurélie / Saland, Estelle / Rives, Arnaud / Lamaziere, Antonin / Despres, Gaëtan / Sarry, Jean-Emmanuel / Larrue, Clément / Vergez, François / Largeaud, Laetitia / Record, Michel / Récher, Christian / Silvente-Poirot, Sandrine / Poirot, Marc

Cancers

2020 Volume 12, Issue 7

Abstract: Dendrogenin A (DDA) is a mammalian cholesterol metabolite that displays potent antitumor properties on acute myeloid leukemia (AML). DDA triggers lethal autophagy in cancer cells through a biased activation of the oxysterol receptor LXRβ, and the ... ...

Abstract	Dendrogenin A (DDA) is a mammalian cholesterol metabolite that displays potent antitumor properties on acute myeloid leukemia (AML). DDA triggers lethal autophagy in cancer cells through a biased activation of the oxysterol receptor LXRβ, and the inhibition of a sterol isomerase. We hypothesize that DDA could potentiate the activity of an anticancer drug acting through a different molecular mechanism, and conducted in vitro and in vivo combination tests on AML cell lines and patient primary tumors. We report here results from tests combining DDA with antimetabolite cytarabine (Ara-C), one of the main drugs used for AML treatment worldwide. We demonstrated that DDA potentiated and sensitized AML cells, including primary patient samples, to Ara-C in vitro and in vivo. Mechanistic studies revealed that this sensitization was LXRβ-dependent and was due to the activation of lethal autophagy. This study demonstrates a positive in vitro and in vivo interaction between DDA and Ara-C, and supports the clinical evaluation of DDA in combination with Ara-C for the treatment of AML.
Language	English
Publishing date	2020-06-29
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2527080-1
ISSN	2072-6694
ISSN	2072-6694
DOI	10.3390/cancers12071725
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins.

Danis, Clément / Despres, Clément / Bessa, Luiza M / Malki, Idir / Merzougui, Hamida / Huvent, Isabelle / Qi, Haoling / Lippens, Guy / Cantrelle, François-Xavier / Schneider, Robert / Hanoulle, Xavier / Smet-Nocca, Caroline / Landrieu, Isabelle

Journal of visualized experiments : JoVE

2016 , Issue 118

Abstract: Aggregates of the neuronal Tau protein are found inside neurons of Alzheimer's disease patients. Development of the disease is accompanied by increased, abnormal phosphorylation of Tau. In the course of the molecular investigation of Tau functions and ... ...

Abstract	Aggregates of the neuronal Tau protein are found inside neurons of Alzheimer's disease patients. Development of the disease is accompanied by increased, abnormal phosphorylation of Tau. In the course of the molecular investigation of Tau functions and dysfunctions in the disease, nuclear magnetic resonance (NMR) spectroscopy is used to identify the multiple phosphorylations of Tau. We present here detailed protocols of recombinant production of Tau in bacteria, with isotopic enrichment for NMR studies. Purification steps that take advantage of Tau's heat stability and high isoelectric point are described. The protocol for in vitro phosphorylation of Tau by recombinant activated ERK2 allows for generating multiple phosphorylations. The protein sample is ready for data acquisition at the issue of these steps. The parameter setup to start recording on the spectrometer is considered next. Finally, the strategy to identify phosphorylation sites of modified Tau, based on NMR data, is explained. The benefit of this methodology compared to other techniques used to identify phosphorylation sites, such as immuno-detection or mass spectrometry (MS), is discussed.
MeSH term(s)	Alzheimer Disease ; Humans ; Intrinsically Disordered Proteins/chemistry ; Magnetic Resonance Spectroscopy ; Phosphorylation ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/chemistry ; tau Proteins/chemistry
Chemical Substances	Intrinsically Disordered Proteins ; Recombinant Proteins ; tau Proteins
Language	English
Publishing date	2016-12-27
Publishing country	United States
Document type	Journal Article ; Video-Audio Media
ISSN	1940-087X
ISSN (online)	1940-087X
DOI	10.3791/55001
Database	MEDical Literature Analysis and Retrieval System OnLINE

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.

Article ; Online: NMR Meets Tau: Insights into Its Function and Pathology.

Lippens, Guy / Landrieu, Isabelle / Smet, Caroline / Huvent, Isabelle / Gandhi, Neha S / Gigant, Benoît / Despres, Clément / Qi, Haoling / Lopez, Juan

Biomolecules

2016 Volume 6, Issue 2

Abstract: In this review, we focus on what we have learned from Nuclear Magnetic Resonance (NMR) studies on the neuronal microtubule-associated protein Tau. We consider both the mechanistic details of Tau: the tubulin relationship and its aggregation process. ... ...

Abstract	In this review, we focus on what we have learned from Nuclear Magnetic Resonance (NMR) studies on the neuronal microtubule-associated protein Tau. We consider both the mechanistic details of Tau: the tubulin relationship and its aggregation process. Phosphorylation of Tau is intimately linked to both aspects. NMR spectroscopy has depicted accurate phosphorylation patterns by different kinases, and its non-destructive character has allowed functional assays with the same samples. Finally, we will discuss other post-translational modifications of Tau and its interaction with other cellular factors in relationship to its (dys)function.
MeSH term(s)	Intrinsically Disordered Proteins/chemistry ; Intrinsically Disordered Proteins/metabolism ; Nuclear Magnetic Resonance, Biomolecular ; Protein Processing, Post-Translational ; Tubulin/chemistry ; Tubulin/metabolism ; tau Proteins/chemistry ; tau Proteins/metabolism
Chemical Substances	Intrinsically Disordered Proteins ; Tubulin ; tau Proteins
Language	English
Publishing date	2016-06-07
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom6020028
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Full text

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: NMR Meets Tau

Guy Lippens / Isabelle Landrieu / Caroline Smet / Isabelle Huvent / Neha S. Gandhi / Benoît Gigant / Clément Despres / Haoling Qi / Juan Lopez

Biomolecules, Vol 6, Iss 2, p

Insights into Its Function and Pathology

2016 Volume 28

Abstract	In this review, we focus on what we have learned from Nuclear Magnetic Resonance (NMR) studies on the neuronal microtubule-associated protein Tau. We consider both the mechanistic details of Tau: the tubulin relationship and its aggregation process. Phosphorylation of Tau is intimately linked to both aspects. NMR spectroscopy has depicted accurate phosphorylation patterns by different kinases, and its non-destructive character has allowed functional assays with the same samples. Finally, we will discuss other post-translational modifications of Tau and its interaction with other cellular factors in relationship to its (dys)function.
Keywords	Tau ; NMR spectroscopy ; intrinsically disordered protein ; tubulin ; aggregation ; phosphorylation ; protein/protein interactions ; Biology (General) ; QH301-705.5 ; Science ; Q
Language	English
Publishing date	2016-06-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

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.

Article ; Online: The relationship between adiposopathy and glucose-insulin homeostasis is not affected by moderate-intensity aerobic training in healthy women with obesity.

Clément, Andrée-Anne / Riesco, Eléonor / Tessier, Sébastien / Lacaille, Michel / Pérusse, Francine / Coté, Mélanie / Després, Jean-Pierre / Weisnagel, John / Doré, Jean / Joanisse, Denis R / Mauriège, Pascale

Journal of physiology and biochemistry

2018 Volume 74, Issue 4, Page(s) 591–601

Abstract: The contribution of adiposopathy to glucose-insulin homeostasis remains unclear. This longitudinal study examined the potential relationship between the adiponectin/leptin ratio (A/L, a marker of adiposopathy) and insulin resistance (IR: homeostasis ... ...

Abstract	The contribution of adiposopathy to glucose-insulin homeostasis remains unclear. This longitudinal study examined the potential relationship between the adiponectin/leptin ratio (A/L, a marker of adiposopathy) and insulin resistance (IR: homeostasis model assessment (HOMA)), insulin sensitivity (IS: Matsuda), and insulin response to an oral glucose tolerance test before and after a 16-week walking program, in 29 physically inactive pre- and postmenopausal women with obesity (BMI, 29-35 kg/m
MeSH term(s)	Adiponectin/blood ; Adiposity ; Biomarkers/blood ; Body Mass Index ; Cardiorespiratory Fitness ; Female ; Glucose Tolerance Test ; Humans ; Insulin Resistance ; Leptin/blood ; Longitudinal Studies ; Middle Aged ; Obesity, Metabolically Benign/blood ; Obesity, Metabolically Benign/immunology ; Obesity, Metabolically Benign/metabolism ; Obesity, Metabolically Benign/therapy ; Oxygen Consumption ; Physical Conditioning, Human ; Postmenopause ; Premenopause ; Quebec ; Urban Health ; Walking
Chemical Substances	ADIPOQ protein, human ; Adiponectin ; Biomarkers ; LEP protein, human ; Leptin
Language	English
Publishing date	2018-04-26
Publishing country	Spain
Document type	Comparative Study ; Journal Article
ZDB-ID	1325104-1
ISSN	1877-8755 ; 0034-9402 ; 1138-7548
ISSN (online)	1877-8755
ISSN	0034-9402 ; 1138-7548
DOI	10.1007/s13105-018-0630-4
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.B 198: 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: Native Top-Down Mass Spectrometry and Ion Mobility Spectrometry of the Interaction of Tau Protein with a Molecular Tweezer Assembly Modulator.

Nshanian, Michael / Lantz, Carter / Wongkongkathep, Piriya / Schrader, Thomas / Klärner, Frank-Gerrit / Blümke, Anika / Despres, Clément / Ehrmann, Michael / Smet-Nocca, Caroline / Bitan, Gal / Loo, Joseph A

Journal of the American Society for Mass Spectrometry

2018 Volume 30, Issue 1, Page(s) 16–23

Abstract: Native top-down mass spectrometry (MS) and ion mobility spectrometry (IMS) were applied to characterize the interaction of a molecular tweezer assembly modulator, CLR01, with tau, a protein believed to be involved in a number of neurodegenerative ... ...

Abstract	Native top-down mass spectrometry (MS) and ion mobility spectrometry (IMS) were applied to characterize the interaction of a molecular tweezer assembly modulator, CLR01, with tau, a protein believed to be involved in a number of neurodegenerative disorders, including Alzheimer's disease. The tweezer CLR01 has been shown to inhibit aggregation of amyloidogenic polypeptides without toxic side effects. ESI-MS spectra for different forms of tau protein (full-length, fragments, phosphorylated, etc.) in the presence of CLR01 indicate a primary binding stoichiometry of 1:1. The relatively high charging of the protein measured from non-denaturing solutions is typical of intrinsically disordered proteins, such as tau. Top-down mass spectrometry using electron capture dissociation (ECD) is a tool used to determine not only the sites of post-translational modifications but also the binding site(s) of non-covalent interacting ligands to biomolecules. The intact protein and the protein-modulator complex were subjected to ECD-MS to obtain sequence information, map phosphorylation sites, and pinpoint the sites of inhibitor binding. The ESI-MS study of intact tau proteins indicates that top-down MS is amenable to the study of various tau isoforms and their post-translational modifications (PTMs). The ECD-MS data point to a CLR01 binding site in the microtubule-binding region of tau, spanning residues K294-K331, which includes a six-residue nucleating segment PHF6 (VQIVYK) implicated in aggregation. Furthermore, ion mobility experiments on the tau fragment in the presence of CLR01 and phosphorylated tau reveal a shift towards a more compact structure. The mass spectrometry study suggests a picture for the molecular mechanism of the modulation of protein-protein interactions in tau by CLR01. Graphical Abstract ᅟ.
MeSH term(s)	Binding Sites ; Bridged-Ring Compounds/chemistry ; Bridged-Ring Compounds/metabolism ; Hydrogen-Ion Concentration ; Ion Mobility Spectrometry/methods ; Organophosphates/chemistry ; Organophosphates/metabolism ; Phosphorylation ; Spectrometry, Mass, Electrospray Ionization/methods ; tau Proteins/chemistry ; tau Proteins/metabolism
Chemical Substances	Bridged-Ring Compounds ; CLR01 compound ; Organophosphates ; tau Proteins
Language	English
Publishing date	2018-07-30
Publishing country	United States
Document type	Journal Article
ZDB-ID	1073671-2
ISSN	1879-1123 ; 1044-0305
ISSN (online)	1879-1123
ISSN	1044-0305
DOI	10.1007/s13361-018-2027-6
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4618: 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 241: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Major Differences between the Self-Assembly and Seeding Behavior of Heparin-Induced and in Vitro Phosphorylated Tau and Their Modulation by Potential Inhibitors.

Despres, Clément / Di, Jing / Cantrelle, François-Xavier / Li, Zizheng / Huvent, Isabelle / Chambraud, Béatrice / Zhao, Jing / Chen, Jianle / Chen, Shiguo / Lippens, Guy / Zhang, Fuming / Linhardt, Robert / Wang, Chunyu / Klärner, Frank-Gerrit / Schrader, Thomas / Landrieu, Isabelle / Bitan, Gal / Smet-Nocca, Caroline

ACS chemical biology

2019 Volume 14, Issue 6, Page(s) 1363–1379

Abstract: ... to produce aggregation-competent forms recently have been introduced ( Despres et al. ( 2017 ) Proc. Natl ...

Abstract	Self-assembly of the microtubule-associated protein tau into neurotoxic oligomers, fibrils, and paired helical filaments, and cell-to-cell spreading of these pathological tau species are critical processes underlying the pathogenesis of Alzheimer's disease and other tauopathies. Modulating the self-assembly process and inhibiting formation and spreading of such toxic species are promising strategies for therapy development. A challenge in investigating tau self-assembly in vitro is that, unlike most amyloidogenic proteins, tau does not aggregate in the absence of posttranslational modifications (PTM), aggregation inducers, or preformed seeds. The most common induction method is addition of polyanions, such as heparin; yet, this artificial system may not represent adequately tau self-assembly in vivo, which is driven by aberrant phosphorylation and other PTMs, potentially leading to in vitro data that do not reflect the behavior of tau and its interaction with modulators in vivo. To tackle these challenges, methods for in vitro phosphorylation of tau to produce aggregation-competent forms recently have been introduced ( Despres et al. ( 2017 ) Proc. Natl. Acad. Sci. U.S.A. , 114 , 9080 - 9085 ). However, the oligomerization, seeding, and interaction with assembly modulators of the different forms of tau have not been studied to date. To address these knowledge gaps, we compared here side-by-side the self-assembly and seeding activity of heparin-induced tau with two forms of in vitro phosphorylated tau and tested how the molecular tweezer CLR01, a negatively charged compound, affected these processes. Tau was phosphorylated by incubation either with activated extracellular signal-regulated kinase 2 or with a whole rat brain extract. Seeding activity was measured using a fluorescence-resonance energy transfer-based biosensor-cell method. We also used solution-state NMR to investigate the binding sites of CLR01 on tau and how they were impacted by phosphorylation. Our systematic structure-activity relationship study demonstrates that heparin-induced tau behaves differently from in vitro phosphorylated tau. The aggregation rates of the different forms are distinct as is the intracellular localization of the induced aggregates, which resemble brain-derived tau strains suggesting that heparin-induced tau and in vitro phosphorylated tau have different conformations, properties, and activities. CLR01 inhibits aggregation and seeding of both heparin-induced and in vitro phosphorylated tau dose-dependently, although heparin induction interferes with the interaction between CLR01 and tau.
MeSH term(s)	Alzheimer Disease/metabolism ; Animals ; Heparin/pharmacology ; Humans ; Phosphorylation ; Rats ; tau Proteins/antagonists & inhibitors ; tau Proteins/metabolism
Chemical Substances	tau Proteins ; Heparin (9005-49-6)
Language	English
Publishing date	2019-05-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.9b00325
Database	MEDical Literature Analysis and Retrieval System OnLINE

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.

To top

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

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED