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Article ; Online: A Quantitative Method to Distinguish Cytosolic from Endosome-Trapped Cell-Penetrating Peptides.

Illien, Françoise / Bánóczi, Zoltán / Sagan, Sandrine

Chembiochem : a European journal of chemical biology

2024 , Page(s) e202400198

Abstract: Cell-penetrating peptides are known to penetrate cells through endocytosis and translocation. The two pathways are hardly distinguished in current cell assays. We developed a reliable, simple and robust method to distinguish and quantify independently ... ...

Abstract	Cell-penetrating peptides are known to penetrate cells through endocytosis and translocation. The two pathways are hardly distinguished in current cell assays. We developed a reliable, simple and robust method to distinguish and quantify independently the two routes. The assay requires (DABCYL) 4-(dimethylaminoazo)benzene-4-carboxylic acid- and (CF) carboxyfluorescein-labeled peptides. When the labeled peptide is intact, the fluorescence signal is weak thanks to the dark quenching property of DABCYL. A 10-fold higher fluorescence signal is measured when the labeled peptide is degraded. By referring to a standard fluorescent curve according to the concentration of the hydrolyzed peptide, we have access to the internalized peptide quantity. Therefore, cell lysis after internalization permits to determine the total quantity of intracellular peptide. The molecular state of the internalized peptide (intact or degraded), depends on its location in cells (cytosol vs endo-lysosomes), and can be blocked by boiling cells. This boiling step results indeed in denaturation and inhibition of the cellular enzymes. The advantage of this method is the possibility to quantify translocation at 37 °C and to compare it to the 4 °C condition, where all endocytosis processes are inhibited. We found that ranking of the translocation efficacy is DABCYL-R
Language	English
Publishing date	2024-04-08
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2020469-3
ISSN	1439-7633 ; 1439-4227
ISSN (online)	1439-7633
ISSN	1439-4227
DOI	10.1002/cbic.202400198
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Article ; Online: Tryptophan, more than just an interfacial amino acid in the membrane activity of cationic cell-penetrating and antimicrobial peptides.

Khemaissa, Sonia / Walrant, Astrid / Sagan, Sandrine

Quarterly reviews of biophysics

2022 Volume 55, Page(s) e10

Abstract: Trp is unique among the amino acids since it is involved in many different types of noncovalent interactions such as electrostatic and hydrophobic ones, but also in π-π, π-cation, π-anion and π-ion pair interactions. In membranotropic peptides and ... ...

Abstract	Trp is unique among the amino acids since it is involved in many different types of noncovalent interactions such as electrostatic and hydrophobic ones, but also in π-π, π-cation, π-anion and π-ion pair interactions. In membranotropic peptides and proteins, Trp locates preferentially at the water-membrane interface. In antimicrobial or cell-penetrating peptides (AMPs and CPPs respectively), Trp is well-known for its strong role in the capacity of these peptides to interact and affect the membrane organisation of both bacteria and animal cells at the level of the lipid bilayer. This essential amino acid can however be involved in other types of interactions, not only with lipids, but also with other membrane partners, that are crucial to understand the functional roles of membranotropic peptides. This review is focused on this latter less known role of Trp and describes in details, both in qualitative and quantitative ways: (i) the physico-chemical properties of Trp; (ii) its effect in CPP internalisation; (iii) its importance in AMP activity; (iv) its role in the interaction of AMPs with glycoconjugates or lipids in bacteria membranes and the consequences on the activity of the peptides; (v) its role in the interaction of CPPs with negatively charged polysaccharides or lipids of animal membranes and the consequences on the activity of the peptides. We intend to bring highlights of the physico-chemical properties of Trp and describe its extensive possibilities of interactions, not only at the well-known level of the lipid bilayer, but with other less considered cell membrane components, such as carbohydrates and the extracellular matrix. The focus on these interactions will allow the reader to reevaluate reported studies. Altogether, our review gathers dedicated studies to show how unique are Trp properties, which should be taken into account to design future membranotropic peptides with expected antimicrobial or cell-penetrating activity.
MeSH term(s)	Adenosine Monophosphate ; Amino Acids ; Animals ; Anti-Bacterial Agents/chemistry ; Anti-Infective Agents/chemistry ; Antimicrobial Cationic Peptides/metabolism ; Antimicrobial Peptides ; Carbohydrates ; Cations ; Cell-Penetrating Peptides ; Lipid Bilayers ; Tryptophan/chemistry ; Tryptophan/metabolism ; Water
Chemical Substances	Amino Acids ; Anti-Bacterial Agents ; Anti-Infective Agents ; Antimicrobial Cationic Peptides ; Antimicrobial Peptides ; Carbohydrates ; Cations ; Cell-Penetrating Peptides ; Lipid Bilayers ; Water (059QF0KO0R) ; Adenosine Monophosphate (415SHH325A) ; Tryptophan (8DUH1N11BX)
Language	English
Publishing date	2022-08-18
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	209912-3
ISSN	1469-8994 ; 0033-5835
ISSN (online)	1469-8994
ISSN	0033-5835
DOI	10.1017/S0033583522000105
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Article ; Online: Challenges and Methods for the Study of CPP Translocation Mechanisms.

Walrant, Astrid / Illien, Françoise / Sagan, Sandrine / Rodriguez, Nicolas

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

2021 Volume 2383, Page(s) 143–152

Abstract: Fluorescence-based methods are widely used to detect crossing of peptides across model or biological membranes. For membrane-active peptides, i.e., peptides that have strong membrane tropism, fluorescence experiments must be accompanied by relevant ... ...

Abstract	Fluorescence-based methods are widely used to detect crossing of peptides across model or biological membranes. For membrane-active peptides, i.e., peptides that have strong membrane tropism, fluorescence experiments must be accompanied by relevant controls, otherwise they can lead to inconsistent interpretation and underestimation of their limitations. Here we describe how to prepare samples to study fluorescent peptide crossing droplet interface bilayer (model membrane) or cell membrane (biological membrane) and the pitfalls that can affect observational qualitative and quantitative data.
MeSH term(s)	Cell Membrane/metabolism ; Cell Membrane Permeability ; Cell-Penetrating Peptides/metabolism ; Fluorescence ; Lipid Bilayers/metabolism
Chemical Substances	Cell-Penetrating Peptides ; Lipid Bilayers
Language	English
Publishing date	2021-11-12
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-1752-6_9
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Article ; Online: Binding and crossing: Methods for the characterization of membrane-active peptides interactions with membranes at the molecular level.

Sachon, Emmanuelle / Walrant, Astrid / Sagan, Sandrine / Cribier, Sophie / Rodriguez, Nicolas

Archives of biochemistry and biophysics

2021 Volume 699, Page(s) 108751

Abstract: Antimicrobial and cell-penetrating peptides have been the object of extensive studies for more than 60 years. Initially these two families were studied separately, and more recently parallels have been drawn. These studies have given rise to numerous ... ...

Abstract	Antimicrobial and cell-penetrating peptides have been the object of extensive studies for more than 60 years. Initially these two families were studied separately, and more recently parallels have been drawn. These studies have given rise to numerous methodological developments both in terms of observation techniques and membrane models. This review presents some of the most recent original and innovative developments in this field, namely droplet interface bilayers (DIBs), new fluorescence approaches, force measurements, and photolabelling.
MeSH term(s)	Amino Acid Sequence ; Antimicrobial Cationic Peptides/chemistry ; Antimicrobial Cationic Peptides/metabolism ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Cell-Penetrating Peptides/chemistry ; Cell-Penetrating Peptides/metabolism ; Fluorescent Dyes/chemistry ; Lipid Bilayers/chemistry ; Lipid Bilayers/metabolism ; Microscopy, Fluorescence/methods ; Photoaffinity Labels/chemistry ; Spectrometry, Fluorescence/methods
Chemical Substances	Antimicrobial Cationic Peptides ; Cell-Penetrating Peptides ; Fluorescent Dyes ; Lipid Bilayers ; Photoaffinity Labels
Language	English
Publishing date	2021-01-07
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2021.108751
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Article ; Online: Corrigendum to "Binding and crossing: Methods for the characterization of membrane-active peptides interactions with membranes at the molecular level" [Arch. Biochem. Biophys. 699 (2021) 108751].

Sachon, Emmanuelle / Walrant, Astrid / Sagan, Sandrine / Cribier, Sophie / Rodriguez, Nicolas

Archives of biochemistry and biophysics

2021 Volume 707, Page(s) 108827

Language	English
Publishing date	2021-03-09
Publishing country	United States
Document type	Published Erratum
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2021.108827
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Article: Binding and crossing: Methods for the characterization of membrane-active peptides interactions with membranes at the molecular level

Sachon, Emmanuelle / Walrant, Astrid / Sagan, Sandrine / Cribier, Sophie / Rodriguez, Nicolas

Archives of biochemistry and biophysics. 2021 Mar. 15, v. 699

2021

Abstract	Antimicrobial and cell-penetrating peptides have been the object of extensive studies for more than 60 years. Initially these two families were studied separately, and more recently parallels have been drawn. These studies have given rise to numerous methodological developments both in terms of observation techniques and membrane models. This review presents some of the most recent original and innovative developments in this field, namely droplet interface bilayers (DIBs), new fluorescence approaches, force measurements, and photolabelling.
Keywords	biophysics ; droplets ; fluorescence ; peptides
Language	English
Dates of publication	2021-0315
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2021.108751
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Article: Conjugation of Oligo-His Peptides to Magnetic γ-Fe₂O₃@SiO₂ Core–Shell Nanoparticles Promotes Their Access to the Cytosol

Le Jeune, Mathilde / Secret, Emilie / Trichet, Michaël / Michel, Aude / Ravault, Delphine / Illien, Françoise / Siaugue, Jean-Michel / Sagan, Sandrine / Burlina, Fabienne / Ménager, Christine

ACS applied materials & interfaces. 2022 Mar. 23, v. 14, no. 13

2022

Abstract: The endosomal entrapment of functional nanoparticles is a severe limitation to their use for biomedical applications. In the case of magnetic nanoparticles (MNPs), this entrapment leads to poor heating efficiency for magnetic hyperthermia and suppresses ... ...

Abstract	The endosomal entrapment of functional nanoparticles is a severe limitation to their use for biomedical applications. In the case of magnetic nanoparticles (MNPs), this entrapment leads to poor heating efficiency for magnetic hyperthermia and suppresses the possibility to manipulate them in the cytosol. Current strategies to limit their entrapment include functionalization with cell-penetrating peptides to promote translocation directly across the cell membrane or facilitate endosomal escape. However, these strategies suffer from the potential release of free peptides in the cell, and to the best of our knowledge, there is currently a lack of effective methods for the cytosolic delivery of MNPs after incubation with cells. Herein, we report the conjugation of fluorescently labeled cationic peptides to γ-Fe₂O₃@SiO₂ core–shell nanoparticles by click chemistry to improve MNP access to the cytosol. We compare the effect of Arg₉ and His₄ peptides. On the one hand, Arg₉ is a classical cell-penetrating peptide able to enter cells by direct translocation, and on the other hand, it has been demonstrated that sequences rich in histidine residues can promote endosomal escape, possibly by the proton sponge effect. The methodology developed here allows a high colocalization of the peptides and core–shell nanoparticles in cells and confirms that grafting peptides rich in histidine residues onto nanoparticles promotes NPs’ access to the cytosol. Endosomal escape was confirmed by a calcein leakage assay and by ultrastructural analysis in transmission electron microscopy. No toxicity was observed for the peptide–nanoparticles conjugates. We also show that our conjugation strategy is compatible with the addition of multiple substrates and can thus be used for the delivery of cytoplasm-targeted therapeutics.
Keywords	cell membranes ; chemistry ; cytosol ; fever ; histidine ; magnetism ; peptides ; therapeutics ; toxicity ; transmission electron microscopy
Language	English
Dates of publication	2022-0323
Size	p. 15021-15034.
Publishing place	American Chemical Society
Document type	Article
ISSN	1944-8252
DOI	10.1021/acsami.2c01346
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Article ; Online: Membrane Crossing and Membranotropic Activity of Cell-Penetrating Peptides: Dangerous Liaisons?

Walrant, Astrid / Cardon, Sébastien / Burlina, Fabienne / Sagan, Sandrine

Accounts of chemical research

2017 Volume 50, Issue 12, Page(s) 2968–2975

Abstract: Living organisms have to maintain a stable balance in molecules and ions in the changing environment in which they are living, a process known as homeostasis. At the level of cells, the plasma membrane has a major role in homeostasis, since this ... ...

Abstract	Living organisms have to maintain a stable balance in molecules and ions in the changing environment in which they are living, a process known as homeostasis. At the level of cells, the plasma membrane has a major role in homeostasis, since this hydrophobic film prevents passive diffusion of large and hydrophilic molecules between the extracellular and intracellular milieu. Living organisms have evolved with highly sophisticated transport systems to control exchanges across this barrier: import of nutrients and fuel essential for their survival; recognition of chemical or physical messengers allowing information interchanges with surrounding cells. Besides specialized proteins, endocytosis mechanisms at the level of the lipid bilayer can transport molecules from the outside across the cell membrane, in an energy-dependent manner. The cell membrane is highly heterogeneous in its molecular composition (tens of different lipids, proteins, polysaccharides, and combinations of these) and dynamic with bending, deformation, and elastic properties that depend on the local composition of membrane domains. Many viruses, microorganisms, and toxins exploit the plasma membrane to enter into cells. Chemists develop strategies to target the plasma membrane with molecules capable of circumventing this hydrophobic barrier, in particular to transport and deliver nonpermeable drugs in cells for biotechnological or pharmaceutical purposes. Drug delivery systems are numerous and include lipid-, sugar-, protein-, and peptide-based delivery systems, since these biomolecules generally have good biocompatibility, biodegradability, environmental sustainability, cost effectiveness, and availability. Among those, cell-penetrating peptides (CPPs), reported for the first time in the early 1990s, are attracting major interest not only as potential drug delivery systems but also at the level of fundamental research. It was indeed demonstrated very early that these peptides, which generally correspond to highly cationic sequences, can still cross the cell membrane at 4 °C, a temperature at which all active transport and endocytosis pathways are totally inhibited. Therefore, how these charged hydrophilic peptides cross the hydrophobic membrane barrier is of utmost interest as a pure basic and physicochemical question. In this Account, we focus on cationic cell-penetrating peptides (CPPs) and the way they cross cell membranes. We summarize the history of this field that emerged around 20 years ago. CPPs were indeed first identified as protein-transduction domains from the human immunodeficiency virus (HIV) TAT protein and the Antennapedia homeoprotein, a transcription factor from Drosophila. We highlight our contribution to the elucidation of CPP internalization pathways, in particular translocation, which implies perturbation and reorganization of the lipid bilayer, and endocytosis depending on sulfated glycosaminoglycans. We show a particular role of Trp (indole side chain) and Arg (guanidinium side chain), which are essential amino acids for CPP internalization. Interactions with the cell-surface are not only Coulombic; H-bonds and hydrophobic interactions contribute also significantly to CPP entry. The capacity of CPPs to cross cell membrane is not related to their strength of membrane binding. Finally, we present optimized methods based on mass spectrometry and fluorescence spectroscopy that allow unequivocal quantification of CPPs inside cells or bound to the outer leaflet of the membrane, and discuss some limitations of the technique of flow cytometry that we have recently highlighted.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Cell-Penetrating Peptides/chemistry ; Cell-Penetrating Peptides/metabolism ; Endocytosis ; Fluorometry ; Glycosaminoglycans/chemistry ; Kinetics ; Lipid Bilayers/chemistry ; Lipid Bilayers/metabolism ; Oligopeptides/chemistry ; Oligopeptides/metabolism ; Protein Transport ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Thermodynamics
Chemical Substances	Cell-Penetrating Peptides ; Glycosaminoglycans ; Lipid Bilayers ; Oligopeptides
Language	English
Publishing date	2017-11-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	1483291-4
ISSN	1520-4898 ; 0001-4842
ISSN (online)	1520-4898
ISSN	0001-4842
DOI	10.1021/acs.accounts.7b00455
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Article ; Online: A cationic motif upstream Engrailed2 homeodomain controls cell internalization through selective interaction with heparan sulfates.

Cardon, Sébastien / Hervis, Yadira P / Bolbach, Gérard / Lopin-Bon, Chrystel / Jacquinet, Jean-Claude / Illien, Françoise / Walrant, Astrid / Ravault, Delphine / He, Bingwei / Molina, Laura / Burlina, Fabienne / Lequin, Olivier / Joliot, Alain / Carlier, Ludovic / Sagan, Sandrine

Nature communications

2023 Volume 14, Issue 1, Page(s) 1998

Abstract: Engrailed2 (En2) is a transcription factor that transfers from cell to cell through unconventional pathways. The poorly understood internalization mechanism of this cationic protein is proposed to require an initial interaction with cell-surface ... ...

Abstract	Engrailed2 (En2) is a transcription factor that transfers from cell to cell through unconventional pathways. The poorly understood internalization mechanism of this cationic protein is proposed to require an initial interaction with cell-surface glycosaminoglycans (GAGs). To decipher the role of GAGs in En2 internalization, we have quantified the entry of its homeodomain region in model cells that differ in their content in cell-surface GAGs. The binding specificity to GAGs and the influence of this interaction on the structure and dynamics of En2 was also investigated at the amino acid level. Our results show that a high-affinity GAG-binding sequence (RKPKKKNPNKEDKRPR), upstream of the homeodomain, controls En2 internalization through selective interactions with highly-sulfated heparan sulfate GAGs. Our data underline the functional importance of the intrinsically disordered basic region upstream of En2 internalization domain, and demonstrate the critical role of GAGs as an entry gate, finely tuning homeoprotein capacity to internalize into cells.
MeSH term(s)	Heparitin Sulfate/metabolism ; Glycosaminoglycans/metabolism ; Transcription Factors ; Homeodomain Proteins/genetics ; Sulfates ; Chondroitin Sulfates/metabolism
Chemical Substances	Heparitin Sulfate (9050-30-0) ; Glycosaminoglycans ; Transcription Factors ; Homeodomain Proteins ; Sulfates ; Chondroitin Sulfates (9007-28-7)
Language	English
Publishing date	2023-04-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-37757-6
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Article ; Online: Cell-penetrating peptides: 20 years later, where do we stand?

Bechara, Chérine / Sagan, Sandrine

FEBS letters

2013 Volume 587, Issue 12, Page(s) 1693–1702

Abstract: Twenty years ago, the discovery of peptides able to cross cellular membranes launched a novel field in molecular delivery based on these non-invasive vectors, most commonly called cell-penetrating peptides (CPPs) or protein transduction domains (PTDs). ... ...

Abstract	Twenty years ago, the discovery of peptides able to cross cellular membranes launched a novel field in molecular delivery based on these non-invasive vectors, most commonly called cell-penetrating peptides (CPPs) or protein transduction domains (PTDs). These peptides were shown to efficiently transport various biologically active molecules inside living cells, and thus are considered promising devices for medical and biotechnological developments. Moreover, CPPs emerged as potential tools to study the prime mechanisms of cellular entry across the plasma membrane. This review is dedicated to CPP fundamentals, with an emphasis on the molecular requirements and mechanism of their entry into eukaryotic cells.
MeSH term(s)	Amino Acid Sequence ; Animals ; Anti-Infective Agents/chemistry ; Anti-Infective Agents/metabolism ; Cell-Penetrating Peptides/chemistry ; Cell-Penetrating Peptides/metabolism ; Endocytosis ; Humans ; Molecular Sequence Data ; Protein Transport
Chemical Substances	Anti-Infective Agents ; Cell-Penetrating Peptides
Language	English
Publishing date	2013-06-19
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/j.febslet.2013.04.031
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