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Article ; Online: A direct gateway into the extracellular space: Unconventional secretion of FGF2 through self-sustained plasma membrane pores.

Steringer, Julia P / Nickel, Walter

Seminars in cell & developmental biology

2018 Volume 83, Page(s) 3–7

Abstract: As illustrated by a diverse set of examples in this special issue, multiple mechanisms of protein secretion have been identified in eukaryotes that do not involve the endoplasmic reticulum (ER) and the Golgi apparatus. Here we focus on the type I pathway ...

Abstract	As illustrated by a diverse set of examples in this special issue, multiple mechanisms of protein secretion have been identified in eukaryotes that do not involve the endoplasmic reticulum (ER) and the Golgi apparatus. Here we focus on the type I pathway with Fibroblast Growth Factor 2 (FGF2) being the most prominent example. Unconventional secretion of FGF2 from cells is mediated by direct protein translocation across the plasma membrane. A unique feature of this process is the ability of FGF2 to form its own membrane translocation intermediate through oligomerization and membrane insertion. This process depends on the phosphoinositide PI(4,5)P
MeSH term(s)	Cell Membrane/metabolism ; Extracellular Space/metabolism ; Fibroblast Growth Factor 2/metabolism ; Humans
Chemical Substances	Fibroblast Growth Factor 2 (103107-01-3)
Language	English
Publishing date	2018-03-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1312473-0
ISSN	1096-3634 ; 1084-9521
ISSN (online)	1096-3634
ISSN	1084-9521
DOI	10.1016/j.semcdb.2018.02.010
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Article ; Online: The molecular mechanism underlying unconventional secretion of Fibroblast Growth Factor 2 from tumour cells.

Steringer, Julia P / Nickel, Walter

Biology of the cell

2017 Volume 109, Issue 11, Page(s) 375–380

Abstract: Fibroblast Growth Factor 2 (FGF2) is a potent cell survival factor involved in tumour-induced angiogenesis. FGF2 is secreted from cells through an unconventional secretory mechanism based upon direct translocation across the plasma membrane. The ... ...

Abstract	Fibroblast Growth Factor 2 (FGF2) is a potent cell survival factor involved in tumour-induced angiogenesis. FGF2 is secreted from cells through an unconventional secretory mechanism based upon direct translocation across the plasma membrane. The molecular mechanism underlying this process depends on a surprisingly small set of trans-acting factors that are physically associated with the plasma membrane. FGF2 membrane translocation is mediated by the ability of FGF2 to oligomerise and to insert into the plasma membrane in a PI(4,5)P
Language	English
Publishing date	2017-11
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	245745-3
ISSN	1768-322X ; 0399-0311 ; 0248-4900
ISSN (online)	1768-322X
ISSN	0399-0311 ; 0248-4900
DOI	10.1111/boc.201700036
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Article ; Online: Determining the Functional Oligomeric State of Membrane-Associated Protein Oligomers Forming Membrane Pores on Giant Lipid Vesicles.

Singh, Vandana / Macharová, Sabína / Riegerová, Petra / Steringer, Julia P / Müller, Hans-Michael / Lolicato, Fabio / Nickel, Walter / Hof, Martin / Šachl, Radek

Analytical chemistry

2023 Volume 95, Issue 23, Page(s) 8807–8815

Abstract: Several peripheral membrane proteins are known to form membrane pores through multimerization. In many cases, in biochemical reconstitution experiments, a complex distribution of oligomeric states has been observed that may, in part, be irrelevant to ... ...

Abstract	Several peripheral membrane proteins are known to form membrane pores through multimerization. In many cases, in biochemical reconstitution experiments, a complex distribution of oligomeric states has been observed that may, in part, be irrelevant to their physiological functions. This phenomenon makes it difficult to identify the functional oligomeric states of membrane lipid interacting proteins, for example, during the formation of transient membrane pores. Using fibroblast growth factor 2 (FGF2) as an example, we present a methodology applicable to giant lipid vesicles by which functional oligomers can be distinguished from nonspecifically aggregated proteins without functionality. Two distinct populations of fibroblast growth factor 2 were identified with (i) dimers to hexamers and (ii) a broad population of higher oligomeric states of membrane-associated FGF2 oligomers significantly distorting the original unfiltered histogram of all detectable oligomeric species of FGF2. The presented statistical approach is relevant for various techniques for characterizing membrane-dependent protein oligomerization.
MeSH term(s)	Cell Membrane/metabolism ; Membrane Proteins/metabolism ; Fibroblast Growth Factor 2/metabolism ; Membranes ; Lipids ; Protein Multimerization
Chemical Substances	Membrane Proteins ; Fibroblast Growth Factor 2 (103107-01-3) ; Lipids
Language	English
Publishing date	2023-05-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.2c05692
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Article ; Online: Determining the Functional Oligomeric State of Membrane-Associated Protein Oligomers Forming Membrane Pores on Giant Lipid Vesicles

Singh, Vandana / Macharová, Sabína / Riegerová, Petra / Steringer, Julia P. / Müller, Hans-Michael / Lolicato, Fabio / Nickel, Walter / Hof, M. / Šachl, Radek

Analytical Chemistry. 2023 May 06, v. 95, no. 23 p.8807-8815

2023

Abstract	Several peripheral membrane proteins are known to form membrane pores through multimerization. In many cases, in biochemical reconstitution experiments, a complex distribution of oligomeric states has been observed that may, in part, be irrelevant to their physiological functions. This phenomenon makes it difficult to identify the functional oligomeric states of membrane lipid interacting proteins, for example, during the formation of transient membrane pores. Using fibroblast growth factor 2 (FGF2) as an example, we present a methodology applicable to giant lipid vesicles by which functional oligomers can be distinguished from nonspecifically aggregated proteins without functionality. Two distinct populations of fibroblast growth factor 2 were identified with (i) dimers to hexamers and (ii) a broad population of higher oligomeric states of membrane-associated FGF2 oligomers significantly distorting the original unfiltered histogram of all detectable oligomeric species of FGF2. The presented statistical approach is relevant for various techniques for characterizing membrane-dependent protein oligomerization.
Keywords	analytical chemistry ; fibroblast growth factor 2 ; lipids ; membrane proteins ; oligomerization ; protein subunits ; statistical analysis
Language	English
Dates of publication	2023-0506
Size	p. 8807-8815.
Publishing place	American Chemical Society
Document type	Article ; Online
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.2c05692
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Article ; Online: Disulfide bridge-dependent dimerization triggers FGF2 membrane translocation into the extracellular space.

Lolicato, Fabio / Steringer, Julia P / Saleppico, Roberto / Beyer, Daniel / Fernandez-Sobaberas, Jaime / Unger, Sebastian / Klein, Steffen / Riegerová, Petra / Wegehingel, Sabine / Müller, Hans-Michael / Schmitt, Xiao J / Kaptan, Shreyas / Freund, Christian / Hof, Martin / Šachl, Radek / Chlanda, Petr / Vattulainen, Ilpo / Nickel, Walter

eLife

2024 Volume 12

Abstract: Fibroblast growth factor 2 (FGF2) exits cells by direct translocation across the plasma membrane, a type I pathway of unconventional protein secretion. This process is initiated by phosphatidylinositol-4,5-bisphosphate (PI(4,5) ... ...

Abstract	Fibroblast growth factor 2 (FGF2) exits cells by direct translocation across the plasma membrane, a type I pathway of unconventional protein secretion. This process is initiated by phosphatidylinositol-4,5-bisphosphate (PI(4,5)P
MeSH term(s)	Extracellular Space ; Dimerization ; Fibroblast Growth Factor 2 ; Sodium-Potassium-Exchanging ATPase ; Disulfides
Chemical Substances	Fibroblast Growth Factor 2 (103107-01-3) ; Sodium-Potassium-Exchanging ATPase (EC 7.2.2.13) ; Disulfides
Language	English
Publishing date	2024-01-22
Publishing country	England
Document type	Journal Article
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.88579
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Article ; Online: Unconventional secretion of fibroblast growth factor 2--a novel type of protein translocation across membranes?

Steringer, Julia P / Müller, Hans-Michael / Nickel, Walter

Journal of molecular biology

2015 Volume 427, Issue 6 Pt A, Page(s) 1202–1210

Abstract: N-terminal signal peptides are a hallmark of the vast majority of soluble secretory proteins that are transported along the endoplasmic reticulum/Golgi-dependent pathway. They are recognized by signal recognition particle, a process that initiates ... ...

Abstract	N-terminal signal peptides are a hallmark of the vast majority of soluble secretory proteins that are transported along the endoplasmic reticulum/Golgi-dependent pathway. They are recognized by signal recognition particle, a process that initiates membrane translocation into the lumen of the endoplasmic reticulum followed by vesicular transport to the cell surface and release into the extracellular space. Beyond this well-established mechanism of protein secretion from eukaryotic cells, a number of extracellular proteins with critical physiological functions in immune surveillance and tissue organization are known to be secreted in a manner independent of signal recognition particle. Such processes have collectively been termed "unconventional protein secretion" and, while known for more than two decades, their underlying mechanisms are only beginning to emerge. Different types of unconventional secretory mechanisms have been described with the best-characterized example being based on direct translocation of cytoplasmic proteins across plasma membranes. The aim of this review is to critically assess our current knowledge of this type of unconventional secretion focusing on fibroblast growth factor 2 (FGF2) as the most established example.
MeSH term(s)	Animals ; Cell Membrane/metabolism ; Fibroblast Growth Factor 2/metabolism ; Humans ; Phosphoinositide Phospholipase C/metabolism ; Protein Multimerization ; Protein Transport
Chemical Substances	Fibroblast Growth Factor 2 (103107-01-3) ; Phosphoinositide Phospholipase C (EC 3.1.4.11)
Language	English
Publishing date	2015-03-27
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2014.07.012
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Article ; Online: Functional Assay to Correlate Protein Oligomerization States with Membrane Pore Formation.

Šachl, Radek / Čujová, Sabína / Singh, Vandana / Riegerová, Petra / Kapusta, Peter / Müller, Hans-Michael / Steringer, Julia P / Hof, Martin / Nickel, Walter

Analytical chemistry

2020 Volume 92, Issue 22, Page(s) 14861–14866

Abstract: In-membrane oligomerization is decisive for the function (or dysfunction) of many proteins. Techniques were developed to characterize membrane-inserted oligomers and the hereby obtained oligomerization states were intuitively related to the function of ... ...

Abstract	In-membrane oligomerization is decisive for the function (or dysfunction) of many proteins. Techniques were developed to characterize membrane-inserted oligomers and the hereby obtained oligomerization states were intuitively related to the function of these proteins. However, in many cases, it is unclear whether the obtained oligomerization states are functionally relevant or are merely the consequence of nonspecific aggregation. Using fibroblast growth factor 2 (FGF2) as a model system, we addressed this methodological challenge. FGF2 oligomerizes in a PI(4,5)P
MeSH term(s)	Cell Membrane/chemistry ; Cell Membrane/metabolism ; Fibroblast Growth Factor 2/chemistry ; Fibroblast Growth Factor 2/metabolism ; Permeability ; Porosity ; Protein Multimerization ; Protein Structure, Quaternary ; Spectrometry, Fluorescence ; Unilamellar Liposomes/chemistry ; Unilamellar Liposomes/metabolism
Chemical Substances	Unilamellar Liposomes ; Fibroblast Growth Factor 2 (103107-01-3)
Language	English
Publishing date	2020-10-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.0c03276
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Article: Unconventional Secretion of Fibroblast Growth Factor 2âA Novel Type of Protein Translocation across Membranes?

Steringer, Julia P / Hans-Michael MÃ¼ller / Walter Nickel

Journal of Molecular Biology. 2015 Mar. 27, v. 427

2015

Abstract	N-terminal signal peptides are a hallmark of the vast majority of soluble secretory proteins that are transported along the endoplasmic reticulum/Golgi-dependent pathway. They are recognized by signal recognition particle, a process that initiates membrane translocation into the lumen of the endoplasmic reticulum followed by vesicular transport to the cell surface and release into the extracellular space. Beyond this well-established mechanism of protein secretion from eukaryotic cells, a number of extracellular proteins with critical physiological functions in immune surveillance and tissue organization are known to be secreted in a manner independent of signal recognition particle. Such processes have collectively been termed âunconventional protein secretionâ and, while known for more than two decades, their underlying mechanisms are only beginning to emerge. Different types of unconventional secretory mechanisms have been described with the best-characterized example being based on direct translocation of cytoplasmic proteins across plasma membranes. The aim of this review is to critically assess our current knowledge of this type of unconventional secretion focusing on fibroblast growth factor 2 (FGF2) as the most established example.
Keywords	endoplasmic reticulum ; eukaryotic cells ; extracellular space ; fibroblast growth factor 2 ; monitoring ; plasma membrane ; protein secretion ; protein transport ; proteins ; signal peptide
Language	English
Dates of publication	2015-0327
Size	p. 1202-1210.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2014.07.012
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Article ; Online: The Na,K-ATPase acts upstream of phosphoinositide PI(4,5)P

Legrand, Cyril / Saleppico, Roberto / Sticht, Jana / Lolicato, Fabio / Müller, Hans-Michael / Wegehingel, Sabine / Dimou, Eleni / Steringer, Julia P / Ewers, Helge / Vattulainen, Ilpo / Freund, Christian / Nickel, Walter

Communications biology

2020 Volume 3, Issue 1, Page(s) 141

Abstract: FGF2 is a tumor cell survival factor that is exported from cells by an ER/Golgi-independent secretory pathway. This unconventional mechanism of protein secretion is based on direct translocation of FGF2 across the plasma membrane. The Na,K-ATPase has ... ...

Abstract	FGF2 is a tumor cell survival factor that is exported from cells by an ER/Golgi-independent secretory pathway. This unconventional mechanism of protein secretion is based on direct translocation of FGF2 across the plasma membrane. The Na,K-ATPase has previously been shown to play a role in this process, however, the underlying mechanism has remained elusive. Here, we define structural elements that are critical for a direct physical interaction between FGF2 and the α1 subunit of the Na,K-ATPase. In intact cells, corresponding FGF2 mutant forms were impaired regarding both recruitment at the inner plasma membrane leaflet and secretion. Ouabain, a drug that inhibits both the Na,K-ATPase and FGF2 secretion, was found to impair the interaction of FGF2 with the Na,K-ATPase in cells. Our findings reveal the Na,K-ATPase as the initial recruitment factor for FGF2 at the inner plasma membrane leaflet being required for efficient membrane translocation of FGF2 to cell surfaces.
MeSH term(s)	Animals ; CHO Cells ; Cell Membrane/enzymology ; Cricetulus ; Fibroblast Growth Factor 2/chemistry ; Fibroblast Growth Factor 2/genetics ; Fibroblast Growth Factor 2/metabolism ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Transport ; Second Messenger Systems ; Secretory Pathway ; Sodium-Potassium-Exchanging ATPase/chemistry ; Sodium-Potassium-Exchanging ATPase/genetics ; Sodium-Potassium-Exchanging ATPase/metabolism
Chemical Substances	Phosphatidylinositol 4,5-Diphosphate ; Fibroblast Growth Factor 2 (103107-01-3) ; ATP1A1 protein, human (EC 3.6.1.-) ; Sodium-Potassium-Exchanging ATPase (EC 7.2.2.13)
Language	English
Publishing date	2020-03-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-020-0871-y
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Article ; Online: HIV-Tat Protein Forms Phosphoinositide-dependent Membrane Pores Implicated in Unconventional Protein Secretion.

Zeitler, Marcel / Steringer, Julia P / Müller, Hans-Michael / Mayer, Matthias P / Nickel, Walter

The Journal of biological chemistry

2015 Volume 290, Issue 36, Page(s) 21976–21984

Abstract: HIV-Tat has been demonstrated to be secreted from cells in a phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-dependent manner. Here we show that HIV-Tat forms membrane-inserted oligomers, a process that is accompanied by changes in secondary structure ... ...

Abstract	HIV-Tat has been demonstrated to be secreted from cells in a phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-dependent manner. Here we show that HIV-Tat forms membrane-inserted oligomers, a process that is accompanied by changes in secondary structure with a strong increase in antiparallel β sheet content. Intriguingly, oligomerization of HIV-Tat on membrane surfaces leads to the formation of membrane pores, as demonstrated by physical membrane passage of small fluorescent tracer molecules. Although membrane binding of HIV-Tat did not strictly depend on PI(4,5)P2 but, rather, was mediated by a range of acidic membrane lipids, a functional interaction between PI(4,5)P2 and HIV-Tat was critically required for efficient membrane pore formation by HIV-Tat oligomers. These properties are strikingly similar to what has been reported previously for fibroblast growth factor 2 (FGF2), providing strong evidence of a common core mechanism of unconventional secretion shared by HIV-Tat and fibroblast growth factor 2.
MeSH term(s)	Cell Membrane/metabolism ; Cell Membrane/virology ; Electrophoresis, Polyacrylamide Gel ; Fibroblast Growth Factor 2/chemistry ; Fibroblast Growth Factor 2/metabolism ; Humans ; Lipid Bilayers/metabolism ; Liposomes/metabolism ; Mutation ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Phosphatidylinositols/metabolism ; Protein Binding ; Protein Conformation ; Protein Multimerization ; Protein Structure, Secondary ; Protein Transport ; Spectroscopy, Fourier Transform Infrared ; tat Gene Products, Human Immunodeficiency Virus/chemistry ; tat Gene Products, Human Immunodeficiency Virus/genetics ; tat Gene Products, Human Immunodeficiency Virus/metabolism
Chemical Substances	Lipid Bilayers ; Liposomes ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositols ; tat Gene Products, Human Immunodeficiency Virus ; Fibroblast Growth Factor 2 (103107-01-3)
Language	English
Publishing date	2015-07-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M115.667097
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