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Article ; Online: A novel sterol-binding protein reveals heterogeneous cholesterol distribution in neurite outgrowth and in late endosomes/lysosomes.

Yamaji-Hasegawa, Akiko / Murate, Motohide / Inaba, Takehiko / Dohmae, Naoshi / Sato, Masayuki / Fujimori, Fumihiro / Sako, Yasushi / Greimel, Peter / Kobayashi, Toshihide

Cellular and molecular life sciences : CMLS

2022 Volume 79, Issue 6, Page(s) 324

Abstract: We identified a mushroom-derived protein, maistero-2 that specifically binds 3-hydroxy sterol including cholesterol (Chol). Maistero-2 bound lipid mixture in Chol-dependent manner with a binding threshold of around 30%. Changing lipid composition did not ...

Abstract	We identified a mushroom-derived protein, maistero-2 that specifically binds 3-hydroxy sterol including cholesterol (Chol). Maistero-2 bound lipid mixture in Chol-dependent manner with a binding threshold of around 30%. Changing lipid composition did not significantly affect the threshold concentration. EGFP-maistero-2 labeled cell surface and intracellular organelle Chol with higher sensitivity than that of well-established Chol probe, D4 fragment of perfringolysin O. EGFP-maistero-2 revealed increase of cell surface Chol during neurite outgrowth and heterogeneous Chol distribution between CD63-positive and LAMP1-positive late endosomes/lysosomes. The absence of strictly conserved Thr-Leu pair present in Chol-dependent cytolysins suggests a distinct Chol-binding mechanism for maistero-2.
MeSH term(s)	Carrier Proteins/metabolism ; Cholesterol/metabolism ; Endosomes/metabolism ; Lysosomes/metabolism ; Neuronal Outgrowth ; Sterols/metabolism
Chemical Substances	Carrier Proteins ; Sterols ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2022-05-29
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-022-04339-6
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Article: A novel sterol-binding protein reveals heterogeneous cholesterol distribution in neurite outgrowth and in late endosomes/lysosomes

Yamaji-Hasegawa, Akiko / Murate, Motohide / Inaba, Takehiko / Dohmae, Naoshi / Sato, Masayuki / Fujimori, Fumihiro / Sako, Yasushi / Greimel, Peter / Kobayashi, Toshihide

Cellular and molecular life sciences. 2022 June, v. 79, no. 6

2022

Abstract	We identified a mushroom-derived protein, maistero-2 that specifically binds 3-hydroxy sterol including cholesterol (Chol). Maistero-2 bound lipid mixture in Chol-dependent manner with a binding threshold of around 30%. Changing lipid composition did not significantly affect the threshold concentration. EGFP-maistero-2 labeled cell surface and intracellular organelle Chol with higher sensitivity than that of well-established Chol probe, D4 fragment of perfringolysin O. EGFP-maistero-2 revealed increase of cell surface Chol during neurite outgrowth and heterogeneous Chol distribution between CD63-positive and LAMP1-positive late endosomes/lysosomes. The absence of strictly conserved Thr-Leu pair present in Chol-dependent cytolysins suggests a distinct Chol-binding mechanism for maistero-2.
Keywords	cholesterol ; endosomes ; lipid composition ; lysosomes ; neurites
Language	English
Dates of publication	2022-06
Size	p. 324.
Publishing place	Springer International Publishing
Document type	Article
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-022-04339-6
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Article ; Online: Impact of Intrinsic and Extrinsic Factors on Cellular Sphingomyelin Imaging with Specific Reporter Proteins.

Kobayashi, Toshihide / Tomishige, Nario / Inaba, Takehiko / Makino, Asami / Murata, Michio / Yamaji-Hasegawa, Akiko / Murate, Motohide

Contact (Thousand Oaks (Ventura County, Calif.))

2021 Volume 4, Page(s) 25152564211042456

Abstract: Sphingomyelin (SM) is a major sphingolipid in mammalian cells. Although SM is enriched in the outer leaflet of the cell plasma membrane, lipids are also observed in the inner leaflet of the plasma membrane and intracellular organelles such as ... ...

Abstract	Sphingomyelin (SM) is a major sphingolipid in mammalian cells. Although SM is enriched in the outer leaflet of the cell plasma membrane, lipids are also observed in the inner leaflet of the plasma membrane and intracellular organelles such as endolysosomes, the Golgi apparatus and nuclei. SM is postulated to form clusters with glycosphingolipids (GSLs), cholesterol (Chol), and other SM molecules through hydrophobic interactions and hydrogen bonding. Thus, different clusters composed of SM, SM/Chol, SM/GSL and SM/GSL/Chol with different stoichiometries may exist in biomembranes. In addition, SM monomers may be located in the glycerophospholipid-rich areas of membranes. Recently developed SM-binding proteins (SBPs) distinguish these different SM assemblies. Here, we summarize the effects of intrinsic factors regulating the lipid-binding specificity of SBPs and extrinsic factors, such as the lipid phase and lipid density, on SM recognition by SBPs. The combination of different SBPs revealed the heterogeneity of SM domains in biomembranes.
Language	English
Publishing date	2021-09-27
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2964312-0
ISSN	2515-2564 ; 2515-2564
ISSN (online)	2515-2564
ISSN	2515-2564
DOI	10.1177/25152564211042456
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Article ; Online: Molecular mechanisms of action of sphingomyelin-specific pore-forming toxin, lysenin.

Yilmaz, Neval / Yamaji-Hasegawa, Akiko / Hullin-Matsuda, Françoise / Kobayashi, Toshihide

Seminars in cell & developmental biology

2017 Volume 73, Page(s) 188–198

Abstract: Lysenin, which is an earthworm toxin, strongly binds to sphingomyelin (SM). Lysenin oligomerizes on SM-rich domains and can induce cell death by forming pores in the membrane. In this review, the assembly of lysenin on SM-containing membranes is ... ...

Abstract	Lysenin, which is an earthworm toxin, strongly binds to sphingomyelin (SM). Lysenin oligomerizes on SM-rich domains and can induce cell death by forming pores in the membrane. In this review, the assembly of lysenin on SM-containing membranes is discussed mostly on the basis of the information gained by atomic force microscopy (AFM). AFM data show that lysenin assembles into a hexagonal close packed (hcp) structure by rapid reorganization of its oligomers on an SM/cholesterol membrane. In case of a phase-separated membrane of SM, lysenin induces phase mixing as a result of pore formation in SM-rich domains, and consequently its hcp assembly covers the entire membrane. Besides the lytic action, lysenin is important as an SM marker and its pore has the potential to be used as a biosensor in the future. These points are also highlighted in this review.
MeSH term(s)	Microscopy, Atomic Force ; Sphingomyelins/chemistry ; Sphingomyelins/metabolism ; Sphingomyelins/pharmacology ; Thermodynamics ; Toxins, Biological/chemistry ; Toxins, Biological/metabolism ; Toxins, Biological/pharmacology
Chemical Substances	Sphingomyelins ; Toxins, Biological ; lysenin
Language	English
Publishing date	2017-07-24
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.2017.07.036
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Article ; Online: Pore-forming moss protein bryoporin is structurally and mechanistically related to actinoporins from evolutionarily distant cnidarians.

Šolinc, Gašper / Švigelj, Tomaž / Omersa, Neža / Snoj, Tina / Pirc, Katja / Žnidaršič, Nada / Yamaji-Hasegawa, Akiko / Kobayashi, Toshihide / Anderluh, Gregor / Podobnik, Marjetka

The Journal of biological chemistry

2022 Volume 298, Issue 10, Page(s) 102455

Abstract: Pore-forming proteins perforate lipid membranes and consequently affect their integrity and cell fitness. Therefore, it is not surprising that many of these proteins from bacteria, fungi, or certain animals act as toxins. While pore-forming proteins have ...

Abstract	Pore-forming proteins perforate lipid membranes and consequently affect their integrity and cell fitness. Therefore, it is not surprising that many of these proteins from bacteria, fungi, or certain animals act as toxins. While pore-forming proteins have also been found in plants, there is little information about their molecular structure and mode of action. Bryoporin is a protein from the moss Physcomitrium patens, and its corresponding gene was found to be upregulated by various abiotic stresses, especially dehydration, as well as upon fungal infection. Based on the amino acid sequence, it was suggested that bryoporin was related to the actinoporin family of pore-forming proteins, originally discovered in sea anemones. Here, we provide the first detailed structural and functional analysis of this plant cytolysin. The crystal structure of monomeric bryoporin is highly similar to those of actinoporins. Our cryo-EM analysis of its pores showed an actinoporin-like octameric structure, thereby revealing a close kinship of proteins from evolutionarily distant organisms. This was further confirmed by our observation of bryoporin's preferential binding to and formation of pores in membranes containing animal sphingolipids, such as sphingomyelin and ceramide phosphoethanolamine; however, its binding affinity was weaker than that of actinoporin equinatoxin II. We determined bryoporin did not bind to major sphingolipids found in fungi or plants, and its membrane-binding and pore-forming activity was enhanced by various sterols. Our results suggest that bryoporin could represent a part of the moss defense arsenal, acting as a pore-forming toxin against membranes of potential animal pathogens, parasites, or predators.
MeSH term(s)	Animals ; Amino Acid Sequence ; Bryopsida/genetics ; Bryopsida/metabolism ; Cnidarian Venoms/chemistry ; Cytotoxins ; Porins/genetics ; Porins/metabolism ; Sea Anemones/chemistry
Chemical Substances	Cnidarian Venoms ; Cytotoxins ; Porins
Language	English
Publishing date	2022-09-03
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	10.1016/j.jbc.2022.102455
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Article ; Online: Impact of Intrinsic and Extrinsic Factors on Cellular Sphingomyelin Imaging with Specific Reporter Proteins

Toshihide Kobayashi / Nario Tomishige / Takehiko Inaba / Asami Makino / Michio Murata / Akiko Yamaji-Hasegawa / Motohide Murate

Contact, Vol

2021 Volume 4

Abstract	Sphingomyelin (SM) is a major sphingolipid in mammalian cells. Although SM is enriched in the outer leaflet of the cell plasma membrane, lipids are also observed in the inner leaflet of the plasma membrane and intracellular organelles such as endolysosomes, the Golgi apparatus and nuclei. SM is postulated to form clusters with glycosphingolipids (GSLs), cholesterol (Chol), and other SM molecules through hydrophobic interactions and hydrogen bonding. Thus, different clusters composed of SM, SM/Chol, SM/GSL and SM/GSL/Chol with different stoichiometries may exist in biomembranes. In addition, SM monomers may be located in the glycerophospholipid-rich areas of membranes. Recently developed SM-binding proteins (SBPs) distinguish these different SM assemblies. Here, we summarize the effects of intrinsic factors regulating the lipid-binding specificity of SBPs and extrinsic factors, such as the lipid phase and lipid density, on SM recognition by SBPs. The combination of different SBPs revealed the heterogeneity of SM domains in biomembranes.
Keywords	Biology (General) ; QH301-705.5 ; Biochemistry ; QD415-436
Language	English
Publishing date	2021-09-01T00:00:00Z
Publisher	SAGE Publishing
Document type	Article ; Online
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Article: Pore-forming toxins: Properties, diversity, and uses as tools to image sphingomyelin and ceramide phosphoethanolamine.

Yamaji-Hasegawa, Akiko / Hullin-Matsuda, Françoise / Greimel, Peter / Kobayashi, Toshihide

Biochimica et biophysica acta

2016 Volume 1858, Issue 3, Page(s) 576–592

Abstract: Pore-forming toxins (PFTs) represent a unique class of highly specific lipid-binding proteins. The cytotoxicity of these compounds has been overcome through crystallographic structure and mutation studies, facilitating the development of non-toxic lipid ... ...

Abstract	Pore-forming toxins (PFTs) represent a unique class of highly specific lipid-binding proteins. The cytotoxicity of these compounds has been overcome through crystallographic structure and mutation studies, facilitating the development of non-toxic lipid probes. As a consequence, non-toxic PFTs have been utilized as highly specific probes to visualize the diversity and dynamics of lipid nanostructures in living and fixed cells. This review is focused on the application of PFTs and their non-toxic analogs as tools to visualize sphingomyelin and ceramide phosphoethanolamine, two major phosphosphingolipids in mammalian and insect cells, respectively. This article is part of a Special Issue entitled: Pore-Forming Toxins edited by Mauro Dalla Serra and Franco Gambale.
MeSH term(s)	Animals ; Humans ; Insecta/metabolism ; Molecular Imaging/methods ; Molecular Probes/chemistry ; Pore Forming Cytotoxic Proteins/chemistry ; Sphingomyelins/metabolism
Chemical Substances	Molecular Probes ; Pore Forming Cytotoxic Proteins ; Sphingomyelins ; ceramide phosphoethanolamine (112130-78-6)
Language	English
Publishing date	2016-03
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamem.2015.10.012
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Article ; Online: Intrinsically disordered region of influenza A NP regulates viral genome packaging via interactions with viral RNA and host PI(4,5)P2.

Kakisaka, Michinori / Yamada, Kazunori / Yamaji-Hasegawa, Akiko / Kobayashi, Toshihide / Aida, Yoko

Virology

2016 Volume 496, Page(s) 116–126

Abstract: To be incorporated into progeny virions, the viral genome must be transported to the inner leaflet of the plasma membrane (PM) and accumulate there. Some viruses utilize lipid components to assemble at the PM. For example, simian virus 40 (SV40) targets ... ...

Abstract	To be incorporated into progeny virions, the viral genome must be transported to the inner leaflet of the plasma membrane (PM) and accumulate there. Some viruses utilize lipid components to assemble at the PM. For example, simian virus 40 (SV40) targets the ganglioside GM1 and human immunodeficiency virus type 1 (HIV-1) utilizes phosphatidylinositol (4,5) bisphosphate [PI(4,5)P2]. Recent studies clearly indicate that Rab11-mediated recycling endosomes are required for influenza A virus (IAV) trafficking of vRNPs to the PM but it remains unclear how IAV vRNP localized or accumulate underneath the PM for viral genome incorporation into progeny virions. In this study, we found that the second intrinsically disordered region (IDR2) of NP regulates two binding steps involved in viral genome packaging. First, IDR2 facilitates NP oligomer binding to viral RNA to form vRNP. Secondly, vRNP assemble by interacting with PI(4,5)P2 at the PM via IDR2. These findings suggest that PI(4,5)P2 functions as the determinant of vRNP accumulation at the PM.
MeSH term(s)	Animals ; Cell Line ; Dogs ; Genome, Viral ; Host-Pathogen Interactions ; Humans ; Influenza A virus/physiology ; Influenza, Human/metabolism ; Influenza, Human/virology ; Intrinsically Disordered Proteins/metabolism ; Models, Molecular ; Molecular Conformation ; Phosphatidylinositol 4,5-Diphosphate/chemistry ; Phosphatidylinositol 4,5-Diphosphate/metabolism ; Protein Binding ; Protein Multimerization ; Protein Transport ; RNA, Viral/chemistry ; RNA, Viral/metabolism ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/metabolism ; Structure-Activity Relationship ; Viral Core Proteins/chemistry ; Viral Core Proteins/metabolism ; Virus Assembly ; Virus Replication
Chemical Substances	Intrinsically Disordered Proteins ; NP protein, Influenza A virus ; Phosphatidylinositol 4,5-Diphosphate ; RNA, Viral ; RNA-Binding Proteins ; Viral Core Proteins
Language	English
Publishing date	2016-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/j.virol.2016.05.018
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Article: Asymmetric distribution of phospholipids in biomembranes.

Yamaji-Hasegawa, Akiko / Tsujimoto, Masafumi

Biological & pharmaceutical bulletin

2006 Volume 29, Issue 8, Page(s) 1547–1553

Abstract: In eukaryotic cells, the biological membrane is characterized by a non-uniform distribution of membrane lipids, vertically as well as laterally. The paradigm for the vertical non-random distribution is the plasma membrane, where phosphatidylcholine (PC), ...

Abstract	In eukaryotic cells, the biological membrane is characterized by a non-uniform distribution of membrane lipids, vertically as well as laterally. The paradigm for the vertical non-random distribution is the plasma membrane, where phosphatidylcholine (PC), sphingomyelin (SM), and glycosphingolipids are primarily located on the exoplasmic leaflet, while aminophospholipids, including phosphatidylserine (PS) and phosphatidylethanolamine (PE), are generally enriched in the cytoplasmic leaflet. Other minor phospholipids, such as phosphatidic acid and phosphatidylinositol (PI), are also enriched on the cytoplasmic face. Such asymmetrical distribution is related to each lipid regulating various biological events through interaction with other molecules. The clarification of the regulatory mechanism of the distribution and movement of membrane lipids is crucial to understanding the physiological roles of lipids. Here we focus on PS, which has been reported to be involved in apoptosis, blood coagulation and other biological phenomena, and summarize the present understanding of the dynamics of this phospholipid, including biosynthesis, metabolism, transport, and transbilayer movement. We also refer to diseases that have been reported to be related to phospholipid asymmetry.
MeSH term(s)	Biological Transport ; Cell Membrane/metabolism ; Humans ; Lipid Bilayers ; Phospholipids/metabolism
Chemical Substances	Lipid Bilayers ; Phospholipids
Language	English
Publishing date	2006-06-14
Publishing country	Japan
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1150271-x
ISSN	1347-5215 ; 0918-6158
ISSN (online)	1347-5215
ISSN	0918-6158
DOI	10.1248/bpb.29.1547
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Article: [Proteins which recognize sphingomyelin].

Yamaji-Hasegawa, Akiko / Kobayashi, Toshihide

Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme

2002 Volume 47, Issue 4 Suppl, Page(s) 519–525

MeSH term(s)	Animals ; Antibodies, Monoclonal/metabolism ; Carrier Proteins/metabolism ; Humans ; Immunoglobulin M/metabolism ; Membrane Microdomains ; Molecular Probes ; Protein Binding ; Proteins/metabolism ; Sphingomyelin Phosphodiesterase/metabolism ; Sphingomyelins/chemistry ; Sphingomyelins/metabolism ; Toxins, Biological
Chemical Substances	Antibodies, Monoclonal ; Carrier Proteins ; Immunoglobulin M ; Molecular Probes ; Proteins ; Sphingomyelins ; Toxins, Biological ; lysenin ; sphingomyelin transfer protein, rat ; Sphingomyelin Phosphodiesterase (EC 3.1.4.12)
Language	Japanese
Publishing date	2002-03
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	391163-9
ISSN	0039-9450
ISSN	0039-9450
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