LIVIVO - Search results -

Search results

Result 1 - 10 of total 68

Search options

Article ; Online: ACAT1/SOAT1 Blockade Suppresses LPS-Mediated Neuroinflammation by Modulating the Fate of Toll-like Receptor 4 in Microglia.

Li, Haibo / Huynh, Thao N / Duong, Michael Tran / Gow, James G / Chang, Catherine C Y / Chang, Ta Yuan

International journal of molecular sciences

2023 Volume 24, Issue 6

Abstract: Cholesterol is stored as cholesteryl esters by the enzymes acyl-CoA:cholesterol acyltransferases/sterol O:acyltransferases (ACATs/SOATs). ACAT1 blockade (A1B) ameliorates the pro-inflammatory responses of macrophages to lipopolysaccharides (LPS) and ... ...

Abstract	Cholesterol is stored as cholesteryl esters by the enzymes acyl-CoA:cholesterol acyltransferases/sterol O:acyltransferases (ACATs/SOATs). ACAT1 blockade (A1B) ameliorates the pro-inflammatory responses of macrophages to lipopolysaccharides (LPS) and cholesterol loading. However, the mediators involved in transmitting the effects of A1B in immune cells is unknown. Microglial
MeSH term(s)	Animals ; Mice ; Acyltransferases/metabolism ; Cholesterol/metabolism ; Lipopolysaccharides/toxicity ; Lipopolysaccharides/metabolism ; Mice, Knockout ; Microglia/metabolism ; Neuroinflammatory Diseases ; Toll-Like Receptor 4/metabolism
Chemical Substances	Acyltransferases (EC 2.3.-) ; Cholesterol (97C5T2UQ7J) ; Lipopolysaccharides ; Toll-Like Receptor 4 ; Acat1 protein, mouse (EC 2.3.1.9) ; sterol O-acyltransferase 1 (EC 2.3.1.26)
Language	English
Publishing date	2023-03-15
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms24065616
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: Acute ACAT1/SOAT1 Blockade Increases MAM Cholesterol and Strengthens ER-Mitochondria Connectivity.

Harned, Taylor C / Stan, Radu V / Cao, Ze / Chakrabarti, Rajarshi / Higgs, Henry N / Chang, Catherine C Y / Chang, Ta Yuan

International journal of molecular sciences

2023 Volume 24, Issue 6

Abstract: Cholesterol is a key component of all mammalian cell membranes. Disruptions in cholesterol metabolism have been observed in the context of various diseases, including neurodegenerative disorders such as Alzheimer's disease (AD). The genetic and ... ...

Abstract	Cholesterol is a key component of all mammalian cell membranes. Disruptions in cholesterol metabolism have been observed in the context of various diseases, including neurodegenerative disorders such as Alzheimer's disease (AD). The genetic and pharmacological blockade of acyl-CoA:cholesterol acyltransferase 1/sterol O-acyltransferase 1 (ACAT1/SOAT1), a cholesterol storage enzyme found on the endoplasmic reticulum (ER) and enriched at the mitochondria-associated ER membrane (MAM), has been shown to reduce amyloid pathology and rescue cognitive deficits in mouse models of AD. Additionally, blocking ACAT1/SOAT1 activity stimulates autophagy and lysosomal biogenesis; however, the exact molecular connection between the ACAT1/SOAT1 blockade and these observed benefits remain unknown. Here, using biochemical fractionation techniques, we observe cholesterol accumulation at the MAM which leads to ACAT1/SOAT1 enrichment in this domain. MAM proteomics data suggests that ACAT1/SOAT1 inhibition strengthens the ER-mitochondria connection. Confocal and electron microscopy confirms that ACAT1/SOAT1 inhibition increases the number of ER-mitochondria contact sites and strengthens this connection by shortening the distance between these two organelles. This work demonstrates how directly manipulating local cholesterol levels at the MAM can alter inter-organellar contact sites and suggests that cholesterol buildup at the MAM is the impetus behind the therapeutic benefits of ACAT1/SOAT1 inhibition.
MeSH term(s)	Animals ; Mice ; Alzheimer Disease/metabolism ; Cholesterol/metabolism ; Endoplasmic Reticulum/metabolism ; Mammals/metabolism ; Mitochondria/metabolism ; Sterols/metabolism ; Acetyl-CoA C-Acyltransferase/metabolism ; Sterol O-Acyltransferase/metabolism
Chemical Substances	Cholesterol (97C5T2UQ7J) ; Sterols ; Acetyl-CoA C-Acyltransferase (EC 2.3.1.16) ; Sterol O-Acyltransferase (EC 2.3.1.26)
Language	English
Publishing date	2023-03-14
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms24065525
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: A simple method to disrupt and restore subunit interaction of acyl-CoA:cholesterol acyltransferase 1.

Neumann, Bryan / Chang, Catherine C Y / Chang, Ta-Yuan

MethodsX

2019 Volume 6, Page(s) 2242–2247

Abstract: Acyl-CoA:cholestereol acyltransferase 1 (ACAT1) is a two-fold dimer (homotetramer) and has two distinct dimerization domains. One domain is in an alpha-helical rich region near the cytoplasmic N-terminus. The other is proposed to be near the C-terminus ... ...

Abstract	Acyl-CoA:cholestereol acyltransferase 1 (ACAT1) is a two-fold dimer (homotetramer) and has two distinct dimerization domains. One domain is in an alpha-helical rich region near the cytoplasmic N-terminus. The other is proposed to be near the C-terminus where multiple transmembrane domains promote hydrophobic interactions between two ACAT1 subunits. The truncation of the ACAT1 N-terminal dimerization domain, Δ1-65, creates a dimer which is fully enzymatically active. It is currently not known how the C-terminal dimerization domain contributes to ACAT1 enzymatic activity. Here we describe a simple method that dissociates ACAT1 dimers through the addition of the non-ionic detergents Triton X-100 or octyl glucoside which disrupt the C-terminal dimerization domain. We also document the protocols for a method to exchange Triton X-100 with CHAPS to restore C-terminal dimerization of the ACAT1 protein, and an optimized liposomal assay to assess ACAT enzymatic activity. •This method can be applied to dissociate ACAT1 subunits by using Triton X-100 or octyl glucoside.•ACAT1 dimerization can be restored by exchanging Triton X-100 with CHAPS.•The liposomal ACAT activity assay conditions have been optimized.
Language	English
Publishing date	2019-09-20
Publishing country	Netherlands
Document type	Journal Article
ISSN	2215-0161
ISSN	2215-0161
DOI	10.1016/j.mex.2019.09.021
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: Triton X-100 or octyl glucoside inactivates acyl-CoA:cholesterol acyltransferase 1 by dissociating it from a two-fold dimer to a two-fold monomer.

Neumann, Bryan / Chang, Catherine C Y / Chang, Ta-Yuan

Archives of biochemistry and biophysics

2019 Volume 671, Page(s) 103–110

Abstract: Cholesterol is an important lipid molecule and is needed for all mammalian cells. In various cell types, excess cholesterol is stored as cholesteryl esters; acyl-CoA:cholesterol acyltransferase 1 (ACAT1) plays an essential role in this storage process. ... ...

Abstract	Cholesterol is an important lipid molecule and is needed for all mammalian cells. In various cell types, excess cholesterol is stored as cholesteryl esters; acyl-CoA:cholesterol acyltransferase 1 (ACAT1) plays an essential role in this storage process. ACAT1 is located at the endoplasmic reticulum and has nine transmembrane domains (TMDs). It is a member of the membrane-bound O-acyltransferase (MBOAT) family, in which members contain multiple TMDs and participate in a variety of biological functions. When solubilized in the zwitterionic detergent CHAPS, ACAT1 can be purified to homogeneity with full enzyme activity and behaves as a homotetrameric protein. ACAT1 contains two dimerization motifs. The first motif is located near the N-terminus and is not conserved in MBOATs. Deletion of the N-terminal dimerization domain converts ACAT1 to a dimer with full catalytic activity; therefore, ACAT1 is a two-fold dimer. The second dimerization domain, located near the C-terminus, is conserved in MBOATs; however, it was not known whether the C-terminal dimerization domain is required for enzyme activity. Here we show that treating ACAT1 with non-ionic detergent, Triton X-100 or octyl glucoside, causes the enzyme to become a two-fold monomer without any enzymatic activity. Detergent exchange of Triton X-100 with CHAPS restores ACAT1 to a two-fold dimer but fails to restore its enzymatic activity. These results implicate that ACAT1 requires hydrophobic subunit interactions near the C-terminus in order to remain active as a two-fold dimer. Our results also caution the use of Triton X-100 or octyl glucoside to purify other MBOATs.
MeSH term(s)	Acetyl-CoA C-Acetyltransferase/antagonists & inhibitors ; Acetyl-CoA C-Acetyltransferase/metabolism ; Animals ; CHO Cells ; Cholic Acids/chemistry ; Cricetulus ; Detergents/chemistry ; Enzyme Inhibitors/chemistry ; Glucosides/chemistry ; Goats ; HEK293 Cells ; Humans ; Mice ; Octoxynol/chemistry ; Protein Multimerization/drug effects ; Rabbits
Chemical Substances	Cholic Acids ; Detergents ; Enzyme Inhibitors ; Glucosides ; octyl-beta-D-glucoside (29836-26-8) ; Octoxynol (9002-93-1) ; ACAT1 protein, human (EC 2.3.1.9) ; Acetyl-CoA C-Acetyltransferase (EC 2.3.1.9) ; 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate (QBP25342AG)
Language	English
Publishing date	2019-06-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2019.06.006
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

Uc I Zs.237: 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: Nanodisc scaffold peptide (NSP

Neumann, Bryan / Chao, Kevin / Chang, Catherine C Y / Chang, Ta-Yuan

Archives of biochemistry and biophysics

2020 Volume 691, Page(s) 108518

Abstract: To conduct biochemical studies in vitro, membrane proteins (MPs) must be solubilized with detergents. While detergents are great tools, they can also inhibit the biological activity and/or perturb oligomerization of individual MPs. Nanodisc scaffold ... ...

Abstract	To conduct biochemical studies in vitro, membrane proteins (MPs) must be solubilized with detergents. While detergents are great tools, they can also inhibit the biological activity and/or perturb oligomerization of individual MPs. Nanodisc scaffold peptide (NSP
MeSH term(s)	Amino Acid Sequence ; Animals ; CHO Cells ; Cholic Acids/chemistry ; Cricetulus ; Detergents/chemistry ; Digitonin/chemistry ; Humans ; Peptides/chemistry ; Protein Domains ; Protein Multimerization ; Sterol O-Acyltransferase/chemistry ; Sterol O-Acyltransferase/metabolism ; Surface-Active Agents/chemistry
Chemical Substances	Cholic Acids ; Detergents ; Peptides ; Surface-Active Agents ; Sterol O-Acyltransferase (EC 2.3.1.26) ; sterol O-acyltransferase 1 (EC 2.3.1.26) ; Digitonin (KOO5CM684H) ; 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate (QBP25342AG)
Language	English
Publishing date	2020-07-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2020.108518
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

Uc I Zs.237: 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: Cholesterol, Atherosclerosis, and APOE in Vascular Contributions to Cognitive Impairment and Dementia (VCID): Potential Mechanisms and Therapy.

Duong, Michael Tran / Nasrallah, Ilya M / Wolk, David A / Chang, Catherine C Y / Chang, Ta-Yuan

Frontiers in aging neuroscience

2021 Volume 13, Page(s) 647990

Abstract: Vascular contributions to cognitive impairment and dementia (VCID) are a common cause of cognitive decline, yet limited therapies exist. This cerebrovascular disease results in ... ...

Abstract	Vascular contributions to cognitive impairment and dementia (VCID) are a common cause of cognitive decline, yet limited therapies exist. This cerebrovascular disease results in neurodegeneration
Language	English
Publishing date	2021-03-25
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2558898-9
ISSN	1663-4365
ISSN	1663-4365
DOI	10.3389/fnagi.2021.647990
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Nanodisc scaffold peptide (NSPr) replaces detergent by reconstituting acyl-CoA:cholesterol acyltransferase 1 into peptidiscs

Neumann, Bryan / Chao, Kevin / Chang, Catherine C.Y / Chang, Ta-Yuan

Archives of biochemistry and biophysics. 2020 Sept. 30, v. 691

2020

Abstract	To conduct biochemical studies in vitro, membrane proteins (MPs) must be solubilized with detergents. While detergents are great tools, they can also inhibit the biological activity and/or perturb oligomerization of individual MPs. Nanodisc scaffold peptide (NSPᵣ), an amphipathic peptide analog of ApoA1, was recently shown to reconstitute detergent solubilized MPs into peptidiscs in vitro. Acyl-coenzyme A:cholesterol acyltransferase 1 (ACAT1), also known as sterol O-acyltransferase 1 (SOAT1), plays a key role in cellular cholesterol storage in various cell types and is a drug target to treat multiple human diseases. ACAT1 contains nine transmembrane domains (TMDs) and primarily forms a homotetramer in vitro and in intact cells; deletion of the N-terminal dimerization domain produces a homodimer with full retention in catalytic activity. ACAT1 is prone to inactivation by numerous detergents. Here we pursued the use of NSPᵣ to overcome the detergent-induced inactivation of ACAT1 by generating near detergent-free ACAT1 peptidiscs. Based on native-PAGE analysis, we showed that NSPᵣ reconstitutes ACAT1 into soluble peptidiscs, in which ACAT1 exists predominantly in oligomeric states greater than a homotetramer. The formation of these higher-order oligomeric states was independent of the N-terminal dimerization domain, suggesting that the oligomerization is mediated through hydrophobic interactions of multiple ACAT1 subunits. ACAT1 peptidiscs were still susceptible to heat-mediated inactivation, presumably due to the residual detergent (CHAPS) bound to ACAT1. We then conditioned ACAT1 with phosphatidylcholine (PC) to replace CHAPS prior to the formation of ACAT1 peptidiscs. The results showed, when PC was included, ACAT1 was present mainly in higher-order oligomeric states with greater enzymatic activity. With PC present, the enzymatic activity of ACAT1 peptidiscs was protected from heat-mediated inactivation. These results support the use of NSPᵣ to create a near detergent-free solution of ACAT1 in peptidiscs for various in vitro studies. Our current results also raise the possibility that, under certain conditions, ACAT1 may form higher-order oligomeric states in vivo.
Keywords	bioactive properties ; biophysics ; catalytic activity ; cholesterol ; cholesterol acyltransferase ; detergents ; dimerization ; drugs ; enzyme activity ; humans ; hydrophobicity ; oligomerization ; peptides ; phosphatidylcholines ; solubilization ; surfactants
Language	English
Dates of publication	2020-0930
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.2020.108518
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 4' 70/107: Show issues
Archiv: 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: Stealth Liposomes Encapsulating a Potent ACAT1/SOAT1 Inhibitor F12511: Pharmacokinetic, Biodistribution, and Toxicity Studies in Wild-Type Mice and Efficacy Studies in Triple Transgenic Alzheimer's Disease Mice.

De La Torre, Adrianna L / Huynh, Thao N / Chang, Catherine C Y / Pooler, Darcy B / Ness, Dylan B / Lewis, Lionel D / Pannem, Sanjana / Feng, Yichen / Samkoe, Kimberley S / Hickey, William F / Chang, Ta Yuan

International journal of molecular sciences

2023 Volume 24, Issue 13

Abstract: Cholesterol is essential for cellular function and is stored as cholesteryl esters (CEs). CEs biosynthesis is catalyzed by the enzymes acyl-CoA:cholesterol acyltransferase 1 and 2 (ACAT1 and ACAT2), with ACAT1 being the primary isoenzyme in most cells in ...

Abstract	Cholesterol is essential for cellular function and is stored as cholesteryl esters (CEs). CEs biosynthesis is catalyzed by the enzymes acyl-CoA:cholesterol acyltransferase 1 and 2 (ACAT1 and ACAT2), with ACAT1 being the primary isoenzyme in most cells in humans. In Alzheimer's Disease, CEs accumulate in vulnerable brain regions. Therefore, ACATs may be promising targets for treating AD. F12511 is a high-affinity ACAT1 inhibitor that has passed phase 1 safety tests for antiatherosclerosis. Previously, we developed a nanoparticle system to encapsulate a large concentration of F12511 into a stealth liposome (DSPE-PEG
MeSH term(s)	Humans ; Mice ; Animals ; Mice, Transgenic ; Alzheimer Disease/drug therapy ; Alzheimer Disease/pathology ; Liposomes ; Tissue Distribution ; Tandem Mass Spectrometry ; Acetyl-CoA C-Acetyltransferase/metabolism
Chemical Substances	eflucimibe (3DK1X2C37M) ; Liposomes ; ACAT1 protein, human (EC 2.3.1.9) ; Acetyl-CoA C-Acetyltransferase (EC 2.3.1.9)
Language	English
Publishing date	2023-07-02
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms241311013
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: A simple method to disrupt and restore subunit interaction of acyl-CoA:cholesterol acyltransferase 1

Neumann, Bryan / Chang, Catherine C.Y / Chang, Ta-Yuan

MethodsX. 2019, v. 6

2019

Abstract	Acyl-CoA:cholestereol acyltransferase 1 (ACAT1) is a two-fold dimer (homotetramer) and has two distinct dimerization domains. One domain is in an alpha-helical rich region near the cytoplasmic N-terminus. The other is proposed to be near the C-terminus where multiple transmembrane domains promote hydrophobic interactions between two ACAT1 subunits. The truncation of the ACAT1 N-terminal dimerization domain, Δ1-65, creates a dimer which is fully enzymatically active. It is currently not known how the C-terminal dimerization domain contributes to ACAT1 enzymatic activity. Here we describe a simple method that dissociates ACAT1 dimers through the addition of the non-ionic detergents Triton X-100 or octyl glucoside which disrupt the C-terminal dimerization domain. We also document the protocols for a method to exchange Triton X-100 with CHAPS to restore C-terminal dimerization of the ACAT1 protein, and an optimized liposomal assay to assess ACAT enzymatic activity.•This method can be applied to dissociate ACAT1 subunits by using Triton X-100 or octyl glucoside.•ACAT1 dimerization can be restored by exchanging Triton X-100 with CHAPS.•The liposomal ACAT activity assay conditions have been optimized.
Keywords	cholesterol acyltransferase ; detergents ; dimerization ; enzyme activity ; glucosides ; hydrophobic bonding ; octoxynol
Language	English
Size	p. 2242-2247.
Publishing place	Elsevier B.V.
Document type	Article
ISSN	2215-0161
DOI	10.1016/j.mex.2019.09.021
Database	NAL-Catalogue (AGRICOLA)

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: Triton X-100 or octyl glucoside inactivates acyl-CoA:cholesterol acyltransferase 1 by dissociating it from a two-fold dimer to a two-fold monomer

Neumann, Bryan / Chang, Catherine C.Y / Chang, Ta-Yuan

Archives of biochemistry and biophysics. 2019 Aug. 15, v. 671

2019

Abstract	Cholesterol is an important lipid molecule and is needed for all mammalian cells. In various cell types, excess cholesterol is stored as cholesteryl esters; acyl-CoA:cholesterol acyltransferase 1 (ACAT1) plays an essential role in this storage process. ACAT1 is located at the endoplasmic reticulum and has nine transmembrane domains (TMDs). It is a member of the membrane-bound O-acyltransferase (MBOAT) family, in which members contain multiple TMDs and participate in a variety of biological functions. When solubilized in the zwitterionic detergent CHAPS, ACAT1 can be purified to homogeneity with full enzyme activity and behaves as a homotetrameric protein. ACAT1 contains two dimerization motifs. The first motif is located near the N-terminus and is not conserved in MBOATs. Deletion of the N-terminal dimerization domain converts ACAT1 to a dimer with full catalytic activity; therefore, ACAT1 is a two-fold dimer. The second dimerization domain, located near the C-terminus, is conserved in MBOATs; however, it was not known whether the C-terminal dimerization domain is required for enzyme activity. Here we show that treating ACAT1 with non-ionic detergent, Triton X-100 or octyl glucoside, causes the enzyme to become a two-fold monomer without any enzymatic activity. Detergent exchange of Triton X-100 with CHAPS restores ACAT1 to a two-fold dimer but fails to restore its enzymatic activity. These results implicate that ACAT1 requires hydrophobic subunit interactions near the C-terminus in order to remain active as a two-fold dimer. Our results also caution the use of Triton X-100 or octyl glucoside to purify other MBOATs.
Keywords	catalytic activity ; cholesterol ; cholesterol acyltransferase ; cholesteryl esters ; detergents ; dimerization ; endoplasmic reticulum ; enzyme activity ; glucosides ; hydrophobicity ; mammals ; octoxynol ; solubilization ; zwitterions
Language	English
Dates of publication	2019-0815
Size	p. 103-110.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2019.06.006
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 4' 70/107: Show issues
Archiv: 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 ▾

To top

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

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

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

More links

Kategorien

Order via subito

More links

Kategorien

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