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Article ; Online: Lysine acylation causes collateral damage in inborn errors of metabolism.

Goetzman, Eric S / Vockley, Jerry

2022 Volume 14, Issue 646, Page(s) eabq4863

Abstract: Posttranslational modifications contribute to the pathology of methylmalonic acidemia and may be targetable via an acylation-resistant sirtuin ( ... ...

Abstract	Posttranslational modifications contribute to the pathology of methylmalonic acidemia and may be targetable via an acylation-resistant sirtuin (Head
MeSH term(s)	Acylation ; Amino Acid Metabolism, Inborn Errors ; Humans ; Lysine/metabolism ; Protein Processing, Post-Translational
Chemical Substances	Lysine (K3Z4F929H6)
Language	English
Publishing date	2022-05-25
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	2518854-9
ISSN	1946-6242 ; 1946-6234
ISSN (online)	1946-6242
ISSN	1946-6234
DOI	10.1126/scitranslmed.abq4863
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Article: Advances in the Understanding and Treatment of Mitochondrial Fatty Acid Oxidation Disorders.

Goetzman, Eric S

Current genetic medicine reports

2017 Volume 5, Issue 3, Page(s) 132–142

Abstract: Purpose of review: This review focuses on advances made in the past three years with regards to understanding the mitochondrial fatty acid oxidation (FAO) pathway, the pathophysiological ramifications of genetic lesions in FAO enzymes, and emerging ... ...

Abstract	Purpose of review: This review focuses on advances made in the past three years with regards to understanding the mitochondrial fatty acid oxidation (FAO) pathway, the pathophysiological ramifications of genetic lesions in FAO enzymes, and emerging therapies for FAO disorders. Recent findings: FAO has now been recognized to play a key energetic role in pulmonary surfactant synthesis, T-cell differentiation and memory, and the response of the proximal tubule to kidney injury. Patients with FAO disorders may face defects in these cellular systems as they age. Aspirin, statins, and nutritional supplements modulate the rate of FAO under normal conditions and could be risk factors for triggering symptoms in patients with FAO disorders. Patients have been identified with mutations in the Summary: Recent research has led to a deeper understanding of FAO. New therapeutic avenues are being pursued that may ultimately cause a paradigm shift for patient care.
Language	English
Publishing date	2017-07-25
Publishing country	United States
Document type	Journal Article
ISSN	2167-4876
ISSN	2167-4876
DOI	10.1007/s40142-017-0125-6
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Article ; Online: A Novel Transgenic Mouse Model Implicates

Schmidt, Alexandra V / Monga, Satdarshan P / Prochownik, Edward V / Goetzman, Eric S

International journal of molecular sciences

2023 Volume 24, Issue 16

Abstract: Hepatocellular carcinoma (HCC) is one of the leading causes of cancer deaths globally. Incidence rates are steadily increasing, creating an unmet need for new therapeutic options. Recently, the inhibition of sirtuin-2 ( ...

Abstract	Hepatocellular carcinoma (HCC) is one of the leading causes of cancer deaths globally. Incidence rates are steadily increasing, creating an unmet need for new therapeutic options. Recently, the inhibition of sirtuin-2 (
MeSH term(s)	Animals ; Mice ; Mice, Transgenic ; Carcinoma, Hepatocellular/genetics ; Sirtuin 2/genetics ; Liver Neoplasms/genetics ; Carcinogens ; Disease Models, Animal
Chemical Substances	Sirtuin 2 (EC 3.5.1.-) ; Carcinogens
Language	English
Publishing date	2023-08-09
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/ijms241612618
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Article: The Role for Myc in Coordinating Glycolysis, Oxidative Phosphorylation, Glutaminolysis, and Fatty Acid Metabolism in Normal and Neoplastic Tissues.

Goetzman, Eric S / Prochownik, Edward V

Frontiers in endocrinology

2018 Volume 9, Page(s) 129

Abstract: That cancer cells show patterns of metabolism different from normal cells has been known for over 50 years. Yet, it is only in the past decade or so that an appreciation of the benefits of these changes has begun to emerge. Altered cancer cell metabolism ...

Abstract	That cancer cells show patterns of metabolism different from normal cells has been known for over 50 years. Yet, it is only in the past decade or so that an appreciation of the benefits of these changes has begun to emerge. Altered cancer cell metabolism was initially attributed to defective mitochondria. However, we now realize that most cancers do not have mitochondrial mutations and that normal cells can transiently adopt cancer-like metabolism during periods of rapid proliferation. Indeed, an encompassing, albeit somewhat simplified, conceptual framework to explain both normal and cancer cell metabolism rests on several simple premises. First, the metabolic pathways used by cancer cells and their normal counterparts are the same. Second, normal quiescent cells use their metabolic pathways and the energy they generate largely to maintain cellular health and organelle turnover and, in some cases, to provide secreted products necessary for the survival of the intact organism. By contrast, undifferentiated cancer cells minimize the latter functions and devote their energy to producing the anabolic substrates necessary to maintain high rates of unremitting cellular proliferation. Third, as a result of the uncontrolled proliferation of cancer cells, a larger fraction of the metabolic intermediates normally used by quiescent cells purely as a source of energy are instead channeled into competing proliferation-focused and energy-consuming anabolic pathways. Fourth, cancer cell clones with the most plastic and rapidly adaptable metabolism will eventually outcompete their less well-adapted brethren during tumor progression and evolution. This attribute becomes increasingly important as tumors grow and as their individual cells compete in a constantly changing and inimical environment marked by nutrient, oxygen, and growth factor deficits. Here, we review some of the metabolic pathways whose importance has gained center stage for tumor growth, particularly those under the control of the c-Myc (Myc) oncoprotein. We discuss how these pathways differ functionally between quiescent and proliferating normal cells, how they are kidnapped and corrupted during the course of transformation, and consider potential therapeutic strategies that take advantage of common features of neoplastic and metabolic disorders.
Language	English
Publishing date	2018
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2592084-4
ISSN	1664-2392
ISSN	1664-2392
DOI	10.3389/fendo.2018.00129
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Article: Adjusted vascular contractility relies on integrity of progranulin pathway: Insights into mitochondrial function.

Singh, Shubhnita / Bruder-Nascimento, Ariane / Costa, Rafael M / Alves, Juliano V / Bharathi, Sivakama / Goetzman, Eric S / Bruder-Nascimento, Thiago

bioRxiv : the preprint server for biology

2023

Abstract: Objective: Cardiovascular disease (CVD) is a global health crisis and a leading cause of mortality. The intricate interplay between vascular contractility and mitochondrial function is central to CVD pathogenesis. The progranulin gene (GRN) encodes ... ...

Abstract	Objective: Cardiovascular disease (CVD) is a global health crisis and a leading cause of mortality. The intricate interplay between vascular contractility and mitochondrial function is central to CVD pathogenesis. The progranulin gene (GRN) encodes glycoprotein progranulin (PGRN), a ubiquitous molecule with known anti-inflammatory property. However, the role of PGRN in CVD remains enigmatic. In this study, we sought to dissect the significance of PGRN in the regulation vascular contractility and investigate the interface between PGRN and mitochondrial quality. Method: Our investigation utilized aortae from male and female C57BL6/J wild-type (PGRN+/+) and B6(Cg)-Grntm1.1Aidi/J (PGRN-/-) mice, encompassing wire myograph assays to assess vascular contractility and primary aortic vascular smooth muscle cells (VSMCs) for mechanistic insights. Results: Our results showed suppression of contractile activity in PGRN-/- VSMCs and aorta, followed by reduced α-smooth muscle actin expression. Mechanistically, PGRN deficiency impaired mitochondrial oxygen consumption rate (OCR), complex I activity, mitochondrial turnover, and mitochondrial redox signaling, while restoration of PGRN levels in aortae from PGRN-/- mice via lentivirus delivery ameliorated contractility and boosted OCR. In addition, VSMC overexpressing PGRN displayed higher mitochondrial respiration and complex I activity accompanied by cellular hypercontractility. Furthermore, increased PGRN triggered lysosome biogenesis by regulating transcription factor EB and accelerated mitophagy flux in VSMC, while treatment with spermidine, an autophagy inducer, improved mitochondrial phenotype and enhanced vascular contractility. Finally, angiotensin II failed to induce vascular contractility in PGRN-/- suggesting a key role of PGRN to maintain the vascular tone. Conclusion: Our findings suggest that PGRN preserves the vascular contractility via regulating mitophagy flux, mitochondrial complex I activity, and redox signaling. Therefore, loss of PGRN function appears as a pivotal risk factor in CVD development.
Language	English
Publishing date	2023-11-01
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.10.27.564485
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Article ; Online: Modeling disorders of fatty acid metabolism in the mouse.

Goetzman, Eric S

Progress in molecular biology and translational science

2011 Volume 100, Page(s) 389–417

Abstract: There are at least 17 enzymes involved in mitochondrial fatty acid oxidation encoded by at least 21 genes. For most of these genes, humans with genetic deficiencies have been identified. The mouse possesses a very similar fatty acid oxidation system and ... ...

Abstract	There are at least 17 enzymes involved in mitochondrial fatty acid oxidation encoded by at least 21 genes. For most of these genes, humans with genetic deficiencies have been identified. The mouse possesses a very similar fatty acid oxidation system and has served well as an organism for modeling genetic loss of function. Knockout mice have been created for 12 fatty acid oxidation genes, including all three carnitine palmitoyltransferase-1 genes, four of the acyl-CoA dehydrogenases, both subunits of trifunctional protein, short/medium-chain hydroxyacyl-CoA dehydrogenase, and two enzymes required for oxidation of polyunsaturated fatty acids (enoyl-CoA isomerase and 2,4 dienoyl-CoA reductase). This review covers the knowledge that has been gained from these mouse models in terms of understanding both single-gene fatty acid oxidation disorders and the contribution of the fatty acid oxidation pathway to polygenic diseases such as obesity and type 2 diabetes. Also reviewed are other mouse models displaying phenotypic aspects of a fatty acid oxidation disorder such as knockout mice lacking the carnitine transporter and knockouts of key regulators of the pathway such as peroxisome proliferator-activated receptor-α and sirtuin-3. Finally, nongenetic means of manipulating fatty acid oxidation in the mouse are discussed, in particular the various chemical inhibitors that have been used successfully in vivo.
MeSH term(s)	Animals ; Disease Models, Animal ; Fatty Acids/metabolism ; Humans ; Lipid Metabolism, Inborn Errors/pathology ; Mice ; Mitochondria/metabolism ; Models, Genetic ; Oxidation-Reduction
Chemical Substances	Fatty Acids
Language	English
Publishing date	2011
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	2471995-X
ISSN	1878-0814 ; 0079-6603 ; 1877-1173
ISSN (online)	1878-0814
ISSN	0079-6603 ; 1877-1173
DOI	10.1016/B978-0-12-384878-9.00010-8
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Article ; Online: The fatty acid oxidation enzyme long-chain acyl-CoA dehydrogenase can be a source of mitochondrial hydrogen peroxide.

Zhang, Yuxun / Bharathi, Sivakama S / Beck, Megan E / Goetzman, Eric S

Redox biology

2019 Volume 26, Page(s) 101253

Abstract: Fatty acid oxidation (FAO)-driven ... ...

Abstract	Fatty acid oxidation (FAO)-driven H
MeSH term(s)	Acyl-CoA Dehydrogenase, Long-Chain/genetics ; Acyl-CoA Dehydrogenase, Long-Chain/metabolism ; Acyl-CoA Oxidase/genetics ; Acyl-CoA Oxidase/metabolism ; Animals ; Cloning, Molecular ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Fatty Acids/metabolism ; Gene Expression ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Hep G2 Cells ; Humans ; Hydrogen Peroxide/metabolism ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Kidney/enzymology ; Kinetics ; Liver/enzymology ; Lung/enzymology ; Male ; Mice ; Mice, Knockout ; Mitochondria, Liver/enzymology ; Organ Specificity ; Oxidation-Reduction ; Oxidative Stress ; Pancreas/enzymology ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism
Chemical Substances	Fatty Acids ; Isoenzymes ; Recombinant Proteins ; Hydrogen Peroxide (BBX060AN9V) ; Acyl-CoA Oxidase (EC 1.3.3.6) ; Acyl-CoA Dehydrogenase, Long-Chain (EC 1.3.8.8)
Language	English
Publishing date	2019-06-15
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	2213-2317
ISSN (online)	2213-2317
DOI	10.1016/j.redox.2019.101253
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Article: The regulation of acyl-CoA dehydrogenases in adipose tissue by rosiglitazone.

Goetzman, Eric S

Obesity (Silver Spring, Md.)

2009 Volume 17, Issue 1, Page(s) 196–198

Abstract: The acyl-CoA dehydrogenases (ACADs), which catalyze the rate-limiting step in the mitochondrial beta-oxidation spiral, were investigated in white adipose tissue (WAT) of C57Bl/6 mice treated with 10 mg/kg/day rosiglitazone. Rosiglitazone was also ... ...

Abstract	The acyl-CoA dehydrogenases (ACADs), which catalyze the rate-limiting step in the mitochondrial beta-oxidation spiral, were investigated in white adipose tissue (WAT) of C57Bl/6 mice treated with 10 mg/kg/day rosiglitazone. Rosiglitazone was also administered to PPAR-alpha knockout mice. ACAD abundance and activity were determined using western blotting and an ACAD enzyme activity assay. Rosiglitazone increased ACAD activity in both epididymal and inguinal WAT but not in brown adipose tissue, liver, or muscle. Given the known function of PPAR-alpha in regulating the expression of ACAD genes in liver, it was hypothesized that PPAR-alpha may be involved in upregulating the ACADs during rosiglitazone-mediated adipose tissue remodeling. However, the effect of rosiglitazone on adipose tissue ACAD activity was the same in wild-type and PPAR-alpha knockout mice. In conclusion, rosiglitazone increases expression and activity of ACAD enzymes in WAT independently of PPAR-alpha.
MeSH term(s)	Acyl-CoA Dehydrogenase/metabolism ; Acyl-CoA Dehydrogenase, Long-Chain/metabolism ; Acyl-CoA Dehydrogenases/metabolism ; Adipose Tissue/drug effects ; Adipose Tissue/enzymology ; Animals ; Epididymis/drug effects ; Epididymis/enzymology ; Liver/drug effects ; Liver/enzymology ; Male ; Mice ; Mice, Inbred C57BL ; Muscle, Skeletal/drug effects ; Muscle, Skeletal/enzymology ; Thiazolidinediones/pharmacology
Chemical Substances	Thiazolidinediones ; rosiglitazone (05V02F2KDG) ; Acyl-CoA Dehydrogenases (EC 1.3.-) ; Acyl-CoA Dehydrogenase (EC 1.3.8.7) ; Acyl-CoA Dehydrogenase, Long-Chain (EC 1.3.8.8)
Language	English
Publishing date	2009-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	2230457-5
ISSN	1930-739X ; 1930-7381 ; 1071-7323
ISSN (online)	1930-739X
ISSN	1930-7381 ; 1071-7323
DOI	10.1038/oby.2008.467
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Article: Role of mitochondrial acyl-CoA dehydrogenases in the metabolism of dicarboxylic fatty acids

Bharathi, Sivakama S / Zhang, Yuxun / Gong, Zhenwei / Muzumdar, Radhika / Goetzman, Eric S

Biochemical and biophysical research communications. 2020 June 18, v. 527, no. 1

2020

Abstract: Dicarboxylic fatty acids, taken as a nutritional supplement or produced endogenously via omega oxidation of monocarboxylic fatty acids, may have therapeutic potential for rare inborn errors of metabolism as well as common metabolic diseases such as type ... ...

Abstract	Dicarboxylic fatty acids, taken as a nutritional supplement or produced endogenously via omega oxidation of monocarboxylic fatty acids, may have therapeutic potential for rare inborn errors of metabolism as well as common metabolic diseases such as type 2 diabetes. Breakdown of dicarboxylic acids yields acetyl-CoA and succinyl-CoA as products, the latter of which is anaplerotic for the TCA cycle. However, little is known about the metabolic pathways responsible for degradation of dicarboxylic acids. Here, we demonstrated with whole-cell fatty acid oxidation assays that both mitochondria and peroxisomes contribute to dicarboxylic acid degradation. Several mitochondrial acyl-CoA dehydrogenases were tested for activity against dicarboxylyl-CoAs. Medium-chain acyl-CoA dehydrogenase (MCAD) exhibited activity with both six and 12 carbon dicarboxylyl-CoAs, and the capacity for dehydrogenation of these substrates was significantly reduced in MCAD knockout mouse liver. However, when dicarboxylic acids were fed to normal mice, the expression of MCAD did not change, while expression of peroxisomal fatty acid oxidation enzymes was greatly upregulated. In conclusion, mitochondrial fatty acid oxidation, and in particular MCAD, contributes to dicarboxylic acid degradation, but feeding dicarboxylic acids induces only the peroxisomal pathway.
Keywords	acetyl coenzyme A ; acyl coenzyme A ; acyl-CoA dehydrogenase ; beta oxidation ; carbon ; dehydrogenation ; dicarboxylic acids ; knockout mutants ; liver ; mitochondria ; noninsulin-dependent diabetes mellitus ; oxidation ; peroxisomes ; research ; therapeutics ; tricarboxylic acid cycle
Language	English
Dates of publication	2020-0618
Size	p. 162-166.
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2020.04.105
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Article ; Online: Role of mitochondrial acyl-CoA dehydrogenases in the metabolism of dicarboxylic fatty acids.

Bharathi, Sivakama S / Zhang, Yuxun / Gong, Zhenwei / Muzumdar, Radhika / Goetzman, Eric S

Biochemical and biophysical research communications

2020 Volume 527, Issue 1, Page(s) 162–166

Abstract	Dicarboxylic fatty acids, taken as a nutritional supplement or produced endogenously via omega oxidation of monocarboxylic fatty acids, may have therapeutic potential for rare inborn errors of metabolism as well as common metabolic diseases such as type 2 diabetes. Breakdown of dicarboxylic acids yields acetyl-CoA and succinyl-CoA as products, the latter of which is anaplerotic for the TCA cycle. However, little is known about the metabolic pathways responsible for degradation of dicarboxylic acids. Here, we demonstrated with whole-cell fatty acid oxidation assays that both mitochondria and peroxisomes contribute to dicarboxylic acid degradation. Several mitochondrial acyl-CoA dehydrogenases were tested for activity against dicarboxylyl-CoAs. Medium-chain acyl-CoA dehydrogenase (MCAD) exhibited activity with both six and 12 carbon dicarboxylyl-CoAs, and the capacity for dehydrogenation of these substrates was significantly reduced in MCAD knockout mouse liver. However, when dicarboxylic acids were fed to normal mice, the expression of MCAD did not change, while expression of peroxisomal fatty acid oxidation enzymes was greatly upregulated. In conclusion, mitochondrial fatty acid oxidation, and in particular MCAD, contributes to dicarboxylic acid degradation, but feeding dicarboxylic acids induces only the peroxisomal pathway.
MeSH term(s)	Acyl-CoA Dehydrogenases/metabolism ; Animals ; Dicarboxylic Acids/metabolism ; Fatty Acids/metabolism ; Male ; Mice ; Mice, Knockout ; Mitochondria/enzymology
Chemical Substances	Dicarboxylic Acids ; Fatty Acids ; Acyl-CoA Dehydrogenases (EC 1.3.-)
Language	English
Publishing date	2020-04-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2020.04.105
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