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Article ; Online: Inequitable COVID-19 vaccine distribution and the intellectual property rights prolong the pandemic.

Altindis, Emrah

2022 Volume 21, Issue 4, Page(s) 427–430

MeSH term(s)	COVID-19/epidemiology ; COVID-19/prevention & control ; COVID-19 Vaccines ; Global Health ; Humans ; Intellectual Property ; Pandemics
Chemical Substances	COVID-19 Vaccines
Language	English
Publishing date	2022-01-27
Publishing country	England
Document type	Editorial
ZDB-ID	2181284-6
ISSN	1744-8395 ; 1476-0584
ISSN (online)	1744-8395
ISSN	1476-0584
DOI	10.1080/14760584.2022.2014819
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Article ; Online: Vaccinology in the 21st century.

Altindis, Emrah

Current topics in medicinal chemistry

2013 Volume 13, Issue 20, Page(s) 2533–2534

MeSH term(s)	History, 20th Century ; History, 21st Century ; Humans ; Vaccination/history ; Vaccines/history
Chemical Substances	Vaccines
Language	English
Publishing date	2013-09-22
Publishing country	United Arab Emirates
Document type	Editorial ; Historical Article ; Introductory Journal Article
ZDB-ID	2064823-6
ISSN	1873-4294 ; 1568-0266
ISSN (online)	1873-4294
ISSN	1568-0266
DOI	10.2174/15680266113136660179
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Article ; Online: Vaccines for all: Institut Pasteur vaccinology course, 2010.

Altindiş, Emrah

Expert review of vaccines

2010 Volume 9, Issue 9, Page(s) 1023–1026

Abstract: A comprehensive 5-week vaccinology course was recently held in Paris (1 March-2 April 2010) hosted by the Institut Pasteur, a world-renowned center for science and vaccinology. A total of 25 young scientists from different parts of the world participated ...

Abstract	A comprehensive 5-week vaccinology course was recently held in Paris (1 March-2 April 2010) hosted by the Institut Pasteur, a world-renowned center for science and vaccinology. A total of 25 young scientists from different parts of the world participated and 63 world experts gave lectures in six specific modules that covered all aspects of vaccinology, from basic research to clinical studies. Students also had the opportunity to attend a 2-day "Pandemic Influenza Workshop". This article summarizes the issues discussed during this course and highlights the importance of global access to vaccines.
MeSH term(s)	Communicable Diseases/epidemiology ; Curriculum ; Education, Medical, Continuing ; Humans ; Paris ; Vaccination/methods ; Vaccines/immunology
Chemical Substances	Vaccines
Language	English
Publishing date	2010-09
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2181284-6
ISSN	1744-8395 ; 1476-0584
ISSN (online)	1744-8395
ISSN	1476-0584
DOI	10.1586/erv.10.96
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Article ; Online: Antibacterial vaccine research in 21st century: from inoculation to genomics approaches.

Altindis, Emrah

Current topics in medicinal chemistry

2013 Volume 13, Issue 20, Page(s) 2638–2646

Abstract: Vaccination is one of the safest and most cost-effective public health interventions, which save millions of lives annually. Thanks to all the genius pioneers of the field, we have already developed many effective vaccines. On the other hand, there are ... ...

Abstract	Vaccination is one of the safest and most cost-effective public health interventions, which save millions of lives annually. Thanks to all the genius pioneers of the field, we have already developed many effective vaccines. On the other hand, there are still many pathogens for which we do not yet have an effective or optimal vaccine, including malaria, HIV, and tuberculosis. In the 21(st) century, biological sciences are at the edge of a growing and fruitful genomics era, which provide many opportunities for vaccine research to have a better understanding of host-pathogen interactions, immune responses, targets and thus allow the scientists to design better vaccines. After the publication of the first bacterial genome of a pathogen, Haemophilus influenza, genomics technology revolutionized the field and created novel vaccine discovery approaches like reverse vaccinology, antigenome technology, surfome analysis, immunoproteomics, and genetics vaccinology to discover novel immunogenic antigens. This review is an attempt to briefly explain these methodologies and the history of their development since the beginning of the century.
MeSH term(s)	Bacterial Vaccines/genetics ; Bacterial Vaccines/history ; Bacterial Vaccines/immunology ; Genomics ; History, 18th Century ; History, 20th Century ; History, 21st Century ; Vaccination
Chemical Substances	Bacterial Vaccines
Language	English
Publishing date	2013-09-22
Publishing country	United Arab Emirates
Document type	Historical Article ; Journal Article ; Review
ZDB-ID	2064823-6
ISSN	1873-4294 ; 1568-0266
ISSN (online)	1873-4294
ISSN	1568-0266
DOI	10.2174/15680266113136660188
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Article ; Online: Tissue differences in the exosomal/small extracellular vesicle proteome and their potential as indicators of altered tissue metabolism.

Garcia-Martin, Ruben / Brandao, Bruna Brasil / Thomou, Thomas / Altindis, Emrah / Kahn, C Ronald

Cell reports

2022 Volume 38, Issue 3, Page(s) 110277

Abstract: Exosomes/small extracellular vesicles (sEVs) can serve as multifactorial mediators of cell-to-cell communication through their miRNA and protein cargo. Quantitative proteomic analysis of five cell lines representing metabolically important tissues ... ...

Abstract	Exosomes/small extracellular vesicles (sEVs) can serve as multifactorial mediators of cell-to-cell communication through their miRNA and protein cargo. Quantitative proteomic analysis of five cell lines representing metabolically important tissues reveals that each cell type has a unique sEV proteome. While classical sEV markers such as CD9/CD63/CD81 vary markedly in abundance, we identify six sEV markers (ENO1, GPI, HSPA5, YWHAB, CSF1R, and CNTN1) that are similarly abundant in sEVs of all cell types. In addition, each cell type has specific sEV markers. Using fat-specific Dicer-knockout mice with decreased white adipose tissue and increased brown adipose tissue, we show that these cell-type-specific markers can predict the changing origin of the serum sEVs. These results provide a valuable resource for understanding the sEV proteome of the cells and tissues important in metabolic homeostasis, identify unique sEV markers, and demonstrate how these markers can help in predicting the tissue of origin of serum sEVs.
MeSH term(s)	3T3 Cells ; Adiponectin/blood ; Adipose Tissue/metabolism ; Animals ; Biomarkers/blood ; Exosomes/metabolism ; Mice ; Proteome/metabolism
Chemical Substances	Adiponectin ; Biomarkers ; Proteome
Language	English
Publishing date	2022-01-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2021.110277
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Article ; Online: A viral insulin-like peptide inhibits IGF-1 receptor phosphorylation and regulates IGF1R gene expression.

Chrudinová, Martina / Kirk, Nicholas S / Chuard, Aurelien / Venugopal, Hari / Zhang, Fa / Lubos, Marta / Gelfanov, Vasily / Páníková, Terezie / Žáková, Lenka / Cutone, Julianne / Mojares, Matthew / DiMarchi, Richard / Jiráček, Jiří / Altindis, Emrah

Molecular metabolism

2024 Volume 80, Page(s) 101863

Abstract: Objective: The insulin/IGF superfamily is conserved across vertebrates and invertebrates. Our team has identified five viruses containing genes encoding viral insulin/IGF-1 like peptides (VILPs) closely resembling human insulin and IGF-1. This study ... ...

Abstract	Objective: The insulin/IGF superfamily is conserved across vertebrates and invertebrates. Our team has identified five viruses containing genes encoding viral insulin/IGF-1 like peptides (VILPs) closely resembling human insulin and IGF-1. This study aims to characterize the impact of Mandarin fish ranavirus (MFRV) and Lymphocystis disease virus-Sa (LCDV-Sa) VILPs on the insulin/IGF system for the first time. Methods: We chemically synthesized single chain (sc, IGF-1 like) and double chain (dc, insulin like) forms of MFRV and LCDV-Sa VILPs. Using cell lines overexpressing either human insulin receptor isoform A (IR-A), isoform B (IR-B) or IGF-1 receptor (IGF1R), and AML12 murine hepatocytes, we characterized receptor binding, insulin/IGF signaling. We further characterized the VILPs' effects of proliferation and IGF1R and IR gene expression, and compared them to native ligands. Additionally, we performed insulin tolerance test in CB57BL/6 J mice to examine in vivo effects of VILPs on blood glucose levels. Finally, we employed cryo-electron microscopy (cryoEM) to analyze the structure of scMFRV-VILP in complex with the IGF1R ectodomain. Results: VILPs can bind to human IR and IGF1R, stimulate receptor autophosphorylation and downstream signaling pathways. Notably, scMFRV-VILP exhibited a particularly strong affinity for IGF1R, with a mere 10-fold decrease compared to human IGF-1. At high concentrations, scMFRV-VILP selectively reduced IGF-1 stimulated IGF1R autophosphorylation and Erk phosphorylation (Ras/MAPK pathway), while leaving Akt phosphorylation (PI3K/Akt pathway) unaffected, indicating a potential biased inhibitory function. Prolonged exposure to MFRV-VILP led to a significant decrease in IGF1R gene expression in IGF1R overexpressing cells and AML12 hepatocytes. Furthermore, insulin tolerance test revealed scMFRV-VILP's sustained glucose-lowering effect compared to insulin and IGF-1. Finally, cryo-EM analysis revealed that scMFRV-VILP engages with IGF1R in a manner closely resembling IGF-1 binding, resulting in a highly analogous structure. Conclusions: This study introduces MFRV and LCDV-Sa VILPs as novel members of the insulin/IGF superfamily. Particularly, scMFRV-VILP exhibits a biased inhibitory effect on IGF1R signaling at high concentrations, selectively inhibiting IGF-1 stimulated IGF1R autophosphorylation and Erk phosphorylation, without affecting Akt phosphorylation. In addition, MFRV-VILP specifically regulates IGF-1R gene expression and IGF1R protein levels without affecting IR. CryoEM analysis confirms that scMFRV-VILP' binding to IGF1R is mirroring the interaction pattern observed with IGF-1. These findings offer valuable insights into IGF1R action and inhibition, suggesting potential applications in development of IGF1R specific inhibitors and advancing long-lasting insulins.
MeSH term(s)	Humans ; Animals ; Mice ; Receptor, IGF Type 1/genetics ; Receptor, IGF Type 1/metabolism ; Insulin-Like Growth Factor I/genetics ; Insulin-Like Growth Factor I/metabolism ; Phosphorylation ; Proto-Oncogene Proteins c-akt/metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Cryoelectron Microscopy ; Insulin/metabolism ; Protein Isoforms/metabolism ; Gene Expression
Chemical Substances	Receptor, IGF Type 1 (EC 2.7.10.1) ; Insulin-Like Growth Factor I (67763-96-6) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Insulin ; Protein Isoforms ; IGF1R protein, human
Language	English
Publishing date	2024-01-03
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2708735-9
ISSN	2212-8778 ; 2212-8778
ISSN (online)	2212-8778
ISSN	2212-8778
DOI	10.1016/j.molmet.2023.101863
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Article ; Online: Viral Hormones: Expanding Dimensions in Endocrinology.

Huang, Qian / Kahn, C Ronald / Altindis, Emrah

Endocrinology

2019 Volume 160, Issue 9, Page(s) 2165–2179

Abstract: Viruses have developed different mechanisms to manipulate their hosts, including the process of viral mimicry in which viruses express important host proteins. Until recently, examples of viral mimicry were limited to mimics of growth factors and ... ...

Abstract	Viruses have developed different mechanisms to manipulate their hosts, including the process of viral mimicry in which viruses express important host proteins. Until recently, examples of viral mimicry were limited to mimics of growth factors and immunomodulatory proteins. Using a comprehensive bioinformatics approach, we have shown that viruses possess the DNA/RNA with potential to encode 16 different peptides with high sequence similarity to human peptide hormones and metabolically important regulatory proteins. We have characterized one of these families, the viral insulin/IGF-1-like peptides (VILPs), which we identified in four members of the Iridoviridae family. VILPs can bind to human insulin and IGF-1 receptors and stimulate classic postreceptor signaling pathways. Moreover, VILPs can stimulate glucose uptake in vitro and in vivo and stimulate DNA synthesis. DNA sequences of some VILP-carrying viruses have been identified in the human enteric virome. In addition to VILPs, sequences with homology to 15 other peptide hormones or cytokines can be identified in viral DNA/RNA sequences, some with a very high identity to hormones. Recent data by others has identified a peptide that resembles and mimics α-melanocyte-stimulating hormone's anti-inflammatory effects in in vitro and in vivo models. Taken together, these studies reveal novel mechanisms of viral and bacterial pathogenesis in which the microbe can directly target or mimic the host endocrine system. These findings also introduce the concept of a system of microbial hormones that provides new insights into the evolution of peptide hormones, as well as potential new roles of microbial hormones in health and disease.
MeSH term(s)	Animals ; Endocrinology ; Endothelin-1/physiology ; Fish Diseases/etiology ; Host-Pathogen Interactions/physiology ; Humans ; Insulin-Like Growth Factor I/chemistry ; Insulin-Like Growth Factor I/physiology ; Viral Proteins/chemistry ; Viral Proteins/physiology
Chemical Substances	Endothelin-1 ; Viral Proteins ; Insulin-Like Growth Factor I (67763-96-6)
Language	English
Publishing date	2019-07-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	427856-2
ISSN	1945-7170 ; 0013-7227
ISSN (online)	1945-7170
ISSN	0013-7227
DOI	10.1210/en.2019-00271
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Article ; Online: A viral insulin-like peptide inhibits IGF-1 receptor phosphorylation and regulates IGF1R gene expression

Martina Chrudinová / Nicholas S. Kirk / Aurelien Chuard / Hari Venugopal / Fa Zhang / Marta Lubos / Vasily Gelfanov / Terezie Páníková / Lenka Žáková / Julianne Cutone / Matthew Mojares / Richard DiMarchi / Jiří Jiráček / Emrah Altindis

Molecular Metabolism, Vol 80, Iss , Pp 101863- (2024)

2024

Abstract	Objective: The insulin/IGF superfamily is conserved across vertebrates and invertebrates. Our team has identified five viruses containing genes encoding viral insulin/IGF-1 like peptides (VILPs) closely resembling human insulin and IGF-1. This study aims to characterize the impact of Mandarin fish ranavirus (MFRV) and Lymphocystis disease virus-Sa (LCDV-Sa) VILPs on the insulin/IGF system for the first time. Methods: We chemically synthesized single chain (sc, IGF-1 like) and double chain (dc, insulin like) forms of MFRV and LCDV-Sa VILPs. Using cell lines overexpressing either human insulin receptor isoform A (IR-A), isoform B (IR-B) or IGF-1 receptor (IGF1R), and AML12 murine hepatocytes, we characterized receptor binding, insulin/IGF signaling. We further characterized the VILPs’ effects of proliferation and IGF1R and IR gene expression, and compared them to native ligands. Additionally, we performed insulin tolerance test in CB57BL/6 J mice to examine in vivo effects of VILPs on blood glucose levels. Finally, we employed cryo-electron microscopy (cryoEM) to analyze the structure of scMFRV-VILP in complex with the IGF1R ectodomain. Results: VILPs can bind to human IR and IGF1R, stimulate receptor autophosphorylation and downstream signaling pathways. Notably, scMFRV-VILP exhibited a particularly strong affinity for IGF1R, with a mere 10-fold decrease compared to human IGF-1. At high concentrations, scMFRV-VILP selectively reduced IGF-1 stimulated IGF1R autophosphorylation and Erk phosphorylation (Ras/MAPK pathway), while leaving Akt phosphorylation (PI3K/Akt pathway) unaffected, indicating a potential biased inhibitory function. Prolonged exposure to MFRV-VILP led to a significant decrease in IGF1R gene expression in IGF1R overexpressing cells and AML12 hepatocytes. Furthermore, insulin tolerance test revealed scMFRV-VILP's sustained glucose-lowering effect compared to insulin and IGF-1. Finally, cryo-EM analysis revealed that scMFRV-VILP engages with IGF1R in a manner closely resembling IGF-1 binding, ...
Keywords	Viral insulin/IGF-1 like peptides (VILPs) ; IGF-1 ; Insulin ; IGF1 receptor ; IGF1 receptor inhibition ; Biased signaling ; Internal medicine ; RC31-1245
Subject code	616
Language	English
Publishing date	2024-02-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article ; Online: A viral insulin-like peptide is a natural competitive antagonist of the human IGF-1 receptor.

Zhang, Fa / Altindis, Emrah / Kahn, C Ronald / DiMarchi, Richard D / Gelfanov, Vasily

Molecular metabolism

2021 Volume 53, Page(s) 101316

Abstract: Objective: Natural sources of molecular diversity remain of utmost importance as a reservoir of proteins and peptides with unique biological functions. We recently identified such a family of viral insulin-like peptides (VILPs). We sought to advance the ...

Abstract	Objective: Natural sources of molecular diversity remain of utmost importance as a reservoir of proteins and peptides with unique biological functions. We recently identified such a family of viral insulin-like peptides (VILPs). We sought to advance the chemical methods in synthesis to explore the structure-function relationship within these VILPs, and the molecular basis for differential biological activities relative to human IGF-1 and insulin. Methods: Optimized chemical methods in synthesis were established for a set of VILPs and related analogs. These modified forms included the substitution of select VILP chains with those derived from human insulin and IGF-1. Each peptide was assessed in vitro for agonism and antagonism at the human insulin and the human insulin-like growth factor 1 receptor (IGF-1R). Results: We report here that one of these VILPs, lymphocystis disease virus-1 (LCDV1)-VILP, has the unique property to be a potent and full antagonist of the IGF-1R. We demonstrate the coordinated importance of the B- and C-chains of the VILP in regulating this activity. Moreover, mutation of the glycine following the first cysteine in the B-chain of IGF-1 to serine, in concert with substitution to the connecting peptide of LCDV1-VILP, converted native IGF-1 to a high potency antagonist. Conclusions: The results reveal novel aspects in ligand-receptor interactions at the IGF-1 receptor and identify a set of antagonists of potential medicinal importance.
MeSH term(s)	Humans ; Iridoviridae/chemistry ; Neuropeptides/chemistry ; Neuropeptides/pharmacology ; Receptor, IGF Type 1/antagonists & inhibitors ; Receptor, IGF Type 1/metabolism
Chemical Substances	IGF1R protein, human ; Neuropeptides ; insulin-related neuropeptide ; Receptor, IGF Type 1 (EC 2.7.10.1)
Language	English
Publishing date	2021-08-13
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2708735-9
ISSN	2212-8778 ; 2212-8778
ISSN (online)	2212-8778
ISSN	2212-8778
DOI	10.1016/j.molmet.2021.101316
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Article ; Online: Viruses and Metabolism: The Effects of Viral Infections and Viral Insulins on Host Metabolism.

Girdhar, Khyati / Powis, Amaya / Raisingani, Amol / Chrudinová, Martina / Huang, Ruixu / Tran, Tu / Sevgi, Kaan / Dogus Dogru, Yusuf / Altindis, Emrah

Annual review of virology

2022 Volume 8, Issue 1, Page(s) 373–391

Abstract: Over the past decades, there have been tremendous efforts to understand the cross-talk between viruses and host metabolism. Several studies have elucidated the mechanisms through which viral infections manipulate metabolic pathways including glucose, ... ...

Abstract	Over the past decades, there have been tremendous efforts to understand the cross-talk between viruses and host metabolism. Several studies have elucidated the mechanisms through which viral infections manipulate metabolic pathways including glucose, fatty acid, protein, and nucleotide metabolism. These pathways are evolutionarily conserved across the tree of life and extremely important for the host's nutrient utilization and energy production. In this review, we focus on host glucose, glutamine, and fatty acid metabolism and highlight the pathways manipulated by the different classes of viruses to increase their replication. We also explore a new system of viral hormones in which viruses mimic host hormones to manipulate the host endocrine system. We discuss viral insulin/IGF-1-like peptides and their potential effects on host metabolism. Together, these pathogenesis mechanisms targeting cellular signaling pathways create a multidimensional network of interactions between host and viral proteins. Defining and better understanding these mechanisms will help us to develop new therapeutic tools to prevent and treat viral infections.
MeSH term(s)	Glycolysis ; Host-Pathogen Interactions ; Humans ; Insulins/pharmacology ; Virus Diseases/drug therapy ; Virus Replication ; Viruses
Chemical Substances	Insulins
Language	English
Publishing date	2022-02-09
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2764224-0
ISSN	2327-0578 ; 2327-056X
ISSN (online)	2327-0578
ISSN	2327-056X
DOI	10.1146/annurev-virology-091919-102416
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