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Article ; Online: Rapid Detection and Quantification of Patulin and Citrinin Contamination in Fruits.

Sadhasivam, Sudharsan / Barda, Omer / Zakin, Varda / Reifen, Ram / Sionov, Edward

2021 Volume 26, Issue 15

Abstract: Patulin (PAT) and citrinin (CTN) are the most common mycotoxins produced ... ...

Abstract	Patulin (PAT) and citrinin (CTN) are the most common mycotoxins produced by
MeSH term(s)	Aspergillus/metabolism ; Chromatography, High Pressure Liquid/economics ; Chromatography, High Pressure Liquid/methods ; Citrinin/analysis ; Cost-Benefit Analysis ; Data Accuracy ; Food Contamination/analysis ; Food Quality ; Fruit/chemistry ; Limit of Detection ; Malus/chemistry ; Patulin/analysis ; Penicillium/metabolism ; Pyrus/chemistry ; Time Factors
Chemical Substances	Citrinin (3S697X6SNZ) ; Patulin (95X2BV4W8R)
Language	English
Publishing date	2021-07-27
Publishing country	Switzerland
Document type	Journal Article ; Validation Study
ZDB-ID	1413402-0
ISSN	1420-3049 ; 1431-5165 ; 1420-3049
ISSN (online)	1420-3049
ISSN	1431-5165 ; 1420-3049
DOI	10.3390/molecules26154545
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Zs.MO 81: Show issues

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Article ; Online: Ensiling process and pomegranate peel extract as a natural additive in potential prevention of fungal and mycotoxin contamination in silage.

Sadhasivam, Sudharsan / Marshi, Rula / Barda, Omer / Zakin, Varda / Britzi, Malka / Gamliel, Abraham / Sionov, Edward

Toxicology reports

2022 Volume 9, Page(s) 1557–1565

Abstract: A study was conducted on six animal feed centers in Israel where fungal and mycotoxin presence was examined in maize and wheat silages. Fumonisin mycotoxins ... ...

Abstract	A study was conducted on six animal feed centers in Israel where fungal and mycotoxin presence was examined in maize and wheat silages. Fumonisin mycotoxins FB
Language	English
Publishing date	2022-07-25
Publishing country	Ireland
Document type	Journal Article
ZDB-ID	2805786-7
ISSN	2214-7500 ; 2214-7500
ISSN (online)	2214-7500
ISSN	2214-7500
DOI	10.1016/j.toxrep.2022.07.011
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Article: Dissecting the role of crosstalk between glioblastoma subpopulations in tumor cell spreading.

Jubran, Maria R / Rubinstein, Ariel M / Cojocari, Irina / Adejumobi, Ibukun Adesoji / Mogilevsky, Maxim / Tibi, Sama / Sionov, Ronit V / Verreault, Maïté / Idbaih, Ahmed / Karni, Rotem / Kravchenko-Balasha, Nataly

Oncogenesis

2020 Volume 9, Issue 2, Page(s) 11

Abstract: Glioblastoma (GBM) is a highly infiltrative brain cancer, which is thus difficult to operate. GBM cells frequently harbor Epidermal Growth Factor Receptor amplification (EGFRwt) and/or activating mutation (EGFRvIII), generating at least two different ... ...

Abstract	Glioblastoma (GBM) is a highly infiltrative brain cancer, which is thus difficult to operate. GBM cells frequently harbor Epidermal Growth Factor Receptor amplification (EGFRwt) and/or activating mutation (EGFRvIII), generating at least two different cellular subpopulations within the tumor. We examined the relationship between the diffusive architectures of GBM tumors and the paracrine interactions between those subpopulations. Our aim was to shed light on what drives GBM cells to reach large cell-cell distances, and whether this characteristic can be manipulated. We established a methodology that quantifies the infiltration abilities of cancer cells through computation of cell-cell separation distance distributions in 3D. We found that aggressive EGFRvIII cells modulate the migration and infiltrative properties of EGFRwt cells. EGFRvIII cells secrete HGF and IL6, leading to enhanced activity of Src protein in EGFRwt cells, and rendering EGFRwt cells higher velocity and augmented ability to spread. Src inhibitor, dasatinib, at low non-toxic concentrations, reduced the infiltrative properties of EGFRvIII/EGFRwt neurospheres. Furthermore, dasatinib treatment induced compact multicellular microstructure packing of EGFRvIII/EGFRwt cells, impairing their ability to spread. Prevention of cellular infiltration or induction of compact microstructures may assist the detection of GBM tumors and tumor remnants in the brains and improve their surgical removal.
Language	English
Publishing date	2020-02-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	2674437-5
ISSN	2157-9024
ISSN	2157-9024
DOI	10.1038/s41389-020-0199-y
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Article: The cellular response to p53: the decision between life and death.

Sionov, R V / Haupt, Y

Oncogene

1999 Volume 18, Issue 45, Page(s) 6145–6157

Abstract: The p53 tumor suppressor protein plays a crucial role in regulating cell growth following exposure to various stress stimuli. p53 induces either growth arrest, which prevents the replication of damaged DNA, or programmed cell death (apoptosis), which is ... ...

Abstract	The p53 tumor suppressor protein plays a crucial role in regulating cell growth following exposure to various stress stimuli. p53 induces either growth arrest, which prevents the replication of damaged DNA, or programmed cell death (apoptosis), which is important for eliminating defective cells. Whether the cell enters growth arrest or undergoes apoptosis, depends on the final integration of incoming signals with antagonistic effects on cell growth. Many factors affect the cellular response to activated p53. These include the cell type, the oncogenic status of the cell with emphasis on the Rb/E2F balance, the extracellular growth and survival stimuli, the intensity of the stress signals, the level of p53 expression and the interaction of p53 with specific proteins. p53 is regulated both at the levels of protein stability and biochemical activities. This complex regulation is mediated by a range of viral and cellular proteins. This review discusses this intriguing complexity which affects the cell response to p53 activation.
MeSH term(s)	Animals ; Apoptosis/physiology ; Cell Cycle/physiology ; Cell Survival/physiology ; Enzyme Activation ; Gene Expression Regulation, Enzymologic ; Humans ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism
Chemical Substances	Tumor Suppressor Protein p53
Language	English
Publishing date	1999-11-01
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	639046-8
ISSN	1476-5594 ; 0950-9232
ISSN (online)	1476-5594
ISSN	0950-9232
DOI	10.1038/sj.onc.1203130
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Zs.A 2218: Show issues

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Article: Apoptosis by p53: mechanisms, regulation, and clinical implications.

Sionov, R V / Haupt, Y

Springer seminars in immunopathology

1998 Volume 19, Issue 3, Page(s) 345–362

MeSH term(s)	Apoptosis/genetics ; Genes, p53/physiology ; Humans
Language	English
Publishing date	1998
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	6177-3
ISSN	1432-2196 ; 0344-4325 ; 0172-6641
ISSN (online)	1432-2196
ISSN	0344-4325 ; 0172-6641
DOI	10.1007/BF00787230
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Zs.A 1425: Show issues

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Article: Calcium- and calmodulin-dependent PMA-activation of the CD44 adhesion molecule.

Sionov, R V / Naor, D

Cell adhesion and communication

1998 Volume 6, Issue 6, Page(s) 503–523

Abstract: The ability of the CD44 adhesion molecule to interact with its ligand hyaluronic acid (HA) is tightly regulated. CD44-positive mouse LB lymphoma cells are unable to bind HA unless activated by the tumor promoter phorbol 12-myristate 13-acetate (PMA). PMA ...

Abstract	The ability of the CD44 adhesion molecule to interact with its ligand hyaluronic acid (HA) is tightly regulated. CD44-positive mouse LB lymphoma cells are unable to bind HA unless activated by the tumor promoter phorbol 12-myristate 13-acetate (PMA). PMA causes a dose-dependent increase in both CD44 expression level and HA-binding capacity, with the binding of HA observed only above a threshold amount of CD44 molecules. This induction of HA-binding as well as the increase in CD44 expression are prevented by cycloheximide, suggesting a requirement for new additional CD44 molecules on the cell surface and/or cooperating proteins. In the present study, we have investigated which of the signal transduction pathways activated by PMA leads to the increased CD44 expression with subsequent acquisition of HA-binding capacity. By comparing the influence of each inhibitory agent on PMA-activated LB lymphoma cells versus that on a constitutive HA-binder cell line derived from LB cells (designated HA9 cells), we could distinguish between an effect on the PMA-activation phase and a one on the HA-binding phase. Our data show that the PMA-induced HA-binding could not be blocked by agents inhibiting protein kinase C (PKC) (staurosporine, sphingosine, polymyxin B, quercetin) or genestein, an inhibitor of tyrosine protein kinases. However, this PMA response was strongly inhibited by calmodulin antagonists (chlorpromazine, trifluoperazine, W-7) and the calcium blocker verapamil. The calmodulin antagonists inhibited the PMA-induced increase in CD44 expression on LB cells, but had no influence on the ability of the constitutive HA-binder HA9 cell line to interact with HA, indicating an effect on the PMA induction phase rather than on the binding itself. Verapamil also blocked the PMA-induced increase in CD44 expression on LB cells, but in addition it slightly reduced the ability of the HA9 cells to bind HA without affecting their CD44 expression level. In conclusion, our data suggest that CD44 activation by PMA is calcium and calmodulin dependent, rather than mediated by protein kinase C.
MeSH term(s)	Animals ; Calcium/metabolism ; Calcium Channel Blockers/pharmacology ; Calmodulin/antagonists & inhibitors ; Calmodulin/metabolism ; Cycloheximide/pharmacology ; Cytoskeleton ; Dose-Response Relationship, Drug ; Hyaluronan Receptors/metabolism ; Hyaluronic Acid/metabolism ; Ionomycin/pharmacology ; Ionophores/pharmacology ; Mice ; Mice, Inbred BALB C ; Protein Kinase C/antagonists & inhibitors ; Protein Kinase C/metabolism ; Suramin/pharmacology ; Tetradecanoylphorbol Acetate/pharmacology ; Tumor Cells, Cultured ; Verapamil/pharmacology
Chemical Substances	Calcium Channel Blockers ; Calmodulin ; Hyaluronan Receptors ; Ionophores ; Ionomycin (56092-81-0) ; Suramin (6032D45BEM) ; Hyaluronic Acid (9004-61-9) ; Cycloheximide (98600C0908) ; Verapamil (CJ0O37KU29) ; Protein Kinase C (EC 2.7.11.13) ; Tetradecanoylphorbol Acetate (NI40JAQ945) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	1998
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	916142-9
ISSN	1061-5385
ISSN	1061-5385
DOI	10.3109/15419069809010798
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Zs.A 4377: Show issues

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Article: Differential H-2 antigen expression in teratocarcinoma-fibroblast hybrids.

Sionov, R V / Gallily, R

Experimental and clinical immunogenetics

1995 Volume 12, Issue 4, Page(s) 238–244

Abstract: Embryo-derived teratocarcinoma cells, like early embryonic cells, do not express the classical MHC class I antigens. The mRNAs for both the H-2 alpha chain and beta2-microglobulin are also undetectable in these cells. We observed that upon fusion of H-2- ... ...

Abstract	Embryo-derived teratocarcinoma cells, like early embryonic cells, do not express the classical MHC class I antigens. The mRNAs for both the H-2 alpha chain and beta2-microglobulin are also undetectable in these cells. We observed that upon fusion of H-2-negative mouse P19 teratocarcinoma cells (H-2k allotype) with H-2-positive embryonic fibroblasts of C57BL/6 origin (H-2b allotype), teratocarcinoma-like cell hybrids were obtained which express the H-2Kb antigen derived from the embryonic fibroblasts, but not the H-2KkDk antigens of the teratocarcinoma. This finding demonstrates that the teratocarcinoma H-2 genes do not respond to the positive regulatory factors present in the hybrids. The H-2k allele was not lost during fusion, as shown by its expression in retinoic-acid-differentiated hybrids treated with interferon-gamma (10 U/ml, 4 days). H-2KkDk antigen expression could also be induced in the undifferentiated hybrids by treating the cells with the protein synthesis inhibitor cycloheximide (1-10 mu g/ml, 18 h), but not with the demethylating agent 5-azacytidine (5 mu M, 2-4 days). These data suggest the presence of a labile, negative regulating protein factor which selectively prevents the expression of the teratocarcinoma-derived H-2 antigens. When the level of this factor(s) is reduced, the teratocarcinoma H-2 genes are capable of responding to the positive regulatory factors.
MeSH term(s)	Animals ; Antigens, Neoplasm/drug effects ; Antigens, Neoplasm/genetics ; Azacitidine/pharmacology ; Cell Fusion/drug effects ; Cell Fusion/immunology ; Cycloheximide/pharmacology ; Fibroblasts/drug effects ; Fibroblasts/immunology ; Fibroblasts/metabolism ; Flow Cytometry ; Gene Expression Regulation, Neoplastic/drug effects ; Gene Expression Regulation, Neoplastic/immunology ; H-2 Antigens/drug effects ; H-2 Antigens/genetics ; Hybridomas/chemistry ; Hybridomas/immunology ; Interferon-gamma/pharmacology ; Mice ; Mice, Inbred C57BL ; Teratocarcinoma/genetics ; Teratocarcinoma/immunology
Chemical Substances	Antigens, Neoplasm ; H-2 Antigens ; H-2Kb protein, mouse ; Interferon-gamma (82115-62-6) ; Cycloheximide (98600C0908) ; Azacitidine (M801H13NRU)
Language	English
Publishing date	1995
Publishing country	Switzerland
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	605860-7
ISSN	0254-9670
ISSN	0254-9670
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Zs.A 1997: Show issues

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Article ; Online: TRPM2 Mediates Neutrophil Killing of Disseminated Tumor Cells.

Gershkovitz, Maya / Caspi, Yaki / Fainsod-Levi, Tanya / Katz, Ben / Michaeli, Janna / Khawaled, Saleh / Lev, Shaya / Polyansky, Lola / Shaul, Merav E / Sionov, Ronit V / Cohen-Daniel, Leonor / Aqeilan, Rami I / Shaul, Yoav D / Mori, Yasuo / Karni, Rotem / Fridlender, Zvi G / Binshtok, Alexander M / Granot, Zvi

Cancer research

2018 Volume 78, Issue 10, Page(s) 2680–2690

Abstract: Neutrophils play a critical role in cancer, with both protumor and antitumor neutrophil subpopulations reported. The antitumor neutrophil subpopulation has the capacity to kill tumor cells and limit metastatic spread, yet not all tumor cells are equally ... ...

Abstract	Neutrophils play a critical role in cancer, with both protumor and antitumor neutrophil subpopulations reported. The antitumor neutrophil subpopulation has the capacity to kill tumor cells and limit metastatic spread, yet not all tumor cells are equally susceptible to neutrophil cytotoxicity. Because cells that evade neutrophils have greater chances of forming metastases, we explored the mechanism neutrophils use to kill tumor cells. Neutrophil cytotoxicity was previously shown to be mediated by secretion of H
MeSH term(s)	Animals ; Breast Neoplasms/pathology ; CRISPR-Cas Systems/genetics ; Calcium/metabolism ; Calcium Channels/metabolism ; Cell Line, Tumor ; Cell Proliferation/genetics ; Female ; Humans ; Hydrogen Peroxide/metabolism ; Mice ; Mice, Inbred BALB C ; Neoplastic Cells, Circulating/immunology ; Neoplastic Cells, Circulating/pathology ; Neutrophils/immunology ; Neutrophils/metabolism ; TRPM Cation Channels/genetics ; TRPM Cation Channels/metabolism
Chemical Substances	Calcium Channels ; TRPM Cation Channels ; TRPM2 protein, mouse ; Hydrogen Peroxide (BBX060AN9V) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2018-02-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-17-3614
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Uh III Zs.135/5: Show issues

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Article: The unique killing of embryo-derived teratocarcinoma cells by nonactivated murine macrophages is not due to a lack of H-2 antigen expression.

Sionov, R V / Gallily, R

Cellular immunology

1992 Volume 142, Issue 2, Page(s) 416–425

Abstract: It is well documented that activated macrophages, but not nonactivated ones, kill tumor cells in vitro without damaging normal cells. We, however, have previously shown that embryo-derived teratocarcinoma cells (F9, P19, PCC4) are efficiently killed by ... ...

Abstract	It is well documented that activated macrophages, but not nonactivated ones, kill tumor cells in vitro without damaging normal cells. We, however, have previously shown that embryo-derived teratocarcinoma cells (F9, P19, PCC4) are efficiently killed by nonactivated macrophages as well as by activated ones. Whereas other tumor cells are killed extracellularly by macrophages, we found that F9 teratocarcinoma cells are phagocytosed alive by macrophages and subsequently killed intracellularly by a process dependent on intact lysosomal function. Neither the H-2 antigens nor the mRNAs for the alpha-chain and beta 2-microglobulin are detectable in embryo-derived teratocarcinoma cells. An obvious explanation for this unique killing is that the nonactivated macrophages recognize and kill these cells due to their lack of class I MHC antigen expression, assuming that class I MHC gene products on the target cells switch off the cytolytic machinery of nonactivated macrophages. Our present findings demonstrate that there is no correlation between H-2 antigen expression on tumor cells and their susceptibility to killing by macrophages. Retinoic acid-differentiated F9 cells and P19 cells expressing H-2 antigen after exposure to MAF (IFN-gamma) were sensitive to the killing by nonactivated macrophages. Hybrids that arose from fusion of P19 teratocarcinoma cells with embryonal normal fibroblasts (C57BL/6), which displayed the morphology of embryonal carcinoma stem cells and expressed H-2 antigens, were also sensitive to the killing by nonactivated macrophages. On the other hand, the H-2-negative testicular 402AX teratocarcinoma cells and K1735P melanoma cells were both resistant to the killing by nonactivated macrophages. We concluded that the unique killing of embryo-derived teratocarcinoma cells by nonactivated murine macrophages is not related to a lack of H-2 antigen expression.
MeSH term(s)	Animals ; Cell Death ; Cell Differentiation ; Cytotoxicity Tests, Immunologic ; H-2 Antigens ; Lysosomes ; Macrophages/immunology ; Mice ; Mice, Inbred C57BL ; Phagocytosis ; Teratoma/immunology ; Tretinoin/pharmacology ; Tumor Cells, Cultured/drug effects
Chemical Substances	H-2 Antigens ; Tretinoin (5688UTC01R)
Language	English
Publishing date	1992-07
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80094-6
ISSN	1090-2163 ; 0008-8749
ISSN (online)	1090-2163
ISSN	0008-8749
DOI	10.1016/0008-8749(92)90301-5
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Zs.A 417: Show issues

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Article: Newly discovered ergot alkaloids in Sorghum ergot Claviceps africana occurring for the first time in Israel

Shimshoni, J.A / E. Sionov / M. Sulyok / O. Cuneah / R. Krska / S. Barel / Y. Meller Harel

Food chemistry. 2017 Mar. 15, v. 219

2017

Abstract: Sorghum ergot is a disease caused commonly by C. africana. In 2015, ergot was identified for the first time in sorghum fields in Israel, leading to measures of eradication and quarantine. The aims of the study were to identify the ergot species by ... ...

Abstract	Sorghum ergot is a disease caused commonly by C. africana. In 2015, ergot was identified for the first time in sorghum fields in Israel, leading to measures of eradication and quarantine. The aims of the study were to identify the ergot species by molecular and ergot alkaloid profile analysis, to determine the ergot alkaloid profile in pure honeydew and in infected sorghum silages and to estimate the safety of sorghum silages as a feed source. C. africana was rapidly and reliably identified by microscopical and molecular analysis. Dihydroergosine was identified as the major ergot alkaloid. Dihydrolysergol and dihydroergotamine were identified for the first time as significant ergot alkaloid components within the C. africana sclerotia, thereby providing for the first time a proof for the natural occurrence of dihydroergotamine. The sorghum silages were found to be safe for feed consumption, since the ergot alkaloids and the regulated mycotoxins were below their regulated limits.
Keywords	Claviceps ; ergot ; ergot alkaloids ; feed intake ; honeydew ; mycotoxins ; quarantine ; sclerotia ; Sorghum (Poaceae) ; sorghum silage ; Israel
Language	English
Dates of publication	2017-0315
Size	p. 459-467.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	243123-3
ISSN	1873-7072 ; 0308-8146
ISSN (online)	1873-7072
ISSN	0308-8146
DOI	10.1016/j.foodchem.2016.09.182
Database	NAL-Catalogue (AGRICOLA)

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