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Article ; Online: Inhibition of Polyamine Catabolism Reduces Cellular Senescence.

Uemura, Takeshi / Matsunaga, Miki / Yokota, Yuka / Takao, Koichi / Furuchi, Takemitsu

International journal of molecular sciences

2023 Volume 24, Issue 17

Abstract: The aging of the global population has necessitated the identification of effective anti-aging technologies based on scientific evidence. Polyamines (putrescine, spermidine, and spermine) are essential for cell growth and function. Age-related reductions ...

Abstract	The aging of the global population has necessitated the identification of effective anti-aging technologies based on scientific evidence. Polyamines (putrescine, spermidine, and spermine) are essential for cell growth and function. Age-related reductions in polyamine levels have been shown to be associated with reduced cognitive and physical functions. We have previously found that the expression of spermine oxidase (SMOX) increases with age; however, the relationship between SMOX expression and cellular senescence remains unclear. Therefore, we investigated the relationship between increased SMOX expression and cellular senescence using human-liver-derived HepG2 cells. Intracellular spermine levels decreased and spermidine levels increased with the serial passaging of cells (aged cells), and aged cells showed increased expression of SMOX. The levels of acrolein-conjugated protein, which is produced during spermine degradation, also increases. Senescence-associated β-gal activity was increased in aged cells, and the increase was suppressed by MDL72527, an inhibitor of acetylpolyamine oxidase (AcPAO) and SMOX, both of which are enzymes that catalyze polyamine degradation. DNA damage accumulated in aged cells and MDL72527 reduced DNA damage. These results suggest that the SMOX-mediated degradation of spermine plays an important role in cellular senescence. Our results demonstrate that cellular senescence can be controlled by inhibiting spermine degradation using a polyamine-catabolizing enzyme inhibitor.
MeSH term(s)	Humans ; Spermidine/pharmacology ; Spermine/pharmacology ; Cellular Senescence ; Aging ; Polyamines
Chemical Substances	Spermidine (U87FK77H25) ; Spermine (2FZ7Y3VOQX) ; Polyamines
Language	English
Publishing date	2023-08-29
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/ijms241713397
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Article ; Online: Caldomycin, a new guanidopolyamine produced by a novel agmatine homocoupling enzyme involved in homospermidine biosynthesis.

Kobayashi, Teruyuki / Sakamoto, Akihiko / Hisano, Tamao / Kashiwagi, Keiko / Igarashi, Kazuei / Takao, Koichi / Uemura, Takeshi / Furuchi, Takemitsu / Sugita, Yoshiaki / Moriya, Toshiyuki / Oshima, Tairo / Terui, Yusuke

Scientific reports

2024 Volume 14, Issue 1, Page(s) 7566

Abstract: An extreme thermophilic bacterium, Thermus thermophilus produces more than 20 unusual polyamines, but their biosynthetic pathways, including homospermidine, are not yet fully understood. Two types of homospermidine synthases have been identified in ... ...

Abstract	An extreme thermophilic bacterium, Thermus thermophilus produces more than 20 unusual polyamines, but their biosynthetic pathways, including homospermidine, are not yet fully understood. Two types of homospermidine synthases have been identified in plants and bacteria, which use spermidine and putrescine or two molecules of putrescine as substrates. However, homospermidine synthases with such substrate specificity have not been identified in T. thermophilus. Here we identified a novel agmatine homocoupling enzyme that is involved in homospermidine biosynthesis in T. thermophilus. The reaction mechanism is different from that of a previously described homospermidine synthase, and involves conjugation of two molecules of agmatine, which produces a diamidino derivative of homospermidine (caldomycin) as an immediate precursor of homospermidine. We conclude that there is a homospermidine biosynthetic pathway from agmatine via caldomycin synthase followed by ureohydrolase in T. thermophilus. Furthermore, it is shown that caldomycin is a novel compound existing in nature.
MeSH term(s)	Putrescine/metabolism ; Agmatine/metabolism ; Polyamines/metabolism ; Spermidine/metabolism ; Plants/metabolism
Chemical Substances	Putrescine (V10TVZ52E4) ; Agmatine (70J407ZL5Q) ; Polyamines ; Spermidine (U87FK77H25)
Language	English
Publishing date	2024-03-30
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-024-58296-0
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Article ; Online: Occurrence of penta-amines, hexa-amines and N-methylated polyamines in unicellular eukaryotic organisms belonging to the phyla Heterokontophyta and Labyrinthulomycota of the subdomain Stramenopiles.

Hamana, Koei / Furuchi, Takemitsu / Nakamura, Tsuzuri / Hayashi, Hidenori / Niitsu, Masaru

The Journal of general and applied microbiology

2017 Volume 62, Issue 6, Page(s) 320–325

MeSH term(s)	Amines/chemistry ; Amines/isolation & purification ; Chromatography, Gas ; Culture Media/chemistry ; Polyamines/chemistry ; Polyamines/isolation & purification ; Stramenopiles/chemistry ; Stramenopiles/growth & development
Chemical Substances	Amines ; Culture Media ; Polyamines
Language	English
Publishing date	2017-01-25
Publishing country	Japan
Document type	Journal Article
ZDB-ID	218355-9
ISSN	1349-8037 ; 0022-1260
ISSN (online)	1349-8037
ISSN	0022-1260
DOI	10.2323/jgam.2016.05.001
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Article ; Online: Polyamines produced by an extreme thermophile are essential for cell growth at high temperature.

Sakamoto, Akihiko / Tamakoshi, Masatada / Moriya, Toshiyuki / Oshima, Tairo / Takao, Koichi / Sugita, Yoshiaki / Furuchi, Takemitsu / Niitsu, Masaru / Uemura, Takeshi / Igarashi, Kazuei / Kashiwagi, Keiko / Terui, Yusuke

Journal of biochemistry

2022 Volume 172, Issue 2, Page(s) 109–115

Abstract: An extreme thermophile, Thermus thermophilus grows at an optimum temperature of around 70°C and produces 16 different polyamines including long-chain and branched-chain polyamines. We found that the composition of polyamines in the thermophile cells ... ...

Abstract	An extreme thermophile, Thermus thermophilus grows at an optimum temperature of around 70°C and produces 16 different polyamines including long-chain and branched-chain polyamines. We found that the composition of polyamines in the thermophile cells changes with culture temperature. Long-chain and branched-chain polyamines (unusual polyamines) were increased in the cells grown at high temperature such as 80°C, but they were minor components in the cells grown at relatively lower temperature such as 60°C. The effects of polyamines on cell growth were studied using T. thermophilus HB8 ΔspeA deficient in arginine decarboxylase. Cell growth of this mutant strain was significantly decreased at 70°C. This mutant strain cannot produce polyamines and grows poorly at 75°C. It was also determined whether polyamines are directly involved in protecting DNA from DNA double-strand breaks (DSBs) induced by heat. Polyamines protected DNA against double-strand breaks. Therefore, polyamines play essential roles in cell growth at extremely high temperature through maintaining a functional conformation of DNA against DSBs and depurination.
MeSH term(s)	DNA ; Hot Temperature ; Polyamines ; Temperature ; Thermus thermophilus
Chemical Substances	Polyamines ; DNA (9007-49-2)
Language	English
Publishing date	2022-07-08
Publishing country	England
Document type	Journal Article
ZDB-ID	218073-x
ISSN	1756-2651 ; 0021-924X
ISSN (online)	1756-2651
ISSN	0021-924X
DOI	10.1093/jb/mvac048
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Article ; Online: Occurrence of two novel linear penta-amines, pyropentamine and homopyropentamine, in extremely thermophilic Thermus composti.

Hamana, Koei / Furuchi, Takemitsu / Hayashi, Hidenori / Itoh, Takashi / Ohkuma, Moriya / Niitsu, Masaru

The Journal of general and applied microbiology

2017 Volume 62, Issue 6, Page(s) 334–339

MeSH term(s)	Amines/analysis ; Amines/chemistry ; Chromatography, High Pressure Liquid ; Escherichia coli/genetics ; Hot Temperature ; Species Specificity ; Thermus/chemistry ; Thermus/isolation & purification ; Thermus/metabolism
Chemical Substances	Amines
Language	English
Publishing date	2017-01-25
Publishing country	Japan
Document type	Journal Article
ZDB-ID	218355-9
ISSN	1349-8037 ; 0022-1260
ISSN (online)	1349-8037
ISSN	0022-1260
DOI	10.2323/jgam.2016.05.007
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Article ; Online: Identification of a novel acetylated form of branched-chain polyamine from a hyperthermophilic archaeon Thermococcus kodakarensis.

Hidese, Ryota / Im, Ki-Hwan / Kobayashi, Masaki / Niitsu, Masaru / Furuchi, Takemitsu / Fujiwara, Shinsuke

Bioscience, biotechnology, and biochemistry

2017 Volume 81, Issue 9, Page(s) 1845–1849

Abstract: Long/branched-chain polyamines are unique polycations found in thermophiles. The hyperthermophilic archaeon Thermococcus kodakarensis contains spermidine and a branched-chain polyamine, ... ...

Abstract	Long/branched-chain polyamines are unique polycations found in thermophiles. The hyperthermophilic archaeon Thermococcus kodakarensis contains spermidine and a branched-chain polyamine, N
MeSH term(s)	Acetylation ; Intracellular Space/metabolism ; Polyamines/chemistry ; Polyamines/isolation & purification ; Polyamines/metabolism ; Temperature ; Thermococcus/cytology ; Thermococcus/metabolism ; Thermococcus/physiology
Chemical Substances	Polyamines
Language	English
Publishing date	2017-09
Publishing country	England
Document type	Journal Article
ZDB-ID	1106450-x
ISSN	1347-6947 ; 0916-8451
ISSN (online)	1347-6947
ISSN	0916-8451
DOI	10.1080/09168451.2017.1345616
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Article: Identification of a novel acetylated form of branched-chain polyamine from a hyperthermophilic archaeon Thermococcus kodakarensis

Hidese, Ryota / Im, Ki-Hwan / Kobayashi, Masaki / Niitsu, Masaru / Furuchi, Takemitsu / Fujiwara, Shinsuke

Bioscience, biotechnology, and biochemistry. 2017 Sept. 2, v. 81, no. 9

2017

Abstract	Long/branched-chain polyamines are unique polycations found in thermophiles. The hyperthermophilic archaeon Thermococcus kodakarensis contains spermidine and a branched-chain polyamine, N⁴-bis(aminopropyl)spermidine, as major polyamines. The metabolic pathways associated with branched-chain polyamines remain unknown. Here, we used gas chromatography and liquid chromatography-tandem mass spectrometry analyses to identify a new acetylated polyamine, N⁴-bis(aminopropyl)-N¹-acetylspermidine, from T. kodakarensis; this polyamine was not found in other micro-organisms. The amounts of branched-chain polyamine and its acetylated form increased with temperature, indicating that branched-chain polyamines are important for growth at higher temperatures. The amount of quaternary acetylated polyamine produced was associated with the amount of N⁴-bis(aminopropyl)spermidine in the cell. The ratio of acetylated to non-acetylated forms was higher in the stationary phase than in the logarithmic growth phase under high-temperature stress condition.
Keywords	Thermococcus kodakarensis ; biotechnology ; gas chromatography ; liquid chromatography ; spermidine ; tandem mass spectrometry ; temperature ; thermophiles
Language	English
Dates of publication	2017-0902
Size	p. 1845-1849.
Publishing place	Taylor & Francis
Document type	Article
Note	NAL-light
ZDB-ID	1106450-x
ISSN	1347-6947 ; 0916-8451
ISSN (online)	1347-6947
ISSN	0916-8451
DOI	10.1080/09168451.2017.1345616
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Article: [Role of isomerized protein repair enzyme, PIMT, in cellular functions].

Furuchi, Takemitsu / Homma, Hiroshi

Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan

2007 Volume 127, Issue 12, Page(s) 1927–1936

Abstract: Proteins are subject to various types of spontaneous modifications that can disrupt their structures with sometimes adverse affects on biological activity. The formation of L-isoaspartyl (or D-aspartyl) residues, through either the deamidation of ... ...

Abstract	Proteins are subject to various types of spontaneous modifications that can disrupt their structures with sometimes adverse affects on biological activity. The formation of L-isoaspartyl (or D-aspartyl) residues, through either the deamidation of asparagine or dehydration of aspartate, is one of the most frequent types of deterioration occurring under physiological conditions. Protein L-isoaspartate/D-aspartate o-methyltransferase (PIMT) is a conserved and ubiquitous enzyme that participates in the repair of various isomerized proteins. PIMT catalyzes the transfer of the methyl group of S-adenosyl-L-methionine onto the alpha-carboxyl group of an L-isoaspartyl (or the beta-carboxyl group of an D-aspartyl) residue, which initiates the conversion of this residue to an L-aspartyl residue. PIMT-deficient mice have been shown to die at a mean age of 42 days from progressive epileptic seizures with grand mal and myoclonus. Although PIMT-deficiency clearly leads to the accumulation of isomerized proteins, it is currently unclear how this causes progressive epilepsy in PIMT-deficient mice. As a first step towards understanding this, we developed a new assay to measure PIMT activity in cell lysates. Additionally, we isolated PIMT knockdown cells from HEK293 cells that were stably transfected with a PIMT small interfering RNA expression vector. PIMT activities were significantly decreased in the PIMT knockdown cells, and analysis of the transfectants revealed that MEK and ERK were hyperactivated after cell stimulation with epidermal growth factor (EGF). These results indicate that the ability to repair L-isoaspartyl-(or D-aspartyl-) containing proteins is important for the maintenance of normal MEK-ERK signaling.
MeSH term(s)	Animals ; Cell Physiological Phenomena ; D-Aspartic Acid ; Extracellular Signal-Regulated MAP Kinases/physiology ; Isoaspartic Acid ; MAP Kinase Signaling System/physiology ; Mice ; Mitogen-Activated Protein Kinase Kinases/physiology ; Protein D-Aspartate-L-Isoaspartate Methyltransferase/physiology ; Protein Isoforms/chemistry ; Protein Isoforms/metabolism
Chemical Substances	Isoaspartic Acid ; Protein Isoforms ; D-Aspartic Acid (4SR0Q8YD1X) ; Protein D-Aspartate-L-Isoaspartate Methyltransferase (EC 2.1.1.77) ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase Kinases (EC 2.7.12.2)
Language	Japanese
Publishing date	2007-07-06
Publishing country	Japan
Document type	English Abstract ; Journal Article ; Review
ZDB-ID	200514-1
ISSN	1347-5231 ; 0031-6903 ; 0372-7750 ; 0919-2085 ; 0919-2131
ISSN (online)	1347-5231
ISSN	0031-6903 ; 0372-7750 ; 0919-2085 ; 0919-2131
DOI	10.1248/yakushi.127.1927
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Zs.A 643: Show issues

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Article: Free D-aspartate in mammals.

Furuchi, Takemitsu / Homma, Hiroshi

Biological & pharmaceutical bulletin

2005 Volume 28, Issue 9, Page(s) 1566–1570

Abstract: D-Aspartate (D-Asp) is an endogenous amino acid present in nervous and endocrine tissues in mammals. A high concentration of D-Asp is observed in embryos, which disappears in nervous tissues after delivery, but increases temporarily in endocrine glands, ... ...

Abstract	D-Aspartate (D-Asp) is an endogenous amino acid present in nervous and endocrine tissues in mammals. A high concentration of D-Asp is observed in embryos, which disappears in nervous tissues after delivery, but increases temporarily in endocrine glands, particularly in the pituitary, pineal and adrenal glands at the specific stages. In the pineal gland, D-Asp that is apparently derived from other tissues suppresses melatonin secretion from parenchymal cells. Additionally, D-Asp levels increase in the testis just before birth and during maturation. The amino acid is presumed to be synthesized by the pituitary gland and testis. In the testis, D-Asp produced inside the seminiferous tubules acts on Leydig cells following release to enhance testosterone synthesis by activating the expression of Steroidogenic Acute Regulatory protein. Mammalian cells appear to contain all the molecular components required to regulate D-Asp homeostasis, as they can synthesize, release, take up, and degrade the amino acid. These findings collectively indicate that D-Asp is a novel type of messenger in the mammalian body.
MeSH term(s)	Animals ; Aspartic Acid/analysis ; Aspartic Acid/biosynthesis ; Aspartic Acid/metabolism ; Aspartic Acid/physiology ; Humans ; Mammals/physiology
Chemical Substances	Aspartic Acid (30KYC7MIAI)
Language	English
Publishing date	2005-03-15
Publishing country	Japan
Document type	Journal Article ; Review
ZDB-ID	1150271-x
ISSN	1347-5215 ; 0918-6158
ISSN (online)	1347-5215
ISSN	0918-6158
DOI	10.1248/bpb.28.1566
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Zs.A 1474: Show issues

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Article: The ubiquitin-conjugating enzymes, Ubc4 and Cdc34, mediate cadmium resistance in budding yeast through different mechanisms.

Hwang, Gi-Wook / Furuchi, Takemitsu / Naganuma, Akira

Life sciences

2008 Volume 82, Issue 23-24, Page(s) 1182–1185

Abstract: The expression of the genes encoding the ubiquitin-conjugating enzymes, Ubc4, Ubc5, and Ubc7, has been reported to be induced by cadmium in budding yeast. In contrast, we have reported that the overexpression of Cdc34, another ubiquitin-conjugating ... ...

Abstract	The expression of the genes encoding the ubiquitin-conjugating enzymes, Ubc4, Ubc5, and Ubc7, has been reported to be induced by cadmium in budding yeast. In contrast, we have reported that the overexpression of Cdc34, another ubiquitin-conjugating enzyme, confers resistance to cadmium. In the present study, we examined the effects of overexpression of Ubc4, Ubc5, or Ubc7 on the sensitivity of budding yeast to cadmium. We found that yeast cells that overexpressed Ubc4, but not Ubc5 or Ubc7, showed similar cadmium resistance as yeast cells that overexpressed Cdc34. The ubiquitination levels of cellular proteins were significantly increased by overexpression of Ubc4 as well as by Cdc34. As previously reported, yeast cells overexpressing Cdc34 were resistant to cadmium even in the presence of the proteasome inhibitor MG132. However, the acquired resistance to cadmium by overexpression of Ubc4 was not observed in the presence of MG132. Cdc34 overexpression has been shown to inactivate the transcriptional activity of Met4 by accelerating its ubiquitination and to reduce expression of the MET25 gene, a target gene of Met4. Unlike Cdc34, overexpression of Ubc4 did not affect the expression of the MET25 gene. These findings suggest that the mechanism of acquired resistance to cadmium by overexpression of Ubc4 is different from that of Cdc34 and that Ubc4 confers resistance to cadmium by ubiquitination of proteins other than Met4 and accelerates the degradation of these proteins in the proteasomes.
MeSH term(s)	Anaphase-Promoting Complex-Cyclosome ; Cadmium Chloride/toxicity ; Cloning, Molecular ; Cysteine Proteinase Inhibitors/pharmacology ; Dose-Response Relationship, Drug ; Drug Resistance, Fungal/genetics ; Environmental Pollutants/toxicity ; Leupeptins/pharmacology ; Plasmids ; Saccharomyces cerevisiae/drug effects ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/biosynthesis ; Ubiquitin-Conjugating Enzymes/biosynthesis ; Ubiquitin-Protein Ligase Complexes/biosynthesis ; beta-Galactosidase/metabolism
Chemical Substances	Cysteine Proteinase Inhibitors ; Environmental Pollutants ; Leupeptins ; Saccharomyces cerevisiae Proteins ; CDC34 protein, S cerevisiae (EC 2.3.2.23) ; Ubc4 protein, S cerevisiae (EC 2.3.2.23) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Ubiquitin-Protein Ligase Complexes (EC 2.3.2.23) ; Anaphase-Promoting Complex-Cyclosome (EC 2.3.2.27) ; beta-Galactosidase (EC 3.2.1.23) ; Cadmium Chloride (J6K4F9V3BA) ; benzyloxycarbonylleucyl-leucyl-leucine aldehyde (RF1P63GW3K)
Language	English
Publishing date	2008-04-11
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3378-9
ISSN	1879-0631 ; 0024-3205
ISSN (online)	1879-0631
ISSN	0024-3205
DOI	10.1016/j.lfs.2008.04.002
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