LIVIVO - Search results -

Search results

Result 1 - 10 of total 215

Search options

Article ; Online: An Introduction to the Special Issue “Protein Glycation in Food, Nutrition, Health and Disease”

Naila Rabbani / Paul J. Thornalley

International Journal of Molecular Sciences, Vol 23, Iss 13053, p

2022 Volume 13053

Abstract: On 20–24 September 2021, leading researchers in the field of glycation met online at the 14th International Symposium on the Maillard Reaction (IMARS-14), hosted by the authors of this introductory editorial, who are from Doha, Qatar [.] ...

Abstract	On 20–24 September 2021, leading researchers in the field of glycation met online at the 14th International Symposium on the Maillard Reaction (IMARS-14), hosted by the authors of this introductory editorial, who are from Doha, Qatar [.]
Keywords	n/a ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Language	English
Publishing date	2022-10-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

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: Emerging Glycation-Based Therapeutics—Glyoxalase 1 Inducers and Glyoxalase 1 Inhibitors

Naila Rabbani / Paul J. Thornalley

International Journal of Molecular Sciences, Vol 23, Iss 2453, p

2022 Volume 2453

Abstract: ... related multidrug-resistant tumors. The prototype Glo1 inhibitor is prodrug S-p-bromobenzylglutathione ...

Abstract	The abnormal accumulation of methylglyoxal (MG) leading to increased glycation of protein and DNA has emerged as an important metabolic stress, dicarbonyl stress, linked to aging, and disease. Increased MG glycation produces inactivation and misfolding of proteins, cell dysfunction, activation of the unfolded protein response, and related low-grade inflammation. Glycation of DNA and the spliceosome contribute to an antiproliferative and apoptotic response of high, cytotoxic levels of MG. Glyoxalase 1 (Glo1) of the glyoxalase system has a major role in the metabolism of MG. Small molecule inducers of Glo1, Glo1 inducers, have been developed to alleviate dicarbonyl stress as a prospective treatment for the prevention and early-stage reversal of type 2 diabetes and prevention of vascular complications of diabetes. The first clinical trial with the Glo1 inducer, trans -resveratrol and hesperetin combination (tRES-HESP)—a randomized, double-blind, placebo-controlled crossover phase 2A study for correction of insulin resistance in overweight and obese subjects, was completed successfully. tRES-HESP corrected insulin resistance, improved dysglycemia, and low-grade inflammation. Cell permeable Glo1 inhibitor prodrugs have been developed to induce severe dicarbonyl stress as a prospective treatment for cancer—particularly for high Glo1 expressing-related multidrug-resistant tumors. The prototype Glo1 inhibitor is prodrug S-p-bromobenzylglutathione cyclopentyl diester (BBGD). It has antitumor activity in vitro and in tumor-bearing mice in vivo. In the National Cancer Institute human tumor cell line screen, BBGD was most active against the glioblastoma SNB-19 cell line. Recently, potent antitumor activity was found in glioblastoma multiforme tumor-bearing mice. High Glo1 expression is a negative survival factor in chemotherapy of breast cancer where adjunct therapy with a Glo1 inhibitor may improve treatment outcomes. BBGD has not yet been evaluated clinically. Glycation by MG now appears to be a pathogenic process that ...
Keywords	methylglyoxal ; glyoxalase ; dicarbonyl stress ; diabetes ; cancer chemotherapy ; malaria ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	610
Language	English
Publishing date	2022-02-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

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: Methylglyoxal, glyoxalases and the development of diabetic complications.

Thornalley, P J

Amino acids

2013 Volume 6, Issue 1, Page(s) 15–23

Abstract: The formation of the reactiveα,β-dicarbonyl metabolite, methylglyoxal, is increased during hyperglycaemia associated with diabetes mellitus. Methylglyoxal is metabolised to S-D-lactoylglutathione and D-lactate by the glyoxalase system and to ... ...

Abstract	The formation of the reactiveα,β-dicarbonyl metabolite, methylglyoxal, is increased during hyperglycaemia associated with diabetes mellitus. Methylglyoxal is metabolised to S-D-lactoylglutathione and D-lactate by the glyoxalase system and to hydroxyacetone (95%) and D-lactaldehyde by aldose reductase. Methylglyoxal and hydroxyacetone bind and modify protein, producing fluorescent products. Red blood cell activities of glyoxalase enzymes are risk factors for the development of clinical complications of diabetes. Aldose reductase inhibitors decrease the concentration of methylglyoxal in experimental diabetic rats to normal levels, aminoguanidine and L-arginine scavenge methylglyoxal; these effects may be involved in their prospective preventive therapy of diabetic complications. Biochemical and clinical evidence suggests that the metabolism of methylglyoxal in diabetes mellitus is linked to the development of diabetic complications. A causal relationship may involve modification of protein by methylglyoxal and hydroxyacetone.
Language	English
Publishing date	2013-11-05
Publishing country	Austria
Document type	Journal Article
ZDB-ID	1121341-3
ISSN	1438-2199 ; 0939-4451
ISSN (online)	1438-2199
ISSN	0939-4451
DOI	10.1007/BF00808119
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

Zs.A 3490: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

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.

Details ▾

Article ; Online: Autism Spectrum Disorders — in Search of Mechanistic Biomarkers

Rabbani N. / Thornalley P.J.

Аутизм и нарушение развития, Vol 17, Iss 1, Pp 15-

2019 Volume 23

Abstract: Autism spectrum disorders are a group of neuropsychiatric conditions of increasing prevalence. They are initially detected in early development of children. Diagnosis is currently made on the basis of clinical behaviour and cognition. Improvements in ... ...

Abstract	Autism spectrum disorders are a group of neuropsychiatric conditions of increasing prevalence. They are initially detected in early development of children. Diagnosis is currently made on the basis of clinical behaviour and cognition. Improvements in accuracy, timeliness and access to diagnosis to help manage the condition is high on the agenda of the autistic communities. A blood test may help for early-stage detection of autism spectrum disorders to focus support where required — particularly when symptoms are most challenging. This article discusses briefly the scientific basis of diagnosis of autism spectrum disorders and recent emergence of candidate blood tests for autism. We conclude that further validation and improvements in understanding of autism spectrum disorders are required to provide the scientific basis and classifier characteristics for accurate and reliable diagnosis by clinical chemistry blood test.
Keywords	blood test ; diagnosis ; proteomics ; autistic adults ; Internal medicine ; RC31-1245
Subject code	610
Language	Russian
Publishing date	2019-03-01T00:00:00Z
Publisher	Moscow State University of Psychology and Education
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

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: Hexokinase-2-Linked Glycolytic Overload and Unscheduled Glycolysis—Driver of Insulin Resistance and Development of Vascular Complications of Diabetes

Naila Rabbani / Mingzhan Xue / Paul J. Thornalley

International Journal of Molecular Sciences, Vol 23, Iss 2165, p

2022 Volume 2165

Abstract: The recent discovery of the glucose-induced stabilization of hexokinase-2 (HK2) to proteolysis in cell dysfunction in model hyperglycemia has revealed a likely key initiating factor contributing to the development of insulin resistance and vascular ... ...

Abstract	The recent discovery of the glucose-induced stabilization of hexokinase-2 (HK2) to proteolysis in cell dysfunction in model hyperglycemia has revealed a likely key initiating factor contributing to the development of insulin resistance and vascular complications in diabetes. Consequently, the increased flux of glucose metabolism without a change in the expression and activity of glycolytic enzymes produces a wave of increased glycolytic intermediates driving mitochondrial dysfunction and increased reactive oxygen species (ROS) formation, the activation of hexosamine and protein kinase C pathways, the increased formation of methylglyoxal-producing dicarbonyl stress, and the activation of the unfolded protein response. This is called HK2-linked glycolytic overload and unscheduled glycolysis. The conditions required to sustain this are GLUT1 and/or GLUT3 glucose uptake and the expression of HK2. A metabolic biomarker of its occurrence is the abnormally increased deposition of glycogen, which is produced by metabolic channeling when HK2 becomes detached from mitochondria. These conditions and metabolic consequences are found in the vasculature, kidneys, retina, peripheral nerves, and early-stage embryo development in diabetes and likely sustain the development of diabetic vascular complications and embryopathy. In insulin resistance, HK2-linked unscheduled glycolysis may also be established in skeletal muscle and adipose tissue. This may explain the increased glucose disposal by skeletal uptake in the fasting phase in patients with type 2 diabetes mellitus, compared to healthy controls, and the presence of insulin resistance in patients with type 1 diabetes mellitus. Importantly, glyoxalase 1 inducer— trans -resveratrol and hesperetin in combination (tRES-HESP)—corrected HK2-linked glycolytic overload and unscheduled glycolysis and reversed insulin resistance and improved vascular inflammation in overweight and obese subjects in clinical trial. Further studies are now required to evaluate tRES-HESP for the ...
Keywords	hexokinase-2 ; hyperglycemia ; glycolysis ; diabetes ; diabetic complications ; insulin resistance ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	571
Language	English
Publishing date	2022-02-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

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: Decreased methylglyoxal-mediated protein glycation in the healthy aging mouse model of ectopic expression of UCP1 in skeletal muscle.

Masania, Jinit / Wijten, Patrick / Keipert, Susanne / Ost, Mario / Klaus, Susanne / Rabbani, Naila / Thornalley, Paul J

Redox biology

2022 Volume 59, Page(s) 102574

Abstract: Mice with ectopic expression of uncoupling protein-1 (UCP1) in skeletal muscle exhibit a healthy aging phenotype with increased longevity and resistance to impaired metabolic health. This may be achieved by decreasing protein glycation by the reactive ... ...

Abstract	Mice with ectopic expression of uncoupling protein-1 (UCP1) in skeletal muscle exhibit a healthy aging phenotype with increased longevity and resistance to impaired metabolic health. This may be achieved by decreasing protein glycation by the reactive metabolite, methylglyoxal (MG). We investigated protein glycation and oxidative damage in skeletal muscle of mice with UCP1 expression under control of the human skeletal actin promoter (HSA-mUCP1) at age 12 weeks (young) and 70 weeks (aged). We found both young and aged HSA-mUCP1 mice had decreased advanced glycation endproducts (AGEs) formed from MG, lysine-derived N
MeSH term(s)	Humans ; Mice ; Animals ; Aged ; Infant ; Glycation End Products, Advanced/metabolism ; Lysine/metabolism ; Pyruvaldehyde/metabolism ; Maillard Reaction ; Healthy Aging ; Uncoupling Protein 1/metabolism ; Ectopic Gene Expression ; Proteins/metabolism ; Muscle, Skeletal/metabolism ; Tumor Suppressor Proteins/metabolism ; Ubiquitin-Protein Ligases/metabolism
Chemical Substances	Glycation End Products, Advanced ; Lysine (K3Z4F929H6) ; Pyruvaldehyde (722KLD7415) ; Uncoupling Protein 1 ; Proteins ; UCP1 protein, human ; HUWE1 protein, human (EC 2.3.2.26) ; Tumor Suppressor Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Ucp1 protein, mouse
Language	English
Publishing date	2022-12-06
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701011-9
ISSN	2213-2317 ; 2213-2317
ISSN (online)	2213-2317
ISSN	2213-2317
DOI	10.1016/j.redox.2022.102574
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Protein Glycation in Plants—An Under-Researched Field with Much Still to Discover

Naila Rabbani / Maryam Al-Motawa / Paul J. Thornalley

International Journal of Molecular Sciences, Vol 21, Iss 3942, p

2020 Volume 3942

Abstract: Recent research has identified glycation as a non-enzymatic post-translational modification of proteins in plants with a potential contributory role to the functional impairment of the plant proteome. Reducing sugars with a free aldehyde or ketone group ... ...

Abstract	Recent research has identified glycation as a non-enzymatic post-translational modification of proteins in plants with a potential contributory role to the functional impairment of the plant proteome. Reducing sugars with a free aldehyde or ketone group such as glucose, fructose and galactose react with the N-terminal and lysine side chain amino groups of proteins. A common early-stage glycation adduct formed from glucose is N ε -fructosyl-lysine (FL). Saccharide-derived reactive dicarbonyls are arginine residue-directed glycating agents, forming advanced glycation endproducts (AGEs). A dominant dicarbonyl is methylglyoxal—formed mainly by the trace-level degradation of triosephosphates, including through the Calvin cycle of photosynthesis. Methylglyoxal forms the major quantitative AGE, hydroimidazolone MG-H1. Glucose and methylglyoxal concentrations in plants change with the developmental stage, senescence, light and dark cycles and also likely biotic and abiotic stresses. Proteomics analysis indicates that there is an enrichment of the amino acid residue targets of glycation, arginine and lysine residues, in predicted functional sites of the plant proteome, suggesting the susceptibility of proteins to functional inactivation by glycation. In this review, we give a brief introduction to glycation, glycating agents and glycation adducts in plants. We consider dicarbonyl stress, the functional vulnerability of the plant proteome to arginine-directed glycation and the likely role of methylglyoxal-mediated glycation in the activation of the unfolded protein response in plants. The latter is linked to the recent suggestion of protein glycation in sugar signaling in plant metabolism. The overexpression of glyoxalase 1, which suppresses glycation by methylglyoxal and glyoxal, produced plants resistant to high salinity, drought, extreme temperature and other stresses. Further research to decrease protein glycation in plants may lead to improved plant growth and assist the breeding of plant varieties resistant to ...
Keywords	glycation ; advanced glycation end products (AGEs) ; methylglyoxal ; glyoxalase ; dicarbonyl stress ; unfolded protein response ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	580
Language	English
Publishing date	2020-05-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

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: Emerging role of thiamine therapy for prevention and treatment of early-stage diabetic nephropathy.

Rabbani, N / Thornalley, P J

Diabetes, obesity & metabolism

2011 Volume 13, Issue 7, Page(s) 577–583

Abstract: Thiamine supplementation may prevent and reverse early-stage diabetic nephropathy. This probably occurs by correcting diabetes-linked increased clearance of thiamine, maintaining activity and expression of thiamine pyrophosphate-dependent enzymes that ... ...

Abstract	Thiamine supplementation may prevent and reverse early-stage diabetic nephropathy. This probably occurs by correcting diabetes-linked increased clearance of thiamine, maintaining activity and expression of thiamine pyrophosphate-dependent enzymes that help counter the adverse effects of high glucose concentrations-particularly transketolase. Evidence from experimental and clinical studies suggests that metabolism and clearance of thiamine is disturbed in diabetes leading to tissue-specific thiamine deficiency in the kidney and other sites of development of vascular complications. Thiamine supplementation prevented the development of early-stage nephropathy in diabetic rats and reversed increased urinary albumin excretion in patients with type 2 diabetes and microalbuminuria in two recent clinical trials. The thiamine monophosphate prodrug, Benfotiamine, whilst preventing early-stage development of diabetic nephropathy experimentally, has failed to produce similar clinical effect. The probable explanations for this are discussed. Further definitive trials for prevention of progression of early-stage diabetic nephropathy by thiamine are now required.
MeSH term(s)	Albuminuria/complications ; Albuminuria/prevention & control ; Animals ; Diabetes Mellitus, Experimental/complications ; Diabetes Mellitus, Experimental/drug therapy ; Diabetes Mellitus, Type 2/complications ; Diabetes Mellitus, Type 2/drug therapy ; Diabetes Mellitus, Type 2/prevention & control ; Diabetic Nephropathies/drug therapy ; Diabetic Nephropathies/prevention & control ; Dietary Supplements ; Humans ; Rats ; Thiamine/pharmacokinetics ; Thiamine/therapeutic use
Chemical Substances	Thiamine (X66NSO3N35)
Language	English
Publishing date	2011-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1454944-x
ISSN	1463-1326 ; 1462-8902
ISSN (online)	1463-1326
ISSN	1462-8902
DOI	10.1111/j.1463-1326.2011.01384.x
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 5442: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: The enzymatic defence against glycation in health, disease and therapeutics: a symposium to examine the concept.

Thornalley, P J

Biochemical Society transactions

2003 Volume 31, Issue Pt 6, Page(s) 1341–1342

Abstract: Glycation of proteins, nucleotides and basic phospholipids by glucose, glyoxal, methylglyoxal, 3-deoxyglucosone and other saccharide derivatives is potentially damaging to the proteome and mutagenic. It is now recognized that there is an enzymatic ... ...

Abstract	Glycation of proteins, nucleotides and basic phospholipids by glucose, glyoxal, methylglyoxal, 3-deoxyglucosone and other saccharide derivatives is potentially damaging to the proteome and mutagenic. It is now recognized that there is an enzymatic defence against glycation--a group of enzymes that suppress the physiological levels of potent glycating agents and repair glycated proteins: glyoxalase I, aldehyde reductases and dehydrogenases, amadoriase and fructosamine 3-phosphokinase. The enzymatic defence against glycation influences morbidity and the efficiency of drug therapy in certain diseases. Improved understanding of the balance between glycation and the enzymatic anti-glycation defence will advance disease diagnosis and therapy.
MeSH term(s)	Glucose/metabolism ; Humans ; Therapeutics
Chemical Substances	Glucose (IY9XDZ35W2)
Language	English
Publishing date	2003-12
Publishing country	England
Document type	Congress ; Research Support, Non-U.S. Gov't
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/bst0311341
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 944: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Protecting the genome: defence against nucleotide glycation and emerging role of glyoxalase I overexpression in multidrug resistance in cancer chemotherapy.

Thornalley, P J

Biochemical Society transactions

2003 Volume 31, Issue Pt 6, Page(s) 1372–1377

Abstract: ... marked increases in triosephosphate concentration and increased formation of methylglyoxal. S - p ...

Abstract	Glycation of nucleotides in DNA forms AGEs (advanced glycation end-products). Nucleotide AGEs are: the imidazopurinone derivative dG-G [3-(2'-deoxyribosyl)-6,7-dihydro-6,7-dihydroxyimidazo[2,3-b]purin-9(8)one], CMdG ( N (2)-carboxymethyldeoxyguanosine) and gdC (5-glycolyldeoxycytidine) derived from glyoxal, dG-MG [6,7-dihydro-6,7-dihydroxy-6-methylimidazo-[2,3-b]purine-9(8)one], dG-MG(2) [ N (2),7-bis-(1-hydroxy-2-oxopropyl)deoxyguanosine] and CEdG [ N (2)-(1-carboxyethyl)deoxyguanosine] derived from methylglyoxal, and dG-3DG [ N (2)-(1-oxo-2,4,5,6-tetrahydroxyhexyl)deoxyguanosine] derived from 3-deoxyglucosone and others. Glyoxal and methylglyoxal induce multi-base deletions, and base-pair substitutions - mostly occurring at G:C sites with G:C-->C:G and G:C-->T:A transversions. Suppression of nucleotide glycation by glyoxalase I and aldehyde reductases and dehydrogenases, and base excision repair, protects and recovers DNA from damaging glycation. The effects of DNA glycation may be most marked in diabetes and uraemia. Mutations arising from DNA glycation may explain the link of non-dietary carbohydrate intake to incidence of colorectal cancer. Overexpression of glyoxalase I was found in drug-resistant tumour cells and may be an example of an undesirable effect of the enzymatic protection against DNA glycation. Experimental overexpression of glyoxalase I conferred resistance to drug-induced apoptosis. Glyoxalase I-mediated drug resistance was found in human leukaemia and lung carcinoma cells. Methylglyoxal-mediated glycation of DNA may contribute to the cytotoxicity of some antitumour agents as a consequence of depletion of NAD(+) by poly(ADP-ribose) polymerase, marked increases in triosephosphate concentration and increased formation of methylglyoxal. S - p -Bromobenzylglutathione cyclopentyl diester is a cell-permeable glyoxalase I inhibitor. It countered drug resistance and was a potent antitumour agent against lung and prostate carcinoma. Glyoxalase I overexpression was also found in invasive ovarian cancer and breast cancer.
MeSH term(s)	Antineoplastic Agents/therapeutic use ; DNA/metabolism ; DNA Repair ; Drug Resistance, Multiple ; Drug Resistance, Neoplasm ; Genome ; Glucose/metabolism ; Humans ; Lactoylglutathione Lyase/metabolism ; Mutagenesis ; Neoplasms/drug therapy
Chemical Substances	Antineoplastic Agents ; DNA (9007-49-2) ; Lactoylglutathione Lyase (EC 4.4.1.5) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2003-12
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/bst0311372
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 944: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

Full text online

More links

Kategorien

Inter-library loan at ZB MED

Full text online

More links

Kategorien

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

Inter-library loan at ZB MED

Full text online

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito