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Article ; Online: Endosomal structure and APP biology are not altered in a preclinical mouse cellular model of Down syndrome.

Cannavo, Claudia / Cleverley, Karen / Maduro, Cheryl / Mumford, Paige / Moulding, Dale / Fisher, Elizabeth M C / Wiseman, Frances K

PloS one

2022 Volume 17, Issue 5, Page(s) e0262558

Abstract: Individuals who have Down syndrome (trisomy 21) are at greatly increased risk of developing Alzheimer's disease, characterised by the accumulation in the brain of amyloid-β plaques. Amyloid-β is a product of the processing of the amyloid precursor ... ...

Abstract	Individuals who have Down syndrome (trisomy 21) are at greatly increased risk of developing Alzheimer's disease, characterised by the accumulation in the brain of amyloid-β plaques. Amyloid-β is a product of the processing of the amyloid precursor protein, encoded by the APP gene on chromosome 21. In Down syndrome the first site of amyloid-β accumulation is within endosomes, and changes to endosome biology occur early in Alzheimer's disease. Here, we determine if primary mouse embryonic fibroblasts isolated from a mouse model of Down syndrome can be used to study endosome and APP cell biology. We report that in this cellular model, endosome number, size and APP processing are not altered, likely because APP is not dosage sensitive in the model, despite three copies of App.
MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Biology ; Down Syndrome/genetics ; Down Syndrome/metabolism ; Endosomes/metabolism ; Fibroblasts/metabolism ; Mice ; Plaque, Amyloid/metabolism
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor
Language	English
Publishing date	2022-05-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0262558
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Article ; Online: Cognitive impairments in a Down syndrome model with abnormal hippocampal and prefrontal dynamics and cytoarchitecture.

Muza, Phillip M / Bush, Daniel / Pérez-González, Marta / Zouhair, Ines / Cleverley, Karen / Sopena, Miriam L / Aoidi, Rifdat / West, Steven J / Good, Mark / Tybulewicz, Victor L J / Walker, Matthew C / Fisher, Elizabeth M C / Chang, Pishan

iScience

2023 Volume 26, Issue 2, Page(s) 106073

Abstract: The Dp(10)2Yey mouse carries a ∼2.3-Mb intra-chromosomal duplication of mouse chromosome 10 (Mmu10) that has homology to human chromosome 21, making it an essential model for aspects of Down syndrome (DS, trisomy 21). In this study, we investigated ... ...

Abstract	The Dp(10)2Yey mouse carries a ∼2.3-Mb intra-chromosomal duplication of mouse chromosome 10 (Mmu10) that has homology to human chromosome 21, making it an essential model for aspects of Down syndrome (DS, trisomy 21). In this study, we investigated neuronal dysfunction in the Dp(10)2Yey mouse and report spatial memory impairment and anxiety-like behavior alongside altered neural activity in the medial prefrontal cortex (mPFC) and hippocampus (HPC). Specifically, Dp(10)2Yey mice showed impaired spatial alternation associated with increased sharp-wave ripple activity in mPFC during a period of memory consolidation, and reduced mobility in a novel environment accompanied by reduced theta-gamma phase-amplitude coupling in HPC. Finally, we found alterations in the number of interneuron subtypes in mPFC and HPC that may contribute to the observed phenotypes and highlight potential approaches to ameliorate the effects of human trisomy 21.
Language	English
Publishing date	2023-01-28
Publishing country	United States
Document type	Journal Article
ISSN	2589-0042
ISSN (online)	2589-0042
DOI	10.1016/j.isci.2023.106073
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Article ; Online: Cathepsin B abundance, activity and microglial localisation in Alzheimer's disease-Down syndrome and early onset Alzheimer's disease; the role of elevated cystatin B.

Wu, Yixing / Mumford, Paige / Noy, Suzanna / Cleverley, Karen / Mrzyglod, Alicja / Luo, Dinghao / van Dalen, Floris / Verdoes, Martijn / Fisher, Elizabeth M C / Wiseman, Frances K

Acta neuropathologica communications

2023 Volume 11, Issue 1, Page(s) 132

Abstract: Cathepsin B is a cysteine protease that is implicated in multiple aspects of Alzheimer's disease pathogenesis. The endogenous inhibitor of this enzyme, cystatin B (CSTB) is encoded on chromosome 21. Thus, individuals who have Down syndrome, a genetic ... ...

Abstract	Cathepsin B is a cysteine protease that is implicated in multiple aspects of Alzheimer's disease pathogenesis. The endogenous inhibitor of this enzyme, cystatin B (CSTB) is encoded on chromosome 21. Thus, individuals who have Down syndrome, a genetic condition caused by having an additional copy of chromosome 21, have an extra copy of an endogenous inhibitor of the enzyme. Individuals who have Down syndrome are also at significantly increased risk of developing early-onset Alzheimer's disease (EOAD). The impact of the additional copy of CSTB on Alzheimer's disease development in people who have Down syndrome is not well understood. Here we compared the biology of cathepsin B and CSTB in individuals who had Down syndrome and Alzheimer's disease, with disomic individuals who had Alzheimer's disease or were ageing healthily. We find that the activity of cathepsin B enzyme is decreased in the brain of people who had Down syndrome and Alzheimer's disease compared with disomic individuals who had Alzheimer's disease. This change occurs independently of an alteration in the abundance of the mature enzyme or the number of cathepsin B
MeSH term(s)	Humans ; Mice ; Animals ; Down Syndrome/pathology ; Alzheimer Disease/pathology ; Cystatin B/genetics ; Cathepsin B ; Microglia/metabolism
Chemical Substances	Cystatin B (88844-95-5) ; Cathepsin B (EC 3.4.22.1)
Language	English
Publishing date	2023-08-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2715589-4
ISSN	2051-5960 ; 2051-5960
ISSN (online)	2051-5960
ISSN	2051-5960
DOI	10.1186/s40478-023-01632-8
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Article ; Online: The effects of Cstb duplication on APP/amyloid-β pathology and cathepsin B activity in a mouse model.

Wu, Yixing / Whittaker, Heather T / Noy, Suzanna / Cleverley, Karen / Brault, Veronique / Herault, Yann / Fisher, Elizabeth M C / Wiseman, Frances K

PloS one

2021 Volume 16, Issue 7, Page(s) e0242236

Abstract: People with Down syndrome (DS), caused by trisomy of chromosome 21 have a greatly increased risk of developing Alzheimer's disease (AD). This is in part because of triplication of a chromosome 21 gene, APP. This gene encodes amyloid precursor protein, ... ...

Abstract	People with Down syndrome (DS), caused by trisomy of chromosome 21 have a greatly increased risk of developing Alzheimer's disease (AD). This is in part because of triplication of a chromosome 21 gene, APP. This gene encodes amyloid precursor protein, which is cleaved to form amyloid-β that accumulates in the brains of people who have AD. Recent experimental results demonstrate that a gene or genes on chromosome 21, other than APP, when triplicated significantly accelerate amyloid-β pathology in a transgenic mouse model of amyloid-β deposition. Multiple lines of evidence indicate that cysteine cathepsin activity influences APP cleavage and amyloid-β accumulation. Located on human chromosome 21 (Hsa21) is an endogenous inhibitor of cathepsin proteases, CYSTATIN B (CSTB) which is proposed to regulate cysteine cathepsin activity in vivo. Here we determined if three copies of the mouse gene Cstb is sufficient to modulate amyloid-β accumulation and cathepsin activity in a transgenic APP mouse model. Duplication of Cstb resulted in an increase in transcriptional and translational levels of Cstb in the mouse cortex but had no effect on the deposition of insoluble amyloid-β plaques or the levels of soluble or insoluble amyloid-β42, amyloid-β40, or amyloid-β38 in 6-month old mice. In addition, the increased CSTB did not alter the activity of cathepsin B enzyme in the cortex of 3-month or 6-month old mice. These results indicate that the single-gene duplication of Cstb is insufficient to elicit a disease-modifying phenotype in the dupCstb x tgAPP mice, underscoring the complexity of the genetic basis of AD-DS and the importance of multiple gene interactions in disease.
MeSH term(s)	Aging ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/genetics ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Cathepsin B/metabolism ; Cerebral Cortex/enzymology ; Cerebral Cortex/metabolism ; Cystatin B/genetics ; Cystatin B/metabolism ; Disease Models, Animal ; Female ; Gene Duplication ; Hippocampus/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Cystatin B (88844-95-5) ; Cathepsin B (EC 3.4.22.1)
Language	English
Publishing date	2021-07-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0242236
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Article ; Online: Genetic dissection of down syndrome-associated alterations in APP/amyloid-β biology using mouse models.

Tosh, Justin L / Rhymes, Elena R / Mumford, Paige / Whittaker, Heather T / Pulford, Laura J / Noy, Sue J / Cleverley, Karen / Walker, Matthew C / Tybulewicz, Victor L J / Wykes, Rob C / Fisher, Elizabeth M C / Wiseman, Frances K

Scientific reports

2021 Volume 11, Issue 1, Page(s) 5736

Abstract: Individuals who have Down syndrome (caused by trisomy of chromosome 21), have a greatly elevated risk of early-onset Alzheimer's disease, in which amyloid-β accumulates in the brain. Amyloid-β is a product of the chromosome 21 gene APP (amyloid precursor ...

Abstract	Individuals who have Down syndrome (caused by trisomy of chromosome 21), have a greatly elevated risk of early-onset Alzheimer's disease, in which amyloid-β accumulates in the brain. Amyloid-β is a product of the chromosome 21 gene APP (amyloid precursor protein) and the extra copy or 'dose' of APP is thought to be the cause of this early-onset Alzheimer's disease. However, other chromosome 21 genes likely modulate disease when in three-copies in people with Down syndrome. Here we show that an extra copy of chromosome 21 genes, other than APP, influences APP/Aβ biology. We crossed Down syndrome mouse models with partial trisomies, to an APP transgenic model and found that extra copies of subgroups of chromosome 21 gene(s) modulate amyloid-β aggregation and APP transgene-associated mortality, independently of changing amyloid precursor protein abundance. Thus, genes on chromosome 21, other than APP, likely modulate Alzheimer's disease in people who have Down syndrome.
MeSH term(s)	Alzheimer Disease/complications ; Alzheimer Disease/genetics ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/genetics ; Amyloid beta-Protein Precursor/genetics ; Animals ; Brain/pathology ; Chromosomes, Mammalian/genetics ; Disease Models, Animal ; Down Syndrome/complications ; Down Syndrome/genetics ; Mice ; Mice, Transgenic ; Phenotype ; Phosphotransferases/metabolism ; Protein Aggregates ; Protein-Arginine N-Methyltransferases/metabolism ; Segmental Duplications, Genomic ; Seizures/complications ; Seizures/pathology ; Solubility ; Survival Analysis ; Transgenes
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Protein Aggregates ; PRMT2 protein, mouse (EC 2.1.1.319) ; Protein-Arginine N-Methyltransferases (EC 2.1.1.319) ; Pdxk protein, mouse (EC 2.7.-) ; Phosphotransferases (EC 2.7.-)
Language	English
Publishing date	2021-03-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-85062-3
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Article ; Online: Publisher Correction: Genetic dissection of down syndrome‑associated alterations in APP/amyloid‑β biology using mouse models.

Scientific reports

2021 Volume 11, Issue 1, Page(s) 14966

Language	English
Publishing date	2021-07-16
Publishing country	England
Document type	Published Erratum
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-94313-2
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Article ; Online: Genetic Mapping of APP and Amyloid-β Biology Modulation by Trisomy 21.

Mumford, Paige / Tosh, Justin / Anderle, Silvia / Gkanatsiou Wikberg, Eleni / Lau, Gloria / Noy, Sue / Cleverley, Karen / Saito, Takashi / Saido, Takaomi C / Yu, Eugene / Brinkmalm, Gunnar / Portelius, Erik / Blennow, Kaj / Zetterberg, Henrik / Tybulewicz, Victor / Fisher, Elizabeth M C / Wiseman, Frances K

The Journal of neuroscience : the official journal of the Society for Neuroscience

2022 Volume 42, Issue 33, Page(s) 6453–6468

Abstract: Individuals who have Down syndrome (DS) frequently develop early onset Alzheimer's disease (AD), a neurodegenerative condition caused by the buildup of aggregated amyloid-β (Aβ) and tau proteins in the brain. Aβ is produced by amyloid precursor protein ( ...

Abstract	Individuals who have Down syndrome (DS) frequently develop early onset Alzheimer's disease (AD), a neurodegenerative condition caused by the buildup of aggregated amyloid-β (Aβ) and tau proteins in the brain. Aβ is produced by amyloid precursor protein (
MeSH term(s)	Alzheimer Disease/complications ; Alzheimer Disease/genetics ; Amyloid beta-Peptides/genetics ; Amyloid beta-Protein Precursor/genetics ; Animals ; Brain/metabolism ; Disease Models, Animal ; Down Syndrome/complications ; Down Syndrome/genetics ; Female ; Humans ; Male ; Mice
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor
Language	English
Publishing date	2022-07-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	604637-x
ISSN	1529-2401 ; 0270-6474
ISSN (online)	1529-2401
ISSN	0270-6474
DOI	10.1523/JNEUROSCI.0521-22.2022
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Article: A novel knockout mouse for the small EDRK-rich factor 2 (Serf2) showing developmental and other deficits

Cleverley, Karen / Lee, Weaverly Colleen / Mumford, Paige / Collins, Toby / Rickman, Matthew / Cunningham, Thomas J / Cleak, James / Mianne, Joffrey / Szoke-Kovacs, Zsombor / Stewart, Michelle / Teboul, Lydia / Maduro, Cheryl / Wells, Sara / Wiseman, Frances K / Fisher, Elizabeth M. C

Mammalian genome. 2021 Apr., v. 32, no. 2

2021

Abstract: The small EDRK-rich factor 2 (SERF2) is a highly conserved protein that modifies amyloid fibre assembly in vitro and promotes protein misfolding. However, the role of SERF2 in regulating age-related proteotoxicity remains largely unexplored due to a lack ...

Abstract	The small EDRK-rich factor 2 (SERF2) is a highly conserved protein that modifies amyloid fibre assembly in vitro and promotes protein misfolding. However, the role of SERF2 in regulating age-related proteotoxicity remains largely unexplored due to a lack of in vivo models. Here, we report the generation of Serf2 knockout mice using an ES cell targeting approach, with Serf2 knockout alleles being bred onto different defined genetic backgrounds. We highlight phenotyping data from heterozygous Serf2⁺/⁻ mice, including unexpected male-specific phenotypes in startle response and pre-pulse inhibition. We report embryonic lethality in Serf2⁻/⁻ null animals when bred onto a C57BL/6 N background. However, homozygous null animals were viable on a mixed genetic background and, remarkably, developed without obvious abnormalities. The Serf2 knockout mice provide a powerful tool to further investigate the role of SERF2 protein in previously unexplored pathophysiological pathways in the context of a whole organism.
Keywords	amyloid ; embryonic mortality ; genetic background ; heterozygosity ; homozygosity ; knockout mutants ; phenotype ; protein folding
Language	English
Dates of publication	2021-04
Size	p. 94-103.
Publishing place	Springer US
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	1058547-3
ISSN	1432-1777 ; 0938-8990
ISSN (online)	1432-1777
ISSN	0938-8990
DOI	10.1007/s00335-021-09864-6
Database	NAL-Catalogue (AGRICOLA)

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Zs.A 3489: Show issues

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Article ; Online: A novel knockout mouse for the small EDRK-rich factor 2 (Serf2) showing developmental and other deficits.

Mammalian genome : official journal of the International Mammalian Genome Society

2021 Volume 32, Issue 2, Page(s) 94–103

Abstract	The small EDRK-rich factor 2 (SERF2) is a highly conserved protein that modifies amyloid fibre assembly in vitro and promotes protein misfolding. However, the role of SERF2 in regulating age-related proteotoxicity remains largely unexplored due to a lack of in vivo models. Here, we report the generation of Serf2 knockout mice using an ES cell targeting approach, with Serf2 knockout alleles being bred onto different defined genetic backgrounds. We highlight phenotyping data from heterozygous Serf2
MeSH term(s)	Age Factors ; Alleles ; Alternative Splicing ; Animals ; Cell Line ; Developmental Disabilities/diagnosis ; Developmental Disabilities/genetics ; Disease Models, Animal ; Embryonic Stem Cells/metabolism ; Female ; Gene Expression Regulation ; Genetic Association Studies/methods ; Genetic Background ; Genetic Loci ; Genetic Predisposition to Disease ; Genotype ; Intracellular Signaling Peptides and Proteins/genetics ; Male ; Mice ; Mice, Knockout ; Organ Specificity ; Phenotype ; X-Ray Microtomography
Chemical Substances	Intracellular Signaling Peptides and Proteins ; Serf2 protein, mouse
Language	English
Publishing date	2021-03-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1058547-3
ISSN	1432-1777 ; 0938-8990
ISSN (online)	1432-1777
ISSN	0938-8990
DOI	10.1007/s00335-021-09864-6
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Article ; Online: Downregulated Wnt/β-catenin signalling in the Down syndrome hippocampus.

Granno, Simone / Nixon-Abell, Jonathon / Berwick, Daniel C / Tosh, Justin / Heaton, George / Almudimeegh, Sultan / Nagda, Zenisha / Rain, Jean-Christophe / Zanda, Manuela / Plagnol, Vincent / Tybulewicz, Victor L J / Cleverley, Karen / Wiseman, Frances K / Fisher, Elizabeth M C / Harvey, Kirsten

Scientific reports

2019 Volume 9, Issue 1, Page(s) 7322

Abstract: Pathological mechanisms underlying Down syndrome (DS)/Trisomy 21, including dysregulation of essential signalling processes remain poorly understood. Combining bioinformatics with RNA and protein analysis, we identified downregulation of the Wnt/β- ... ...

Abstract	Pathological mechanisms underlying Down syndrome (DS)/Trisomy 21, including dysregulation of essential signalling processes remain poorly understood. Combining bioinformatics with RNA and protein analysis, we identified downregulation of the Wnt/β-catenin pathway in the hippocampus of adult DS individuals with Alzheimer's disease and the 'Tc1' DS mouse model. Providing a potential underlying molecular pathway, we demonstrate that the chromosome 21 kinase DYRK1A regulates Wnt signalling via a novel bimodal mechanism. Under basal conditions, DYRK1A is a negative regulator of Wnt/β-catenin. Following pathway activation, however, DYRK1A exerts the opposite effect, increasing signalling activity. In summary, we identified downregulation of hippocampal Wnt/β-catenin signalling in DS, possibly mediated by a dose dependent effect of the chromosome 21-encoded kinase DYRK1A. Overall, we propose that dosage imbalance of the Hsa21 gene DYRK1A affects downstream Wnt target genes. Therefore, modulation of Wnt signalling may open unexplored avenues for DS and Alzheimer's disease treatment.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Aged ; Alzheimer Disease/pathology ; Animals ; Axin Protein/metabolism ; Catechin/analogs & derivatives ; Catechin/pharmacology ; Chromosomes, Human, Pair 21/genetics ; Disease Models, Animal ; Down Syndrome/genetics ; Down Syndrome/pathology ; Down-Regulation/drug effects ; Female ; HEK293 Cells ; HeLa Cells ; Hippocampus/pathology ; Humans ; Male ; Mice ; Middle Aged ; Protein Serine-Threonine Kinases/genetics ; Protein Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/genetics ; Protein-Tyrosine Kinases/metabolism ; RNA-Seq ; Wnt Signaling Pathway/drug effects ; Wnt Signaling Pathway/genetics ; Dyrk Kinases
Chemical Substances	AXIN2 protein, human ; Adaptor Proteins, Signal Transducing ; Axin Protein ; Axin2 protein, mouse ; DKK3 protein, human ; Dkk3 protein, mouse ; Catechin (8R1V1STN48) ; epigallocatechin gallate (BQM438CTEL) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2019-05-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-019-43820-4
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