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Article ; Online: Establishment of centromere identity is dependent on nuclear spatial organization.

Wu, Weifang / McHugh, Toni / Kelly, David A / Pidoux, Alison L / Allshire, Robin C

2022 Volume 32, Issue 14, Page(s) 3121–3136.e6

Abstract: The establishment of centromere-specific CENP-A chromatin is influenced by epigenetic and genetic processes. Central domain sequences from fission yeast centromeres are preferred substrates for CENP- ... ...

Abstract	The establishment of centromere-specific CENP-A chromatin is influenced by epigenetic and genetic processes. Central domain sequences from fission yeast centromeres are preferred substrates for CENP-A
MeSH term(s)	Centromere/metabolism ; Centromere Protein A/metabolism ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; DNA/genetics ; Heterochromatin/genetics ; Heterochromatin/metabolism ; Histones/metabolism ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism
Chemical Substances	Centromere Protein A ; Chromosomal Proteins, Non-Histone ; Cnp1 protein, S pombe ; Heterochromatin ; Histones ; Schizosaccharomyces pombe Proteins ; DNA (9007-49-2)
Language	English
Publishing date	2022-07-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2022.06.048
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Article ; Online: Proteasome-dependent truncation of the negative heterochromatin regulator Epe1 mediates antifungal resistance.

Yaseen, Imtiyaz / White, Sharon A / Torres-Garcia, Sito / Spanos, Christos / Lafos, Marcel / Gaberdiel, Elisabeth / Yeboah, Rebecca / El Karoui, Meriem / Rappsilber, Juri / Pidoux, Alison L / Allshire, Robin C

Nature structural & molecular biology

2022 Volume 29, Issue 8, Page(s) 745–758

Abstract: Epe1 histone demethylase restricts H3K9-methylation-dependent heterochromatin, preventing it from spreading over, and silencing, gene-containing regions in fission yeast. External stress induces an adaptive response allowing heterochromatin island ... ...

Abstract	Epe1 histone demethylase restricts H3K9-methylation-dependent heterochromatin, preventing it from spreading over, and silencing, gene-containing regions in fission yeast. External stress induces an adaptive response allowing heterochromatin island formation that confers resistance on surviving wild-type lineages. Here we investigate the mechanism by which Epe1 is regulated in response to stress. Exposure to caffeine or antifungals results in Epe1 ubiquitylation and proteasome-dependent removal of the N-terminal 150 residues from Epe1, generating truncated Epe1 (tEpe1) which accumulates in the cytoplasm. Constitutive tEpe1 expression increases H3K9 methylation over several chromosomal regions, reducing expression of underlying genes and enhancing resistance. Reciprocally, constitutive non-cleavable Epe1 expression decreases resistance. tEpe1-mediated resistance requires a functional JmjC demethylase domain. Moreover, caffeine-induced Epe1-to-tEpe1 cleavage is dependent on an intact cell integrity MAP kinase stress signaling pathway, mutations in which alter resistance. Thus, environmental changes elicit a mechanism that curtails the function of this key epigenetic modifier, allowing heterochromatin to reprogram gene expression, thereby bestowing resistance to some cells within a population. H3K9me-heterochromatin components are conserved in human and crop-plant fungal pathogens for which a limited number of antifungals exist. Our findings reveal how transient heterochromatin-dependent antifungal resistant epimutations develop and thus inform on how they might be countered.
MeSH term(s)	Antifungal Agents/metabolism ; Caffeine/metabolism ; Cytoplasm/metabolism ; Heterochromatin/genetics ; Heterochromatin/metabolism ; Humans ; Nuclear Proteins/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/metabolism
Chemical Substances	Antifungal Agents ; Heterochromatin ; Nuclear Proteins ; Schizosaccharomyces pombe Proteins ; epe1 protein, S pombe ; Caffeine (3G6A5W338E) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2022-07-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2126708-X
ISSN	1545-9985 ; 1545-9993
ISSN (online)	1545-9985
ISSN	1545-9993
DOI	10.1038/s41594-022-00801-y
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Article ; Online: Epigenetic gene silencing by heterochromatin primes fungal resistance.

Torres-Garcia, Sito / Yaseen, Imtiyaz / Shukla, Manu / Audergon, Pauline N C B / White, Sharon A / Pidoux, Alison L / Allshire, Robin C

Nature

2020 Volume 585, Issue 7825, Page(s) 453–458

Abstract: Heterochromatin that depends on histone H3 lysine 9 methylation (H3K9me) renders embedded genes transcriptionally ... ...

Abstract	Heterochromatin that depends on histone H3 lysine 9 methylation (H3K9me) renders embedded genes transcriptionally silent
MeSH term(s)	Caffeine/pharmacology ; Drug Resistance, Fungal/drug effects ; Drug Resistance, Fungal/genetics ; Gene Silencing/drug effects ; Heterochromatin/drug effects ; Heterochromatin/genetics ; Heterochromatin/metabolism ; Histone Acetyltransferases/metabolism ; Nuclear Proteins/metabolism ; Phenotype ; Schizosaccharomyces/cytology ; Schizosaccharomyces/drug effects ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/metabolism
Chemical Substances	Heterochromatin ; Nuclear Proteins ; Schizosaccharomyces pombe Proteins ; epe1 protein, S pombe ; Caffeine (3G6A5W338E) ; Histone Acetyltransferases (EC 2.3.1.48) ; Mst2 protein, S pombe (EC 2.3.1.48)
Language	English
Publishing date	2020-09-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-020-2706-x
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Zs.A 26: 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)
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Article ; Online: Large domains of heterochromatin direct the formation of short mitotic chromosome loops.

Fitz-James, Maximilian H / Tong, Pin / Pidoux, Alison L / Ozadam, Hakan / Yang, Liyan / White, Sharon A / Dekker, Job / Allshire, Robin C

eLife

2020 Volume 9

Abstract: During mitosis chromosomes reorganise into highly compact, rod-shaped forms, thought to consist of consecutive chromatin loops around a central protein scaffold. Condensin complexes are involved in chromatin compaction, but the contribution of other ... ...

Abstract	During mitosis chromosomes reorganise into highly compact, rod-shaped forms, thought to consist of consecutive chromatin loops around a central protein scaffold. Condensin complexes are involved in chromatin compaction, but the contribution of other chromatin proteins, DNA sequence and histone modifications is less understood. A large region of fission yeast DNA inserted into a mouse chromosome was previously observed to adopt a mitotic organisation distinct from that of surrounding mouse DNA. Here, we show that a similar distinct structure is common to a large subset of insertion events in both mouse and human cells and is coincident with the presence of high levels of heterochromatic H3 lysine nine trimethylation (H3K9me3). Hi-C and microscopy indicate that the heterochromatinised fission yeast DNA is organised into smaller chromatin loops than flanking euchromatic mouse chromatin. We conclude that heterochromatin alters chromatin loop size, thus contributing to the distinct appearance of heterochromatin on mitotic chromosomes.
MeSH term(s)	Animals ; Chromosomes/chemistry ; Chromosomes/genetics ; Chromosomes/metabolism ; DNA, Fungal/chemistry ; DNA, Fungal/genetics ; DNA, Fungal/metabolism ; DNA, Recombinant/chemistry ; DNA, Recombinant/genetics ; DNA, Recombinant/metabolism ; HeLa Cells ; Heterochromatin/chemistry ; Heterochromatin/genetics ; Heterochromatin/metabolism ; Histones/chemistry ; Histones/genetics ; Histones/metabolism ; Humans ; Mice ; Mitosis/genetics ; NIH 3T3 Cells ; Schizosaccharomyces/genetics ; Transfection
Chemical Substances	DNA, Fungal ; DNA, Recombinant ; Heterochromatin ; Histones
Language	English
Publishing date	2020-09-11
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.57212
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Article: SpEDIT

Torres-Garcia, Sito / Di Pompeo, Lorenza / Eivers, Luke / Gaborieau, Baptiste / White, Sharon A / Pidoux, Alison L / Kanigowska, Paulina / Yaseen, Imtiyaz / Cai, Yizhi / Allshire, Robin C

Wellcome open research

2020 Volume 5, Page(s) 274

Abstract: The CRISPR/Cas9 system allows scarless, marker-free genome editing. Current CRISPR/Cas9 systems for the fission ... ...

Abstract	The CRISPR/Cas9 system allows scarless, marker-free genome editing. Current CRISPR/Cas9 systems for the fission yeast
Language	English
Publishing date	2020-11-24
Publishing country	England
Document type	Journal Article
ISSN	2398-502X
ISSN	2398-502X
DOI	10.12688/wellcomeopenres.16405.1
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Article ; Online: Sequence features and transcriptional stalling within centromere DNA promote establishment of CENP-A chromatin.

Catania, Sandra / Pidoux, Alison L / Allshire, Robin C

PLoS genetics

2015 Volume 11, Issue 3, Page(s) e1004986

Abstract: Centromere sequences are not conserved between species, and there is compelling evidence for epigenetic regulation of centromere identity, with location being dictated by the presence of chromatin containing the histone H3 variant CENP-A. Paradoxically, ... ...

Abstract	Centromere sequences are not conserved between species, and there is compelling evidence for epigenetic regulation of centromere identity, with location being dictated by the presence of chromatin containing the histone H3 variant CENP-A. Paradoxically, in most organisms CENP-A chromatin generally occurs on particular sequences. To investigate the contribution of primary DNA sequence to establishment of CENP-A chromatin in vivo, we utilised the fission yeast Schizosaccharomyces pombe. CENP-ACnp1 chromatin is normally assembled on ∼10 kb of central domain DNA within these regional centromeres. We demonstrate that overproduction of S. pombe CENP-ACnp1 bypasses the usual requirement for adjacent heterochromatin in establishing CENP-ACnp1 chromatin, and show that central domain DNA is a preferred substrate for de novo establishment of CENP-ACnp1 chromatin. When multimerised, a 2 kb sub-region can establish CENP-ACnp1 chromatin and form functional centromeres. Randomization of the 2 kb sequence to generate a sequence that maintains AT content and predicted nucleosome positioning is unable to establish CENP-ACnp1 chromatin. These analyses indicate that central domain DNA from fission yeast centromeres contains specific information that promotes CENP-ACnp1 incorporation into chromatin. Numerous transcriptional start sites were detected on the forward and reverse strands within the functional 2 kb sub-region and active promoters were identified. RNAPII is enriched on central domain DNA in wild-type cells, but only low levels of transcripts are detected, consistent with RNAPII stalling during transcription of centromeric DNA. Cells lacking factors involved in restarting transcription-TFIIS and Ubp3-assemble CENP-ACnp1 on central domain DNA when CENP-ACnp1 is at wild-type levels, suggesting that persistent stalling of RNAPII on centromere DNA triggers chromatin remodelling events that deposit CENP-ACnp1. Thus, sequence-encoded features of centromeric DNA create an environment of pervasive low quality RNAPII transcription that is an important determinant of CENP-ACnp1 assembly. These observations emphasise roles for both genetic and epigenetic processes in centromere establishment.
MeSH term(s)	Autoantigens/genetics ; Centromere/genetics ; Centromere Protein A ; Chromatin/genetics ; Chromatin Assembly and Disassembly/genetics ; Chromosomal Proteins, Non-Histone/genetics ; DNA/genetics ; Epigenesis, Genetic ; Heterochromatin/genetics ; Histones/genetics ; Kinetochores ; Schizosaccharomyces ; Transcription, Genetic
Chemical Substances	Autoantigens ; Centromere Protein A ; Chromatin ; Chromosomal Proteins, Non-Histone ; Heterochromatin ; Histones ; DNA (9007-49-2)
Language	English
Publishing date	2015-03-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2186725-2
ISSN	1553-7404 ; 1553-7390
ISSN (online)	1553-7404
ISSN	1553-7390
DOI	10.1371/journal.pgen.1004986
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Article ; Online: Hap2-Ino80-facilitated transcription promotes de novo establishment of CENP-A chromatin.

Singh, Puneet P / Shukla, Manu / White, Sharon A / Lafos, Marcel / Tong, Pin / Auchynnikava, Tatsiana / Spanos, Christos / Rappsilber, Juri / Pidoux, Alison L / Allshire, Robin C

Genes & development

2020 Volume 34, Issue 3-4, Page(s) 226–238

Abstract: Centromeres are maintained epigenetically by the presence of CENP-A, an evolutionarily conserved histone H3 variant, which directs kinetochore assembly and hence centromere function. To identify factors that promote assembly of CENP-A chromatin, we ... ...

Abstract	Centromeres are maintained epigenetically by the presence of CENP-A, an evolutionarily conserved histone H3 variant, which directs kinetochore assembly and hence centromere function. To identify factors that promote assembly of CENP-A chromatin, we affinity-selected solubilized fission yeast CENP-A
MeSH term(s)	Chromatin/genetics ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; Chromosomes, Fungal/genetics ; Chromosomes, Fungal/metabolism ; DNA, Fungal/metabolism ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism ; Transcription Factors/metabolism ; Transcription, Genetic/physiology
Chemical Substances	Chromatin ; Chromosomal Proteins, Non-Histone ; Cnp1 protein, S pombe ; DNA, Fungal ; Ino80 protein, S pombe ; Schizosaccharomyces pombe Proteins ; Transcription Factors
Language	English
Publishing date	2020-01-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	806684-x
ISSN	1549-5477 ; 0890-9369
ISSN (online)	1549-5477
ISSN	0890-9369
DOI	10.1101/gad.332536.119
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Zs.A 2292: 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)
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Article ; Online: Centromere DNA Destabilizes H3 Nucleosomes to Promote CENP-A Deposition during the Cell Cycle.

Shukla, Manu / Tong, Pin / White, Sharon A / Singh, Puneet P / Reid, Angus M / Catania, Sandra / Pidoux, Alison L / Allshire, Robin C

Current biology : CB

2018 Volume 28, Issue 24, Page(s) 3924–3936.e4

Abstract: Active centromeres are defined by the presence of nucleosomes containing CENP-A, a histone H3 variant, which alone is sufficient to direct kinetochore assembly. Once assembled at a location, CENP-A chromatin and kinetochores are maintained at that ... ...

Abstract	Active centromeres are defined by the presence of nucleosomes containing CENP-A, a histone H3 variant, which alone is sufficient to direct kinetochore assembly. Once assembled at a location, CENP-A chromatin and kinetochores are maintained at that location through a positive feedback loop where kinetochore proteins recruited by CENP-A promote deposition of new CENP-A following replication. Although CENP-A chromatin itself is a heritable entity, it is normally associated with specific sequences. Intrinsic properties of centromeric DNA may favor the assembly of CENP-A rather than H3 nucleosomes. Here we investigate histone dynamics on centromere DNA. We show that during S phase, histone H3 is deposited as a placeholder at fission yeast centromeres and is subsequently evicted in G2, when we detect deposition of the majority of new CENP-A
MeSH term(s)	Centromere/metabolism ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; DNA, Fungal/metabolism ; Histones/metabolism ; Mitosis ; Nucleosomes/metabolism ; S Phase ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism
Chemical Substances	Chromosomal Proteins, Non-Histone ; Cnp1 protein, S pombe ; DNA, Fungal ; Histones ; Nucleosomes ; Schizosaccharomyces pombe Proteins
Language	English
Publishing date	2018-11-29
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2018.10.049
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Article ; Online: Common ancestry of the CENP-A chaperones Scm3 and HJURP.

Sanchez-Pulido, Luis / Pidoux, Alison L / Ponting, Chris P / Allshire, Robin C

Cell

2015 Volume 137, Issue 7, Page(s) 1173–1174

MeSH term(s)	Animals ; Autoantigens/metabolism ; Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Centromere Protein A ; Chromosomal Proteins, Non-Histone/chemistry ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Humans ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism
Chemical Substances	Autoantigens ; CENPA protein, human ; Carrier Proteins ; Centromere Protein A ; Chromosomal Proteins, Non-Histone ; DNA-Binding Proteins ; HJURP protein, human ; Saccharomyces cerevisiae Proteins ; Schizosaccharomyces pombe Proteins ; Scm3 protein, S cerevisiae ; Scm3 protein, S pombe
Language	English
Publishing date	2015-02-09
Publishing country	United States
Document type	Letter ; Research Support, Non-U.S. Gov't
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2009.06.010
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Zs.A 1167: 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)
Zs.MG 58: Show issues

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Article ; Online: Large domains of heterochromatin direct the formation of short mitotic chromosome loops

Maximilian H Fitz-James / Pin Tong / Alison L Pidoux / Hakan Ozadam / Liyan Yang / Sharon A White / Job Dekker / Robin C Allshire

eLife, Vol

2020 Volume 9

Abstract	During mitosis chromosomes reorganise into highly compact, rod-shaped forms, thought to consist of consecutive chromatin loops around a central protein scaffold. Condensin complexes are involved in chromatin compaction, but the contribution of other chromatin proteins, DNA sequence and histone modifications is less understood. A large region of fission yeast DNA inserted into a mouse chromosome was previously observed to adopt a mitotic organisation distinct from that of surrounding mouse DNA. Here, we show that a similar distinct structure is common to a large subset of insertion events in both mouse and human cells and is coincident with the presence of high levels of heterochromatic H3 lysine nine trimethylation (H3K9me3). Hi-C and microscopy indicate that the heterochromatinised fission yeast DNA is organised into smaller chromatin loops than flanking euchromatic mouse chromatin. We conclude that heterochromatin alters chromatin loop size, thus contributing to the distinct appearance of heterochromatin on mitotic chromosomes.
Keywords	chromosome structure ; heterochromatin ; condensin ; loop extrusion ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
Subject code	571
Language	English
Publishing date	2020-09-01T00:00:00Z
Publisher	eLife Sciences Publications Ltd
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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