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Article ; Online: KH-like Domains in PARP9/DTX3L and PARP14 Coordinate Protein-Protein Interactions to Promote Cancer Cell Survival.

Saleh, Hadil / Liloglou, Triantafillos / Rigden, Daniel J / Parsons, Jason L / Grundy, Gabrielle J

2024 Volume 436, Issue 4, Page(s) 168434

Abstract: Certain members of the ADP-ribosyltransferase superfamily (ARTD or PARP enzymes) catalyse ADP-ribosylation in response to cellular stress, DNA damage and viral infection and are upregulated in various tumours. PARP9, its binding partner DTX3L and PARP14 ... ...

Abstract	Certain members of the ADP-ribosyltransferase superfamily (ARTD or PARP enzymes) catalyse ADP-ribosylation in response to cellular stress, DNA damage and viral infection and are upregulated in various tumours. PARP9, its binding partner DTX3L and PARP14 protein levels are significantly correlated in head and neck squamous cell carcinoma (HNSCC) and other tumour types though a mechanism where PARP9/DTX3L regulates PARP14 post-transcriptionally. Depleting PARP9, DTX3L or PARP14 expression in HNSCC or HeLa cell lines decreases cell survival through a reduction of proliferation and an increase in apoptosis. A partial rescue of survival was achieved by expressing a PARP14 truncation containing a predicted eukaryotic type I KH domain. KH-like domains were also found in PARP9 and in DTX3L and contributed to protein-protein interactions between PARP9-DTX3L and PARP14-DTX3L. Homodimerization of DTX3L was also coordinated by a KH-like domain and was disrupted by site-specific mutation. Although, cell survival promoted by PARP14 did not require ADP-ribosyltransferase activity, interaction of DTX3L in vitro suppressed PARP14 auto-ADP-ribosylation and promoted trans-ADP-ribosylation of PARP9 and DTX3L. In summary, we characterised PARP9-DTX3L-PARP14 interactions important to pro-survival signalling in HNSCC cells, albeit in PARP14 catalytically independent fashion.
MeSH term(s)	Humans ; Cell Survival ; Head and Neck Neoplasms/enzymology ; Head and Neck Neoplasms/pathology ; HeLa Cells ; Neoplasm Proteins/chemistry ; Poly(ADP-ribose) Polymerases/chemistry ; Squamous Cell Carcinoma of Head and Neck/enzymology ; Squamous Cell Carcinoma of Head and Neck/pathology ; Ubiquitin-Protein Ligases/chemistry ; Protein Domains
Chemical Substances	DTX3L protein, human (EC 2.3.2.27) ; Neoplasm Proteins ; PARP14 protein, human (EC 2.4.2.30) ; PARP9 protein, human ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2024-01-03
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2023.168434
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Article ; Online: Base excision repair and its implications to cancer therapy.

Grundy, Gabrielle J / Parsons, Jason L

Essays in biochemistry

2020 Volume 64, Issue 5, Page(s) 831–843

Abstract: Base excision repair (BER) has evolved to preserve the integrity of DNA following cellular oxidative stress and in response to exogenous insults. The pathway is a coordinated, sequential process involving 30 proteins or more in which single strand breaks ...

Abstract	Base excision repair (BER) has evolved to preserve the integrity of DNA following cellular oxidative stress and in response to exogenous insults. The pathway is a coordinated, sequential process involving 30 proteins or more in which single strand breaks are generated as intermediates during the repair process. While deficiencies in BER activity can lead to high mutation rates and tumorigenesis, cancer cells often rely on increased BER activity to tolerate oxidative stress. Targeting BER has been an attractive strategy to overwhelm cancer cells with DNA damage, improve the efficacy of radiotherapy and/or chemotherapy, or form part of a lethal combination with a cancer specific mutation/loss of function. We provide an update on the progress of inhibitors to enzymes involved in BER, and some of the challenges faced with targeting the BER pathway.
MeSH term(s)	DNA Repair ; Humans ; Neoplasms/drug therapy ; Neoplasms/genetics ; Neoplasms/radiotherapy ; Oxidative Stress
Language	English
Publishing date	2020-07-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	1744-1358 ; 0071-1365
ISSN (online)	1744-1358
ISSN	0071-1365
DOI	10.1042/EBC20200013
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Article ; Online: The role of autophagy in hypoxia-induced radioresistance.

Hill, Rhianna Mae / Fok, Matthew / Grundy, Gabrielle / Parsons, Jason Luke / Rocha, Sonia

Radiotherapy and oncology : journal of the European Society for Therapeutic Radiology and Oncology

2023 Volume 189, Page(s) 109951

Abstract: Radiotherapy is a widely used treatment modality against cancer, and although survival rates are increasing, radioresistant properties of tumours remain a significant barrier for curative treatment. Tumour hypoxia is one of the main contributors to ... ...

Abstract	Radiotherapy is a widely used treatment modality against cancer, and although survival rates are increasing, radioresistant properties of tumours remain a significant barrier for curative treatment. Tumour hypoxia is one of the main contributors to radioresistance and is common in most solid tumours. Hypoxia is responsible for many molecular changes within the cell which helps tumours to survive under such challenging conditions. These hypoxia-induced molecular changes are predominantly coordinated by the hypoxia inducible factor (HIF) and have been linked with the ability to confer resistance to radiation-induced cell death. To overcome this obstacle research has been directed towards autophagy, a cellular process involved in self degradation and recycling of macromolecules, as HIF plays a large role in its coordination under hypoxic conditions. The role that autophagy has following radiotherapy treatment is conflicted with evidence of both cytoprotective and cytotoxic effects. This literature review aims to explore the intricate relationship between radiotherapy, hypoxia, and autophagy in the context of cancer treatment. It provides valuable insights into the potential of targeting autophagy as a therapeutic strategy to improve the response of hypoxic tumours to radiotherapy.
MeSH term(s)	Humans ; Radiation Tolerance ; Neoplasms/radiotherapy ; Hypoxia ; Cell Hypoxia ; Autophagy ; Cell Line, Tumor ; Hypoxia-Inducible Factor 1, alpha Subunit
Chemical Substances	Hypoxia-Inducible Factor 1, alpha Subunit
Language	English
Publishing date	2023-10-12
Publishing country	Ireland
Document type	Journal Article ; Review
ZDB-ID	605646-5
ISSN	1879-0887 ; 0167-8140
ISSN (online)	1879-0887
ISSN	0167-8140
DOI	10.1016/j.radonc.2023.109951
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Article: Effectiveness of PARP inhibition in enhancing the radiosensitivity of 3D spheroids of head and neck squamous cell carcinoma.

Zhou, Chumin / Fabbrizi, Maria Rita / Hughes, Jonathan R / Grundy, Gabrielle J / Parsons, Jason L

Frontiers in oncology

2022 Volume 12, Page(s) 940377

Abstract: A critical risk factor for head and neck squamous cell carcinoma (HNSCC), particularly of the oropharynx, and the response to radiotherapy is human papillomavirus (HPV) type-16/18 infection. Specifically, HPV-positive HNSCC display increased ... ...

Abstract	A critical risk factor for head and neck squamous cell carcinoma (HNSCC), particularly of the oropharynx, and the response to radiotherapy is human papillomavirus (HPV) type-16/18 infection. Specifically, HPV-positive HNSCC display increased radiosensitivity and improved outcomes, which has been linked with defective signalling and repair of DNA double-strand breaks (DSBs). This differential response to radiotherapy has been recapitulated
Language	English
Publishing date	2022-08-16
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2649216-7
ISSN	2234-943X
ISSN	2234-943X
DOI	10.3389/fonc.2022.940377
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Article ; Online: Non-homologous end joining: Common interaction sites and exchange of multiple factors in the DNA repair process.

Rulten, Stuart L / Grundy, Gabrielle J

BioEssays : news and reviews in molecular, cellular and developmental biology

2017 Volume 39, Issue 3

Abstract: Non-homologous end-joining (NHEJ) is the dominant means of repairing chromosomal DNA double strand breaks (DSBs), and is essential in human cells. Fifteen or more proteins can be involved in the detection, signalling, synapsis, end-processing and ... ...

Abstract	Non-homologous end-joining (NHEJ) is the dominant means of repairing chromosomal DNA double strand breaks (DSBs), and is essential in human cells. Fifteen or more proteins can be involved in the detection, signalling, synapsis, end-processing and ligation events required to repair a DSB, and must be assembled in the confined space around the DNA ends. We review here a number of interaction points between the core NHEJ components (Ku70, Ku80, DNA-PKcs, XRCC4 and Ligase IV) and accessory factors such as kinases, phosphatases, polymerases and structural proteins. Conserved protein-protein interaction sites such as Ku-binding motifs (KBMs), XLF-like motifs (XLMs), FHA and BRCT domains illustrate that different proteins compete for the same binding sites on the core machinery, and must be spatially and temporally regulated. We discuss how post-translational modifications such as phosphorylation, ADP-ribosylation and ubiquitinylation may regulate sequential steps in the NHEJ pathway or control repair at different types of DNA breaks.
Language	English
Publishing date	2017-03
Publishing country	United States
Document type	Journal Article
ZDB-ID	50140-2
ISSN	1521-1878 ; 0265-9247
ISSN (online)	1521-1878
ISSN	0265-9247
DOI	10.1002/bies.201600209
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Article ; Online: Enhancing radiotherapy outcomes in rectal cancer: A systematic review of targeting hypoxia-induced radioresistance.

Fok, Matthew / Hill, Rhianna / Fowler, Hayley / Clifford, Rachael / Kler, Aaron / Uzzi-Daniel, Jayanma / Rocha, Sonia / Grundy, Gabrielle / Parsons, Jason / Vimalachandran, Dale

Clinical and translational radiation oncology

2023 Volume 44, Page(s) 100695

Abstract: Introduction: Neoadjuvant radiotherapy is successfully used in rectal cancer to improve overall survival. However, treatment response is both unpredictable and variable. There is strong evidence to show that the phenomenon of tumour hypoxia is ... ...

Abstract	Introduction: Neoadjuvant radiotherapy is successfully used in rectal cancer to improve overall survival. However, treatment response is both unpredictable and variable. There is strong evidence to show that the phenomenon of tumour hypoxia is associated with radioresistance, however the mechanism(s) behind this are poorly understood. Consequently, there have only been a small number of studies evaluating methods targeting hypoxia-induced radioresistance. The purpose of this systematic review is to evaluate the potential effectiveness of targeting hypoxia-induced radioresistance in rectal cancer and provide recommendations for future research in this area. Methods: A comprehensive literature search was performed following the PRISMA guidelines. This study was registered on the Prospero database (CRD42023441983). Results: Eight articles met the inclusion criteria. All studies identified were Discussion: The importance of investigating hypoxia-induced radioresistance in rectal cancer is crucial. However, to date, only a small number of preclinical studies exist evaluating this phenomenon. This systematic review highlights the importance of further research to fully understand the mechanism behind this radioresistance. There are promising targets identified in this systematic review however, substantially more pre-clinical and clinical research as a priority for future research is needed.
Language	English
Publishing date	2023-10-28
Publishing country	Ireland
Document type	Journal Article
ISSN	2405-6308
ISSN (online)	2405-6308
DOI	10.1016/j.ctro.2023.100695
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Article ; Online: One ring to bring them all--the role of Ku in mammalian non-homologous end joining.

Grundy, Gabrielle J / Moulding, Hayley A / Caldecott, Keith W / Rulten, Stuart L

DNA repair

2014 Volume 17, Page(s) 30–38

Abstract: The repair of DNA double strand breaks is essential for cell survival and several conserved pathways have evolved to ensure their rapid and efficient repair. The non-homologous end joining pathway is initiated when Ku binds to the DNA break site. Ku is ... ...

Abstract	The repair of DNA double strand breaks is essential for cell survival and several conserved pathways have evolved to ensure their rapid and efficient repair. The non-homologous end joining pathway is initiated when Ku binds to the DNA break site. Ku is an abundant nuclear heterodimer of Ku70 and Ku80 with a toroidal structure that allows the protein to slide over the broken DNA end and bind with high affinity. Once locked into placed, Ku acts as a tool-belt to recruit multiple interacting proteins, forming one or more non-homologous end joining complexes that act in a regulated manner to ensure efficient repair of DNA ends. Here we review the structure and functions of Ku and the proteins with which it interacts during non-homologous end joining.
MeSH term(s)	Animals ; Antigens, Nuclear/chemistry ; Antigens, Nuclear/metabolism ; Chromatin/metabolism ; DNA Breaks, Double-Stranded ; DNA End-Joining Repair ; DNA Ligases/metabolism ; DNA-Activated Protein Kinase/metabolism ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Humans ; Ku Autoantigen ; Models, Molecular ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Telomere/metabolism
Chemical Substances	Antigens, Nuclear ; Chromatin ; DNA-Binding Proteins ; DNA-Activated Protein Kinase (EC 2.7.11.1) ; Xrcc6 protein, human (EC 3.6.4.12) ; Ku Autoantigen (EC 4.2.99.-) ; DNA Ligases (EC 6.5.1.-)
Language	English
Publishing date	2014-03-26
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	2071608-4
ISSN	1568-7856 ; 1568-7864
ISSN (online)	1568-7856
ISSN	1568-7864
DOI	10.1016/j.dnarep.2014.02.019
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Article: Autoinhibition of DNA cleavage mediated by RAG1 and RAG2 is overcome by an epigenetic signal in V(D)J recombination

Grundy, Gabrielle J / Yang, Wei / Gellert, Martin

Proceedings of the National Academy of Sciences of the United States of America. 2010 Dec. 28, v. 107, no. 52

2010

Abstract: Gene assembly of the variable domain of antigen receptors is initiated by DNA cleavage by the RAG1-RAG2 protein complex at sites flanking V, D, and J gene segments. Double-strand breaks are produced via a single-strand nick that is converted to a hairpin ...

Abstract	Gene assembly of the variable domain of antigen receptors is initiated by DNA cleavage by the RAG1-RAG2 protein complex at sites flanking V, D, and J gene segments. Double-strand breaks are produced via a single-strand nick that is converted to a hairpin end on coding DNA and a blunt end on the neighboring recombination signal sequence. We demonstrate that the C-terminal regions of purified murine RAG1 (aa 1009-1040) and RAG2 (aa 388-520, including a plant homeodomain [PHD domain]) collaborate to inhibit the hairpinning stage of DNA cleavage. The C-terminal region of RAG2 stabilizes the RAG1/2 heterotetramer but destabilizes the RAG-DNA precleavage complex. This destabilization is reversed by binding of the PHD domain to a histone H3 peptide trimethylated on lysine 4 (H3K4me3). The addition of H3K4me3 likewise alleviates the RAG1/RAG2 C-terminus-mediated inhibition of hairpinning and the PHD-mediated inhibition of transposition activity. Thus a negative regulatory function of the noncore regions of RAG1/2 limits the RAG endonuclease activity in the absence of an activating methylated histone tail bound to the complex.
Keywords	DNA ; DNA damage ; antigens ; epigenetics ; genes ; histones ; lysine ; mice ; receptors ; signal peptide
Language	English
Dates of publication	2010-1228
Size	p. 22487-22492.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1014958107
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Article ; Online: Autoinhibition of DNA cleavage mediated by RAG1 and RAG2 is overcome by an epigenetic signal in V(D)J recombination.

Grundy, Gabrielle J / Yang, Wei / Gellert, Martin

Proceedings of the National Academy of Sciences of the United States of America

2010 Volume 107, Issue 52, Page(s) 22487–22492

Abstract	Gene assembly of the variable domain of antigen receptors is initiated by DNA cleavage by the RAG1-RAG2 protein complex at sites flanking V, D, and J gene segments. Double-strand breaks are produced via a single-strand nick that is converted to a hairpin end on coding DNA and a blunt end on the neighboring recombination signal sequence. We demonstrate that the C-terminal regions of purified murine RAG1 (aa 1009-1040) and RAG2 (aa 388-520, including a plant homeodomain [PHD domain]) collaborate to inhibit the hairpinning stage of DNA cleavage. The C-terminal region of RAG2 stabilizes the RAG1/2 heterotetramer but destabilizes the RAG-DNA precleavage complex. This destabilization is reversed by binding of the PHD domain to a histone H3 peptide trimethylated on lysine 4 (H3K4me3). The addition of H3K4me3 likewise alleviates the RAG1/RAG2 C-terminus-mediated inhibition of hairpinning and the PHD-mediated inhibition of transposition activity. Thus a negative regulatory function of the noncore regions of RAG1/2 limits the RAG endonuclease activity in the absence of an activating methylated histone tail bound to the complex.
MeSH term(s)	Animals ; Binding Sites ; DNA Cleavage ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Electrophoresis, Polyacrylamide Gel ; Electrophoretic Mobility Shift Assay ; Epigenomics ; HEK293 Cells ; Histones/metabolism ; Homeodomain Proteins/chemistry ; Homeodomain Proteins/genetics ; Homeodomain Proteins/metabolism ; Humans ; Lysine/metabolism ; Methylation ; Mice ; Mutation ; Protein Binding ; Protein Multimerization ; Recombination, Genetic ; Signal Transduction ; VDJ Exons/genetics
Chemical Substances	DNA-Binding Proteins ; Histones ; Homeodomain Proteins ; Rag2 protein, mouse ; RAG-1 protein (128559-51-3) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2010-12-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1014958107
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Article ; Online: The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins.

Grundy, Gabrielle J / Rulten, Stuart L / Arribas-Bosacoma, Raquel / Davidson, Kathryn / Kozik, Zuzanna / Oliver, Antony W / Pearl, Laurence H / Caldecott, Keith W

Nature communications

2016 Volume 7, Page(s) 11242

Abstract: The Ku-binding motif (KBM) is a short peptide module first identified in APLF that we now show is also present in Werner syndrome protein (WRN) and in Modulator of retrovirus infection homologue (MRI). We also identify a related but functionally distinct ...

Abstract	The Ku-binding motif (KBM) is a short peptide module first identified in APLF that we now show is also present in Werner syndrome protein (WRN) and in Modulator of retrovirus infection homologue (MRI). We also identify a related but functionally distinct motif in XLF, WRN, MRI and PAXX, which we denote the XLF-like motif. We show that WRN possesses two KBMs; one at the N terminus next to the exonuclease domain and one at the C terminus next to an XLF-like motif. We reveal that the WRN C-terminal KBM and XLF-like motif function cooperatively to bind Ku complexes and that the N-terminal KBM mediates Ku-dependent stimulation of WRN exonuclease activity. We also show that WRN accelerates DSB repair by a mechanism requiring both KBMs, demonstrating the importance of WRN interaction with Ku. These data define a conserved family of KBMs that function as molecular tethers to recruit and/or stimulate enzymes during NHEJ.
MeSH term(s)	Amino Acid Motifs ; Amino Acid Sequence ; Antigens, Nuclear/metabolism ; Conserved Sequence ; DNA Breaks, Double-Stranded ; DNA Damage ; DNA End-Joining Repair ; DNA-Binding Proteins/metabolism ; Exodeoxyribonucleases/chemistry ; Exodeoxyribonucleases/metabolism ; Humans ; Ku Autoantigen ; Models, Biological ; Molecular Sequence Data ; Protein Binding ; Protein Structure, Tertiary ; RecQ Helicases/chemistry ; RecQ Helicases/metabolism ; Werner Syndrome Helicase
Chemical Substances	Antigens, Nuclear ; DNA-Binding Proteins ; Exodeoxyribonucleases (EC 3.1.-) ; RecQ Helicases (EC 3.6.4.12) ; WRN protein, human (EC 3.6.4.12) ; Werner Syndrome Helicase (EC 3.6.4.12) ; Xrcc6 protein, human (EC 3.6.4.12) ; Ku Autoantigen (EC 4.2.99.-)
Language	English
Publishing date	2016-04-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/ncomms11242
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