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Article ; Online: The complex etiology of autism spectrum disorder due to missense mutations of CHD8.

Shiraishi, Taichi / Katayama, Yuta / Nishiyama, Masaaki / Shoji, Hirotaka / Miyakawa, Tsuyoshi / Mizoo, Taisuke / Matsumoto, Akinobu / Hijikata, Atsushi / Shirai, Tsuyoshi / Mayanagi, Kouta / Nakayama, Keiichi I

Molecular psychiatry

2024

Abstract: CHD8 is an ATP-dependent chromatin-remodeling factor encoded by the most frequently mutated gene in individuals with autism spectrum disorder (ASD). Although many studies have examined the consequences of CHD8 haploinsufficiency in cells and mice, few ... ...

Abstract	CHD8 is an ATP-dependent chromatin-remodeling factor encoded by the most frequently mutated gene in individuals with autism spectrum disorder (ASD). Although many studies have examined the consequences of CHD8 haploinsufficiency in cells and mice, few have focused on missense mutations, the most common type of CHD8 alteration in ASD patients. We here characterized CHD8 missense mutations in ASD patients according to six prediction scores and experimentally examined the effects of such mutations on the biochemical activities of CHD8, neural differentiation of embryonic stem cells, and mouse behavior. Only mutations with high prediction scores gave rise to ASD-like phenotypes in mice, suggesting that not all CHD8 missense mutations detected in ASD patients are directly responsible for the development of ASD. Furthermore, we found that mutations with high scores cause ASD by mechanisms either dependent on or independent of loss of chromatin-remodeling function. Our results thus provide insight into the molecular underpinnings of ASD pathogenesis caused by missense mutations of CHD8.
Language	English
Publishing date	2024-03-05
Publishing country	England
Document type	Journal Article
ZDB-ID	1330655-8
ISSN	1476-5578 ; 1359-4184
ISSN (online)	1476-5578
ISSN	1359-4184
DOI	10.1038/s41380-024-02491-y
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Zs.A 4812: Show issues

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Article ; Online: Dynamic action of an intrinsically disordered protein in DNA compaction that induces mycobacterial dormancy.

Nishiyama, Akihito / Shimizu, Masahiro / Narita, Tomoyuki / Kodera, Noriyuki / Ozeki, Yuriko / Yokoyama, Akira / Mayanagi, Kouta / Yamaguchi, Takehiro / Hakamata, Mariko / Shaban, Amina Kaboso / Tateishi, Yoshitaka / Ito, Kosuke / Matsumoto, Sohkichi

Nucleic acids research

2023 Volume 52, Issue 2, Page(s) 816–830

Abstract: Mycobacteria are the major human pathogens with the capacity to become dormant persisters. Mycobacterial DNA-binding protein 1 (MDP1), an abundant histone-like protein in dormant mycobacteria, induces dormancy phenotypes, e.g. chromosome compaction and ... ...

Abstract	Mycobacteria are the major human pathogens with the capacity to become dormant persisters. Mycobacterial DNA-binding protein 1 (MDP1), an abundant histone-like protein in dormant mycobacteria, induces dormancy phenotypes, e.g. chromosome compaction and growth suppression. For these functions, the polycationic intrinsically disordered region (IDR) is essential. However, the disordered property of IDR stands in the way of clarifying the molecular mechanism. Here we clarified the molecular and structural mechanism of DNA compaction by MDP1. Using high-speed atomic force microscopy, we observed that monomeric MDP1 bundles two adjacent DNA duplexes side-by-side via IDR. Combined with coarse-grained molecular dynamics simulation, we revealed the novel dynamic DNA cross-linking model of MDP1 in which a stretched IDR cross-links two DNA duplexes like double-sided tape. IDR is able to hijack HU function, resulting in the induction of strong mycobacterial growth arrest. This IDR-mediated reversible DNA cross-linking is a reasonable model for MDP1 suppression of the genomic function in the resuscitable non-replicating dormant mycobacteria.
MeSH term(s)	DNA/metabolism ; Histones ; Intrinsically Disordered Proteins/metabolism ; Mycobacterium/metabolism ; DNA Packaging
Chemical Substances	DNA (9007-49-2) ; Histones ; Intrinsically Disordered Proteins ; MDP1 protein, Mycobacterium
Language	English
Publishing date	2023-11-27
Publishing country	England
Document type	Journal Article
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkad1149
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Zs.A 1067: Show issues

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Article ; Online: DNA polymerase D temporarily connects primase to the CMG-like helicase before interacting with proliferating cell nuclear antigen.

Oki, Keisuke / Yamagami, Takeshi / Nagata, Mariko / Mayanagi, Kouta / Shirai, Tsuyoshi / Adachi, Naruhiko / Numata, Tomoyuki / Ishino, Sonoko / Ishino, Yoshizumi

Nucleic acids research

2021 Volume 49, Issue 8, Page(s) 4599–4612

Abstract: The eukaryotic replisome is comprised of three family-B DNA polymerases (Polα, δ and ϵ). Polα forms a stable complex with primase to synthesize short RNA-DNA primers, which are subsequently elongated by Polδ and Polϵ in concert with proliferating cell ... ...

Abstract	The eukaryotic replisome is comprised of three family-B DNA polymerases (Polα, δ and ϵ). Polα forms a stable complex with primase to synthesize short RNA-DNA primers, which are subsequently elongated by Polδ and Polϵ in concert with proliferating cell nuclear antigen (PCNA). In some species of archaea, family-D DNA polymerase (PolD) is the only DNA polymerase essential for cell viability, raising the question of how it alone conducts the bulk of DNA synthesis. We used a hyperthermophilic archaeon, Thermococcus kodakarensis, to demonstrate that PolD connects primase to the archaeal replisome before interacting with PCNA. Whereas PolD stably connects primase to GINS, a component of CMG helicase, cryo-EM analysis indicated a highly flexible PolD-primase complex. A conserved hydrophobic motif at the C-terminus of the DP2 subunit of PolD, a PIP (PCNA-Interacting Peptide) motif, was critical for the interaction with primase. The dissociation of primase was induced by DNA-dependent binding of PCNA to PolD. Point mutations in the alternative PIP-motif of DP2 abrogated the molecular switching that converts the archaeal replicase from de novo to processive synthesis mode.
MeSH term(s)	Amino Acid Motifs ; Archaeal Proteins/chemistry ; Archaeal Proteins/metabolism ; Chromatography, Gel ; DNA Helicases/genetics ; DNA Helicases/metabolism ; DNA Polymerase III/chemistry ; DNA Polymerase III/metabolism ; DNA Primase/chemistry ; DNA Primase/genetics ; DNA Primase/metabolism ; Escherichia coli/metabolism ; Hydrophobic and Hydrophilic Interactions ; Mutagenesis, Site-Directed ; Native Polyacrylamide Gel Electrophoresis ; Proliferating Cell Nuclear Antigen/genetics ; Proliferating Cell Nuclear Antigen/metabolism ; Protein Binding ; Recombinant Proteins ; Surface Plasmon Resonance ; Thermococcus/genetics ; Thermococcus/metabolism
Chemical Substances	Archaeal Proteins ; Proliferating Cell Nuclear Antigen ; Recombinant Proteins ; DNA Primase (EC 2.7.7.-) ; DNA Polymerase III (EC 2.7.7.7) ; DNA Helicases (EC 3.6.4.-)
Language	English
Publishing date	2021-03-29
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkab243
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Article: Single-particle analysis of full-length human poly(ADP-ribose) polymerase 1.

Kouyama, Kenichi / Mayanagi, Kouta / Nakae, Setsu / Nishi, Yoshisuke / Miwa, Masanao / Shirai, Tsuyoshi

Biophysics and physicobiology

2019 Volume 16, Page(s) 59–67

Abstract: PolyADP-ribosylation (PARylation) is a posttranslational modification that is involved in the various cellular functions including DNA repair, genomic stability, and transcriptional regulation. PARylation is catalyzed by the poly(ADP-ribose) polymerase ( ... ...

Abstract	PolyADP-ribosylation (PARylation) is a posttranslational modification that is involved in the various cellular functions including DNA repair, genomic stability, and transcriptional regulation. PARylation is catalyzed by the poly(ADP-ribose) polymerase (PARP) family proteins, which mainly recognize damaged DNA and initiate repair processes. PARP inhibitors are expected to be novel anticancer drugs for breast and ovarian cancers having mutation in
Language	English
Publishing date	2019-02-06
Publishing country	Japan
Document type	Journal Article
ISSN	2189-4779
ISSN	2189-4779
DOI	10.2142/biophysico.16.0_59
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Article ; Online: Inhibition of G protein-coupled receptor 68 using homoharringtonine attenuates chronic kidney disease-associated cardiac impairment.

Translational research : the journal of laboratory and clinical medicine

2024 Volume 269, Page(s) 31–46

Abstract: Chronic kidney disease (CKD) induces cardiac inflammation and fibrosis and reduces survival. We previously demonstrated that G protein-coupled receptor 68 (GPR68) promotes cardiac inflammation and fibrosis in mice with 5/6 nephrectomy (5/6Nx) and ... ...

Abstract	Chronic kidney disease (CKD) induces cardiac inflammation and fibrosis and reduces survival. We previously demonstrated that G protein-coupled receptor 68 (GPR68) promotes cardiac inflammation and fibrosis in mice with 5/6 nephrectomy (5/6Nx) and patients with CKD. However, no method of GPR68 inhibition has been found that has potential for therapeutic application. Here, we report that Cephalotaxus harringtonia var. nana extract and homoharringtonine ameliorate cardiac inflammation and fibrosis under CKD by suppressing GPR68 function. Reagents that inhibit the function of GPR68 were explored by high-throughput screening using a medicinal plant extract library (8,008 species), and we identified an extract from Cephalotaxus harringtonia var. nana as a GPR68 inhibitor that suppresses inflammatory cytokine production in a GPR68 expression-dependent manner. Consumption of the extract inhibited inflammatory cytokine expression and cardiac fibrosis and improved the decreased survival attributable to 5/6Nx. Additionally, homoharringtonine, a cephalotaxane compound characteristic of C. harringtonia, inhibited inflammatory cytokine production. Homoharringtonine administration in drinking water alleviated cardiac fibrosis and improved heart failure and survival in 5/6Nx mice. A previously unknown effect of C. harringtonia extract and homoharringtonine was revealed in which GPR68-dependent inflammation and cardiac dysfunction were suppressed. Utilizing these compounds could represent a new strategy for treating GPR68-associated diseases, including CKD.
MeSH term(s)	Animals ; Receptors, G-Protein-Coupled/metabolism ; Renal Insufficiency, Chronic/drug therapy ; Renal Insufficiency, Chronic/metabolism ; Renal Insufficiency, Chronic/pathology ; Renal Insufficiency, Chronic/complications ; Plant Extracts/pharmacology ; Plant Extracts/therapeutic use ; Male ; Mice, Inbred C57BL ; Homoharringtonine/pharmacology ; Homoharringtonine/therapeutic use ; Mice ; Cytokines/metabolism ; Fibrosis ; Humans ; Heart Diseases/drug therapy ; Heart Diseases/etiology
Chemical Substances	Receptors, G-Protein-Coupled ; Plant Extracts ; Homoharringtonine (6FG8041S5B) ; Cytokines
Language	English
Publishing date	2024-02-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2246684-8
ISSN	1878-1810 ; 1532-6543 ; 1931-5244
ISSN (online)	1878-1810 ; 1532-6543
ISSN	1931-5244
DOI	10.1016/j.trsl.2024.02.004
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Ud II Zs 42: Show issues

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Article ; Online: Two conformations of DNA polymerase D-PCNA-DNA, an archaeal replisome complex, revealed by cryo-electron microscopy.

Mayanagi, Kouta / Oki, Keisuke / Miyazaki, Naoyuki / Ishino, Sonoko / Yamagami, Takeshi / Morikawa, Kosuke / Iwasaki, Kenji / Kohda, Daisuke / Shirai, Tsuyoshi / Ishino, Yoshizumi

BMC biology

2020 Volume 18, Issue 1, Page(s) 152

Abstract: Background: DNA polymerase D (PolD) is the representative member of the D family of DNA polymerases. It is an archaea-specific DNA polymerase required for replication and unrelated to other known DNA polymerases. PolD consists of a heterodimer of two ... ...

Abstract	Background: DNA polymerase D (PolD) is the representative member of the D family of DNA polymerases. It is an archaea-specific DNA polymerase required for replication and unrelated to other known DNA polymerases. PolD consists of a heterodimer of two subunits, DP1 and DP2, which contain catalytic sites for 3'-5' editing exonuclease and DNA polymerase activities, respectively, with both proteins being mutually required for the full activities of each enzyme. However, the processivity of the replicase holoenzyme has additionally been shown to be enhanced by the clamp molecule proliferating cell nuclear antigen (PCNA), making it crucial to elucidate the interaction between PolD and PCNA on a structural level for a full understanding of its functional relevance. We present here the 3D structure of a PolD-PCNA-DNA complex from Thermococcus kodakarensis using single-particle cryo-electron microscopy (EM). Results: Two distinct forms of the PolD-PCNA-DNA complex were identified by 3D classification analysis. Fitting the reported crystal structures of truncated forms of DP1 and DP2 from Pyrococcus abyssi onto our EM map showed the 3D atomic structural model of PolD-PCNA-DNA. In addition to the canonical interaction between PCNA and PolD via PIP (PCNA-interacting protein)-box motif, we found a new contact point consisting of a glutamate residue at position 171 in a β-hairpin of PCNA, which mediates interactions with DP1 and DP2. The DNA synthesis activity of a mutant PolD with disruption of the E171-mediated PCNA interaction was not stimulated by PCNA in vitro. Conclusions: Based on our analyses, we propose that glutamate residues at position 171 in each subunit of the PCNA homotrimer ring can function as hooks to lock PolD conformation on PCNA for conversion of its activity. This hook function of the clamp molecule may be conserved in the three domains of life.
Language	English
Publishing date	2020-10-28
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1741-7007
ISSN (online)	1741-7007
DOI	10.1186/s12915-020-00889-y
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Article ; Online: Chemical acetylation of mitochondrial transcription factor A occurs on specific lysine residues and affects its ability to change global DNA topology.

Fang, Yuan / Akimoto, Masaru / Mayanagi, Kouta / Hatano, Atsushi / Matsumoto, Masaki / Matsuda, Shigeru / Yasukawa, Takehiro / Kang, Dongchon

Mitochondrion

2020 Volume 53, Page(s) 99–108

Abstract: Chemical acetylation is postulated to occur in mitochondria. Mitochondrial transcription factor A (TFAM or mtTFA), a mitochondrial transcription initiation factor as well as the major mitochondrial nucleoid protein coating the entire mitochondrial genome, ...

Abstract	Chemical acetylation is postulated to occur in mitochondria. Mitochondrial transcription factor A (TFAM or mtTFA), a mitochondrial transcription initiation factor as well as the major mitochondrial nucleoid protein coating the entire mitochondrial genome, is proposed to be acetylated in animals and cultured cells. This study investigated the properties of human TFAM, in conjunction with the mechanism and effects of TFAM acetylation in vitro. Using highly purified recombinant human TFAM and 3 kb circular DNA as a downsized mtDNA model, we studied how the global TFAM-DNA interaction is affected/regulated by the quantitative TFAM-DNA relationship and TFAM acetylation. Results showed that the TFAM-DNA ratio strictly affects the TFAM property to unwind circular DNA in the presence of topoisomerase I. Mass spectrometry analysis showed that in vitro chemical acetylation of TFAM with acetyl-coenzyme A occurs preferentially on specific lysine residues, including those reported to be acetylated in exogenously expressed TFAM in cultured human cells, indicating that chemical acetylation plays a crucial role in TFAM acetylation in mitochondria. Intriguingly, the modification significantly decreased TFAM's DNA-unwinding ability, while its DNA-binding ability was largely unaffected. Altogether, we propose TFAM is chemically acetylated in vivo, which could change mitochondrial DNA topology, leading to copy number and gene expression modulation.
MeSH term(s)	Acetylation ; DNA/genetics ; DNA/metabolism ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Humans ; Lysine/chemistry ; Mitochondrial Proteins/chemistry ; Mitochondrial Proteins/metabolism ; Models, Molecular ; Protein Conformation ; Transcription Factors/chemistry ; Transcription Factors/metabolism ; Transcription, Genetic
Chemical Substances	DNA-Binding Proteins ; Mitochondrial Proteins ; TFAM protein, human ; Transcription Factors ; DNA (9007-49-2) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2020-05-18
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2056923-3
ISSN	1872-8278 ; 1567-7249
ISSN (online)	1872-8278
ISSN	1567-7249
DOI	10.1016/j.mito.2020.05.003
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Article ; Online: Filopodia formation by crosslinking of F-actin with fascin in two different binding manners.

Aramaki, Shinji / Mayanagi, Kouta / Jin, Mingyue / Aoyama, Kazuhiro / Yasunaga, Takuo

Cytoskeleton (Hoboken, N.J.)

2016 Volume 73, Issue 7, Page(s) 365–374

Abstract: Filopodia are finger-like protrusions at the leading edge of migrating cells that play a crucial antennal function during cell motility. It is known that actin filaments are bundled hexagonally and provide rigidity to filopodia by virtue of fascin, which ...

Abstract	Filopodia are finger-like protrusions at the leading edge of migrating cells that play a crucial antennal function during cell motility. It is known that actin filaments are bundled hexagonally and provide rigidity to filopodia by virtue of fascin, which plays a central role in actin filament bundling. However, the molecular mechanisms underlying their formation remain unclear. Here, we observed the filopodia of intact whole cells fixed by rapid freezing and revealed their three-dimensional structure by cryo-electron tomography and image processing; the actin filament bundling structure by fascin was clarified at high resolution under physiological conditions. It was found that actin filaments in vivo were more numerous than in bundles reconstructed in vitro, and each filopodial actin filament had limited variability in helical twisting. In addition, statistical analysis of actin filament bundles unveiled their detailed architecture. In filopodia, actin filaments had highly ordered structures, and the shift between cross-links of each adjacent actin filament was approximately 2.7 nm, similar to the monomer repeat of actin filaments. We then proposed a plausible actin-fascin cross-link model at the amino acid level and identified three fascin binding sites on two adjacent actin filaments: one filament bound fascin at two discrete, widely separated regions and the other bound fascin in a single small region. We propose that these two different binding modalities should confer rigid bundles that retain flexibility and dynamic performance. © 2016 Wiley Periodicals, Inc.
Language	English
Publishing date	2016-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	2534372-5
ISSN	1949-3592 ; 1949-3584
ISSN (online)	1949-3592
ISSN	1949-3584
DOI	10.1002/cm.21309
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Zs.A 1840: Show issues

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Article ; Online: Structural visualization of key steps in nucleosome reorganization by human FACT.

Mayanagi, Kouta / Saikusa, Kazumi / Miyazaki, Naoyuki / Akashi, Satoko / Iwasaki, Kenji / Nishimura, Yoshifumi / Morikawa, Kosuke / Tsunaka, Yasuo

Scientific reports

2019 Volume 9, Issue 1, Page(s) 10183

Abstract: Facilitates chromatin transcription (FACT) is a histone chaperone, which accomplishes both nucleosome assembly and disassembly. Our combined cryo-electron microscopy (EM) and native mass spectrometry (MS) studies revealed novel key steps of nucleosome ... ...

Abstract	Facilitates chromatin transcription (FACT) is a histone chaperone, which accomplishes both nucleosome assembly and disassembly. Our combined cryo-electron microscopy (EM) and native mass spectrometry (MS) studies revealed novel key steps of nucleosome reorganization conducted by a Mid domain and its adjacent acidic AID segment of human FACT. We determined three cryo-EM structures of respective octasomes complexed with the Mid-AID and AID regions, and a hexasome alone. We discovered extensive contacts between a FACT region and histones H2A, H2B, and H3, suggesting that FACT is competent to direct functional replacement of a nucleosomal DNA end by its phosphorylated AID segment (pAID). Mutational assays revealed that the aromatic and phosphorylated residues within pAID are essential for octasome binding. The EM structure of the hexasome, generated by the addition of Mid-pAID or pAID, indicated that the dissociation of H2A-H2B dimer causes significant alteration from the canonical path of the nucleosomal DNA.
MeSH term(s)	Chromatin/chemistry ; Chromatin Assembly and Disassembly/physiology ; Cryoelectron Microscopy/methods ; DNA/chemistry ; DNA-Binding Proteins/metabolism ; DNA-Binding Proteins/physiology ; High Mobility Group Proteins/metabolism ; High Mobility Group Proteins/physiology ; Histones/metabolism ; Histones/physiology ; Humans ; Mass Spectrometry/methods ; Models, Molecular ; Molecular Chaperones/metabolism ; Nucleosomes/metabolism ; Nucleosomes/physiology ; Protein Binding/physiology ; Transcriptional Elongation Factors/metabolism ; Transcriptional Elongation Factors/physiology
Chemical Substances	Chromatin ; DNA-Binding Proteins ; High Mobility Group Proteins ; Histones ; Molecular Chaperones ; Nucleosomes ; SSRP1 protein, human ; Transcriptional Elongation Factors ; DNA (9007-49-2)
Language	English
Publishing date	2019-07-15
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/s41598-019-46617-7
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Article ; Online: Direct visualization of DNA baton pass between replication factors bound to PCNA.

Mayanagi, Kouta / Ishino, Sonoko / Shirai, Tsuyoshi / Oyama, Takuji / Kiyonari, Shinichi / Kohda, Daisuke / Morikawa, Kosuke / Ishino, Yoshizumi

Scientific reports

2018 Volume 8, Issue 1, Page(s) 16209

Abstract: In Eukarya and Archaea, the lagging strand synthesis is accomplished mainly by three key factors, DNA polymerase (Pol), flap endonuclease (FEN), and DNA ligase (Lig), in the DNA replication process. These three factors form important complexes with ... ...

Abstract	In Eukarya and Archaea, the lagging strand synthesis is accomplished mainly by three key factors, DNA polymerase (Pol), flap endonuclease (FEN), and DNA ligase (Lig), in the DNA replication process. These three factors form important complexes with proliferating cell nuclear antigen (PCNA), thereby constructing a platform that enable each protein factor to act successively and smoothly on DNA. The structures of the Pol-PCNA-DNA and Lig-PCNA-DNA complexes alone have been visualized by single particle analysis. However, the FEN-PCNA-DNA complex structure remains unknown. In this report, we for the first time present this tertiary structure determined by single particle analysis. We also successfully visualized the structure of the FEN-Lig-PCNA-DNA complex, corresponding to a putative intermediate state between the removal of the DNA flap by FEN and the sealing of the nicked DNA by Lig. This structural study presents the direct visualization of the handing-over action, which proceeds between different replication factors on a single PCNA clamp bound to DNA. We detected a drastic conversion of the DNA from a bent form to a straight form, in addition to the dynamic motions of replication factors in the switching process.
MeSH term(s)	Base Sequence ; Binding Sites ; DNA/chemistry ; DNA/genetics ; DNA/metabolism ; DNA Replication ; Models, Biological ; Models, Molecular ; Molecular Conformation ; Proliferating Cell Nuclear Antigen/chemistry ; Proliferating Cell Nuclear Antigen/metabolism ; Protein Binding ; Structure-Activity Relationship
Chemical Substances	Proliferating Cell Nuclear Antigen ; DNA (9007-49-2)
Language	English
Publishing date	2018-11-01
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/s41598-018-34176-2
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