Structure of the human GINS complex and its assembly and functional interface in replication initiation View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2007-04-08

AUTHORS

Katsuhiko Kamada, Yumiko Kubota, Toshiaki Arata, Yosuke Shindo, Fumio Hanaoka

ABSTRACT

The eukaryotic GINS complex is essential for the establishment of DNA replication forks and replisome progression. We report the crystal structure of the human GINS complex. The heterotetrameric complex adopts a pseudo symmetrical layered structure comprising two heterodimers, creating four subunit-subunit interfaces. The subunit structures of the heterodimers consist of two alternating domains. The C-terminal domains of the Sld5 and Psf1 subunits are connected by linker regions to the core complex, and the C-terminal domain of Sld5 is important for core complex assembly. In contrast, the C-terminal domain of Psf1 does not contribute to the stability of the complex but is crucial for chromatin binding and replication activity. These data suggest that the core complex ensures a stable platform for the C-terminal domain of Psf1 to act as a key interaction interface for other proteins in the replication-initiation process. More... »

PAGES

388-396

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb1231

DOI

http://dx.doi.org/10.1038/nsmb1231

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1033117161

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17417653


Indexing Status Check whether this publication has been indexed by Scopus and Web Of Science using the SN Indexing Status Tool
Incoming Citations Browse incoming citations for this publication using opencitations.net

JSON-LD is the canonical representation for SciGraph data.

TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT

[
  {
    "@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json", 
    "about": [
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/06", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Biological Sciences", 
        "type": "DefinedTerm"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0601", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Biochemistry and Cell Biology", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "ATP Binding Cassette Transporter, Subfamily B, Member 2", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "ATP Binding Cassette Transporter, Subfamily B, Member 3", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "ATP-Binding Cassette Transporters", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Carrier Proteins", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Chromosomal Proteins, Non-Histone", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Crystallography, X-Ray", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "DNA Replication", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "DNA-Binding Proteins", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Dimerization", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Humans", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Multiprotein Complexes", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Protein Subunits", 
        "type": "DefinedTerm"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "Cellular Physiology Laboratory, RIKEN Discovery Research Institute, 2-1 Hirosawa, 351-0198, Wako, Saitama, Japan", 
          "id": "http://www.grid.ac/institutes/grid.7597.c", 
          "name": [
            "Cellular Physiology Laboratory, RIKEN Discovery Research Institute, 2-1 Hirosawa, 351-0198, Wako, Saitama, Japan"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Kamada", 
        "givenName": "Katsuhiko", 
        "id": "sg:person.010563553305.63", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.010563553305.63"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama-chyo, 560-0043, Toyonaka, Osaka, Japan", 
          "id": "http://www.grid.ac/institutes/grid.136593.b", 
          "name": [
            "Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama-chyo, 560-0043, Toyonaka, Osaka, Japan"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Kubota", 
        "givenName": "Yumiko", 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama-chyo, 560-0043, Toyonaka, Osaka, Japan", 
          "id": "http://www.grid.ac/institutes/grid.136593.b", 
          "name": [
            "Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama-chyo, 560-0043, Toyonaka, Osaka, Japan"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Arata", 
        "givenName": "Toshiaki", 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama-chyo, 560-0043, Toyonaka, Osaka, Japan", 
          "id": "http://www.grid.ac/institutes/grid.136593.b", 
          "name": [
            "Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama-chyo, 560-0043, Toyonaka, Osaka, Japan"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Shindo", 
        "givenName": "Yosuke", 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamada-oka, 565-0871, Suita, Osaka, Japan", 
          "id": "http://www.grid.ac/institutes/grid.136593.b", 
          "name": [
            "Cellular Physiology Laboratory, RIKEN Discovery Research Institute, 2-1 Hirosawa, 351-0198, Wako, Saitama, Japan", 
            "Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamada-oka, 565-0871, Suita, Osaka, Japan"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Hanaoka", 
        "givenName": "Fumio", 
        "id": "sg:person.01177247732.44", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01177247732.44"
        ], 
        "type": "Person"
      }
    ], 
    "citation": [
      {
        "id": "sg:pub.10.1038/nrm1663", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1012862888", 
          "https://doi.org/10.1038/nrm1663"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/ncb1382", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1020448729", 
          "https://doi.org/10.1038/ncb1382"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1186/1747-1028-1-18", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1037795881", 
          "https://doi.org/10.1186/1747-1028-1-18"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/nature01692", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1002035791", 
          "https://doi.org/10.1038/nature01692"
        ], 
        "type": "CreativeWork"
      }
    ], 
    "datePublished": "2007-04-08", 
    "datePublishedReg": "2007-04-08", 
    "description": "The eukaryotic GINS complex is essential for the establishment of DNA replication forks and replisome progression. We report the crystal structure of the human GINS complex. The heterotetrameric complex adopts a pseudo symmetrical layered structure comprising two heterodimers, creating four subunit-subunit interfaces. The subunit structures of the heterodimers consist of two alternating domains. The C-terminal domains of the Sld5 and Psf1 subunits are connected by linker regions to the core complex, and the C-terminal domain of Sld5 is important for core complex assembly. In contrast, the C-terminal domain of Psf1 does not contribute to the stability of the complex but is crucial for chromatin binding and replication activity. These data suggest that the core complex ensures a stable platform for the C-terminal domain of Psf1 to act as a key interaction interface for other proteins in the replication-initiation process.", 
    "genre": "article", 
    "id": "sg:pub.10.1038/nsmb1231", 
    "inLanguage": "en", 
    "isAccessibleForFree": false, 
    "isPartOf": [
      {
        "id": "sg:journal.1295033", 
        "issn": [
          "1545-9993", 
          "2331-365X"
        ], 
        "name": "Nature Structural & Molecular Biology", 
        "publisher": "Springer Nature", 
        "type": "Periodical"
      }, 
      {
        "issueNumber": "5", 
        "type": "PublicationIssue"
      }, 
      {
        "type": "PublicationVolume", 
        "volumeNumber": "14"
      }
    ], 
    "keywords": [
      "human GINS complex", 
      "GINS complex", 
      "terminal domain", 
      "eukaryotic GINS complex", 
      "core complex assembly", 
      "DNA replication forks", 
      "core complex", 
      "replisome progression", 
      "chromatin binding", 
      "replication initiation", 
      "replication forks", 
      "heterotetrameric complex", 
      "complex assembly", 
      "linker region", 
      "subunit structure", 
      "replication activity", 
      "subunit interface", 
      "interaction interface", 
      "SLD5", 
      "PSF1", 
      "heterodimers", 
      "complexes", 
      "domain", 
      "assembly", 
      "subunits", 
      "forks", 
      "protein", 
      "functional interface", 
      "crystal structure", 
      "binding", 
      "establishment", 
      "structure", 
      "initiation", 
      "activity", 
      "progression", 
      "region", 
      "contrast", 
      "process", 
      "data", 
      "stability", 
      "platform", 
      "interface", 
      "stable platform", 
      "layered structure", 
      "pseudo symmetrical layered structure", 
      "symmetrical layered structure", 
      "Psf1 subunits", 
      "key interaction interface", 
      "replication-initiation process"
    ], 
    "name": "Structure of the human GINS complex and its assembly and functional interface in replication initiation", 
    "pagination": "388-396", 
    "productId": [
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1033117161"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1038/nsmb1231"
        ]
      }, 
      {
        "name": "pubmed_id", 
        "type": "PropertyValue", 
        "value": [
          "17417653"
        ]
      }
    ], 
    "sameAs": [
      "https://doi.org/10.1038/nsmb1231", 
      "https://app.dimensions.ai/details/publication/pub.1033117161"
    ], 
    "sdDataset": "articles", 
    "sdDatePublished": "2021-11-01T18:10", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-springernature-scigraph/baseset/20211101/entities/gbq_results/article/article_434.jsonl", 
    "type": "ScholarlyArticle", 
    "url": "https://doi.org/10.1038/nsmb1231"
  }
]
 

Download the RDF metadata as:  json-ld nt turtle xml License info

HOW TO GET THIS DATA PROGRAMMATICALLY:

JSON-LD is a popular format for linked data which is fully compatible with JSON.

curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1038/nsmb1231'

N-Triples is a line-based linked data format ideal for batch operations.

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/nsmb1231'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/nsmb1231'

RDF/XML is a standard XML format for linked data.

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/nsmb1231'


 

This table displays all metadata directly associated to this object as RDF triples.

206 TRIPLES      22 PREDICATES      91 URIs      79 LITERALS      19 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1038/nsmb1231 schema:about N0eff87454cb84289a0612d270816c759
2 N1351a0f439f4422080e6cccc788bc80e
3 N18babd61ee444d23823a3ac820e27751
4 N206ee33ff693405294e39acb572eabf3
5 N4c2c83cd96a64c8496624efa1c73fffa
6 N8be80444df654a22a157b7b70f4169f2
7 Nd7883669ebc34d41a99ab53bcd223ec5
8 Ne7c962c03ab64c59a11ac9d0865ddccb
9 Ne7d8a939bb4f4c3ea52376afa4b6b59c
10 Ne927657f52ef434e9d4a8b4ad6605eeb
11 Nf44559d8eeda4d8b9ff3ddbcd44afaf3
12 Nf78886d36c964e36bbaf0c10995e1c9b
13 anzsrc-for:06
14 anzsrc-for:0601
15 schema:author Ne0906a74a1d141d2b4b2f51acf2a1288
16 schema:citation sg:pub.10.1038/nature01692
17 sg:pub.10.1038/ncb1382
18 sg:pub.10.1038/nrm1663
19 sg:pub.10.1186/1747-1028-1-18
20 schema:datePublished 2007-04-08
21 schema:datePublishedReg 2007-04-08
22 schema:description The eukaryotic GINS complex is essential for the establishment of DNA replication forks and replisome progression. We report the crystal structure of the human GINS complex. The heterotetrameric complex adopts a pseudo symmetrical layered structure comprising two heterodimers, creating four subunit-subunit interfaces. The subunit structures of the heterodimers consist of two alternating domains. The C-terminal domains of the Sld5 and Psf1 subunits are connected by linker regions to the core complex, and the C-terminal domain of Sld5 is important for core complex assembly. In contrast, the C-terminal domain of Psf1 does not contribute to the stability of the complex but is crucial for chromatin binding and replication activity. These data suggest that the core complex ensures a stable platform for the C-terminal domain of Psf1 to act as a key interaction interface for other proteins in the replication-initiation process.
23 schema:genre article
24 schema:inLanguage en
25 schema:isAccessibleForFree false
26 schema:isPartOf N7a528494c7494eb6b61e8eb935c8eb3a
27 Nda7d1c43858348f8a35e8bcc3408c3b6
28 sg:journal.1295033
29 schema:keywords DNA replication forks
30 GINS complex
31 PSF1
32 Psf1 subunits
33 SLD5
34 activity
35 assembly
36 binding
37 chromatin binding
38 complex assembly
39 complexes
40 contrast
41 core complex
42 core complex assembly
43 crystal structure
44 data
45 domain
46 establishment
47 eukaryotic GINS complex
48 forks
49 functional interface
50 heterodimers
51 heterotetrameric complex
52 human GINS complex
53 initiation
54 interaction interface
55 interface
56 key interaction interface
57 layered structure
58 linker region
59 platform
60 process
61 progression
62 protein
63 pseudo symmetrical layered structure
64 region
65 replication activity
66 replication forks
67 replication initiation
68 replication-initiation process
69 replisome progression
70 stability
71 stable platform
72 structure
73 subunit interface
74 subunit structure
75 subunits
76 symmetrical layered structure
77 terminal domain
78 schema:name Structure of the human GINS complex and its assembly and functional interface in replication initiation
79 schema:pagination 388-396
80 schema:productId N9314ebe37863442c96225f9e3a906e6d
81 Ne3cb7102d0c543c7a95c3f7db759936a
82 Ne908894a9c3445c2af7ab2b9cf83283d
83 schema:sameAs https://app.dimensions.ai/details/publication/pub.1033117161
84 https://doi.org/10.1038/nsmb1231
85 schema:sdDatePublished 2021-11-01T18:10
86 schema:sdLicense https://scigraph.springernature.com/explorer/license/
87 schema:sdPublisher N2c84e4b1ccb947abb2555ac1e917be13
88 schema:url https://doi.org/10.1038/nsmb1231
89 sgo:license sg:explorer/license/
90 sgo:sdDataset articles
91 rdf:type schema:ScholarlyArticle
92 N06ea9b3fa86d4609b5964584a316ee98 schema:affiliation grid-institutes:grid.136593.b
93 schema:familyName Shindo
94 schema:givenName Yosuke
95 rdf:type schema:Person
96 N070707875bba4b138a7aa6a730fde243 schema:affiliation grid-institutes:grid.136593.b
97 schema:familyName Kubota
98 schema:givenName Yumiko
99 rdf:type schema:Person
100 N0eff87454cb84289a0612d270816c759 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
101 schema:name ATP Binding Cassette Transporter, Subfamily B, Member 2
102 rdf:type schema:DefinedTerm
103 N1351a0f439f4422080e6cccc788bc80e schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
104 schema:name Dimerization
105 rdf:type schema:DefinedTerm
106 N14b42b4c3a38452bb1f45a941524f856 rdf:first N06ea9b3fa86d4609b5964584a316ee98
107 rdf:rest N678407814ade4f25aa35c1dec7b09df9
108 N18babd61ee444d23823a3ac820e27751 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
109 schema:name DNA-Binding Proteins
110 rdf:type schema:DefinedTerm
111 N206ee33ff693405294e39acb572eabf3 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
112 schema:name ATP Binding Cassette Transporter, Subfamily B, Member 3
113 rdf:type schema:DefinedTerm
114 N23f96040d8584c34b887eb851d4a743f schema:affiliation grid-institutes:grid.136593.b
115 schema:familyName Arata
116 schema:givenName Toshiaki
117 rdf:type schema:Person
118 N2c84e4b1ccb947abb2555ac1e917be13 schema:name Springer Nature - SN SciGraph project
119 rdf:type schema:Organization
120 N4c2c83cd96a64c8496624efa1c73fffa schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
121 schema:name Chromosomal Proteins, Non-Histone
122 rdf:type schema:DefinedTerm
123 N678407814ade4f25aa35c1dec7b09df9 rdf:first sg:person.01177247732.44
124 rdf:rest rdf:nil
125 N7a528494c7494eb6b61e8eb935c8eb3a schema:issueNumber 5
126 rdf:type schema:PublicationIssue
127 N8b46285eb7604c70b59e94b2109dcd2a rdf:first N070707875bba4b138a7aa6a730fde243
128 rdf:rest Na788b1879ea54e75afe3fcd2a25089a1
129 N8be80444df654a22a157b7b70f4169f2 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
130 schema:name Protein Subunits
131 rdf:type schema:DefinedTerm
132 N9314ebe37863442c96225f9e3a906e6d schema:name pubmed_id
133 schema:value 17417653
134 rdf:type schema:PropertyValue
135 Na788b1879ea54e75afe3fcd2a25089a1 rdf:first N23f96040d8584c34b887eb851d4a743f
136 rdf:rest N14b42b4c3a38452bb1f45a941524f856
137 Nd7883669ebc34d41a99ab53bcd223ec5 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
138 schema:name Carrier Proteins
139 rdf:type schema:DefinedTerm
140 Nda7d1c43858348f8a35e8bcc3408c3b6 schema:volumeNumber 14
141 rdf:type schema:PublicationVolume
142 Ne0906a74a1d141d2b4b2f51acf2a1288 rdf:first sg:person.010563553305.63
143 rdf:rest N8b46285eb7604c70b59e94b2109dcd2a
144 Ne3cb7102d0c543c7a95c3f7db759936a schema:name doi
145 schema:value 10.1038/nsmb1231
146 rdf:type schema:PropertyValue
147 Ne7c962c03ab64c59a11ac9d0865ddccb schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
148 schema:name DNA Replication
149 rdf:type schema:DefinedTerm
150 Ne7d8a939bb4f4c3ea52376afa4b6b59c schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
151 schema:name Multiprotein Complexes
152 rdf:type schema:DefinedTerm
153 Ne908894a9c3445c2af7ab2b9cf83283d schema:name dimensions_id
154 schema:value pub.1033117161
155 rdf:type schema:PropertyValue
156 Ne927657f52ef434e9d4a8b4ad6605eeb schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
157 schema:name Humans
158 rdf:type schema:DefinedTerm
159 Nf44559d8eeda4d8b9ff3ddbcd44afaf3 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
160 schema:name ATP-Binding Cassette Transporters
161 rdf:type schema:DefinedTerm
162 Nf78886d36c964e36bbaf0c10995e1c9b schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
163 schema:name Crystallography, X-Ray
164 rdf:type schema:DefinedTerm
165 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
166 schema:name Biological Sciences
167 rdf:type schema:DefinedTerm
168 anzsrc-for:0601 schema:inDefinedTermSet anzsrc-for:
169 schema:name Biochemistry and Cell Biology
170 rdf:type schema:DefinedTerm
171 sg:journal.1295033 schema:issn 1545-9993
172 2331-365X
173 schema:name Nature Structural & Molecular Biology
174 schema:publisher Springer Nature
175 rdf:type schema:Periodical
176 sg:person.010563553305.63 schema:affiliation grid-institutes:grid.7597.c
177 schema:familyName Kamada
178 schema:givenName Katsuhiko
179 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.010563553305.63
180 rdf:type schema:Person
181 sg:person.01177247732.44 schema:affiliation grid-institutes:grid.136593.b
182 schema:familyName Hanaoka
183 schema:givenName Fumio
184 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01177247732.44
185 rdf:type schema:Person
186 sg:pub.10.1038/nature01692 schema:sameAs https://app.dimensions.ai/details/publication/pub.1002035791
187 https://doi.org/10.1038/nature01692
188 rdf:type schema:CreativeWork
189 sg:pub.10.1038/ncb1382 schema:sameAs https://app.dimensions.ai/details/publication/pub.1020448729
190 https://doi.org/10.1038/ncb1382
191 rdf:type schema:CreativeWork
192 sg:pub.10.1038/nrm1663 schema:sameAs https://app.dimensions.ai/details/publication/pub.1012862888
193 https://doi.org/10.1038/nrm1663
194 rdf:type schema:CreativeWork
195 sg:pub.10.1186/1747-1028-1-18 schema:sameAs https://app.dimensions.ai/details/publication/pub.1037795881
196 https://doi.org/10.1186/1747-1028-1-18
197 rdf:type schema:CreativeWork
198 grid-institutes:grid.136593.b schema:alternateName Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama-chyo, 560-0043, Toyonaka, Osaka, Japan
199 Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamada-oka, 565-0871, Suita, Osaka, Japan
200 schema:name Cellular Physiology Laboratory, RIKEN Discovery Research Institute, 2-1 Hirosawa, 351-0198, Wako, Saitama, Japan
201 Department of Biology, Graduate School of Science, Osaka University, 1-1 Machikaneyama-chyo, 560-0043, Toyonaka, Osaka, Japan
202 Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamada-oka, 565-0871, Suita, Osaka, Japan
203 rdf:type schema:Organization
204 grid-institutes:grid.7597.c schema:alternateName Cellular Physiology Laboratory, RIKEN Discovery Research Institute, 2-1 Hirosawa, 351-0198, Wako, Saitama, Japan
205 schema:name Cellular Physiology Laboratory, RIKEN Discovery Research Institute, 2-1 Hirosawa, 351-0198, Wako, Saitama, Japan
206 rdf:type schema:Organization
 




Preview window. Press ESC to close (or click here)


...