The structure of the GTPase-activating domain from p50rhoGAP View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-01

AUTHORS

Tracey Barrett, Bing Xiao, Eleanor J. Dodson, Guy Dodson, Steven B. Ludbrook, Kurshid Nurmahomed, Steven J. Gamblin, Andrea Musacchio, Stephen J. Smerdon, John F. Eccleston

ABSTRACT

Members of the Rho family of small G proteins transduce signals from plasma-membrane receptors and control cell adhesion, motility and shape by actin cytoskeleton formation1–4. They also activate other kinase cascades. Like all other GTPases, Rho proteins act as molecular switches, with an active GTP-bound form and an inactive GDP-bound form5. The active conformation is promoted by guanine-nucleotide exchange factors, and the inactive state by GTPase-activating proteins (GAPs) which stimulate the intrinsic GTPase activity of small G proteins6. Rho-specific GAP domains are found in a wide variety of large, multi-functional proteins7. Here we report the crystal structure of an active 242-residue C-terminal fragment of human p50rhoGAP8. The structure is an unusual arrangement of nine α-helices, the core of which includes a four-helix bundle. Residues conserved across the rhoGAP family are largely confined to one face of this bundle, which may be an interaction site for target G proteins. In particular, we propose that Arg 85 and Asn 194 are involved in binding G proteins and enhancing GTPase activity. More... »

PAGES

458-461

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/385458a0

DOI

http://dx.doi.org/10.1038/385458a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1024724313

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9009196


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": "Amino Acid Sequence", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Binding Sites", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Crystallography, X-Ray", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Enzyme Activation", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "GTP Phosphohydrolases", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "GTP-Binding Proteins", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "GTPase-Activating Proteins", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Humans", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Models, Molecular", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Molecular Sequence Data", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Protein Conformation", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Sequence Homology, Amino Acid", 
        "type": "DefinedTerm"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.451388.3", 
          "name": [
            "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Barrett", 
        "givenName": "Tracey", 
        "id": "sg:person.0621625522.72", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0621625522.72"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.451388.3", 
          "name": [
            "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Xiao", 
        "givenName": "Bing", 
        "id": "sg:person.01133575026.04", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01133575026.04"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Chemistry, University of York, YO1 5DD, Heslington, York, UK", 
          "id": "http://www.grid.ac/institutes/grid.5685.e", 
          "name": [
            "Department of Chemistry, University of York, YO1 5DD, Heslington, York, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Dodson", 
        "givenName": "Eleanor J.", 
        "id": "sg:person.01012136573.07", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01012136573.07"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Chemistry, University of York, YO1 5DD, Heslington, York, UK", 
          "id": "http://www.grid.ac/institutes/grid.5685.e", 
          "name": [
            "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK", 
            "Department of Chemistry, University of York, YO1 5DD, Heslington, York, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Dodson", 
        "givenName": "Guy", 
        "id": "sg:person.01277614333.11", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01277614333.11"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.451388.3", 
          "name": [
            "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Ludbrook", 
        "givenName": "Steven B.", 
        "id": "sg:person.0627254241.57", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0627254241.57"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.451388.3", 
          "name": [
            "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Nurmahomed", 
        "givenName": "Kurshid", 
        "id": "sg:person.0675367441.52", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0675367441.52"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.451388.3", 
          "name": [
            "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Gamblin", 
        "givenName": "Steven J.", 
        "id": "sg:person.014166377647.07", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.014166377647.07"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Laboratory of Molecular Medicine, Childrens Hospital, 02115, Boston, Massachusetts, USA", 
          "id": "http://www.grid.ac/institutes/grid.2515.3", 
          "name": [
            "Laboratory of Molecular Medicine, Childrens Hospital, 02115, Boston, Massachusetts, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Musacchio", 
        "givenName": "Andrea", 
        "id": "sg:person.01367316326.03", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01367316326.03"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.451388.3", 
          "name": [
            "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Smerdon", 
        "givenName": "Stephen J.", 
        "id": "sg:person.010727525727.84", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.010727525727.84"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK", 
          "id": "http://www.grid.ac/institutes/grid.451388.3", 
          "name": [
            "National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Eccleston", 
        "givenName": "John F.", 
        "id": "sg:person.0647660736.44", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0647660736.44"
        ], 
        "type": "Person"
      }
    ], 
    "citation": [
      {
        "id": "sg:pub.10.1038/366643a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1005902014", 
          "https://doi.org/10.1038/366643a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/348125a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1028867627", 
          "https://doi.org/10.1038/348125a0"
        ], 
        "type": "CreativeWork"
      }
    ], 
    "datePublished": "1997-01", 
    "datePublishedReg": "1997-01-01", 
    "description": "Members of the Rho family of small G proteins transduce signals from plasma-membrane receptors and control cell adhesion, motility and shape by actin cytoskeleton formation1\u20134. They also activate other kinase cascades. Like all other GTPases, Rho proteins act as molecular switches, with an active GTP-bound form and an inactive GDP-bound form5. The active conformation is promoted by guanine-nucleotide exchange factors, and the inactive state by GTPase-activating proteins (GAPs) which stimulate the intrinsic GTPase activity of small G proteins6. Rho-specific GAP domains are found in a wide variety of large, multi-functional proteins7. Here we report the crystal structure of an active 242-residue C-terminal fragment of human p50rhoGAP8. The structure is an unusual arrangement of nine \u03b1-helices, the core of which includes a four-helix bundle. Residues conserved across the rhoGAP family are largely confined to one face of this bundle, which may be an interaction site for target G proteins. In particular, we propose that Arg 85 and Asn 194 are involved in binding G proteins and enhancing GTPase activity.", 
    "genre": "article", 
    "id": "sg:pub.10.1038/385458a0", 
    "isAccessibleForFree": false, 
    "isPartOf": [
      {
        "id": "sg:journal.1018957", 
        "issn": [
          "0028-0836", 
          "1476-4687"
        ], 
        "name": "Nature", 
        "publisher": "Springer Nature", 
        "type": "Periodical"
      }, 
      {
        "issueNumber": "6615", 
        "type": "PublicationIssue"
      }, 
      {
        "type": "PublicationVolume", 
        "volumeNumber": "385"
      }
    ], 
    "keywords": [
      "GTPase-activating proteins", 
      "GTPase activity", 
      "guanine nucleotide exchange factors", 
      "G proteins", 
      "proteins transduce signals", 
      "active GTP-bound form", 
      "intrinsic GTPase activity", 
      "GTP-bound form", 
      "four-helix bundle", 
      "control cell adhesion", 
      "plasma membrane receptors", 
      "target G proteins", 
      "GAP domain", 
      "RhoGAP family", 
      "Rho proteins", 
      "exchange factor", 
      "kinase cascade", 
      "Rho family", 
      "transduce signals", 
      "C-terminal fragment", 
      "Arg-85", 
      "Asn-194", 
      "molecular switch", 
      "inactive state", 
      "active conformation", 
      "cell adhesion", 
      "\u03b1-helix", 
      "interaction sites", 
      "protein", 
      "unusual arrangement", 
      "GTPases", 
      "GTPase", 
      "p50RhoGAP", 
      "family", 
      "domain", 
      "crystal structure", 
      "residues", 
      "wide variety", 
      "cascade", 
      "motility", 
      "activity", 
      "fragments", 
      "conformation", 
      "receptors", 
      "adhesion", 
      "members", 
      "sites", 
      "structure", 
      "bundles", 
      "switch", 
      "variety", 
      "signals", 
      "factors", 
      "form", 
      "arrangement", 
      "shape", 
      "core", 
      "state", 
      "face"
    ], 
    "name": "The structure of the GTPase-activating domain from p50rhoGAP", 
    "pagination": "458-461", 
    "productId": [
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1024724313"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1038/385458a0"
        ]
      }, 
      {
        "name": "pubmed_id", 
        "type": "PropertyValue", 
        "value": [
          "9009196"
        ]
      }
    ], 
    "sameAs": [
      "https://doi.org/10.1038/385458a0", 
      "https://app.dimensions.ai/details/publication/pub.1024724313"
    ], 
    "sdDataset": "articles", 
    "sdDatePublished": "2022-11-24T20:48", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-springernature-scigraph/baseset/20221124/entities/gbq_results/article/article_288.jsonl", 
    "type": "ScholarlyArticle", 
    "url": "https://doi.org/10.1038/385458a0"
  }
]
 

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.10.1038/385458a0'

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

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/385458a0'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/385458a0'

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

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/385458a0'


 

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

246 TRIPLES      21 PREDICATES      99 URIs      89 LITERALS      19 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1038/385458a0 schema:about N18b1303f2e33482e81b941d7a9de293f
2 N23f7a038b68244e69f65d1bba50c67fd
3 N25c94f132b3a4d6b82fca78b3b140432
4 N2fecf4794b1c4051b81a9fe2a0ca2820
5 N4ae644fd9579457e91ce9dd65679204e
6 N555dd23d7ce34363a91290e2905b7890
7 N7ca1d450acbe48dd86691f3e4035cc49
8 N9477e40905e64200896332d4b4c5f5dd
9 N95d4424d8d614afb8a5eb2ca68b85b85
10 Nb7392df07e9d456cb7ae4372503d1273
11 Nb91e86c2a1d84c35bb7dcdaf6a287882
12 Nd9aa6067e3d243fc86c85dc87ab97be0
13 anzsrc-for:06
14 anzsrc-for:0601
15 schema:author Nf2542fa7e8914184957d04fb2213caa2
16 schema:citation sg:pub.10.1038/348125a0
17 sg:pub.10.1038/366643a0
18 schema:datePublished 1997-01
19 schema:datePublishedReg 1997-01-01
20 schema:description Members of the Rho family of small G proteins transduce signals from plasma-membrane receptors and control cell adhesion, motility and shape by actin cytoskeleton formation1–4. They also activate other kinase cascades. Like all other GTPases, Rho proteins act as molecular switches, with an active GTP-bound form and an inactive GDP-bound form5. The active conformation is promoted by guanine-nucleotide exchange factors, and the inactive state by GTPase-activating proteins (GAPs) which stimulate the intrinsic GTPase activity of small G proteins6. Rho-specific GAP domains are found in a wide variety of large, multi-functional proteins7. Here we report the crystal structure of an active 242-residue C-terminal fragment of human p50rhoGAP8. The structure is an unusual arrangement of nine α-helices, the core of which includes a four-helix bundle. Residues conserved across the rhoGAP family are largely confined to one face of this bundle, which may be an interaction site for target G proteins. In particular, we propose that Arg 85 and Asn 194 are involved in binding G proteins and enhancing GTPase activity.
21 schema:genre article
22 schema:isAccessibleForFree false
23 schema:isPartOf Na9f69176377a4f2b968992844d7cbe48
24 Ncda3d65701214a969edfd52da043a7ea
25 sg:journal.1018957
26 schema:keywords Arg-85
27 Asn-194
28 C-terminal fragment
29 G proteins
30 GAP domain
31 GTP-bound form
32 GTPase
33 GTPase activity
34 GTPase-activating proteins
35 GTPases
36 Rho family
37 Rho proteins
38 RhoGAP family
39 active GTP-bound form
40 active conformation
41 activity
42 adhesion
43 arrangement
44 bundles
45 cascade
46 cell adhesion
47 conformation
48 control cell adhesion
49 core
50 crystal structure
51 domain
52 exchange factor
53 face
54 factors
55 family
56 form
57 four-helix bundle
58 fragments
59 guanine nucleotide exchange factors
60 inactive state
61 interaction sites
62 intrinsic GTPase activity
63 kinase cascade
64 members
65 molecular switch
66 motility
67 p50RhoGAP
68 plasma membrane receptors
69 protein
70 proteins transduce signals
71 receptors
72 residues
73 shape
74 signals
75 sites
76 state
77 structure
78 switch
79 target G proteins
80 transduce signals
81 unusual arrangement
82 variety
83 wide variety
84 α-helix
85 schema:name The structure of the GTPase-activating domain from p50rhoGAP
86 schema:pagination 458-461
87 schema:productId N19d8070f791f414bb953f8422c733cb7
88 N1ee9fb07d51846acb0449aded1d8fdd3
89 Nd7ad6dbebda0423f919f1624d94146f9
90 schema:sameAs https://app.dimensions.ai/details/publication/pub.1024724313
91 https://doi.org/10.1038/385458a0
92 schema:sdDatePublished 2022-11-24T20:48
93 schema:sdLicense https://scigraph.springernature.com/explorer/license/
94 schema:sdPublisher Ndc44843c600c48c19ff6e416ce39c0cc
95 schema:url https://doi.org/10.1038/385458a0
96 sgo:license sg:explorer/license/
97 sgo:sdDataset articles
98 rdf:type schema:ScholarlyArticle
99 N18b1303f2e33482e81b941d7a9de293f schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
100 schema:name GTP-Binding Proteins
101 rdf:type schema:DefinedTerm
102 N19d8070f791f414bb953f8422c733cb7 schema:name dimensions_id
103 schema:value pub.1024724313
104 rdf:type schema:PropertyValue
105 N1ee9fb07d51846acb0449aded1d8fdd3 schema:name doi
106 schema:value 10.1038/385458a0
107 rdf:type schema:PropertyValue
108 N23f7a038b68244e69f65d1bba50c67fd schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
109 schema:name Amino Acid Sequence
110 rdf:type schema:DefinedTerm
111 N243557ddec1f43d493db5b22d5df3551 rdf:first sg:person.01277614333.11
112 rdf:rest N892a9d111b744c508104991d39d5da2b
113 N25c94f132b3a4d6b82fca78b3b140432 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
114 schema:name Molecular Sequence Data
115 rdf:type schema:DefinedTerm
116 N26d9e8f445a94de5a8a47aa52688e485 rdf:first sg:person.01133575026.04
117 rdf:rest N690100fe37f84e4395b61dc50fbc30b4
118 N2fecf4794b1c4051b81a9fe2a0ca2820 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
119 schema:name Crystallography, X-Ray
120 rdf:type schema:DefinedTerm
121 N437c3f42ba84452380a436deb7d95300 rdf:first sg:person.014166377647.07
122 rdf:rest Nfbe4835b6ee5447eaa82d45d540d064f
123 N4ae644fd9579457e91ce9dd65679204e schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
124 schema:name Models, Molecular
125 rdf:type schema:DefinedTerm
126 N555dd23d7ce34363a91290e2905b7890 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
127 schema:name Binding Sites
128 rdf:type schema:DefinedTerm
129 N5ace779503644d728365917766c7aa25 rdf:first sg:person.0647660736.44
130 rdf:rest rdf:nil
131 N690100fe37f84e4395b61dc50fbc30b4 rdf:first sg:person.01012136573.07
132 rdf:rest N243557ddec1f43d493db5b22d5df3551
133 N7ca1d450acbe48dd86691f3e4035cc49 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
134 schema:name Enzyme Activation
135 rdf:type schema:DefinedTerm
136 N892a9d111b744c508104991d39d5da2b rdf:first sg:person.0627254241.57
137 rdf:rest Nf0451d2899a244d7a76761d3bd3afe88
138 N9477e40905e64200896332d4b4c5f5dd schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
139 schema:name Humans
140 rdf:type schema:DefinedTerm
141 N95d4424d8d614afb8a5eb2ca68b85b85 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
142 schema:name Protein Conformation
143 rdf:type schema:DefinedTerm
144 Na9f69176377a4f2b968992844d7cbe48 schema:issueNumber 6615
145 rdf:type schema:PublicationIssue
146 Nb7392df07e9d456cb7ae4372503d1273 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
147 schema:name GTP Phosphohydrolases
148 rdf:type schema:DefinedTerm
149 Nb91e86c2a1d84c35bb7dcdaf6a287882 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
150 schema:name Sequence Homology, Amino Acid
151 rdf:type schema:DefinedTerm
152 Nc3244d9394e944af90a522f946ed7a23 rdf:first sg:person.010727525727.84
153 rdf:rest N5ace779503644d728365917766c7aa25
154 Ncda3d65701214a969edfd52da043a7ea schema:volumeNumber 385
155 rdf:type schema:PublicationVolume
156 Nd7ad6dbebda0423f919f1624d94146f9 schema:name pubmed_id
157 schema:value 9009196
158 rdf:type schema:PropertyValue
159 Nd9aa6067e3d243fc86c85dc87ab97be0 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
160 schema:name GTPase-Activating Proteins
161 rdf:type schema:DefinedTerm
162 Ndc44843c600c48c19ff6e416ce39c0cc schema:name Springer Nature - SN SciGraph project
163 rdf:type schema:Organization
164 Nf0451d2899a244d7a76761d3bd3afe88 rdf:first sg:person.0675367441.52
165 rdf:rest N437c3f42ba84452380a436deb7d95300
166 Nf2542fa7e8914184957d04fb2213caa2 rdf:first sg:person.0621625522.72
167 rdf:rest N26d9e8f445a94de5a8a47aa52688e485
168 Nfbe4835b6ee5447eaa82d45d540d064f rdf:first sg:person.01367316326.03
169 rdf:rest Nc3244d9394e944af90a522f946ed7a23
170 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
171 schema:name Biological Sciences
172 rdf:type schema:DefinedTerm
173 anzsrc-for:0601 schema:inDefinedTermSet anzsrc-for:
174 schema:name Biochemistry and Cell Biology
175 rdf:type schema:DefinedTerm
176 sg:journal.1018957 schema:issn 0028-0836
177 1476-4687
178 schema:name Nature
179 schema:publisher Springer Nature
180 rdf:type schema:Periodical
181 sg:person.01012136573.07 schema:affiliation grid-institutes:grid.5685.e
182 schema:familyName Dodson
183 schema:givenName Eleanor J.
184 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01012136573.07
185 rdf:type schema:Person
186 sg:person.010727525727.84 schema:affiliation grid-institutes:grid.451388.3
187 schema:familyName Smerdon
188 schema:givenName Stephen J.
189 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.010727525727.84
190 rdf:type schema:Person
191 sg:person.01133575026.04 schema:affiliation grid-institutes:grid.451388.3
192 schema:familyName Xiao
193 schema:givenName Bing
194 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01133575026.04
195 rdf:type schema:Person
196 sg:person.01277614333.11 schema:affiliation grid-institutes:grid.5685.e
197 schema:familyName Dodson
198 schema:givenName Guy
199 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01277614333.11
200 rdf:type schema:Person
201 sg:person.01367316326.03 schema:affiliation grid-institutes:grid.2515.3
202 schema:familyName Musacchio
203 schema:givenName Andrea
204 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01367316326.03
205 rdf:type schema:Person
206 sg:person.014166377647.07 schema:affiliation grid-institutes:grid.451388.3
207 schema:familyName Gamblin
208 schema:givenName Steven J.
209 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.014166377647.07
210 rdf:type schema:Person
211 sg:person.0621625522.72 schema:affiliation grid-institutes:grid.451388.3
212 schema:familyName Barrett
213 schema:givenName Tracey
214 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0621625522.72
215 rdf:type schema:Person
216 sg:person.0627254241.57 schema:affiliation grid-institutes:grid.451388.3
217 schema:familyName Ludbrook
218 schema:givenName Steven B.
219 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0627254241.57
220 rdf:type schema:Person
221 sg:person.0647660736.44 schema:affiliation grid-institutes:grid.451388.3
222 schema:familyName Eccleston
223 schema:givenName John F.
224 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0647660736.44
225 rdf:type schema:Person
226 sg:person.0675367441.52 schema:affiliation grid-institutes:grid.451388.3
227 schema:familyName Nurmahomed
228 schema:givenName Kurshid
229 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0675367441.52
230 rdf:type schema:Person
231 sg:pub.10.1038/348125a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1028867627
232 https://doi.org/10.1038/348125a0
233 rdf:type schema:CreativeWork
234 sg:pub.10.1038/366643a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1005902014
235 https://doi.org/10.1038/366643a0
236 rdf:type schema:CreativeWork
237 grid-institutes:grid.2515.3 schema:alternateName Laboratory of Molecular Medicine, Childrens Hospital, 02115, Boston, Massachusetts, USA
238 schema:name Laboratory of Molecular Medicine, Childrens Hospital, 02115, Boston, Massachusetts, USA
239 rdf:type schema:Organization
240 grid-institutes:grid.451388.3 schema:alternateName National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK
241 schema:name National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK
242 rdf:type schema:Organization
243 grid-institutes:grid.5685.e schema:alternateName Department of Chemistry, University of York, YO1 5DD, Heslington, York, UK
244 schema:name Department of Chemistry, University of York, YO1 5DD, Heslington, York, UK
245 National Institute for Medical Research, The Ridgeway, Mill Hill, NW7 1AA, London, UK
246 rdf:type schema:Organization
 




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


...