Biochemical and Proteomic Characterization of Recombinant Human α/β Hydrolase Domain 6 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Christina Miyabe Shields, Nikolai Zvonok, Alexander Zvonok, Alexandros Makriyannis

ABSTRACT

Human alpha/beta hydrolase domain 6 (hABHD6) is an enzyme that hydrolyzes 2-arachidonoylglycerol (2-AG), a potent agonist at both cannabinoid CB1 and CB2 receptors. In vivo modulation of ABHD6 expression has been shown to have potential therapeutic applications, making the enzyme a promising drug target. However, the lack of structural information on hABHD6 limits the discovery and design of selective inhibitors. We have performed E. coli expression, purification and activity profiling screening of different hABHD6 constructs and identified a truncated variant without N-terminal transmembrane (TM) domain, hΔ29-3-ABHD6, as the most promising protein for further characterization. The elimination of the TM domain did not affect 2-AG or fluorogenic arachidonoyl, 7-hydroxy-6-methoxy-4-methylcoumarin ester (AHMMCE) substrates hydrolysis, suggesting that the TM is not essential for enzyme catalytic activity. The hΔ29-3-ABHD6 variant was purified in a single step using Immobilized Metal Affinity Chromatography (IMAC), in-solution trypsin digested, and proteomically characterized by Matrix Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry (MALDI-TOF MS). The N-terminal peptide without methionine was identified indicating on a post-translational modification of the recombinant protein. The mechanism of inhibition of hABHD6 with AM6701 and WWL70 covalent probes was elucidated based on MS analysis of trypsin digested hABHD6 following the Ligand Assisted Protein Structure (LAPS) approach. We identified the carbamylated peptides containing catalytic serine (Ser148) suggesting a selective carbamylation of the enzyme by AM6701 or WWL70 and confirming an essential role of this residue in catalysis. The ability to produce substantial quantities of functional, pure hABHD6 will aid in the downstream structural characterization, and development of potent, selective inhibitors. More... »

PAGES

890

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-018-36633-4

DOI

http://dx.doi.org/10.1038/s41598-018-36633-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1111768158

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30696836


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/2008/0601", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Biochemistry and Cell Biology", 
        "type": "DefinedTerm"
      }, 
      {
        "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"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "Northeastern University", 
          "id": "https://www.grid.ac/institutes/grid.261112.7", 
          "name": [
            "Department of Pharmaceutical Sciences, Northeastern University, 02115, Boston, MA, USA", 
            "Center for Drug Discovery, Northeastern University, 02115, Boston, MA, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Shields", 
        "givenName": "Christina Miyabe", 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Northeastern University", 
          "id": "https://www.grid.ac/institutes/grid.261112.7", 
          "name": [
            "Department of Pharmaceutical Sciences, Northeastern University, 02115, Boston, MA, USA", 
            "Center for Drug Discovery, Northeastern University, 02115, Boston, MA, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Zvonok", 
        "givenName": "Nikolai", 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Northeastern University", 
          "id": "https://www.grid.ac/institutes/grid.261112.7", 
          "name": [
            "Department of Pharmaceutical Sciences, Northeastern University, 02115, Boston, MA, USA", 
            "Center for Drug Discovery, Northeastern University, 02115, Boston, MA, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Zvonok", 
        "givenName": "Alexander", 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Northeastern University", 
          "id": "https://www.grid.ac/institutes/grid.261112.7", 
          "name": [
            "Department of Pharmaceutical Sciences, Northeastern University, 02115, Boston, MA, USA", 
            "Center for Drug Discovery, Northeastern University, 02115, Boston, MA, USA", 
            "Department of Chemistry and Chemical Biology, Northeastern University, 02115, Boston, MA, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Makriyannis", 
        "givenName": "Alexandros", 
        "type": "Person"
      }
    ], 
    "citation": [
      {
        "id": "https://doi.org/10.1016/j.chembiol.2008.06.008", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1003560646"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/j.bbalip.2013.01.002", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1004631600"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/j.cmet.2014.04.003", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1013483313"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1073/pnas.0813167106", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1013906615"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/nn.2601", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1025157163", 
          "https://doi.org/10.1038/nn.2601"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.2183/pjab.90.235", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1029494462"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1113/jphysiol.2011.215509", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1030678380"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1194/jlr.m030411", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1030862724"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/j.chembiol.2007.11.006", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1031461743"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1124/mol.109.059030", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1034600259"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1021/pr060507u", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1036332705"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/j.molmet.2015.09.012", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1040443264"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/j.neuron.2012.09.020", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1044365077"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1111/j.1748-1716.2011.02280.x", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1045262186"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1073/pnas.86.21.8247", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1045443792"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1002/cpt.115", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1050064250"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1002/cpt.115", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1050064250"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/j.bbalip.2014.01.004", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1050743678"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/j.celrep.2016.02.076", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1050888684"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/j.celrep.2016.02.076", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1050888684"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1016/j.celrep.2013.08.047", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1052478483"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1002/pro.2257", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1053276142"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1021/cn3000263", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1053955241"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1021/ja073650c", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1055845333"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1021/ja073650c", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1055845333"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1021/pr700839z", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1056294235"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1074/jbc.m115.670257", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1058213665"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "https://doi.org/10.1089/neu.2012.2647", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1059301698"
        ], 
        "type": "CreativeWork"
      }
    ], 
    "datePublished": "2019-12", 
    "datePublishedReg": "2019-12-01", 
    "description": "Human alpha/beta hydrolase domain 6 (hABHD6) is an enzyme that hydrolyzes 2-arachidonoylglycerol (2-AG), a potent agonist at both cannabinoid CB1 and CB2 receptors. In vivo modulation of ABHD6 expression has been shown to have potential therapeutic applications, making the enzyme a promising drug target. However, the lack of structural information on hABHD6 limits the discovery and design of selective inhibitors. We have performed E. coli expression, purification and activity profiling screening of different hABHD6 constructs and identified a truncated variant without N-terminal transmembrane (TM) domain, h\u039429-3-ABHD6, as the most promising protein for further characterization. The elimination of the TM domain did not affect 2-AG or fluorogenic arachidonoyl, 7-hydroxy-6-methoxy-4-methylcoumarin ester (AHMMCE) substrates hydrolysis, suggesting that the TM is not essential for enzyme catalytic activity. The h\u039429-3-ABHD6 variant was purified in a single step using Immobilized Metal Affinity Chromatography (IMAC), in-solution trypsin digested, and proteomically characterized by Matrix Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry (MALDI-TOF MS). The N-terminal peptide without methionine was identified indicating on a post-translational modification of the recombinant protein. The mechanism of\u00a0inhibition of hABHD6 with AM6701 and WWL70 covalent probes was elucidated based on MS analysis of trypsin digested hABHD6 following the Ligand Assisted Protein Structure (LAPS) approach. We identified the carbamylated peptides containing catalytic serine (Ser148) suggesting a selective carbamylation of the\u00a0enzyme by AM6701 or WWL70 and confirming an essential role of this residue in catalysis. The ability to produce substantial quantities of functional, pure hABHD6 will aid in the downstream structural characterization, and development of potent, selective inhibitors.", 
    "genre": "research_article", 
    "id": "sg:pub.10.1038/s41598-018-36633-4", 
    "inLanguage": [
      "en"
    ], 
    "isAccessibleForFree": true, 
    "isFundedItemOf": [
      {
        "id": "sg:grant.2634422", 
        "type": "MonetaryGrant"
      }, 
      {
        "id": "sg:grant.2482869", 
        "type": "MonetaryGrant"
      }
    ], 
    "isPartOf": [
      {
        "id": "sg:journal.1045337", 
        "issn": [
          "2045-2322"
        ], 
        "name": "Scientific Reports", 
        "type": "Periodical"
      }, 
      {
        "issueNumber": "1", 
        "type": "PublicationIssue"
      }, 
      {
        "type": "PublicationVolume", 
        "volumeNumber": "9"
      }
    ], 
    "name": "Biochemical and Proteomic Characterization of Recombinant Human \u03b1/\u03b2 Hydrolase Domain 6", 
    "pagination": "890", 
    "productId": [
      {
        "name": "readcube_id", 
        "type": "PropertyValue", 
        "value": [
          "e222fb91ae8565e520136a1bf53d49c82a8ac32823a929aa70fb6c21fb193570"
        ]
      }, 
      {
        "name": "pubmed_id", 
        "type": "PropertyValue", 
        "value": [
          "30696836"
        ]
      }, 
      {
        "name": "nlm_unique_id", 
        "type": "PropertyValue", 
        "value": [
          "101563288"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1038/s41598-018-36633-4"
        ]
      }, 
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1111768158"
        ]
      }
    ], 
    "sameAs": [
      "https://doi.org/10.1038/s41598-018-36633-4", 
      "https://app.dimensions.ai/details/publication/pub.1111768158"
    ], 
    "sdDataset": "articles", 
    "sdDatePublished": "2019-04-11T09:00", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-uberresearch-data-dimensions-target-20181106-alternative/cleanup/v134/2549eaecd7973599484d7c17b260dba0a4ecb94b/merge/v9/a6c9fde33151104705d4d7ff012ea9563521a3ce/jats-lookup/v90/0000000327_0000000327/records_115001_00000000.jsonl", 
    "type": "ScholarlyArticle", 
    "url": "https://www.nature.com/articles/s41598-018-36633-4"
  }
]
 

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/s41598-018-36633-4'

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/s41598-018-36633-4'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/s41598-018-36633-4'

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

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/s41598-018-36633-4'


 

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

167 TRIPLES      21 PREDICATES      54 URIs      21 LITERALS      9 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1038/s41598-018-36633-4 schema:about anzsrc-for:06
2 anzsrc-for:0601
3 schema:author Nb056c8140de14b63b71c82fccb76257e
4 schema:citation sg:pub.10.1038/nn.2601
5 https://doi.org/10.1002/cpt.115
6 https://doi.org/10.1002/pro.2257
7 https://doi.org/10.1016/j.bbalip.2013.01.002
8 https://doi.org/10.1016/j.bbalip.2014.01.004
9 https://doi.org/10.1016/j.celrep.2013.08.047
10 https://doi.org/10.1016/j.celrep.2016.02.076
11 https://doi.org/10.1016/j.chembiol.2007.11.006
12 https://doi.org/10.1016/j.chembiol.2008.06.008
13 https://doi.org/10.1016/j.cmet.2014.04.003
14 https://doi.org/10.1016/j.molmet.2015.09.012
15 https://doi.org/10.1016/j.neuron.2012.09.020
16 https://doi.org/10.1021/cn3000263
17 https://doi.org/10.1021/ja073650c
18 https://doi.org/10.1021/pr060507u
19 https://doi.org/10.1021/pr700839z
20 https://doi.org/10.1073/pnas.0813167106
21 https://doi.org/10.1073/pnas.86.21.8247
22 https://doi.org/10.1074/jbc.m115.670257
23 https://doi.org/10.1089/neu.2012.2647
24 https://doi.org/10.1111/j.1748-1716.2011.02280.x
25 https://doi.org/10.1113/jphysiol.2011.215509
26 https://doi.org/10.1124/mol.109.059030
27 https://doi.org/10.1194/jlr.m030411
28 https://doi.org/10.2183/pjab.90.235
29 schema:datePublished 2019-12
30 schema:datePublishedReg 2019-12-01
31 schema:description Human alpha/beta hydrolase domain 6 (hABHD6) is an enzyme that hydrolyzes 2-arachidonoylglycerol (2-AG), a potent agonist at both cannabinoid CB1 and CB2 receptors. In vivo modulation of ABHD6 expression has been shown to have potential therapeutic applications, making the enzyme a promising drug target. However, the lack of structural information on hABHD6 limits the discovery and design of selective inhibitors. We have performed E. coli expression, purification and activity profiling screening of different hABHD6 constructs and identified a truncated variant without N-terminal transmembrane (TM) domain, hΔ29-3-ABHD6, as the most promising protein for further characterization. The elimination of the TM domain did not affect 2-AG or fluorogenic arachidonoyl, 7-hydroxy-6-methoxy-4-methylcoumarin ester (AHMMCE) substrates hydrolysis, suggesting that the TM is not essential for enzyme catalytic activity. The hΔ29-3-ABHD6 variant was purified in a single step using Immobilized Metal Affinity Chromatography (IMAC), in-solution trypsin digested, and proteomically characterized by Matrix Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry (MALDI-TOF MS). The N-terminal peptide without methionine was identified indicating on a post-translational modification of the recombinant protein. The mechanism of inhibition of hABHD6 with AM6701 and WWL70 covalent probes was elucidated based on MS analysis of trypsin digested hABHD6 following the Ligand Assisted Protein Structure (LAPS) approach. We identified the carbamylated peptides containing catalytic serine (Ser<sup>148</sup>) suggesting a selective carbamylation of the enzyme by AM6701 or WWL70 and confirming an essential role of this residue in catalysis. The ability to produce substantial quantities of functional, pure hABHD6 will aid in the downstream structural characterization, and development of potent, selective inhibitors.
32 schema:genre research_article
33 schema:inLanguage en
34 schema:isAccessibleForFree true
35 schema:isPartOf Nb2e3e6c63b424644a87790c458146e17
36 Nb8393df3afb94c7cbaae6e54491798da
37 sg:journal.1045337
38 schema:name Biochemical and Proteomic Characterization of Recombinant Human α/β Hydrolase Domain 6
39 schema:pagination 890
40 schema:productId N308ce1bdf2bc43a081cac688c5bf3cb6
41 N6df84838084442eaa7917196f80a7699
42 Nbf2841ee04e94218a7dfe615ec2b95fc
43 Nc421cb4ba1b447cb829571a783393ae7
44 Nf7ed8609f5234967871e894636ebb588
45 schema:sameAs https://app.dimensions.ai/details/publication/pub.1111768158
46 https://doi.org/10.1038/s41598-018-36633-4
47 schema:sdDatePublished 2019-04-11T09:00
48 schema:sdLicense https://scigraph.springernature.com/explorer/license/
49 schema:sdPublisher Nc32ad800c771456c85f915ff4165c5f2
50 schema:url https://www.nature.com/articles/s41598-018-36633-4
51 sgo:license sg:explorer/license/
52 sgo:sdDataset articles
53 rdf:type schema:ScholarlyArticle
54 N0e0429496ac948c59403c34de4776b52 schema:affiliation https://www.grid.ac/institutes/grid.261112.7
55 schema:familyName Zvonok
56 schema:givenName Nikolai
57 rdf:type schema:Person
58 N0f98ce64e3d94929a612e316d2221822 schema:affiliation https://www.grid.ac/institutes/grid.261112.7
59 schema:familyName Zvonok
60 schema:givenName Alexander
61 rdf:type schema:Person
62 N17c89e17fbcc4c4a8152c6472302f65d schema:affiliation https://www.grid.ac/institutes/grid.261112.7
63 schema:familyName Makriyannis
64 schema:givenName Alexandros
65 rdf:type schema:Person
66 N308ce1bdf2bc43a081cac688c5bf3cb6 schema:name doi
67 schema:value 10.1038/s41598-018-36633-4
68 rdf:type schema:PropertyValue
69 N6df84838084442eaa7917196f80a7699 schema:name dimensions_id
70 schema:value pub.1111768158
71 rdf:type schema:PropertyValue
72 N94a02187443d489da674324b93d950c0 rdf:first N0e0429496ac948c59403c34de4776b52
73 rdf:rest Nb62e2f1662e44d549a1d155ee163af9d
74 N9ba82072f9d74cd48638be618ea0c678 rdf:first N17c89e17fbcc4c4a8152c6472302f65d
75 rdf:rest rdf:nil
76 Nb056c8140de14b63b71c82fccb76257e rdf:first Nfcb0a079bd79412bafbca82720f70f6f
77 rdf:rest N94a02187443d489da674324b93d950c0
78 Nb2e3e6c63b424644a87790c458146e17 schema:issueNumber 1
79 rdf:type schema:PublicationIssue
80 Nb62e2f1662e44d549a1d155ee163af9d rdf:first N0f98ce64e3d94929a612e316d2221822
81 rdf:rest N9ba82072f9d74cd48638be618ea0c678
82 Nb8393df3afb94c7cbaae6e54491798da schema:volumeNumber 9
83 rdf:type schema:PublicationVolume
84 Nbf2841ee04e94218a7dfe615ec2b95fc schema:name readcube_id
85 schema:value e222fb91ae8565e520136a1bf53d49c82a8ac32823a929aa70fb6c21fb193570
86 rdf:type schema:PropertyValue
87 Nc32ad800c771456c85f915ff4165c5f2 schema:name Springer Nature - SN SciGraph project
88 rdf:type schema:Organization
89 Nc421cb4ba1b447cb829571a783393ae7 schema:name pubmed_id
90 schema:value 30696836
91 rdf:type schema:PropertyValue
92 Nf7ed8609f5234967871e894636ebb588 schema:name nlm_unique_id
93 schema:value 101563288
94 rdf:type schema:PropertyValue
95 Nfcb0a079bd79412bafbca82720f70f6f schema:affiliation https://www.grid.ac/institutes/grid.261112.7
96 schema:familyName Shields
97 schema:givenName Christina Miyabe
98 rdf:type schema:Person
99 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
100 schema:name Biological Sciences
101 rdf:type schema:DefinedTerm
102 anzsrc-for:0601 schema:inDefinedTermSet anzsrc-for:
103 schema:name Biochemistry and Cell Biology
104 rdf:type schema:DefinedTerm
105 sg:grant.2482869 http://pending.schema.org/fundedItem sg:pub.10.1038/s41598-018-36633-4
106 rdf:type schema:MonetaryGrant
107 sg:grant.2634422 http://pending.schema.org/fundedItem sg:pub.10.1038/s41598-018-36633-4
108 rdf:type schema:MonetaryGrant
109 sg:journal.1045337 schema:issn 2045-2322
110 schema:name Scientific Reports
111 rdf:type schema:Periodical
112 sg:pub.10.1038/nn.2601 schema:sameAs https://app.dimensions.ai/details/publication/pub.1025157163
113 https://doi.org/10.1038/nn.2601
114 rdf:type schema:CreativeWork
115 https://doi.org/10.1002/cpt.115 schema:sameAs https://app.dimensions.ai/details/publication/pub.1050064250
116 rdf:type schema:CreativeWork
117 https://doi.org/10.1002/pro.2257 schema:sameAs https://app.dimensions.ai/details/publication/pub.1053276142
118 rdf:type schema:CreativeWork
119 https://doi.org/10.1016/j.bbalip.2013.01.002 schema:sameAs https://app.dimensions.ai/details/publication/pub.1004631600
120 rdf:type schema:CreativeWork
121 https://doi.org/10.1016/j.bbalip.2014.01.004 schema:sameAs https://app.dimensions.ai/details/publication/pub.1050743678
122 rdf:type schema:CreativeWork
123 https://doi.org/10.1016/j.celrep.2013.08.047 schema:sameAs https://app.dimensions.ai/details/publication/pub.1052478483
124 rdf:type schema:CreativeWork
125 https://doi.org/10.1016/j.celrep.2016.02.076 schema:sameAs https://app.dimensions.ai/details/publication/pub.1050888684
126 rdf:type schema:CreativeWork
127 https://doi.org/10.1016/j.chembiol.2007.11.006 schema:sameAs https://app.dimensions.ai/details/publication/pub.1031461743
128 rdf:type schema:CreativeWork
129 https://doi.org/10.1016/j.chembiol.2008.06.008 schema:sameAs https://app.dimensions.ai/details/publication/pub.1003560646
130 rdf:type schema:CreativeWork
131 https://doi.org/10.1016/j.cmet.2014.04.003 schema:sameAs https://app.dimensions.ai/details/publication/pub.1013483313
132 rdf:type schema:CreativeWork
133 https://doi.org/10.1016/j.molmet.2015.09.012 schema:sameAs https://app.dimensions.ai/details/publication/pub.1040443264
134 rdf:type schema:CreativeWork
135 https://doi.org/10.1016/j.neuron.2012.09.020 schema:sameAs https://app.dimensions.ai/details/publication/pub.1044365077
136 rdf:type schema:CreativeWork
137 https://doi.org/10.1021/cn3000263 schema:sameAs https://app.dimensions.ai/details/publication/pub.1053955241
138 rdf:type schema:CreativeWork
139 https://doi.org/10.1021/ja073650c schema:sameAs https://app.dimensions.ai/details/publication/pub.1055845333
140 rdf:type schema:CreativeWork
141 https://doi.org/10.1021/pr060507u schema:sameAs https://app.dimensions.ai/details/publication/pub.1036332705
142 rdf:type schema:CreativeWork
143 https://doi.org/10.1021/pr700839z schema:sameAs https://app.dimensions.ai/details/publication/pub.1056294235
144 rdf:type schema:CreativeWork
145 https://doi.org/10.1073/pnas.0813167106 schema:sameAs https://app.dimensions.ai/details/publication/pub.1013906615
146 rdf:type schema:CreativeWork
147 https://doi.org/10.1073/pnas.86.21.8247 schema:sameAs https://app.dimensions.ai/details/publication/pub.1045443792
148 rdf:type schema:CreativeWork
149 https://doi.org/10.1074/jbc.m115.670257 schema:sameAs https://app.dimensions.ai/details/publication/pub.1058213665
150 rdf:type schema:CreativeWork
151 https://doi.org/10.1089/neu.2012.2647 schema:sameAs https://app.dimensions.ai/details/publication/pub.1059301698
152 rdf:type schema:CreativeWork
153 https://doi.org/10.1111/j.1748-1716.2011.02280.x schema:sameAs https://app.dimensions.ai/details/publication/pub.1045262186
154 rdf:type schema:CreativeWork
155 https://doi.org/10.1113/jphysiol.2011.215509 schema:sameAs https://app.dimensions.ai/details/publication/pub.1030678380
156 rdf:type schema:CreativeWork
157 https://doi.org/10.1124/mol.109.059030 schema:sameAs https://app.dimensions.ai/details/publication/pub.1034600259
158 rdf:type schema:CreativeWork
159 https://doi.org/10.1194/jlr.m030411 schema:sameAs https://app.dimensions.ai/details/publication/pub.1030862724
160 rdf:type schema:CreativeWork
161 https://doi.org/10.2183/pjab.90.235 schema:sameAs https://app.dimensions.ai/details/publication/pub.1029494462
162 rdf:type schema:CreativeWork
163 https://www.grid.ac/institutes/grid.261112.7 schema:alternateName Northeastern University
164 schema:name Center for Drug Discovery, Northeastern University, 02115, Boston, MA, USA
165 Department of Chemistry and Chemical Biology, Northeastern University, 02115, Boston, MA, USA
166 Department of Pharmaceutical Sciences, Northeastern University, 02115, Boston, MA, USA
167 rdf:type schema:Organization
 




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


...