MHC-linked LMP gene products specifically alter peptidase activities of the proteasome View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-09

AUTHORS

James Driscoll, Michael G. Brown, Daniel Finley, John J. Monaco

ABSTRACT

PROTEASOMES are highly conserved macromolecular structures which function as endopeptidases1–3. They are found in the cyto-plasm and nucleus of eukaryotic tissues and consist of at least 14 non-identical subunits with molecular masses ranging from ∼20 to 32K. Proteasomes are essential in the selective degradation of ubiquitinated and certain non-ubiquitinated proteins, acting as the proteolytic core of an energy-dependent 26S (1,500K) proteolytic complex. Two proteasome subunits, LMP2 and LMP7 (refs 4–7), are encoded within the major histocompatibility complex (MHC), implicating proteasomes in antigen processing8,9. Here we deter-mine the function of these two MHC-linked subunits by comparing the proteolytic activities of purified proteasomes containing (LMP+) or lacking (LMP−) these components. We find that pro-teasomes of both types have endopeptidase activity against sub-strates bearing hydrophobic, basic or acidic residues immediately preceding the cleavage site (the PI position) and at sites following asparagine, glycine and proline residues. The activity of LMP+ proteasomes is much higher than that of LMP− proteasomes against substrates with hydrophobic, basic or asparagine residues at PI, whereas their activities are comparable when acidic and glycine residues are present at PI. The MHC-linked LMP2 and LMP7 subunits therefore function to amplify specific endopeptid-ase activities of the proteasome. More... »

PAGES

262-264

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/365262a0

DOI

http://dx.doi.org/10.1038/365262a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1035838378

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8371781


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/2008/11", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Medical and Health Sciences", 
        "type": "DefinedTerm"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/1107", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Immunology", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Amino Acid Sequence", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Cysteine Endopeptidases", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Humans", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Interferon-gamma", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Major Histocompatibility Complex", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Molecular Sequence Data", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Multienzyme Complexes", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Mutation", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Peptides", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Proteasome Endopeptidase Complex", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Proteins", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Substrate Specificity", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Tumor Cells, Cultured", 
        "type": "DefinedTerm"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "Department of Cellular and Molecular Physiology, Harvard Medical School, 02115, Boston, Massachusetts, USA", 
          "id": "http://www.grid.ac/institutes/grid.38142.3c", 
          "name": [
            "Department of Cellular and Molecular Physiology, Harvard Medical School, 02115, Boston, Massachusetts, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Driscoll", 
        "givenName": "James", 
        "id": "sg:person.01121242412.64", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01121242412.64"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Microbiology and Immunology, Medical College of Virginia, Virginia Commonwealth University, 23298\u20130678, Richmond, Virginia, USA", 
          "id": "http://www.grid.ac/institutes/grid.417264.2", 
          "name": [
            "Department of Microbiology and Immunology, Medical College of Virginia, Virginia Commonwealth University, 23298\u20130678, Richmond, Virginia, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Brown", 
        "givenName": "Michael G.", 
        "id": "sg:person.01045607256.00", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01045607256.00"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Cellular and Molecular Physiology, Harvard Medical School, 02115, Boston, Massachusetts, USA", 
          "id": "http://www.grid.ac/institutes/grid.38142.3c", 
          "name": [
            "Department of Cellular and Molecular Physiology, Harvard Medical School, 02115, Boston, Massachusetts, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Finley", 
        "givenName": "Daniel", 
        "id": "sg:person.0754405533.36", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0754405533.36"
        ], 
        "type": "Person"
      }, 
      {
        "familyName": "Monaco", 
        "givenName": "John J.", 
        "id": "sg:person.01113021256.14", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01113021256.14"
        ], 
        "type": "Person"
      }
    ], 
    "citation": [
      {
        "id": "sg:pub.10.1038/353664a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1047893865", 
          "https://doi.org/10.1038/353664a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/363552a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1004841625", 
          "https://doi.org/10.1038/363552a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/353355a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1016459418", 
          "https://doi.org/10.1038/353355a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/353326a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1040302419", 
          "https://doi.org/10.1038/353326a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/360171a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1016437140", 
          "https://doi.org/10.1038/360171a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/353662a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1014387648", 
          "https://doi.org/10.1038/353662a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/348744a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1014832159", 
          "https://doi.org/10.1038/348744a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/353357a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1016313560", 
          "https://doi.org/10.1038/353357a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/360174a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1013551518", 
          "https://doi.org/10.1038/360174a0"
        ], 
        "type": "CreativeWork"
      }
    ], 
    "datePublished": "1993-09", 
    "datePublishedReg": "1993-09-01", 
    "description": "PROTEASOMES are highly conserved macromolecular structures which function as endopeptidases1\u20133. They are found in the cyto-plasm and nucleus of eukaryotic tissues and consist of at least 14 non-identical subunits with molecular masses ranging from \u223c20 to 32K. Proteasomes are essential in the selective degradation of ubiquitinated and certain non-ubiquitinated proteins, acting as the proteolytic core of an energy-dependent 26S (1,500K) proteolytic complex. Two proteasome subunits, LMP2 and LMP7 (refs 4\u20137), are encoded within the major histocompatibility complex (MHC), implicating proteasomes in antigen processing8,9. Here we deter-mine the function of these two MHC-linked subunits by comparing the proteolytic activities of purified proteasomes containing (LMP+) or lacking (LMP\u2212) these components. We find that pro-teasomes of both types have endopeptidase activity against sub-strates bearing hydrophobic, basic or acidic residues immediately preceding the cleavage site (the PI position) and at sites following asparagine, glycine and proline residues. The activity of LMP+ proteasomes is much higher than that of LMP\u2212 proteasomes against substrates with hydrophobic, basic or asparagine residues at PI, whereas their activities are comparable when acidic and glycine residues are present at PI. The MHC-linked LMP2 and LMP7 subunits therefore function to amplify specific endopeptid-ase activities of the proteasome.", 
    "genre": "article", 
    "id": "sg:pub.10.1038/365262a0", 
    "isAccessibleForFree": false, 
    "isPartOf": [
      {
        "id": "sg:journal.1018957", 
        "issn": [
          "0028-0836", 
          "1476-4687"
        ], 
        "name": "Nature", 
        "publisher": "Springer Nature", 
        "type": "Periodical"
      }, 
      {
        "issueNumber": "6443", 
        "type": "PublicationIssue"
      }, 
      {
        "type": "PublicationVolume", 
        "volumeNumber": "365"
      }
    ], 
    "keywords": [
      "major histocompatibility complex", 
      "histocompatibility complex", 
      "LMP7 subunit", 
      "LMP2", 
      "proteolytic activity", 
      "proteasome subunits", 
      "peptidase activity", 
      "endopeptidase activity", 
      "activity", 
      "antigen", 
      "proteasome", 
      "LMP7", 
      "gene products", 
      "tissue", 
      "subunits", 
      "proteolytic complex", 
      "cleavage site", 
      "PI", 
      "protein", 
      "sites", 
      "nucleus", 
      "glycine", 
      "eukaryotic tissues", 
      "non-identical subunits", 
      "molecular mass", 
      "mass", 
      "proteolytic core", 
      "function", 
      "glycine residue", 
      "lacking", 
      "types", 
      "selective degradation", 
      "asparagine", 
      "asparagine residues", 
      "residues", 
      "proline residues", 
      "complexes", 
      "components", 
      "acidic residues", 
      "products", 
      "non-ubiquitinated proteins", 
      "degradation", 
      "consist", 
      "hydrophobic", 
      "substrate", 
      "core", 
      "macromolecular structure", 
      "structure"
    ], 
    "name": "MHC-linked LMP gene products specifically alter peptidase activities of the proteasome", 
    "pagination": "262-264", 
    "productId": [
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1035838378"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1038/365262a0"
        ]
      }, 
      {
        "name": "pubmed_id", 
        "type": "PropertyValue", 
        "value": [
          "8371781"
        ]
      }
    ], 
    "sameAs": [
      "https://doi.org/10.1038/365262a0", 
      "https://app.dimensions.ai/details/publication/pub.1035838378"
    ], 
    "sdDataset": "articles", 
    "sdDatePublished": "2022-08-04T16:50", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-springernature-scigraph/baseset/20220804/entities/gbq_results/article/article_244.jsonl", 
    "type": "ScholarlyArticle", 
    "url": "https://doi.org/10.1038/365262a0"
  }
]
 

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.10.1038/365262a0'

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

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/365262a0'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/365262a0'

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

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/365262a0'


 

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

220 TRIPLES      21 PREDICATES      96 URIs      79 LITERALS      20 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1038/365262a0 schema:about N174219bebf194a059362b757b685e386
2 N262d02016a2e4939b618e90d9a79a7a3
3 N61b238b37ccf4e08af652251732a7d70
4 N677d48e34c9b4feeb731ae7146221781
5 N68acb857a587419284f9944e02f93c82
6 N6a484e960a224a50840fb575b103b4bf
7 N6ad5f1daa40749e49d02b4b7777c4330
8 Nd316943ac2ae4662af521dc87230e49a
9 Ndf4fc005535e4a0cab71ebcfff80f771
10 Ne8ddb7a4d64e45ffa852eff6059a1672
11 Nf19791a670284b6ab75c16a2e586c61e
12 Nf8624ac8dfe04429b5c4636ad1fe63c4
13 Nfda3a390fa414d9c9e6960a186ca5235
14 anzsrc-for:11
15 anzsrc-for:1107
16 schema:author N4e30d76e52f94811a72ec38a8faa82de
17 schema:citation sg:pub.10.1038/348744a0
18 sg:pub.10.1038/353326a0
19 sg:pub.10.1038/353355a0
20 sg:pub.10.1038/353357a0
21 sg:pub.10.1038/353662a0
22 sg:pub.10.1038/353664a0
23 sg:pub.10.1038/360171a0
24 sg:pub.10.1038/360174a0
25 sg:pub.10.1038/363552a0
26 schema:datePublished 1993-09
27 schema:datePublishedReg 1993-09-01
28 schema:description PROTEASOMES are highly conserved macromolecular structures which function as endopeptidases1–3. They are found in the cyto-plasm and nucleus of eukaryotic tissues and consist of at least 14 non-identical subunits with molecular masses ranging from ∼20 to 32K. Proteasomes are essential in the selective degradation of ubiquitinated and certain non-ubiquitinated proteins, acting as the proteolytic core of an energy-dependent 26S (1,500K) proteolytic complex. Two proteasome subunits, LMP2 and LMP7 (refs 4–7), are encoded within the major histocompatibility complex (MHC), implicating proteasomes in antigen processing8,9. Here we deter-mine the function of these two MHC-linked subunits by comparing the proteolytic activities of purified proteasomes containing (LMP+) or lacking (LMP−) these components. We find that pro-teasomes of both types have endopeptidase activity against sub-strates bearing hydrophobic, basic or acidic residues immediately preceding the cleavage site (the PI position) and at sites following asparagine, glycine and proline residues. The activity of LMP+ proteasomes is much higher than that of LMP− proteasomes against substrates with hydrophobic, basic or asparagine residues at PI, whereas their activities are comparable when acidic and glycine residues are present at PI. The MHC-linked LMP2 and LMP7 subunits therefore function to amplify specific endopeptid-ase activities of the proteasome.
29 schema:genre article
30 schema:isAccessibleForFree false
31 schema:isPartOf N0a1da641a0144868858f3598bdd6e691
32 Nbc13f02d8dc748bebbfe069d1c9c36b3
33 sg:journal.1018957
34 schema:keywords LMP2
35 LMP7
36 LMP7 subunit
37 PI
38 acidic residues
39 activity
40 antigen
41 asparagine
42 asparagine residues
43 cleavage site
44 complexes
45 components
46 consist
47 core
48 degradation
49 endopeptidase activity
50 eukaryotic tissues
51 function
52 gene products
53 glycine
54 glycine residue
55 histocompatibility complex
56 hydrophobic
57 lacking
58 macromolecular structure
59 major histocompatibility complex
60 mass
61 molecular mass
62 non-identical subunits
63 non-ubiquitinated proteins
64 nucleus
65 peptidase activity
66 products
67 proline residues
68 proteasome
69 proteasome subunits
70 protein
71 proteolytic activity
72 proteolytic complex
73 proteolytic core
74 residues
75 selective degradation
76 sites
77 structure
78 substrate
79 subunits
80 tissue
81 types
82 schema:name MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
83 schema:pagination 262-264
84 schema:productId N5ba7731066e6450284bb312db77da3d5
85 N6ef71b9449da4abcad5e520824096369
86 Nbf7aca8722b14852b3e79d73f06b87bd
87 schema:sameAs https://app.dimensions.ai/details/publication/pub.1035838378
88 https://doi.org/10.1038/365262a0
89 schema:sdDatePublished 2022-08-04T16:50
90 schema:sdLicense https://scigraph.springernature.com/explorer/license/
91 schema:sdPublisher Nfa15b90e150c40e7983a5d004af1e136
92 schema:url https://doi.org/10.1038/365262a0
93 sgo:license sg:explorer/license/
94 sgo:sdDataset articles
95 rdf:type schema:ScholarlyArticle
96 N0a1da641a0144868858f3598bdd6e691 schema:issueNumber 6443
97 rdf:type schema:PublicationIssue
98 N149c50f35a624d4d8d09bb3ce1de33c4 rdf:first sg:person.01113021256.14
99 rdf:rest rdf:nil
100 N174219bebf194a059362b757b685e386 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
101 schema:name Tumor Cells, Cultured
102 rdf:type schema:DefinedTerm
103 N262d02016a2e4939b618e90d9a79a7a3 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
104 schema:name Humans
105 rdf:type schema:DefinedTerm
106 N4e30d76e52f94811a72ec38a8faa82de rdf:first sg:person.01121242412.64
107 rdf:rest N87d6cd469ebc4ea6a585d969d11379ee
108 N5ba7731066e6450284bb312db77da3d5 schema:name pubmed_id
109 schema:value 8371781
110 rdf:type schema:PropertyValue
111 N61b238b37ccf4e08af652251732a7d70 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
112 schema:name Molecular Sequence Data
113 rdf:type schema:DefinedTerm
114 N677d48e34c9b4feeb731ae7146221781 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
115 schema:name Major Histocompatibility Complex
116 rdf:type schema:DefinedTerm
117 N68acb857a587419284f9944e02f93c82 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
118 schema:name Mutation
119 rdf:type schema:DefinedTerm
120 N6a484e960a224a50840fb575b103b4bf schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
121 schema:name Cysteine Endopeptidases
122 rdf:type schema:DefinedTerm
123 N6ad5f1daa40749e49d02b4b7777c4330 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
124 schema:name Substrate Specificity
125 rdf:type schema:DefinedTerm
126 N6ef71b9449da4abcad5e520824096369 schema:name dimensions_id
127 schema:value pub.1035838378
128 rdf:type schema:PropertyValue
129 N87d6cd469ebc4ea6a585d969d11379ee rdf:first sg:person.01045607256.00
130 rdf:rest Nb553754c052e4085a22d7a052a3c7a82
131 Nb553754c052e4085a22d7a052a3c7a82 rdf:first sg:person.0754405533.36
132 rdf:rest N149c50f35a624d4d8d09bb3ce1de33c4
133 Nbc13f02d8dc748bebbfe069d1c9c36b3 schema:volumeNumber 365
134 rdf:type schema:PublicationVolume
135 Nbf7aca8722b14852b3e79d73f06b87bd schema:name doi
136 schema:value 10.1038/365262a0
137 rdf:type schema:PropertyValue
138 Nd316943ac2ae4662af521dc87230e49a schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
139 schema:name Proteasome Endopeptidase Complex
140 rdf:type schema:DefinedTerm
141 Ndf4fc005535e4a0cab71ebcfff80f771 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
142 schema:name Interferon-gamma
143 rdf:type schema:DefinedTerm
144 Ne8ddb7a4d64e45ffa852eff6059a1672 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
145 schema:name Peptides
146 rdf:type schema:DefinedTerm
147 Nf19791a670284b6ab75c16a2e586c61e schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
148 schema:name Proteins
149 rdf:type schema:DefinedTerm
150 Nf8624ac8dfe04429b5c4636ad1fe63c4 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
151 schema:name Amino Acid Sequence
152 rdf:type schema:DefinedTerm
153 Nfa15b90e150c40e7983a5d004af1e136 schema:name Springer Nature - SN SciGraph project
154 rdf:type schema:Organization
155 Nfda3a390fa414d9c9e6960a186ca5235 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
156 schema:name Multienzyme Complexes
157 rdf:type schema:DefinedTerm
158 anzsrc-for:11 schema:inDefinedTermSet anzsrc-for:
159 schema:name Medical and Health Sciences
160 rdf:type schema:DefinedTerm
161 anzsrc-for:1107 schema:inDefinedTermSet anzsrc-for:
162 schema:name Immunology
163 rdf:type schema:DefinedTerm
164 sg:journal.1018957 schema:issn 0028-0836
165 1476-4687
166 schema:name Nature
167 schema:publisher Springer Nature
168 rdf:type schema:Periodical
169 sg:person.01045607256.00 schema:affiliation grid-institutes:grid.417264.2
170 schema:familyName Brown
171 schema:givenName Michael G.
172 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01045607256.00
173 rdf:type schema:Person
174 sg:person.01113021256.14 schema:familyName Monaco
175 schema:givenName John J.
176 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01113021256.14
177 rdf:type schema:Person
178 sg:person.01121242412.64 schema:affiliation grid-institutes:grid.38142.3c
179 schema:familyName Driscoll
180 schema:givenName James
181 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01121242412.64
182 rdf:type schema:Person
183 sg:person.0754405533.36 schema:affiliation grid-institutes:grid.38142.3c
184 schema:familyName Finley
185 schema:givenName Daniel
186 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0754405533.36
187 rdf:type schema:Person
188 sg:pub.10.1038/348744a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1014832159
189 https://doi.org/10.1038/348744a0
190 rdf:type schema:CreativeWork
191 sg:pub.10.1038/353326a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1040302419
192 https://doi.org/10.1038/353326a0
193 rdf:type schema:CreativeWork
194 sg:pub.10.1038/353355a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1016459418
195 https://doi.org/10.1038/353355a0
196 rdf:type schema:CreativeWork
197 sg:pub.10.1038/353357a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1016313560
198 https://doi.org/10.1038/353357a0
199 rdf:type schema:CreativeWork
200 sg:pub.10.1038/353662a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1014387648
201 https://doi.org/10.1038/353662a0
202 rdf:type schema:CreativeWork
203 sg:pub.10.1038/353664a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1047893865
204 https://doi.org/10.1038/353664a0
205 rdf:type schema:CreativeWork
206 sg:pub.10.1038/360171a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1016437140
207 https://doi.org/10.1038/360171a0
208 rdf:type schema:CreativeWork
209 sg:pub.10.1038/360174a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1013551518
210 https://doi.org/10.1038/360174a0
211 rdf:type schema:CreativeWork
212 sg:pub.10.1038/363552a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1004841625
213 https://doi.org/10.1038/363552a0
214 rdf:type schema:CreativeWork
215 grid-institutes:grid.38142.3c schema:alternateName Department of Cellular and Molecular Physiology, Harvard Medical School, 02115, Boston, Massachusetts, USA
216 schema:name Department of Cellular and Molecular Physiology, Harvard Medical School, 02115, Boston, Massachusetts, USA
217 rdf:type schema:Organization
218 grid-institutes:grid.417264.2 schema:alternateName Department of Microbiology and Immunology, Medical College of Virginia, Virginia Commonwealth University, 23298–0678, Richmond, Virginia, USA
219 schema:name Department of Microbiology and Immunology, Medical College of Virginia, Virginia Commonwealth University, 23298–0678, Richmond, Virginia, USA
220 rdf:type schema:Organization
 




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


...