The role of tyrosine phosphorylation in angiotensin II mediated intracellular signaling and cell growth View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1996-02

AUTHORS

B. Schieffer, K. E. Bernstein, M. B. Marrero

ABSTRACT

Most cell types, including vascular smooth muscle cells and rat kidney mesangial cells, are controlled mainly by two types of cell surface receptors: (a) single membrane-spanning tyrosine kinase receptors for growth factors and (b) seven-transmembrane G-protein linked receptors for vasoactive peptides such as angiotensin II, vasopressin, and endothelin. These vasoactive peptide hormones also act as growth factors in normal and abnormal cell development. However, in contrast to the growth factor receptors (e.g., epidermal growth factor receptor and platelet-derived growth factor receptor), the G-protein linked receptors, such as the angiotensin II AT1 receptor, lack cytoplasmic tyrosine kinase domains. Nevertheless, angiotensin II has recently been demonstrated to cause increased tyrosine phosphorylation of numerous proteins in several cellular systems. For example, angiotensin II has been reported to induce the tyrosine phosphorylation of the γ-isoform of phospholipase C, pp120, pp125FAK, and members of the janus kinase/signal transducer and activator of transcription pathway. Furthermore, angiotensin II seems to modulate the activity of the soluble cytoplasmic tyrosine kinase pp60c-src, and this tyrosine kinase has been implicated in the phosphorylation of some of the above proteins. Understanding the biochemistry of tyrosine phosphorylation involved in G-protein coupled receptors, such as the AT1 receptor, may therefore lead to the development of new pharmacological interventions important in cardiovascular diseases. More... »

PAGES

85-91

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00196783

DOI

http://dx.doi.org/10.1007/bf00196783

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1048376817

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8820403


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/2008/03", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Chemical Sciences", 
        "type": "DefinedTerm"
      }, 
      {
        "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0304", 
        "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
        "name": "Medicinal and Biomolecular Chemistry", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Angiotensin II", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Animals", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Cell Division", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Models, Biological", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Phosphorylation", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Protein-Tyrosine Kinases", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Rats", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Signal Transduction", 
        "type": "DefinedTerm"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "Department of Pathology, Emory University, 30322, Atlanta, GA, USA", 
          "id": "http://www.grid.ac/institutes/grid.189967.8", 
          "name": [
            "Department of Pathology, Emory University, 30322, Atlanta, GA, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Schieffer", 
        "givenName": "B.", 
        "id": "sg:person.01075113266.30", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01075113266.30"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Pathology, Emory University, 30322, Atlanta, GA, USA", 
          "id": "http://www.grid.ac/institutes/grid.189967.8", 
          "name": [
            "Department of Pathology, Emory University, 30322, Atlanta, GA, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Bernstein", 
        "givenName": "K. E.", 
        "id": "sg:person.01240003301.55", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01240003301.55"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Pathology, and Center for Molecular and Cellular Signaling, Emory University, 1639 Pierce Drive, 30322, Atlanta, GA, USA", 
          "id": "http://www.grid.ac/institutes/grid.189967.8", 
          "name": [
            "Department of Pathology, and Center for Molecular and Cellular Signaling, Emory University, 1639 Pierce Drive, 30322, Atlanta, GA, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Marrero", 
        "givenName": "M. B.", 
        "id": "sg:person.0655015541.06", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0655015541.06"
        ], 
        "type": "Person"
      }
    ], 
    "citation": [
      {
        "id": "sg:pub.10.1038/375247a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1037354896", 
          "https://doi.org/10.1038/375247a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/351230a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1006531293", 
          "https://doi.org/10.1038/351230a0"
        ], 
        "type": "CreativeWork"
      }, 
      {
        "id": "sg:pub.10.1038/351233a0", 
        "sameAs": [
          "https://app.dimensions.ai/details/publication/pub.1035923039", 
          "https://doi.org/10.1038/351233a0"
        ], 
        "type": "CreativeWork"
      }
    ], 
    "datePublished": "1996-02", 
    "datePublishedReg": "1996-02-01", 
    "description": "Most cell types, including vascular smooth muscle cells and rat kidney mesangial cells, are controlled mainly by two types of cell surface receptors: (a) single membrane-spanning tyrosine kinase receptors for growth factors and (b) seven-transmembrane G-protein linked receptors for vasoactive peptides such as angiotensin II, vasopressin, and endothelin. These vasoactive peptide hormones also act as growth factors in normal and abnormal cell development. However, in contrast to the growth factor receptors (e.g., epidermal growth factor receptor and platelet-derived growth factor receptor), the G-protein linked receptors, such as the angiotensin II AT1 receptor, lack cytoplasmic tyrosine kinase domains. Nevertheless, angiotensin II has recently been demonstrated to cause increased tyrosine phosphorylation of numerous proteins in several cellular systems. For example, angiotensin II has been reported to induce the tyrosine phosphorylation of the \u03b3-isoform of phospholipase C, pp120, pp125FAK, and members of the janus kinase/signal transducer and activator of transcription pathway. Furthermore, angiotensin II seems to modulate the activity of the soluble cytoplasmic tyrosine kinase pp60c-src, and this tyrosine kinase has been implicated in the phosphorylation of some of the above proteins. Understanding the biochemistry of tyrosine phosphorylation involved in G-protein coupled receptors, such as the AT1 receptor, may therefore lead to the development of new pharmacological interventions important in cardiovascular diseases.", 
    "genre": "article", 
    "id": "sg:pub.10.1007/bf00196783", 
    "isAccessibleForFree": false, 
    "isFundedItemOf": [
      {
        "id": "sg:grant.2440420", 
        "type": "MonetaryGrant"
      }, 
      {
        "id": "sg:grant.2493831", 
        "type": "MonetaryGrant"
      }, 
      {
        "id": "sg:grant.2634765", 
        "type": "MonetaryGrant"
      }, 
      {
        "id": "sg:grant.2494561", 
        "type": "MonetaryGrant"
      }
    ], 
    "isPartOf": [
      {
        "id": "sg:journal.1057918", 
        "issn": [
          "0946-2716", 
          "1432-1440"
        ], 
        "name": "Journal of Molecular Medicine", 
        "publisher": "Springer Nature", 
        "type": "Periodical"
      }, 
      {
        "issueNumber": "2", 
        "type": "PublicationIssue"
      }, 
      {
        "type": "PublicationVolume", 
        "volumeNumber": "74"
      }
    ], 
    "keywords": [
      "tyrosine phosphorylation", 
      "G proteins", 
      "tyrosine kinase pp60c-src", 
      "Janus kinase/signal transducer", 
      "cytoplasmic tyrosine kinase domain", 
      "kinase/signal transducer", 
      "membrane-spanning tyrosine kinase receptors", 
      "seven-transmembrane G-protein", 
      "most cell types", 
      "abnormal cell development", 
      "cell surface receptors", 
      "tyrosine kinase domain", 
      "tyrosine kinase receptors", 
      "angiotensin II", 
      "pp60c-src", 
      "growth factor", 
      "numerous proteins", 
      "kinase domain", 
      "growth factor receptor", 
      "transcription pathway", 
      "vascular smooth muscle cells", 
      "signal transducer", 
      "tyrosine kinase", 
      "intracellular signaling", 
      "cell development", 
      "\u03b3 isoforms", 
      "kinase receptors", 
      "kidney mesangial cells", 
      "phosphorylation", 
      "rat kidney mesangial cells", 
      "cell types", 
      "AT1 receptor", 
      "phospholipase C", 
      "above proteins", 
      "cell growth", 
      "surface receptors", 
      "smooth muscle cells", 
      "factor receptor", 
      "angiotensin II AT1 receptor", 
      "muscle cells", 
      "II AT1 receptors", 
      "new pharmacological interventions", 
      "protein", 
      "vasoactive peptide hormones", 
      "peptide hormones", 
      "receptors", 
      "mesangial cells", 
      "cellular systems", 
      "vasoactive peptides", 
      "pharmacological interventions", 
      "cardiovascular disease", 
      "pp125FAK", 
      "cells", 
      "pp120", 
      "kinase", 
      "signaling", 
      "activator", 
      "pathway", 
      "biochemistry", 
      "peptides", 
      "domain", 
      "members", 
      "growth", 
      "endothelin", 
      "disease", 
      "vasopressin", 
      "hormone", 
      "development", 
      "role", 
      "intervention", 
      "factors", 
      "activity", 
      "types", 
      "transducer", 
      "contrast", 
      "system", 
      "example"
    ], 
    "name": "The role of tyrosine phosphorylation in angiotensin II mediated intracellular signaling and cell growth", 
    "pagination": "85-91", 
    "productId": [
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1048376817"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1007/bf00196783"
        ]
      }, 
      {
        "name": "pubmed_id", 
        "type": "PropertyValue", 
        "value": [
          "8820403"
        ]
      }
    ], 
    "sameAs": [
      "https://doi.org/10.1007/bf00196783", 
      "https://app.dimensions.ai/details/publication/pub.1048376817"
    ], 
    "sdDataset": "articles", 
    "sdDatePublished": "2022-10-01T06:30", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-springernature-scigraph/baseset/20221001/entities/gbq_results/article/article_290.jsonl", 
    "type": "ScholarlyArticle", 
    "url": "https://doi.org/10.1007/bf00196783"
  }
]
 

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.10.1007/bf00196783'

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

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1007/bf00196783'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1007/bf00196783'

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

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1007/bf00196783'


 

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

206 TRIPLES      21 PREDICATES      114 URIs      103 LITERALS      15 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1007/bf00196783 schema:about N30e73c42056e4f168ccc2ab674eba052
2 N333a30ac179a4a0fb13a9d6b4f5718a7
3 N3cbd079c15344308b1092915b547b09d
4 N3ec2820bf7d54be0b105449df28b6d76
5 N45f8dc17af214585abef01864a73117e
6 N70d3f2c58a4d44868cb87d211ea5a157
7 Na7604fa6102b47d2a114b536e46722bf
8 Na78a8617a7dc4e7b89b32a4c8a29add3
9 anzsrc-for:03
10 anzsrc-for:0304
11 schema:author Nbeeebb11347d4cf1b056a0089a7d3470
12 schema:citation sg:pub.10.1038/351230a0
13 sg:pub.10.1038/351233a0
14 sg:pub.10.1038/375247a0
15 schema:datePublished 1996-02
16 schema:datePublishedReg 1996-02-01
17 schema:description Most cell types, including vascular smooth muscle cells and rat kidney mesangial cells, are controlled mainly by two types of cell surface receptors: (a) single membrane-spanning tyrosine kinase receptors for growth factors and (b) seven-transmembrane G-protein linked receptors for vasoactive peptides such as angiotensin II, vasopressin, and endothelin. These vasoactive peptide hormones also act as growth factors in normal and abnormal cell development. However, in contrast to the growth factor receptors (e.g., epidermal growth factor receptor and platelet-derived growth factor receptor), the G-protein linked receptors, such as the angiotensin II AT1 receptor, lack cytoplasmic tyrosine kinase domains. Nevertheless, angiotensin II has recently been demonstrated to cause increased tyrosine phosphorylation of numerous proteins in several cellular systems. For example, angiotensin II has been reported to induce the tyrosine phosphorylation of the γ-isoform of phospholipase C, pp120, pp125FAK, and members of the janus kinase/signal transducer and activator of transcription pathway. Furthermore, angiotensin II seems to modulate the activity of the soluble cytoplasmic tyrosine kinase pp60c-src, and this tyrosine kinase has been implicated in the phosphorylation of some of the above proteins. Understanding the biochemistry of tyrosine phosphorylation involved in G-protein coupled receptors, such as the AT1 receptor, may therefore lead to the development of new pharmacological interventions important in cardiovascular diseases.
18 schema:genre article
19 schema:isAccessibleForFree false
20 schema:isPartOf N5a17dcd313584f3088d27070b9d20a4e
21 N8f78ca9f774b4c9aa7a782bce55759b8
22 sg:journal.1057918
23 schema:keywords AT1 receptor
24 G proteins
25 II AT1 receptors
26 Janus kinase/signal transducer
27 abnormal cell development
28 above proteins
29 activator
30 activity
31 angiotensin II
32 angiotensin II AT1 receptor
33 biochemistry
34 cardiovascular disease
35 cell development
36 cell growth
37 cell surface receptors
38 cell types
39 cells
40 cellular systems
41 contrast
42 cytoplasmic tyrosine kinase domain
43 development
44 disease
45 domain
46 endothelin
47 example
48 factor receptor
49 factors
50 growth
51 growth factor
52 growth factor receptor
53 hormone
54 intervention
55 intracellular signaling
56 kidney mesangial cells
57 kinase
58 kinase domain
59 kinase receptors
60 kinase/signal transducer
61 members
62 membrane-spanning tyrosine kinase receptors
63 mesangial cells
64 most cell types
65 muscle cells
66 new pharmacological interventions
67 numerous proteins
68 pathway
69 peptide hormones
70 peptides
71 pharmacological interventions
72 phospholipase C
73 phosphorylation
74 pp120
75 pp125FAK
76 pp60c-src
77 protein
78 rat kidney mesangial cells
79 receptors
80 role
81 seven-transmembrane G-protein
82 signal transducer
83 signaling
84 smooth muscle cells
85 surface receptors
86 system
87 transcription pathway
88 transducer
89 types
90 tyrosine kinase
91 tyrosine kinase domain
92 tyrosine kinase pp60c-src
93 tyrosine kinase receptors
94 tyrosine phosphorylation
95 vascular smooth muscle cells
96 vasoactive peptide hormones
97 vasoactive peptides
98 vasopressin
99 γ isoforms
100 schema:name The role of tyrosine phosphorylation in angiotensin II mediated intracellular signaling and cell growth
101 schema:pagination 85-91
102 schema:productId N048dffaafbed4a23bae9fbf6261e23be
103 N883d1a3508d94390ad19085430ac7d7f
104 Nc5cb621ead124e27a8264b0d3b895efc
105 schema:sameAs https://app.dimensions.ai/details/publication/pub.1048376817
106 https://doi.org/10.1007/bf00196783
107 schema:sdDatePublished 2022-10-01T06:30
108 schema:sdLicense https://scigraph.springernature.com/explorer/license/
109 schema:sdPublisher N0554a4a350df4e139a346317f2717665
110 schema:url https://doi.org/10.1007/bf00196783
111 sgo:license sg:explorer/license/
112 sgo:sdDataset articles
113 rdf:type schema:ScholarlyArticle
114 N048dffaafbed4a23bae9fbf6261e23be schema:name doi
115 schema:value 10.1007/bf00196783
116 rdf:type schema:PropertyValue
117 N0554a4a350df4e139a346317f2717665 schema:name Springer Nature - SN SciGraph project
118 rdf:type schema:Organization
119 N274af1324e624caeb3266353981e676a rdf:first sg:person.0655015541.06
120 rdf:rest rdf:nil
121 N30e73c42056e4f168ccc2ab674eba052 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
122 schema:name Animals
123 rdf:type schema:DefinedTerm
124 N333a30ac179a4a0fb13a9d6b4f5718a7 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
125 schema:name Models, Biological
126 rdf:type schema:DefinedTerm
127 N3cbd079c15344308b1092915b547b09d schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
128 schema:name Protein-Tyrosine Kinases
129 rdf:type schema:DefinedTerm
130 N3ec2820bf7d54be0b105449df28b6d76 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
131 schema:name Phosphorylation
132 rdf:type schema:DefinedTerm
133 N45f8dc17af214585abef01864a73117e schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
134 schema:name Signal Transduction
135 rdf:type schema:DefinedTerm
136 N5a17dcd313584f3088d27070b9d20a4e schema:issueNumber 2
137 rdf:type schema:PublicationIssue
138 N70d3f2c58a4d44868cb87d211ea5a157 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
139 schema:name Angiotensin II
140 rdf:type schema:DefinedTerm
141 N883d1a3508d94390ad19085430ac7d7f schema:name pubmed_id
142 schema:value 8820403
143 rdf:type schema:PropertyValue
144 N8f78ca9f774b4c9aa7a782bce55759b8 schema:volumeNumber 74
145 rdf:type schema:PublicationVolume
146 Na7604fa6102b47d2a114b536e46722bf schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
147 schema:name Cell Division
148 rdf:type schema:DefinedTerm
149 Na78a8617a7dc4e7b89b32a4c8a29add3 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
150 schema:name Rats
151 rdf:type schema:DefinedTerm
152 Nbbe6b509960c46bb98a658ba1a8fc1ae rdf:first sg:person.01240003301.55
153 rdf:rest N274af1324e624caeb3266353981e676a
154 Nbeeebb11347d4cf1b056a0089a7d3470 rdf:first sg:person.01075113266.30
155 rdf:rest Nbbe6b509960c46bb98a658ba1a8fc1ae
156 Nc5cb621ead124e27a8264b0d3b895efc schema:name dimensions_id
157 schema:value pub.1048376817
158 rdf:type schema:PropertyValue
159 anzsrc-for:03 schema:inDefinedTermSet anzsrc-for:
160 schema:name Chemical Sciences
161 rdf:type schema:DefinedTerm
162 anzsrc-for:0304 schema:inDefinedTermSet anzsrc-for:
163 schema:name Medicinal and Biomolecular Chemistry
164 rdf:type schema:DefinedTerm
165 sg:grant.2440420 http://pending.schema.org/fundedItem sg:pub.10.1007/bf00196783
166 rdf:type schema:MonetaryGrant
167 sg:grant.2493831 http://pending.schema.org/fundedItem sg:pub.10.1007/bf00196783
168 rdf:type schema:MonetaryGrant
169 sg:grant.2494561 http://pending.schema.org/fundedItem sg:pub.10.1007/bf00196783
170 rdf:type schema:MonetaryGrant
171 sg:grant.2634765 http://pending.schema.org/fundedItem sg:pub.10.1007/bf00196783
172 rdf:type schema:MonetaryGrant
173 sg:journal.1057918 schema:issn 0946-2716
174 1432-1440
175 schema:name Journal of Molecular Medicine
176 schema:publisher Springer Nature
177 rdf:type schema:Periodical
178 sg:person.01075113266.30 schema:affiliation grid-institutes:grid.189967.8
179 schema:familyName Schieffer
180 schema:givenName B.
181 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01075113266.30
182 rdf:type schema:Person
183 sg:person.01240003301.55 schema:affiliation grid-institutes:grid.189967.8
184 schema:familyName Bernstein
185 schema:givenName K. E.
186 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01240003301.55
187 rdf:type schema:Person
188 sg:person.0655015541.06 schema:affiliation grid-institutes:grid.189967.8
189 schema:familyName Marrero
190 schema:givenName M. B.
191 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0655015541.06
192 rdf:type schema:Person
193 sg:pub.10.1038/351230a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1006531293
194 https://doi.org/10.1038/351230a0
195 rdf:type schema:CreativeWork
196 sg:pub.10.1038/351233a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1035923039
197 https://doi.org/10.1038/351233a0
198 rdf:type schema:CreativeWork
199 sg:pub.10.1038/375247a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1037354896
200 https://doi.org/10.1038/375247a0
201 rdf:type schema:CreativeWork
202 grid-institutes:grid.189967.8 schema:alternateName Department of Pathology, Emory University, 30322, Atlanta, GA, USA
203 Department of Pathology, and Center for Molecular and Cellular Signaling, Emory University, 1639 Pierce Drive, 30322, Atlanta, GA, USA
204 schema:name Department of Pathology, Emory University, 30322, Atlanta, GA, USA
205 Department of Pathology, and Center for Molecular and Cellular Signaling, Emory University, 1639 Pierce Drive, 30322, Atlanta, GA, USA
206 rdf:type schema:Organization
 




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


...