Profiling the Tyrosine Phosphorylation State Using SH2 Domains View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2009

AUTHORS

Kevin Dierck , Kazuya Machida , Bruce J. Mayer , Peter Nollau

ABSTRACT

Global monitoring of cellular signaling activity is of great importance for the understanding of the regulation of complex signaling networks and the characterization of signaling pathways deregulated in diseases. Tyrosine phosphorylation of intracellular signaling proteins followed by the recognition and binding of Src homology 2 (SH2) domains are key mechanisms in the downstream transmission of many important biological signals. SH2 domains, comprising 120 members in humans, are small modular protein binding domains that recognize tyrosine phosphorylated signaling proteins with high specificity. Based on these binding properties, the large number of naturally occurring and currently available SH2 domains serve as excellent probes for the comprehensive profiling of the cellular state of signaling activity. Here we have described different experimental strategies for global SH2 profiling: high-resolution phosphoproteomic scanning by far-Western Blot analysis and high-throughput profiling by our recently developed oligonucleotide-tagged multiplex assay (OTM) and Rosette assay. More... »

PAGES

131-155

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-60327-834-8_11

DOI

http://dx.doi.org/10.1007/978-1-60327-834-8_11

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1009845402

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19241011


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": "Animals", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Humans", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Models, Biological", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Phosphoproteins", 
        "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": "Proteomics", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "Tyrosine", 
        "type": "DefinedTerm"
      }, 
      {
        "inDefinedTermSet": "https://www.nlm.nih.gov/mesh/", 
        "name": "src Homology Domains", 
        "type": "DefinedTerm"
      }
    ], 
    "author": [
      {
        "affiliation": {
          "alternateName": "Department of Clinical Chemistry, University Medical Center, Hamburg-Eppendorf, Germany", 
          "id": "http://www.grid.ac/institutes/grid.13648.38", 
          "name": [
            "Department of Clinical Chemistry, University Medical Center, Hamburg-Eppendorf, Germany"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Dierck", 
        "givenName": "Kevin", 
        "id": "sg:person.01256163050.26", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01256163050.26"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Genetics and Developmental Biology, University of Connecticut, Farmington, CT, USA", 
          "id": "http://www.grid.ac/institutes/grid.208078.5", 
          "name": [
            "Department of Genetics and Developmental Biology, University of Connecticut, Farmington, CT, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Machida", 
        "givenName": "Kazuya", 
        "id": "sg:person.01372411450.61", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01372411450.61"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Genetics and Developmental Biology, University of Connecticut, Farmington, CT, USA", 
          "id": "http://www.grid.ac/institutes/grid.208078.5", 
          "name": [
            "Department of Genetics and Developmental Biology, University of Connecticut, Farmington, CT, USA"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Mayer", 
        "givenName": "Bruce J.", 
        "id": "sg:person.01244537451.59", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01244537451.59"
        ], 
        "type": "Person"
      }, 
      {
        "affiliation": {
          "alternateName": "Department of Clinical Chemistry, University Medical Center, Hamburg-Eppendorf, Germany", 
          "id": "http://www.grid.ac/institutes/grid.13648.38", 
          "name": [
            "Department of Clinical Chemistry, University Medical Center, Hamburg-Eppendorf, Germany"
          ], 
          "type": "Organization"
        }, 
        "familyName": "Nollau", 
        "givenName": "Peter", 
        "id": "sg:person.01226132305.67", 
        "sameAs": [
          "https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01226132305.67"
        ], 
        "type": "Person"
      }
    ], 
    "datePublished": "2009", 
    "datePublishedReg": "2009-01-01", 
    "description": "Global monitoring of cellular signaling activity is of great importance for the understanding of the regulation of complex signaling networks and the characterization of signaling pathways deregulated in diseases. Tyrosine phosphorylation of intracellular signaling proteins followed by the recognition and binding of Src homology 2 (SH2) domains are key mechanisms in the downstream transmission of many important biological signals. SH2 domains, comprising 120 members in humans, are small modular protein binding domains that recognize tyrosine phosphorylated signaling proteins with high specificity. Based on these binding properties, the large number of naturally occurring and currently available SH2 domains serve as excellent probes for the comprehensive profiling of the cellular state of signaling activity. Here we have described different experimental strategies for global SH2 profiling: high-resolution phosphoproteomic scanning by far-Western Blot analysis and high-throughput profiling by our recently developed oligonucleotide-tagged multiplex assay (OTM) and Rosette assay.", 
    "editor": [
      {
        "familyName": "Graauw", 
        "givenName": "Marjo de", 
        "type": "Person"
      }
    ], 
    "genre": "chapter", 
    "id": "sg:pub.10.1007/978-1-60327-834-8_11", 
    "isAccessibleForFree": false, 
    "isPartOf": {
      "isbn": [
        "978-1-60327-833-1", 
        "978-1-60327-834-8"
      ], 
      "name": "Phospho-Proteomics", 
      "type": "Book"
    }, 
    "keywords": [
      "SH2 domain", 
      "Src homology 2 domain", 
      "Far Western blot analysis", 
      "tyrosine phosphorylation state", 
      "high-throughput profiling", 
      "modular proteins", 
      "SH2 profiling", 
      "cellular states", 
      "different experimental strategies", 
      "tyrosine phosphorylation", 
      "phosphorylation state", 
      "important biological signals", 
      "comprehensive profiling", 
      "blot analysis", 
      "protein", 
      "profiling", 
      "experimental strategies", 
      "key mechanism", 
      "biological signals", 
      "domain", 
      "phosphorylation", 
      "high specificity", 
      "regulation", 
      "pathway", 
      "intracellular", 
      "binding", 
      "multiplex assay", 
      "large number", 
      "activity", 
      "assays", 
      "rosettes", 
      "members", 
      "excellent probe", 
      "humans", 
      "mechanism", 
      "specificity", 
      "probe", 
      "characterization", 
      "great importance", 
      "understanding", 
      "signals", 
      "importance", 
      "global monitoring", 
      "disease", 
      "analysis", 
      "number", 
      "recognition", 
      "strategies", 
      "transmission", 
      "state", 
      "network", 
      "downstream transmission", 
      "properties", 
      "scanning", 
      "monitoring"
    ], 
    "name": "Profiling the Tyrosine Phosphorylation State Using SH2 Domains", 
    "pagination": "131-155", 
    "productId": [
      {
        "name": "dimensions_id", 
        "type": "PropertyValue", 
        "value": [
          "pub.1009845402"
        ]
      }, 
      {
        "name": "doi", 
        "type": "PropertyValue", 
        "value": [
          "10.1007/978-1-60327-834-8_11"
        ]
      }, 
      {
        "name": "pubmed_id", 
        "type": "PropertyValue", 
        "value": [
          "19241011"
        ]
      }
    ], 
    "publisher": {
      "name": "Springer Nature", 
      "type": "Organisation"
    }, 
    "sameAs": [
      "https://doi.org/10.1007/978-1-60327-834-8_11", 
      "https://app.dimensions.ai/details/publication/pub.1009845402"
    ], 
    "sdDataset": "chapters", 
    "sdDatePublished": "2022-09-02T16:16", 
    "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
    "sdPublisher": {
      "name": "Springer Nature - SN SciGraph project", 
      "type": "Organization"
    }, 
    "sdSource": "s3://com-springernature-scigraph/baseset/20220902/entities/gbq_results/chapter/chapter_416.jsonl", 
    "type": "Chapter", 
    "url": "https://doi.org/10.1007/978-1-60327-834-8_11"
  }
]
 

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.10.1007/978-1-60327-834-8_11'

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

curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1007/978-1-60327-834-8_11'

Turtle is a human-readable linked data format.

curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1007/978-1-60327-834-8_11'

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

curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1007/978-1-60327-834-8_11'


 

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

178 TRIPLES      22 PREDICATES      90 URIs      83 LITERALS      17 BLANK NODES

Subject Predicate Object
1 sg:pub.10.1007/978-1-60327-834-8_11 schema:about N0057401a9e7b47d9974fb71692923be1
2 N0f6bfe1f1bfe4cd0aab432bc8766ed51
3 N31c52a7b41e74902b42b9918ac1e9bea
4 N57ece13508524514a38978aade63ff8b
5 N7eca0fd3f75f44c19a4252c2b4d46b88
6 Nacc7e9f96c72408882b90d729c672555
7 Nbde58828bba14b39abbea1ac2defc8d6
8 Nf192a14c6d164fd180482d931a44947e
9 Nfe7b75c0caac436ab012b2eaf87c8915
10 anzsrc-for:06
11 anzsrc-for:0601
12 schema:author N295506a9dfec4d268757ca60420a450d
13 schema:datePublished 2009
14 schema:datePublishedReg 2009-01-01
15 schema:description Global monitoring of cellular signaling activity is of great importance for the understanding of the regulation of complex signaling networks and the characterization of signaling pathways deregulated in diseases. Tyrosine phosphorylation of intracellular signaling proteins followed by the recognition and binding of Src homology 2 (SH2) domains are key mechanisms in the downstream transmission of many important biological signals. SH2 domains, comprising 120 members in humans, are small modular protein binding domains that recognize tyrosine phosphorylated signaling proteins with high specificity. Based on these binding properties, the large number of naturally occurring and currently available SH2 domains serve as excellent probes for the comprehensive profiling of the cellular state of signaling activity. Here we have described different experimental strategies for global SH2 profiling: high-resolution phosphoproteomic scanning by far-Western Blot analysis and high-throughput profiling by our recently developed oligonucleotide-tagged multiplex assay (OTM) and Rosette assay.
16 schema:editor Nd0758f88c4c9424cad301ea8cbf713f5
17 schema:genre chapter
18 schema:isAccessibleForFree false
19 schema:isPartOf N0845867fd6ba453a90ded91e6616e2c4
20 schema:keywords Far Western blot analysis
21 SH2 domain
22 SH2 profiling
23 Src homology 2 domain
24 activity
25 analysis
26 assays
27 binding
28 biological signals
29 blot analysis
30 cellular states
31 characterization
32 comprehensive profiling
33 different experimental strategies
34 disease
35 domain
36 downstream transmission
37 excellent probe
38 experimental strategies
39 global monitoring
40 great importance
41 high specificity
42 high-throughput profiling
43 humans
44 importance
45 important biological signals
46 intracellular
47 key mechanism
48 large number
49 mechanism
50 members
51 modular proteins
52 monitoring
53 multiplex assay
54 network
55 number
56 pathway
57 phosphorylation
58 phosphorylation state
59 probe
60 profiling
61 properties
62 protein
63 recognition
64 regulation
65 rosettes
66 scanning
67 signals
68 specificity
69 state
70 strategies
71 transmission
72 tyrosine phosphorylation
73 tyrosine phosphorylation state
74 understanding
75 schema:name Profiling the Tyrosine Phosphorylation State Using SH2 Domains
76 schema:pagination 131-155
77 schema:productId N36357905353b4dacae1ae2fb508f2258
78 Na302dcbe64ca432ea20c6afeb34adb6e
79 Ne48443783b5644a6b2f26cf6ba7fea16
80 schema:publisher N52e36f73d2f14e2f936da853b161c684
81 schema:sameAs https://app.dimensions.ai/details/publication/pub.1009845402
82 https://doi.org/10.1007/978-1-60327-834-8_11
83 schema:sdDatePublished 2022-09-02T16:16
84 schema:sdLicense https://scigraph.springernature.com/explorer/license/
85 schema:sdPublisher N6428ef5dac634c8ba9568375f1578378
86 schema:url https://doi.org/10.1007/978-1-60327-834-8_11
87 sgo:license sg:explorer/license/
88 sgo:sdDataset chapters
89 rdf:type schema:Chapter
90 N0057401a9e7b47d9974fb71692923be1 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
91 schema:name src Homology Domains
92 rdf:type schema:DefinedTerm
93 N0845867fd6ba453a90ded91e6616e2c4 schema:isbn 978-1-60327-833-1
94 978-1-60327-834-8
95 schema:name Phospho-Proteomics
96 rdf:type schema:Book
97 N0f6bfe1f1bfe4cd0aab432bc8766ed51 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
98 schema:name Phosphoproteins
99 rdf:type schema:DefinedTerm
100 N295506a9dfec4d268757ca60420a450d rdf:first sg:person.01256163050.26
101 rdf:rest Nb6115528a3f24b80898c1b66f57f3091
102 N31c52a7b41e74902b42b9918ac1e9bea schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
103 schema:name Models, Biological
104 rdf:type schema:DefinedTerm
105 N36357905353b4dacae1ae2fb508f2258 schema:name doi
106 schema:value 10.1007/978-1-60327-834-8_11
107 rdf:type schema:PropertyValue
108 N52e36f73d2f14e2f936da853b161c684 schema:name Springer Nature
109 rdf:type schema:Organisation
110 N57ece13508524514a38978aade63ff8b schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
111 schema:name Humans
112 rdf:type schema:DefinedTerm
113 N6428ef5dac634c8ba9568375f1578378 schema:name Springer Nature - SN SciGraph project
114 rdf:type schema:Organization
115 N7eca0fd3f75f44c19a4252c2b4d46b88 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
116 schema:name Protein-Tyrosine Kinases
117 rdf:type schema:DefinedTerm
118 N9edcc91fa8c0487f94f90b6e0fa80efc rdf:first sg:person.01226132305.67
119 rdf:rest rdf:nil
120 Na302dcbe64ca432ea20c6afeb34adb6e schema:name dimensions_id
121 schema:value pub.1009845402
122 rdf:type schema:PropertyValue
123 Nacc7e9f96c72408882b90d729c672555 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
124 schema:name Phosphorylation
125 rdf:type schema:DefinedTerm
126 Nb6115528a3f24b80898c1b66f57f3091 rdf:first sg:person.01372411450.61
127 rdf:rest Nb627ffa12a92439e9659ffb09ea09dcf
128 Nb627ffa12a92439e9659ffb09ea09dcf rdf:first sg:person.01244537451.59
129 rdf:rest N9edcc91fa8c0487f94f90b6e0fa80efc
130 Nbde58828bba14b39abbea1ac2defc8d6 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
131 schema:name Animals
132 rdf:type schema:DefinedTerm
133 Nc2e29a0ca195402295d2dea738c7fad7 schema:familyName Graauw
134 schema:givenName Marjo de
135 rdf:type schema:Person
136 Nd0758f88c4c9424cad301ea8cbf713f5 rdf:first Nc2e29a0ca195402295d2dea738c7fad7
137 rdf:rest rdf:nil
138 Ne48443783b5644a6b2f26cf6ba7fea16 schema:name pubmed_id
139 schema:value 19241011
140 rdf:type schema:PropertyValue
141 Nf192a14c6d164fd180482d931a44947e schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
142 schema:name Proteomics
143 rdf:type schema:DefinedTerm
144 Nfe7b75c0caac436ab012b2eaf87c8915 schema:inDefinedTermSet https://www.nlm.nih.gov/mesh/
145 schema:name Tyrosine
146 rdf:type schema:DefinedTerm
147 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
148 schema:name Biological Sciences
149 rdf:type schema:DefinedTerm
150 anzsrc-for:0601 schema:inDefinedTermSet anzsrc-for:
151 schema:name Biochemistry and Cell Biology
152 rdf:type schema:DefinedTerm
153 sg:person.01226132305.67 schema:affiliation grid-institutes:grid.13648.38
154 schema:familyName Nollau
155 schema:givenName Peter
156 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01226132305.67
157 rdf:type schema:Person
158 sg:person.01244537451.59 schema:affiliation grid-institutes:grid.208078.5
159 schema:familyName Mayer
160 schema:givenName Bruce J.
161 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01244537451.59
162 rdf:type schema:Person
163 sg:person.01256163050.26 schema:affiliation grid-institutes:grid.13648.38
164 schema:familyName Dierck
165 schema:givenName Kevin
166 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01256163050.26
167 rdf:type schema:Person
168 sg:person.01372411450.61 schema:affiliation grid-institutes:grid.208078.5
169 schema:familyName Machida
170 schema:givenName Kazuya
171 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01372411450.61
172 rdf:type schema:Person
173 grid-institutes:grid.13648.38 schema:alternateName Department of Clinical Chemistry, University Medical Center, Hamburg-Eppendorf, Germany
174 schema:name Department of Clinical Chemistry, University Medical Center, Hamburg-Eppendorf, Germany
175 rdf:type schema:Organization
176 grid-institutes:grid.208078.5 schema:alternateName Department of Genetics and Developmental Biology, University of Connecticut, Farmington, CT, USA
177 schema:name Department of Genetics and Developmental Biology, University of Connecticut, Farmington, CT, USA
178 rdf:type schema:Organization
 




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


...