ACCESSORY PROTEINS FOR G PROTEINS: Partners in Signaling
Accessory proteins involved in signal processing through heterotrimeric G proteins are generally defined as proteins distinct from G protein–coupled receptor (GPCR), G protein, or classical effectors that regulate the strength/efficiency/specificity of signal transfer upon receptor activation or pos...
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E-Artikel |
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| Erschienen: |
2006 |
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37 |
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Annual Reviews Electronic Back Volume Collection 1932-2005ff |
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| Übergeordnetes Werk: |
in: Annual review of pharmacology and toxicology - Palo Alto, Calif., 1961, 46(2006), Seite 151-187 |
| Übergeordnetes Werk: |
volume:46 ; year:2006 ; pages:151-187 ; extent:37 |
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| 520 | |a Accessory proteins involved in signal processing through heterotrimeric G proteins are generally defined as proteins distinct from G protein–coupled receptor (GPCR), G protein, or classical effectors that regulate the strength/efficiency/specificity of signal transfer upon receptor activation or position these entities in the right microenvironment, contributing to the formation of a functional signal transduction complex. A flurry of recent studies have implicated an additional class of accessory proteins for this system that provide signal input to heterotrimeric G proteins in the absence of a cell surface receptor, serve as alternative binding partners for G protein subunits, provide unexpected modes of G protein regulation, and have introduced additional functional roles for G proteins. This group of accessory proteins includes the recently discovered Activators of G protein Signaling (AGS) proteins identified in a functional screen for receptor-independent activators of G protein signaling as well as several proteins identified in protein interaction screens and genetic screens in model organisms. These accessory proteins may influence GDP dissociation and nucleotide exchange at the G subunit, alter subunit interactions within heterotrimeric G independent of nucleotide exchange, or form complexes with G or G independent of the typical G heterotrimer. AGS and related accessory proteins reveal unexpected diversity in G protein subunits as signal transducers within the cell. | ||
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(DE-627)NLEJ164179402 DE-627 ger DE-627 rakwb ACCESSORY PROTEINS FOR G PROTEINS: Partners in Signaling 2006 37 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Accessory proteins involved in signal processing through heterotrimeric G proteins are generally defined as proteins distinct from G protein–coupled receptor (GPCR), G protein, or classical effectors that regulate the strength/efficiency/specificity of signal transfer upon receptor activation or position these entities in the right microenvironment, contributing to the formation of a functional signal transduction complex. A flurry of recent studies have implicated an additional class of accessory proteins for this system that provide signal input to heterotrimeric G proteins in the absence of a cell surface receptor, serve as alternative binding partners for G protein subunits, provide unexpected modes of G protein regulation, and have introduced additional functional roles for G proteins. This group of accessory proteins includes the recently discovered Activators of G protein Signaling (AGS) proteins identified in a functional screen for receptor-independent activators of G protein signaling as well as several proteins identified in protein interaction screens and genetic screens in model organisms. These accessory proteins may influence GDP dissociation and nucleotide exchange at the G subunit, alter subunit interactions within heterotrimeric G independent of nucleotide exchange, or form complexes with G or G independent of the typical G heterotrimer. AGS and related accessory proteins reveal unexpected diversity in G protein subunits as signal transducers within the cell. Annual Reviews Electronic Back Volume Collection 1932-2005ff Sato, Motohiko oth Blumer, Joe B. oth Simon, Violaine oth Lanier, Stephen M. oth in Annual review of pharmacology and toxicology Palo Alto, Calif., 1961 46(2006), Seite 151-187 Online-Ressource (DE-627)NLEJ164018646 (DE-600)1474461-2 0362-1642 nnns volume:46 year:2006 pages:151-187 extent:37 http://dx.doi.org/10.1146/annurev.pharmtox.46.120604.141115 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 46 2006 151-187 37 |
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(DE-627)NLEJ164179402 DE-627 ger DE-627 rakwb ACCESSORY PROTEINS FOR G PROTEINS: Partners in Signaling 2006 37 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Accessory proteins involved in signal processing through heterotrimeric G proteins are generally defined as proteins distinct from G protein–coupled receptor (GPCR), G protein, or classical effectors that regulate the strength/efficiency/specificity of signal transfer upon receptor activation or position these entities in the right microenvironment, contributing to the formation of a functional signal transduction complex. A flurry of recent studies have implicated an additional class of accessory proteins for this system that provide signal input to heterotrimeric G proteins in the absence of a cell surface receptor, serve as alternative binding partners for G protein subunits, provide unexpected modes of G protein regulation, and have introduced additional functional roles for G proteins. This group of accessory proteins includes the recently discovered Activators of G protein Signaling (AGS) proteins identified in a functional screen for receptor-independent activators of G protein signaling as well as several proteins identified in protein interaction screens and genetic screens in model organisms. These accessory proteins may influence GDP dissociation and nucleotide exchange at the G subunit, alter subunit interactions within heterotrimeric G independent of nucleotide exchange, or form complexes with G or G independent of the typical G heterotrimer. AGS and related accessory proteins reveal unexpected diversity in G protein subunits as signal transducers within the cell. Annual Reviews Electronic Back Volume Collection 1932-2005ff Sato, Motohiko oth Blumer, Joe B. oth Simon, Violaine oth Lanier, Stephen M. oth in Annual review of pharmacology and toxicology Palo Alto, Calif., 1961 46(2006), Seite 151-187 Online-Ressource (DE-627)NLEJ164018646 (DE-600)1474461-2 0362-1642 nnns volume:46 year:2006 pages:151-187 extent:37 http://dx.doi.org/10.1146/annurev.pharmtox.46.120604.141115 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 46 2006 151-187 37 |
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(DE-627)NLEJ164179402 DE-627 ger DE-627 rakwb ACCESSORY PROTEINS FOR G PROTEINS: Partners in Signaling 2006 37 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Accessory proteins involved in signal processing through heterotrimeric G proteins are generally defined as proteins distinct from G protein–coupled receptor (GPCR), G protein, or classical effectors that regulate the strength/efficiency/specificity of signal transfer upon receptor activation or position these entities in the right microenvironment, contributing to the formation of a functional signal transduction complex. A flurry of recent studies have implicated an additional class of accessory proteins for this system that provide signal input to heterotrimeric G proteins in the absence of a cell surface receptor, serve as alternative binding partners for G protein subunits, provide unexpected modes of G protein regulation, and have introduced additional functional roles for G proteins. This group of accessory proteins includes the recently discovered Activators of G protein Signaling (AGS) proteins identified in a functional screen for receptor-independent activators of G protein signaling as well as several proteins identified in protein interaction screens and genetic screens in model organisms. These accessory proteins may influence GDP dissociation and nucleotide exchange at the G subunit, alter subunit interactions within heterotrimeric G independent of nucleotide exchange, or form complexes with G or G independent of the typical G heterotrimer. AGS and related accessory proteins reveal unexpected diversity in G protein subunits as signal transducers within the cell. Annual Reviews Electronic Back Volume Collection 1932-2005ff Sato, Motohiko oth Blumer, Joe B. oth Simon, Violaine oth Lanier, Stephen M. oth in Annual review of pharmacology and toxicology Palo Alto, Calif., 1961 46(2006), Seite 151-187 Online-Ressource (DE-627)NLEJ164018646 (DE-600)1474461-2 0362-1642 nnns volume:46 year:2006 pages:151-187 extent:37 http://dx.doi.org/10.1146/annurev.pharmtox.46.120604.141115 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 46 2006 151-187 37 |
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(DE-627)NLEJ164179402 DE-627 ger DE-627 rakwb ACCESSORY PROTEINS FOR G PROTEINS: Partners in Signaling 2006 37 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Accessory proteins involved in signal processing through heterotrimeric G proteins are generally defined as proteins distinct from G protein–coupled receptor (GPCR), G protein, or classical effectors that regulate the strength/efficiency/specificity of signal transfer upon receptor activation or position these entities in the right microenvironment, contributing to the formation of a functional signal transduction complex. A flurry of recent studies have implicated an additional class of accessory proteins for this system that provide signal input to heterotrimeric G proteins in the absence of a cell surface receptor, serve as alternative binding partners for G protein subunits, provide unexpected modes of G protein regulation, and have introduced additional functional roles for G proteins. This group of accessory proteins includes the recently discovered Activators of G protein Signaling (AGS) proteins identified in a functional screen for receptor-independent activators of G protein signaling as well as several proteins identified in protein interaction screens and genetic screens in model organisms. These accessory proteins may influence GDP dissociation and nucleotide exchange at the G subunit, alter subunit interactions within heterotrimeric G independent of nucleotide exchange, or form complexes with G or G independent of the typical G heterotrimer. AGS and related accessory proteins reveal unexpected diversity in G protein subunits as signal transducers within the cell. Annual Reviews Electronic Back Volume Collection 1932-2005ff Sato, Motohiko oth Blumer, Joe B. oth Simon, Violaine oth Lanier, Stephen M. oth in Annual review of pharmacology and toxicology Palo Alto, Calif., 1961 46(2006), Seite 151-187 Online-Ressource (DE-627)NLEJ164018646 (DE-600)1474461-2 0362-1642 nnns volume:46 year:2006 pages:151-187 extent:37 http://dx.doi.org/10.1146/annurev.pharmtox.46.120604.141115 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 46 2006 151-187 37 |
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(DE-627)NLEJ164179402 DE-627 ger DE-627 rakwb ACCESSORY PROTEINS FOR G PROTEINS: Partners in Signaling 2006 37 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Accessory proteins involved in signal processing through heterotrimeric G proteins are generally defined as proteins distinct from G protein–coupled receptor (GPCR), G protein, or classical effectors that regulate the strength/efficiency/specificity of signal transfer upon receptor activation or position these entities in the right microenvironment, contributing to the formation of a functional signal transduction complex. A flurry of recent studies have implicated an additional class of accessory proteins for this system that provide signal input to heterotrimeric G proteins in the absence of a cell surface receptor, serve as alternative binding partners for G protein subunits, provide unexpected modes of G protein regulation, and have introduced additional functional roles for G proteins. This group of accessory proteins includes the recently discovered Activators of G protein Signaling (AGS) proteins identified in a functional screen for receptor-independent activators of G protein signaling as well as several proteins identified in protein interaction screens and genetic screens in model organisms. These accessory proteins may influence GDP dissociation and nucleotide exchange at the G subunit, alter subunit interactions within heterotrimeric G independent of nucleotide exchange, or form complexes with G or G independent of the typical G heterotrimer. AGS and related accessory proteins reveal unexpected diversity in G protein subunits as signal transducers within the cell. Annual Reviews Electronic Back Volume Collection 1932-2005ff Sato, Motohiko oth Blumer, Joe B. oth Simon, Violaine oth Lanier, Stephen M. oth in Annual review of pharmacology and toxicology Palo Alto, Calif., 1961 46(2006), Seite 151-187 Online-Ressource (DE-627)NLEJ164018646 (DE-600)1474461-2 0362-1642 nnns volume:46 year:2006 pages:151-187 extent:37 http://dx.doi.org/10.1146/annurev.pharmtox.46.120604.141115 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 46 2006 151-187 37 |
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| abstract |
Accessory proteins involved in signal processing through heterotrimeric G proteins are generally defined as proteins distinct from G protein–coupled receptor (GPCR), G protein, or classical effectors that regulate the strength/efficiency/specificity of signal transfer upon receptor activation or position these entities in the right microenvironment, contributing to the formation of a functional signal transduction complex. A flurry of recent studies have implicated an additional class of accessory proteins for this system that provide signal input to heterotrimeric G proteins in the absence of a cell surface receptor, serve as alternative binding partners for G protein subunits, provide unexpected modes of G protein regulation, and have introduced additional functional roles for G proteins. This group of accessory proteins includes the recently discovered Activators of G protein Signaling (AGS) proteins identified in a functional screen for receptor-independent activators of G protein signaling as well as several proteins identified in protein interaction screens and genetic screens in model organisms. These accessory proteins may influence GDP dissociation and nucleotide exchange at the G subunit, alter subunit interactions within heterotrimeric G independent of nucleotide exchange, or form complexes with G or G independent of the typical G heterotrimer. AGS and related accessory proteins reveal unexpected diversity in G protein subunits as signal transducers within the cell. |
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Accessory proteins involved in signal processing through heterotrimeric G proteins are generally defined as proteins distinct from G protein–coupled receptor (GPCR), G protein, or classical effectors that regulate the strength/efficiency/specificity of signal transfer upon receptor activation or position these entities in the right microenvironment, contributing to the formation of a functional signal transduction complex. A flurry of recent studies have implicated an additional class of accessory proteins for this system that provide signal input to heterotrimeric G proteins in the absence of a cell surface receptor, serve as alternative binding partners for G protein subunits, provide unexpected modes of G protein regulation, and have introduced additional functional roles for G proteins. This group of accessory proteins includes the recently discovered Activators of G protein Signaling (AGS) proteins identified in a functional screen for receptor-independent activators of G protein signaling as well as several proteins identified in protein interaction screens and genetic screens in model organisms. These accessory proteins may influence GDP dissociation and nucleotide exchange at the G subunit, alter subunit interactions within heterotrimeric G independent of nucleotide exchange, or form complexes with G or G independent of the typical G heterotrimer. AGS and related accessory proteins reveal unexpected diversity in G protein subunits as signal transducers within the cell. |
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Accessory proteins involved in signal processing through heterotrimeric G proteins are generally defined as proteins distinct from G protein–coupled receptor (GPCR), G protein, or classical effectors that regulate the strength/efficiency/specificity of signal transfer upon receptor activation or position these entities in the right microenvironment, contributing to the formation of a functional signal transduction complex. A flurry of recent studies have implicated an additional class of accessory proteins for this system that provide signal input to heterotrimeric G proteins in the absence of a cell surface receptor, serve as alternative binding partners for G protein subunits, provide unexpected modes of G protein regulation, and have introduced additional functional roles for G proteins. This group of accessory proteins includes the recently discovered Activators of G protein Signaling (AGS) proteins identified in a functional screen for receptor-independent activators of G protein signaling as well as several proteins identified in protein interaction screens and genetic screens in model organisms. These accessory proteins may influence GDP dissociation and nucleotide exchange at the G subunit, alter subunit interactions within heterotrimeric G independent of nucleotide exchange, or form complexes with G or G independent of the typical G heterotrimer. AGS and related accessory proteins reveal unexpected diversity in G protein subunits as signal transducers within the cell. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ164179402</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230506101456.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070207s2006 xx |||||o 00| ||und c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ164179402</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">ACCESSORY PROTEINS FOR G PROTEINS: Partners in Signaling</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2006</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">37</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Accessory proteins involved in signal processing through heterotrimeric G proteins are generally defined as proteins distinct from G protein–coupled receptor (GPCR), G protein, or classical effectors that regulate the strength/efficiency/specificity of signal transfer upon receptor activation or position these entities in the right microenvironment, contributing to the formation of a functional signal transduction complex. A flurry of recent studies have implicated an additional class of accessory proteins for this system that provide signal input to heterotrimeric G proteins in the absence of a cell surface receptor, serve as alternative binding partners for G protein subunits, provide unexpected modes of G protein regulation, and have introduced additional functional roles for G proteins. This group of accessory proteins includes the recently discovered Activators of G protein Signaling (AGS) proteins identified in a functional screen for receptor-independent activators of G protein signaling as well as several proteins identified in protein interaction screens and genetic screens in model organisms. These accessory proteins may influence GDP dissociation and nucleotide exchange at the G subunit, alter subunit interactions within heterotrimeric G independent of nucleotide exchange, or form complexes with G or G independent of the typical G heterotrimer. AGS and related accessory proteins reveal unexpected diversity in G protein subunits as signal transducers within the cell.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Annual Reviews Electronic Back Volume Collection 1932-2005ff</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Sato, Motohiko</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Blumer, Joe B.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Simon, Violaine</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lanier, Stephen M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Annual review of pharmacology and toxicology</subfield><subfield code="d">Palo Alto, Calif., 1961</subfield><subfield code="g">46(2006), Seite 151-187</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ164018646</subfield><subfield code="w">(DE-600)1474461-2</subfield><subfield code="x">0362-1642</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:46</subfield><subfield code="g">year:2006</subfield><subfield code="g">pages:151-187</subfield><subfield code="g">extent:37</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1146/annurev.pharmtox.46.120604.141115</subfield><subfield code="q">text/html</subfield><subfield code="z">Deutschlandweit zugänglich</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-ANR</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">46</subfield><subfield code="j">2006</subfield><subfield code="h">151-187</subfield><subfield code="g">37</subfield></datafield></record></collection>
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