STRUCTURAL INSIGHTS INTO THE SIGNAL RECOGNITION PARTICLE
The signal recognition particle (SRP) directs integral membrane and secretory proteins to the cellular protein translocation machinery during translation. The SRP is an evolutionarily conserved RNA-protein complex whose activities are regulated by GTP hydrolysis. Recent structural investigations of...
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E-Artikel |
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2004 |
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19 |
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Annual Reviews Electronic Back Volume Collection 1932-2005ff |
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in: Annual review of biochemistry - Palo Alto, Calif. : Annual Reviews Inc., 1932, 73(2004), Seite 539-557 |
| Übergeordnetes Werk: |
volume:73 ; year:2004 ; pages:539-557 ; extent:19 |
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| 520 | |a The signal recognition particle (SRP) directs integral membrane and secretory proteins to the cellular protein translocation machinery during translation. The SRP is an evolutionarily conserved RNA-protein complex whose activities are regulated by GTP hydrolysis. Recent structural investigations of SRP functional domains and interactions provide new insights into the mechanisms of SRP activity in all cells, leading toward a comprehensive understanding of protein trafficking by this elegant pathway. | ||
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(DE-627)NLEJ164059067 DE-627 ger DE-627 rakwb STRUCTURAL INSIGHTS INTO THE SIGNAL RECOGNITION PARTICLE 2004 19 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The signal recognition particle (SRP) directs integral membrane and secretory proteins to the cellular protein translocation machinery during translation. The SRP is an evolutionarily conserved RNA-protein complex whose activities are regulated by GTP hydrolysis. Recent structural investigations of SRP functional domains and interactions provide new insights into the mechanisms of SRP activity in all cells, leading toward a comprehensive understanding of protein trafficking by this elegant pathway. Annual Reviews Electronic Back Volume Collection 1932-2005ff Doudna, Jennifer A. oth Batey, Robert T. oth in Annual review of biochemistry Palo Alto, Calif. : Annual Reviews Inc., 1932 73(2004), Seite 539-557 Online-Ressource (DE-627)NLEJ164018964 (DE-600)1470446-8 1545-4509 nnns volume:73 year:2004 pages:539-557 extent:19 http://dx.doi.org/10.1146/annurev.biochem.73.011303.074048 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-ANR GBV_NL_ARTICLE AR 73 2004 539-557 19 |
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The signal recognition particle (SRP) directs integral membrane and secretory proteins to the cellular protein translocation machinery during translation. The SRP is an evolutionarily conserved RNA-protein complex whose activities are regulated by GTP hydrolysis. Recent structural investigations of SRP functional domains and interactions provide new insights into the mechanisms of SRP activity in all cells, leading toward a comprehensive understanding of protein trafficking by this elegant pathway. |
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The signal recognition particle (SRP) directs integral membrane and secretory proteins to the cellular protein translocation machinery during translation. The SRP is an evolutionarily conserved RNA-protein complex whose activities are regulated by GTP hydrolysis. Recent structural investigations of SRP functional domains and interactions provide new insights into the mechanisms of SRP activity in all cells, leading toward a comprehensive understanding of protein trafficking by this elegant pathway. |
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The signal recognition particle (SRP) directs integral membrane and secretory proteins to the cellular protein translocation machinery during translation. The SRP is an evolutionarily conserved RNA-protein complex whose activities are regulated by GTP hydrolysis. Recent structural investigations of SRP functional domains and interactions provide new insights into the mechanisms of SRP activity in all cells, leading toward a comprehensive understanding of protein trafficking by this elegant pathway. |
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