Signal Recognition Particle
"Signal Recognition Particle" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A cytosolic ribonucleoprotein complex that acts to induce elongation arrest of nascent presecretory and membrane proteins until the ribosome becomes associated with the rough endoplasmic reticulum. It consists of a 7S RNA and at least six polypeptide subunits (relative molecular masses 9, 14, 19, 54, 68, and 72K).
Descriptor ID |
D018271
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MeSH Number(s) |
D12.776.157.725.500.750.800 D12.776.664.962.500.750.800
|
Concept/Terms |
Signal Recognition Particle- Signal Recognition Particle
- Particle, Signal Recognition
- Recognition Particle, Signal
- SRP (Signal Recognition Particle)
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Below are MeSH descriptors whose meaning is more general than "Signal Recognition Particle".
Below are MeSH descriptors whose meaning is more specific than "Signal Recognition Particle".
This graph shows the total number of publications written about "Signal Recognition Particle" by people in this website by year, and whether "Signal Recognition Particle" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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2003 | 1 | 0 | 1 |
2004 | 1 | 0 | 1 |
2006 | 0 | 1 | 1 |
2008 | 1 | 0 | 1 |
2010 | 2 | 0 | 2 |
2011 | 2 | 0 | 2 |
2012 | 0 | 1 | 1 |
2013 | 5 | 0 | 5 |
2017 | 1 | 0 | 1 |
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Below are the most recent publications written about "Signal Recognition Particle" by people in Profiles.
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Hwang Fu YH, Huang WYC, Shen K, Groves JT, Miller T, Shan SO. Two-step membrane binding by the bacterial SRP receptor enable efficient and accurate Co-translational protein targeting. Elife. 2017 07 28; 6.
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Voigts-Hoffmann F, Schmitz N, Shen K, Shan SO, Ataide SF, Ban N. The structural basis of FtsY recruitment and GTPase activation by SRP RNA. Mol Cell. 2013 Dec 12; 52(5):643-54.
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Shen K, Wang Y, Hwang Fu YH, Zhang Q, Feigon J, Shan SO. Molecular mechanism of GTPase activation at the signal recognition particle (SRP) RNA distal end. J Biol Chem. 2013 Dec 20; 288(51):36385-97.
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Jaru-Ampornpan P, Liang FC, Nisthal A, Nguyen TX, Wang P, Shen K, Mayo SL, Shan SO. Mechanism of an ATP-independent protein disaggregase: II. distinct molecular interactions drive multiple steps during aggregate disassembly. J Biol Chem. 2013 May 10; 288(19):13431-45.
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Akopian D, Shen K, Zhang X, Shan SO. Signal recognition particle: an essential protein-targeting machine. Annu Rev Biochem. 2013; 82:693-721.
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Akopian D, Dalal K, Shen K, Duong F, Shan SO. SecYEG activates GTPases to drive the completion of cotranslational protein targeting. J Cell Biol. 2013 Feb 18; 200(4):397-405.
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Shen K, Arslan S, Akopian D, Ha T, Shan SO. Activated GTPase movement on an RNA scaffold drives co-translational protein targeting. Nature. 2012 Dec 13; 492(7428):271-5.
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Shen K, Zhang X, Shan SO. Synergistic actions between the SRP RNA and translating ribosome allow efficient delivery of the correct cargos during cotranslational protein targeting. RNA. 2011 May; 17(5):892-902.
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Ataide SF, Schmitz N, Shen K, Ke A, Shan SO, Doudna JA, Ban N. The crystal structure of the signal recognition particle in complex with its receptor. Science. 2011 Feb 18; 331(6019):881-6.
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Jaru-Ampornpan P, Shen K, Lam VQ, Ali M, Doniach S, Jia TZ, Shan SO. ATP-independent reversal of a membrane protein aggregate by a chloroplast SRP subunit. Nat Struct Mol Biol. 2010 Jun; 17(6):696-702.