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Literature DB >> 8937977

The signal recognition particle and related small cytoplasmic ribonucleoprotein particles.

Abstract

Recently, a number of novel small cytoplasmic ribonucleoprotein particles have been identified that comprise RNA and protein subunits related to the signal recognition particle (SRP). Here we discuss the latest results on the structure and functions of SRP together with the structures and putative functions of the novel SRP-related ribonucleoprotein particles.

Entities: Chemical

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Year: 1996 PMID： 8937977 DOI： 10.1242/jcs.109.11.2601

Source DB: PubMed Journal: J Cell Sci ISSN： 0021-9533 Impact factor: 5.285

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Cited

12 in total

1. Getting on target: the archaeal signal recognition particle.

Authors: Christian Zwieb; Jerry Eichler
Journal: Archaea Date: 2002-03 Impact factor: 3.273

2. The SRP9/14 subunit of the human signal recognition particle binds to a variety of Alu-like RNAs and with higher affinity than its mouse homolog.

Authors: F Bovia; N Wolff; S Ryser; K Strub
Journal: Nucleic Acids Res Date: 1997-01-15 Impact factor: 16.971

3. Association of Escherichia coli ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle.

Authors: A A Herskovits; E Bibi
Journal: Proc Natl Acad Sci U S A Date: 2000-04-25 Impact factor: 11.205

4. A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle.

Authors: Y Thomas; N Bui; K Strub
Journal: Nucleic Acids Res Date: 1997-05-15 Impact factor: 16.971

The signal recognition particle and related small cytoplasmic ribonucleoprotein particles.

1. Getting on target: the archaeal signal recognition particle.

2. The SRP9/14 subunit of the human signal recognition particle binds to a variety of Alu-like RNAs and with higher affinity than its mouse homolog.

3. Association of Escherichia coli ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle.

4. A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle.

5. Active Alu element "A-tails": size does matter.

Review 6. Emerging landscape of non-coding RNAs in oral health and disease.

7. Alu RNP and Alu RNA regulate translation initiation in vitro.

8. The completed genome sequence of the pathogenic ascomycete fungus Fusarium graminearum.

9. RNA recognition by a human antibody against brain cytoplasmic 200 RNA.

10. Characterization of APOBEC3G binding to 7SL RNA.