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SRP Keeps Polypeptides Translocation-Competent by Slowing Translation to Match Limiting ER-Targeting Sites

Cell, 2008-05, Vol.133 (3), p.440-451

2008

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Characterization of APOBEC3G binding to 7SL RNA

Retrovirology, 2008-07, Vol.5 (1), p.54-54, Article 54

2008

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Alu elements as regulators of gene expression

Nucleic acids research, 2006-11, Vol.34 (19), p.5491

2006

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Alu RNA regulates the cellular pool of active ribosomes by targeted delivery of SRP9/14 to 40S subunits

Nucleic acids research, 2015-03, Vol.43 (5), p.2874

2015

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Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation

Molecular biology of the cell, 2012-07, Vol.23 (14), p.2712-2722

2012

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Alu-like RNA promotes cell differentiation and reduces malignancy of human neuroblastoma cells

The FASEB journal, 2010-10, Vol.24 (10), p.4033-4046

2010

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Alu RNP and Alu RNA regulate translation initiation in vitro

Nucleic acids research, 2006-01, Vol.34 (8), p.2374

2006

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Crystal structure of a signal recognition particle Alu domain in the elongation arrest conformation

RNA (Cambridge), 2014-12, Vol.20 (12), p.1955-1962

2014

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The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure

RNA (Cambridge), 1999-10, Vol.5 (10), p.1333-1347, Article S1355838299991045

1999

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Residues in SRP9/14 essential for elongation arrest activity of the signal recognition particle define a positively charged functional domain on one side of the protein

RNA (Cambridge), 2010-05, Vol.16 (5), p.969-979

2010

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Structure and assembly of the Alu domain of the mammalian signal recognition particle

Nature (London), 2000-11, Vol.408 (6809), p.167-173

2000

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Multiple Roles of Alu-Related Noncoding RNAs

Progress in molecular and subcellular biology, 2011, Vol.51, p.119

2011

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Inefficient targeting to the endoplasmic reticulum by the signal recognition particle elicits selective defects in post-ER membrane trafficking

Experimental cell research, 2007-02, Vol.313 (4), p.834-847

2007

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SRP maintains nascent chains translocation-competent by slowing translation rates to match limiting numbers of targeting sites

Cell, 2008-05, Vol.133 (3), p.440-451

2008

Volltextzugriff (PDF)

Signal Recognition Particle Alu Domain Occupies a Defined Site at the Ribosomal Subunit Interface upon Signal Sequence Recognition

Biochemistry (Easton), 2004-01, Vol.43 (1), p.107-117

2004

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Structure of SRP14 from the Schizosaccharomyces pombe signal recognition particle

Acta crystallographica. Section D, Biological crystallography., 2009-05, Vol.65 (5), p.421-433

2009

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Towards the structure of the mammalian signal recognition particle

Current Opinion in Structural Biology, 2002-02, Vol.12 (1), p.72-81

2002

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New Insights into Signal Recognition and Elongation Arrest Activities of the Signal Recognition Particle

Biological chemistry, 1999-02, Vol.380 (2), p.135-145

1999

Volltextzugriff (PDF)

The signal recognition particle and related small cytoplasmic ribonucleoprotein particles

Journal of cell science, 1996-11, Vol.109 ( Pt 11) (11), p.2601-2608

1996

Volltextzugriff (PDF)

Transcription termination and 3′ processing: the end is in site

Cell, 1985-06, Vol.41 (2), p.349-359

1985

Volltextzugriff (PDF)

A two‐step recognition of signal sequences determines the translocation efficiency of proteins

The EMBO journal, 1996-02, Vol.15 (3), p.468-478

1996

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Conserved tertiary base pairing ensures proper RNA folding and efficient assembly of the signal recognition particle Alu domain

Nucleic acids research, 2004-01, Vol.32 (16), p.4915

2004

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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

Nucleic acids research, 1997-05, Vol.25 (10), p.1920

1997

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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

Nucleic acids research, 1997-01, Vol.25 (2), p.318

1997

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Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle

Nature (London), 1989-08, Vol.340 (6233), p.482-486

1989

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SRP Keeps Polypeptides Translocation-Competent by Slowing Translation to Match Limiting ER-Targeting Sites

Characterization of APOBEC3G binding to 7SL RNA

Alu elements as regulators of gene expression

Alu RNA regulates the cellular pool of active ribosomes by targeted delivery of SRP9/14 to 40S subunits

Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation

Alu-like RNA promotes cell differentiation and reduces malignancy of human neuroblastoma cells

Alu RNP and Alu RNA regulate translation initiation in vitro

Crystal structure of a signal recognition particle Alu domain in the elongation arrest conformation

The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure

Residues in SRP9/14 essential for elongation arrest activity of the signal recognition particle define a positively charged functional domain on one side of the protein

Structure and assembly of the Alu domain of the mammalian signal recognition particle

Multiple Roles of Alu-Related Noncoding RNAs

Inefficient targeting to the endoplasmic reticulum by the signal recognition particle elicits selective defects in post-ER membrane trafficking

SRP maintains nascent chains translocation-competent by slowing translation rates to match limiting numbers of targeting sites

Signal Recognition Particle Alu Domain Occupies a Defined Site at the Ribosomal Subunit Interface upon Signal Sequence Recognition

Structure of SRP14 from the Schizosaccharomyces pombe signal recognition particle

Towards the structure of the mammalian signal recognition particle

New Insights into Signal Recognition and Elongation Arrest Activities of the Signal Recognition Particle

The signal recognition particle and related small cytoplasmic ribonucleoprotein particles

Transcription termination and 3′ processing: the end is in site

A two‐step recognition of signal sequences determines the translocation efficiency of proteins

Conserved tertiary base pairing ensures proper RNA folding and efficient assembly of the signal recognition particle Alu domain

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

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

Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle

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