316 related articles for article (PubMed ID: 9233785)
1. The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14.
Birse DE; Kapp U; Strub K; Cusack S; Aberg A
EMBO J; 1997 Jul; 16(13):3757-66. PubMed ID: 9233785
[TBL] [Abstract][Full Text] [Related]
2. Structure of SRP14 from the Schizosaccharomyces pombe signal recognition particle.
Brooks MA; Ravelli RB; McCarthy AA; Strub K; Cusack S
Acta Crystallogr D Biol Crystallogr; 2009 May; 65(Pt 5):421-33. PubMed ID: 19390147
[TBL] [Abstract][Full Text] [Related]
3. Mutational analysis of the protein subunits of the signal recognition particle Alu-domain.
Bui N; Wolff N; Cusack S; Strub K
RNA; 1997 Jul; 3(7):748-63. PubMed ID: 9214658
[TBL] [Abstract][Full Text] [Related]
4. Structure and assembly of the Alu domain of the mammalian signal recognition particle.
Weichenrieder O; Wild K; Strub K; Cusack S
Nature; 2000 Nov; 408(6809):167-73. PubMed ID: 11089964
[TBL] [Abstract][Full Text] [Related]
5. The heterodimeric subunit SRP9/14 of the signal recognition particle functions as permuted single polypeptide chain.
Bovia F; Bui N; Strub K
Nucleic Acids Res; 1994 Jun; 22(11):2028-35. PubMed ID: 7518078
[TBL] [Abstract][Full Text] [Related]
6. 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.
Bovia F; Wolff N; Ryser S; Strub K
Nucleic Acids Res; 1997 Jan; 25(2):318-26. PubMed ID: 9016560
[TBL] [Abstract][Full Text] [Related]
7. Hierarchical assembly of the Alu domain of the mammalian signal recognition particle.
Weichenrieder O; Stehlin C; Kapp U; Birse DE; Timmins PA; Strub K; Cusack S
RNA; 2001 May; 7(5):731-40. PubMed ID: 11350037
[TBL] [Abstract][Full Text] [Related]
8. Structure of the SRP19 RNA complex and implications for signal recognition particle assembly.
Hainzl T; Huang S; Sauer-Eriksson AE
Nature; 2002 Jun; 417(6890):767-71. PubMed ID: 12050674
[TBL] [Abstract][Full Text] [Related]
9. Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction.
Becker MM; Lapouge K; Segnitz B; Wild K; Sinning I
Nucleic Acids Res; 2017 Jan; 45(1):470-481. PubMed ID: 27899666
[TBL] [Abstract][Full Text] [Related]
10. The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAs.
Bovia F; Fornallaz M; Leffers H; Strub K
Mol Biol Cell; 1995 Apr; 6(4):471-84. PubMed ID: 7542942
[TBL] [Abstract][Full Text] [Related]
11. 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.
Thomas Y; Bui N; Strub K
Nucleic Acids Res; 1997 May; 25(10):1920-9. PubMed ID: 9115358
[TBL] [Abstract][Full Text] [Related]
12. The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure.
Strub K; Fornallaz M; Bui N
RNA; 1999 Oct; 5(10):1333-47. PubMed ID: 10573124
[TBL] [Abstract][Full Text] [Related]
13. A highly conserved nucleotide in the Alu domain of SRP RNA mediates translation arrest through high affinity binding to SRP9/14.
Chang DY; Newitt JA; Hsu K; Bernstein HD; Maraia RJ
Nucleic Acids Res; 1997 Mar; 25(6):1117-22. PubMed ID: 9092618
[TBL] [Abstract][Full Text] [Related]
14. Identification and comparative analysis of components from the signal recognition particle in protozoa and fungi.
Rosenblad MA; Zwieb C; Samuelsson T
BMC Genomics; 2004 Jan; 5(1):5. PubMed ID: 14720308
[TBL] [Abstract][Full Text] [Related]
15. Structures of SRP54 and SRP19, the two proteins that organize the ribonucleic core of the signal recognition particle from Pyrococcus furiosus.
Egea PF; Napetschnig J; Walter P; Stroud RM
PLoS One; 2008; 3(10):e3528. PubMed ID: 18953414
[TBL] [Abstract][Full Text] [Related]
16. Assembly of the Alu domain of the signal recognition particle (SRP): dimerization of the two protein components is required for efficient binding to SRP RNA.
Strub K; Walter P
Mol Cell Biol; 1990 Feb; 10(2):777-84. PubMed ID: 2153922
[TBL] [Abstract][Full Text] [Related]
17. Identification of a minimal Alu RNA folding domain that specifically binds SRP9/14.
Weichenrieder O; Kapp U; Cusack S; Strub K
RNA; 1997 Nov; 3(11):1262-74. PubMed ID: 9409618
[TBL] [Abstract][Full Text] [Related]
18. SRP RNA remodeling by SRP68 explains its role in protein translocation.
Grotwinkel JT; Wild K; Segnitz B; Sinning I
Science; 2014 Apr; 344(6179):101-4. PubMed ID: 24700861
[TBL] [Abstract][Full Text] [Related]
19. Retrotransposition and Crystal Structure of an Alu RNP in the Ribosome-Stalling Conformation.
Ahl V; Keller H; Schmidt S; Weichenrieder O
Mol Cell; 2015 Dec; 60(5):715-727. PubMed ID: 26585389
[TBL] [Abstract][Full Text] [Related]
20. Conserved tertiary base pairing ensures proper RNA folding and efficient assembly of the signal recognition particle Alu domain.
Huck L; Scherrer A; Terzi L; Johnson AE; Bernstein HD; Cusack S; Weichenrieder O; Strub K
Nucleic Acids Res; 2004; 32(16):4915-24. PubMed ID: 15383645
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
