These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
292 related articles for article (PubMed ID: 3010127)
1. The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle. Kurzchalia TV; Wiedmann M; Girshovich AS; Bochkareva ES; Bielka H; Rapoport TA Nature; 1986 Apr 17-23; 320(6063):634-6. PubMed ID: 3010127 [TBL] [Abstract][Full Text] [Related]
2. Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex. Luirink J; High S; Wood H; Giner A; Tollervey D; Dobberstein B Nature; 1992 Oct; 359(6397):741-3. PubMed ID: 1279430 [TBL] [Abstract][Full Text] [Related]
3. Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact. Siegel V; Walter P Nature; 1986 Mar 6-12; 320(6057):81-4. PubMed ID: 2419765 [TBL] [Abstract][Full Text] [Related]
4. A signal sequence receptor in the endoplasmic reticulum membrane. Wiedmann M; Kurzchalia TV; Hartmann E; Rapoport TA Nature; 1987 Aug 27-Sep 2; 328(6133):830-3. PubMed ID: 3041222 [TBL] [Abstract][Full Text] [Related]
5. Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting. Bacher G; Lütcke H; Jungnickel B; Rapoport TA; Dobberstein B Nature; 1996 May; 381(6579):248-51. PubMed ID: 8622769 [TBL] [Abstract][Full Text] [Related]
6. Direct probing of the interaction between the signal sequence of nascent preprolactin and the signal recognition particle by specific cross-linking. Wiedmann M; Kurzchalia TV; Bielka H; Rapoport TA J Cell Biol; 1987 Feb; 104(2):201-8. PubMed ID: 3643215 [TBL] [Abstract][Full Text] [Related]
7. Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains. Römisch K; Webb J; Herz J; Prehn S; Frank R; Vingron M; Dobberstein B Nature; 1989 Aug; 340(6233):478-82. PubMed ID: 2502717 [TBL] [Abstract][Full Text] [Related]
8. A protein complex required for signal-sequence-specific sorting and translocation. Wiedmann B; Sakai H; Davis TA; Wiedmann M Nature; 1994 Aug; 370(6489):434-40. PubMed ID: 8047162 [TBL] [Abstract][Full Text] [Related]
9. Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle. Krieg UC; Walter P; Johnson AE Proc Natl Acad Sci U S A; 1986 Nov; 83(22):8604-8. PubMed ID: 3095839 [TBL] [Abstract][Full Text] [Related]
10. A two-step recognition of signal sequences determines the translocation efficiency of proteins. Belin D; Bost S; Vassalli JD; Strub K EMBO J; 1996 Feb; 15(3):468-78. PubMed ID: 8599930 [TBL] [Abstract][Full Text] [Related]
11. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Halic M; Becker T; Pool MR; Spahn CM; Grassucci RA; Frank J; Beckmann R Nature; 2004 Feb; 427(6977):808-14. PubMed ID: 14985753 [TBL] [Abstract][Full Text] [Related]
12. GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation. Miller JD; Wilhelm H; Gierasch L; Gilmore R; Walter P Nature; 1993 Nov; 366(6453):351-4. PubMed ID: 8247130 [TBL] [Abstract][Full Text] [Related]
13. The affinity of signal recognition particle for presecretory proteins is dependent on nascent chain length. Siegel V; Walter P EMBO J; 1988 Jun; 7(6):1769-75. PubMed ID: 3169004 [TBL] [Abstract][Full Text] [Related]
14. Distinct modes of signal recognition particle interaction with the ribosome. Pool MR; Stumm J; Fulga TA; Sinning I; Dobberstein B Science; 2002 Aug; 297(5585):1345-8. PubMed ID: 12193787 [TBL] [Abstract][Full Text] [Related]
15. Signal recognition particle Alu domain occupies a defined site at the ribosomal subunit interface upon signal sequence recognition. Terzi L; Pool MR; Dobberstein B; Strub K Biochemistry; 2004 Jan; 43(1):107-17. PubMed ID: 14705936 [TBL] [Abstract][Full Text] [Related]
16. Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes. Walter P; Blobel G J Cell Biol; 1981 Nov; 91(2 Pt 1):557-61. PubMed ID: 7309797 [TBL] [Abstract][Full Text] [Related]
17. Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. Bernstein HD; Poritz MA; Strub K; Hoben PJ; Brenner S; Walter P Nature; 1989 Aug; 340(6233):482-6. PubMed ID: 2502718 [TBL] [Abstract][Full Text] [Related]
18. The methionine-rich domain of the 54 kDa subunit of signal recognition particle is sufficient for the interaction with signal sequences. Lütcke H; High S; Römisch K; Ashford AJ; Dobberstein B EMBO J; 1992 Apr; 11(4):1543-51. PubMed ID: 1314169 [TBL] [Abstract][Full Text] [Related]
19. Structure, function and evolution of the signal recognition particle. Nagai K; Oubridge C; Kuglstatter A; Menichelli E; Isel C; Jovine L EMBO J; 2003 Jul; 22(14):3479-85. PubMed ID: 12853463 [TBL] [Abstract][Full Text] [Related]
20. The code for directing proteins for translocation across ER membrane: SRP cotranslationally recognizes specific features of a signal sequence. Nilsson I; Lara P; Hessa T; Johnson AE; von Heijne G; Karamyshev AL J Mol Biol; 2015 Mar; 427(6 Pt A):1191-201. PubMed ID: 24979680 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]