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.
117 related articles for article (PubMed ID: 8407979)
1. Position-specific Asp-Lys pairing can affect signal sequence function and membrane protein topology. Andersson H; von Heijne G J Biol Chem; 1993 Oct; 268(28):21389-93. PubMed ID: 8407979 [TBL] [Abstract][Full Text] [Related]
2. Different positively charged amino acids have similar effects on the topology of a polytopic transmembrane protein in Escherichia coli. Andersson H; Bakker E; von Heijne G J Biol Chem; 1992 Jan; 267(3):1491-5. PubMed ID: 1346135 [TBL] [Abstract][Full Text] [Related]
3. Fine-tuning the topology of a polytopic membrane protein: role of positively and negatively charged amino acids. Nilsson I; von Heijne G Cell; 1990 Sep; 62(6):1135-41. PubMed ID: 2119256 [TBL] [Abstract][Full Text] [Related]
4. Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal. Laws JK; Dalbey RE EMBO J; 1989 Jul; 8(7):2095-9. PubMed ID: 2676512 [TBL] [Abstract][Full Text] [Related]
5. Effect of different positively charged amino acids, C-terminally of the signal peptidase cleavage site, on the translocation kinetics of a precursor protein in Escherichia coli K-12. Struyvé M; Bosch D; Visser J; Tommassen J FEMS Microbiol Lett; 1993 May; 109(2-3):173-8. PubMed ID: 8101824 [TBL] [Abstract][Full Text] [Related]
6. Charge pair interactions in a model transmembrane helix in the ER membrane. Chin CN; von Heijne G J Mol Biol; 2000 Oct; 303(1):1-5. PubMed ID: 11021965 [TBL] [Abstract][Full Text] [Related]
7. Reversible topology of a bifunctional transmembrane protein depends upon the charge balance around its transmembrane domain. Kim H; Paul S; Gennity J; Jennity J [corrected to Gennity J]; Inouye M Mol Microbiol; 1994 Mar; 11(5):819-31. PubMed ID: 8022260 [TBL] [Abstract][Full Text] [Related]
8. A 30-residue-long "export initiation domain" adjacent to the signal sequence is critical for protein translocation across the inner membrane of Escherichia coli. Andersson H; von Heijne G Proc Natl Acad Sci U S A; 1991 Nov; 88(21):9751-4. PubMed ID: 1946398 [TBL] [Abstract][Full Text] [Related]
9. Anionic phospholipids are determinants of membrane protein topology. van Klompenburg W; Nilsson I; von Heijne G; de Kruijff B EMBO J; 1997 Jul; 16(14):4261-6. PubMed ID: 9250669 [TBL] [Abstract][Full Text] [Related]
10. In vitro kinetic analysis of the role of the positive charge at the amino-terminal region of signal peptides in translocation of secretory protein across the cytoplasmic membrane in Escherichia coli. Sasaki S; Matsuyama S; Mizushima S J Biol Chem; 1990 Mar; 265(8):4358-63. PubMed ID: 2106519 [TBL] [Abstract][Full Text] [Related]
12. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. von Heijne G Nature; 1989 Oct; 341(6241):456-8. PubMed ID: 2677744 [TBL] [Abstract][Full Text] [Related]
13. Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes. Johansson M; Nilsson I; von Heijne G Mol Gen Genet; 1993 May; 239(1-2):251-6. PubMed ID: 8510652 [TBL] [Abstract][Full Text] [Related]
14. Membrane protein topology: effects of delta mu H+ on the translocation of charged residues explain the 'positive inside' rule. Andersson H; von Heijne G EMBO J; 1994 May; 13(10):2267-72. PubMed ID: 8194517 [TBL] [Abstract][Full Text] [Related]
15. Positively charged lysine at the N-terminus of the signal peptide of the Escherichia coli alkaline phosphatase provides the secretion efficiency and is involved in the interaction with anionic phospholipids. Nesmeyanova MA; Karamyshev AL; Karamysheva ZN; Kalinin AE; Ksenzenko VN; Kajava AV FEBS Lett; 1997 Feb; 403(2):203-7. PubMed ID: 9042967 [TBL] [Abstract][Full Text] [Related]
16. Structural features in the NH2-terminal region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase. Nothwehr SF; Gordon JI J Biol Chem; 1990 Oct; 265(28):17202-8. PubMed ID: 2120214 [TBL] [Abstract][Full Text] [Related]
17. Different sec-requirements for signal peptide cleavage and protein translocation in a model E. coli protein. Nilsson IM; Gafvelin G; von Heijne G FEBS Lett; 1993 Feb; 318(1):7-10. PubMed ID: 8436228 [TBL] [Abstract][Full Text] [Related]
18. Formation of helical hairpins during membrane protein integration into the endoplasmic reticulum membrane. Role of the N and C-terminal flanking regions. Hermansson M; Monné M; von Heijne G J Mol Biol; 2001 Nov; 313(5):1171-9. PubMed ID: 11700072 [TBL] [Abstract][Full Text] [Related]
19. Hydrophobic core but not amino-terminal charged residues are required for translocation of an integral thylakoid membrane protein in vivo. Baillet B; Kohorn BD J Biol Chem; 1996 Aug; 271(31):18375-8. PubMed ID: 8702480 [TBL] [Abstract][Full Text] [Related]
20. An amphiphilic lipid-binding domain influences the topology of a signal-anchor sequence in the mitochondrial outer membrane. Steenaart NA; Silvius JR; Shore GC Biochemistry; 1996 Mar; 35(12):3764-71. PubMed ID: 8619997 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]