120 related articles for article (PubMed ID: 3533926)
1. Deletion of the propeptide from human preproapolipoprotein A-II redirects cotranslational processing by signal peptidase.
Folz RJ; Gordon JI
J Biol Chem; 1986 Nov; 261(31):14752-9. PubMed ID: 3533926
[TBL] [Abstract][Full Text] [Related]
2. The effects of deleting the propeptide from human preproapolipoprotein A-I on co-translational translocation and signal peptidase processing.
Folz RJ; Gordon JI
J Biol Chem; 1987 Dec; 262(35):17221-30. PubMed ID: 3316231
[TBL] [Abstract][Full Text] [Related]
3. Structural requirements of human preproapolipoprotein AI for translocation and processing studied by site-directed mutagenesis in vitro.
Stoffel W; Binczek E
Biol Chem Hoppe Seyler; 1988 Sep; 369(9):1055-63. PubMed ID: 3228490
[TBL] [Abstract][Full Text] [Related]
4. 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]
5. Substrate specificity of eukaryotic signal peptidase. Site-saturation mutagenesis at position -1 regulates cleavage between multiple sites in human pre (delta pro) apolipoprotein A-II.
Folz RJ; Nothwehr SF; Gordon JI
J Biol Chem; 1988 Feb; 263(4):2070-8. PubMed ID: 3276681
[TBL] [Abstract][Full Text] [Related]
6. Residues flanking the COOH-terminal C-region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase and the extent of coupling of its co-translational translocation and proteolytic processing in vitro.
Nothwehr SF; Hoeltzli SD; Allen KL; Lively MO; Gordon JI
J Biol Chem; 1990 Dec; 265(35):21797-803. PubMed ID: 2123875
[TBL] [Abstract][Full Text] [Related]
7. Uncoupling of co-translational translocation from signal peptidase processing in a mutant rat preapolipoprotein-A-IV with a deletion that includes the COOH-terminal region of its signal peptide.
Nothwehr SF; Folz RJ; Gordon JI
J Biol Chem; 1989 Mar; 264(8):4642-7. PubMed ID: 2647742
[TBL] [Abstract][Full Text] [Related]
8. Human apolipoprotein A-II: complete nucleic acid sequence of preproapo A-II.
Lackner KJ; Law SW; Brewer HB
FEBS Lett; 1984 Sep; 175(1):159-64. PubMed ID: 6090207
[TBL] [Abstract][Full Text] [Related]
9. Biosynthesis of human preproapolipoprotein A-II.
Gordon JI; Budelier KA; Sims HF; Edelstein C; Scanu AM; Strauss AW
J Biol Chem; 1983 Nov; 258(22):14054-9. PubMed ID: 6315718
[TBL] [Abstract][Full Text] [Related]
10. Possible involvement of inefficient cleavage of preprovasopressin by signal peptidase as a cause for familial central diabetes insipidus.
Ito M; Oiso Y; Murase T; Kondo K; Saito H; Chinzei T; Racchi M; Lively MO
J Clin Invest; 1993 Jun; 91(6):2565-71. PubMed ID: 8514868
[TBL] [Abstract][Full Text] [Related]
11. Importance of the propeptide sequence of human preproparathyroid hormone for signal sequence function.
Wiren KM; Potts JT; Kronenberg HM
J Biol Chem; 1988 Dec; 263(36):19771-7. PubMed ID: 3198649
[TBL] [Abstract][Full Text] [Related]
12. Proteolytic processing of human preproapolipoprotein A-I. A proposed defect in the conversion of pro A-I to A-I in Tangier's disease.
Gordon JI; Sims HF; Lentz SR; Edelstein C; Scanu AM; Strauss AW
J Biol Chem; 1983 Mar; 258(6):4037-44. PubMed ID: 6300070
[TBL] [Abstract][Full Text] [Related]
13. Eukaryotic signal peptide structure/function relationships. Identification of conformational features which influence the site and efficiency of co-translational proteolytic processing by site-directed mutagenesis of human pre(delta pro)apolipoprotein A-II.
Nothwehr SF; Gordon JI
J Biol Chem; 1989 Mar; 264(7):3979-87. PubMed ID: 2537299
[TBL] [Abstract][Full Text] [Related]
14. Proteolytic processing of the primary translation product of rat intestinal apolipoprotein A-IV mRNA. Comparison with preproapolipoprotein A-I processing.
Gordon JI; Smith DP; Alpers DH; Strauss AW
J Biol Chem; 1982 Jul; 257(14):8418-23. PubMed ID: 7085674
[TBL] [Abstract][Full Text] [Related]
15. Parallel effects of signal peptide hydrophobic core modifications on co-translational translocation and post-translational cleavage by purified signal peptidase.
Cioffi JA; Allen KL; Lively MO; Kemper B
J Biol Chem; 1989 Sep; 264(25):15052-8. PubMed ID: 2549048
[TBL] [Abstract][Full Text] [Related]
16. Synthesis of precursor maltose-binding protein with proline in the +1 position of the cleavage site interferes with the activity of Escherichia coli signal peptidase I in vivo.
Barkocy-Gallagher GA; Bassford PJ
J Biol Chem; 1992 Jan; 267(2):1231-8. PubMed ID: 1730647
[TBL] [Abstract][Full Text] [Related]
17. Mutations in the NH2-terminal domain of the signal peptide of preproparathyroid hormone inhibit translocation without affecting interaction with signal recognition particle.
Szczesna-Skorupa E; Mead DA; Kemper B
J Biol Chem; 1987 Jun; 262(18):8896-900. PubMed ID: 3036835
[TBL] [Abstract][Full Text] [Related]
18. Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site.
Fikes JD; Barkocy-Gallagher GA; Klapper DG; Bassford PJ
J Biol Chem; 1990 Feb; 265(6):3417-23. PubMed ID: 2406254
[TBL] [Abstract][Full Text] [Related]
19. A deletion that includes the signal peptidase cleavage site impairs processing, glycosylation, and secretion of cell surface yeast acid phosphatase.
Haguenauer-Tsapis R; Hinnen A
Mol Cell Biol; 1984 Dec; 4(12):2668-75. PubMed ID: 6098819
[TBL] [Abstract][Full Text] [Related]
20. Inefficient membrane targeting, translocation, and proteolytic processing by signal peptidase of a mutant preproparathyroid hormone protein.
Karaplis AC; Lim SK; Baba H; Arnold A; Kronenberg HM
J Biol Chem; 1995 Jan; 270(4):1629-35. PubMed ID: 7829495
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]