Mutations in the NH2-terminal domain of the signal peptide of preproparathyroid hormone inhibit translocation without affecting interaction with signal recognition particle.-Reference-Cited by-同舟云学术

Mutations in the NH2-terminal domain of the signal peptide of preproparathyroid hormone inhibit translocation without affecting interaction with signal recognition particle.

Published:1987-06 Issue:18 Volume:262 Page:8896-8900
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Szczesna-Skorupa E,Mead D A,Kemper B

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference28 articles.

1. Protein translocation across the endoplasmic reticulum

2. The mechanism of protein secretion across membranes

3. Signal sequences

4. Predicted secondary structures of amino-terminal extension sequences of secreted proteins

5. Cellular Regulation of Secretion and Release;Chan,1982

Cited by 8 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Basic Amino Acids in a Distinct Subset of Signal Peptides Promote Interaction with the Signal Recognition Particle;Journal of Biological Chemistry;2003-11

2. Analysis of the amino terminal presequence of the feline immunodeficiency virus glycoprotein: Effect of deletions on the intracellular transport of gp95;Virology;1992-10

3. Functional tolerance of the human immunodeficiency virus type 1 envelope signal peptide to mutations in the amino-terminal and hydrophobic regions;Journal of Virology;1992-08

4. The role of the N region in signal sequence and signal-anchor function.;Journal of Biological Chemistry;1992-04

5. Proteolysis in protein import and export: Signal peptide processing in eu-and prokaryotes;Experientia;1992-02