The membrane-interactive tail of cytochrome b5 can function as a stop-transfer sequence in concert with a signal sequence to give inversion of protein topology in the endoplasmic reticulum-Reference-Cited by-同舟云学术

The membrane-interactive tail of cytochrome b5 can function as a stop-transfer sequence in concert with a signal sequence to give inversion of protein topology in the endoplasmic reticulum

Published:2003-04 Issue:2 Volume:412 Page:259-266
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Kaderbhai Mustak A.,Morgan Rachel,Kaderbhai Naheed N.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference33 articles.

1. Cytochrome b5, its functions, structure and membrane topology

2. Efficient Bacterial Export of a Eukaryotic Cytoplasmic Cytochrome

3. Interaction of human CYP17 (P-45017α, 17α-hydroxylase-17,20-lyase) with cytochrome b5: importance of the orientation of the hydrophobic domain of cytochrome b5

4. The carboxy-terminal 10 amino acid residues of cytochrome b5 are necessary for its targeting to the endoplasmic reticulum.

5. The Myristoyl Moiety of Myristoylated Alanine-rich C Kinase Substrate (MARCKS) and MARCKS-related Protein Is Embedded in the Membrane

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1. Mechanistic Basis of Electron Transfer to Cytochromes P450 by Natural Redox Partners and Artificial Donor Constructs;Advances in Experimental Medicine and Biology;2015

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3. Signal peptidase I-mediated processing of an engineered mammalian cytochrome b5precursor is an exocytoplasmic post-translocational event inEscherichia coli;Molecular Membrane Biology;2008-01

4. Towards engineered topogenesis of cytochrome b5 and P450 for in vivo transformation of xenobiotics;Biochemical Society Transactions;2006-10-25

5. Cytochrome b5 modulation of 17α hydroxylase and 17–20 lyase (CYP17) activities in steroidogenesis;Journal of Endocrinology;2005-11