Multiple Molecular Chaperones Interact with Apolipoprotein B during Its Maturation
Open Access
- 1 August 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (33), 21368-21373
- https://doi.org/10.1074/jbc.273.33.21368
Abstract
No abstract availableKeywords
This publication has 54 references indexed in Scilit:
- Functional Analysis of Disulfide Linkages Clustered within the Amino Terminus of Human Apolipoprotein BPublished by Elsevier ,1998
- Microsomal triglyceride transfer proteinBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1997
- Binding of Secretory Precursor Polypeptides to a Translocon Subcomplex Is Regulated by BiPCell, 1997
- Degradation and Endoplasmic Reticulum Retention of Unassembled α- and β-Subunits of Na,K-ATPase Correlate with Interaction of BiPPublished by Elsevier ,1996
- Demonstration of a Physical Interaction between Microsomal Triglyceride Transfer Protein and Apolipoprotein B during the Assembly of ApoB-containing LipoproteinsJournal of Biological Chemistry, 1996
- Apoprotein B100, an Inefficiently Translocated Secretory Protein, Is Bound to the Cytosolic Chaperone, Heat Shock Protein 70Published by Elsevier ,1995
- The Glucose-Regulated Proteins (GRP78 and GRP94): Functions, Gene Regulation, and ApplicationsCritical Reviews™ in Eukaryotic Gene Expression, 1994
- A chaperone with a sweet toothCurrent Biology, 1993
- HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells.The Journal of Experimental Medicine, 1992
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970