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http://dx.doi.org/10.1111/j.1749-6632.1980.tb47252.x | DOI Listing |
Aging Cell
May 2021
Central Arkansas Veterans Healthcare System, Little Rock, AR, USA.
All neurodegenerative diseases feature aggregates, which usually contain disease-specific diagnostic proteins; non-protein constituents, however, have rarely been explored. Aggregates from SY5Y-APP neuroblastoma, a cell model of familial Alzheimer's disease, were crosslinked and sequences of linked peptides identified. We constructed a normalized "contactome" comprising 11 subnetworks, centered on 24 high-connectivity hubs.
View Article and Find Full Text PDFJ Virol
April 2015
Department of Food and Environmental Sciences, University of Helsinki, Helsinki, Finland
Unlabelled: Potato virus A (PVA) is a single-stranded positive-sense RNA virus and a member of the family Potyviridae. The PVA coat protein (CP) has an intrinsic capacity to self-assemble into filamentous virus-like particles, but the mechanism responsible for the initiation of viral RNA encapsidation in vivo remains unclear. Apart from virion assembly, PVA CP is also involved in the inhibition of viral RNA translation.
View Article and Find Full Text PDFJ Biol Chem
January 2012
Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, Oregon 97239, USA.
Protein folding in cells reflects a delicate interplay between biophysical properties of the nascent polypeptide, the vectorial nature and rate of translation, molecular crowding, and cellular biosynthetic machinery. To better understand how this complex environment affects de novo folding pathways as they occur in the cell, we expressed β-barrel fluorescent proteins derived from GFP and RFP in an in vitro system that allows direct analysis of cotranslational folding intermediates. Quantitative analysis of ribosome-bound eCFP and mCherry fusion proteins revealed that productive folding exhibits a sharp threshold as the length of polypeptide from the C terminus to the ribosome peptidyltransferase center is increased.
View Article and Find Full Text PDFJ Nutr
February 1999
Department of Pathology, Wake Forest University School of Medicine, Winston-Salem, NC 27157-1040, USA.
Apolipoprotein (apo) B and the microsomal triglyceride transfer protein are essential for the hepatic assembly and secretion of triglyceride-rich VLDL. To understand how apoB initiates the process of lipoprotein formation, interest has focused on the biogenesis of its amino terminal globular domain (alpha1 domain). When only this domain is expressed in hepatoma cells, no lipoprotein particle will form.
View Article and Find Full Text PDFDNA Cell Biol
September 1995
Department of Molecular Microbiology and Immunology, St. Louis University School of Medicine, MO 63104, USA.
The assembly of a human major histocompatibility complex (MHC) class II molecule was investigated in a cell-free system capable of the synthesis, sequestration, and processing of the protein chains. As assessed by the conformation-sensitive monoclonal antibody L243, the formation of HLA-DR alpha/beta heterodimer required cotranslation of alpha and beta mRNA in the presence of both oxidized glutathione and canine pancreas endoplasmic reticulum (ER) vesicles. The assembly of alpha/beta dimer could also be initiated by the post-translational addition of oxidized glutathione.
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