Protein Biosynthesis and Maturation in the ER
Created March 18, 2026
Updated on March 25, 2026
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Basic
Language
English
MainTitle
Protein Biosynthesis and Maturation in the ER
Original ids
10.1007/978-1-0716-3710-4_14; 10.1007/978-1-4939-7389-7_14; 29043678; 38411815; 20.500.14243/519953; 20.500.14243/326275
Type
publication
bestAccessRight
RESTRICTED
countries
Italy
Creator/Author
Full name
Pedrazzini Emanuela, orcid: 0000-0002-9238-3840 ; Vitale Alessandro, orcid: 0000-0001-5586-2255
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Description
The endoplasmic reticulum takes care of the folding, assembly, and quality control of thousands of proteins destined to the different compartments of the endomembrane system, or to be secreted in the apoplast. Here we describe how these early events in the life of all these proteins can be followed biochemically by using velocity or isopycnic ultracentrifugation, metabolic labeling with radioactive amino acids, and immunoprecipitation in various conditions.
Publication Date
2017-10-17
Publisher
Springer US
Subjects
0301 basic medicine; Protein Folding; Protein-protein interactions; protein oligomerization; immunoprecipitation; Cell Fractionation; Endoplasmic Reticulum; 7. Clean energy; pulse-chase; protein-protein interaction; Endoplasmi; ultracentrifugation; 03 medical and health sciences; Protein oligomerization; protein folding; Chaperones; Immunoglobulin binding protein (BiP); chaperones; Immunoprecipitation; Protein folding; Amino Acids; Plant Proteins; 0303 health sciences; Immunoselection; Biological Transport; 3. Good health; 13. Climate action; Protein Biosynthesis; Pulse-chase; Protein synthesis; Protein Processing, Post-Translational; Ultracentrifugation; Endoplasmic reticulum; Algorithms; Molecular Chaperones; Subcellular Fractions
isGreen
false
isInDiamondJournal
false
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Part of book or chapter of book
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Last Updated
March 25, 2026, 10:40 (UTC)
Created
March 18, 2026, 23:30 (UTC)
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