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Please use this identifier to cite or link to this item: http://hdl.handle.net/2067/1703

Title: A relaxed specificity in interchain disulfide bond formation characterises the assembly of a low-molecular-weight glutenin subunit in the endoplasmic reticulum
Authors: Lombardi, Alessio
Barbante, Alessandra
Della Cristina, Pietro
Rosiello, Daniele
Castellazzi, Chiara Lara
Sbano, Luca
Masci, Stefania
Ceriotti, Aldo
Keywords: Low molecular weight glutenin subunits
Wheat
Disulfide bonds
Cysteine residues
Issue Date: 2009
Publisher: American Society of Plant Biologists
Citation: Lombardi A. et al. 2009. A relaxed specificity in interchain disulfide bond formation characterises the assembly of a low-molecular-weight glutenin subunit in the endoplasmic reticulum. "Plant Physiology" 149(1): 412-423
Abstract: Wheat (Triticum aestivum) grains contain large protein polymers constituted by two main classes of polypeptides: the highmolecular- weight glutenin subunits and the low-molecular-weight glutenin subunits (LMW-GS). These polymers are among the largest protein molecules known in nature and are the main determinants of the superior technological properties of wheat flours. However, little is known about the mechanisms controlling the assembly of the different subunits and the way they are arran
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Description: L'articolo è disponibile sul sito dell'editore: http://www.aspb.org
URI: http://hdl.handle.net/2067/1703
ISSN: 0032-0889
Appears in Collections:DABAC - Archivio della produzione scientifica

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