Proteomic Analysis of Rough and Smooth Endoplasmic Reticulum
Author(s) -
Jacques Paiement,
Line Roy,
Annalyn Gilchrist,
Alex Bell,
Rob Kearney,
David Y. Thomas,
John Bergeron
Publication year - 2002
Publication title -
the scientific world journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.453
H-Index - 93
eISSN - 2356-6140
pISSN - 1537-744X
DOI - 10.1100/tsw.2002.12
Subject(s) - endoplasmic reticulum , computer science , computational biology , microbiology and biotechnology , biology
. The membrane subcompartments of the endoplasmic reticulum (ER) are known to be continuous but yet complete structural and functional identity is maintained in each. This is achieved by membrane differentiation and maturation and likely involves sorting and transport that are mediated by different classes of vesicles and tubules. Cytosolic proteins and signalling molecules[1] probably assemble on the membranes to effect vesicle and tubule formation. Study of the ER using proteomic analysis should help define the molecular components involved in ER differentiation.
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