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Molecular characterization of the endoplasmic reticulum: Insights from proteomic studies

dc.contributor.authorChen, Xuequnen_US
dc.contributor.authorKarnovsky, Allaen_US
dc.contributor.authorSans, Maria Dolorsen_US
dc.contributor.authorAndrews, Philip C.en_US
dc.contributor.authorWilliams, John A.en_US
dc.date.accessioned2010-11-18T20:26:56Z
dc.date.available2011-03-01T16:26:45Zen_US
dc.date.issued2010-11en_US
dc.identifier.citationChen, Xuequn; Karnovsky, Alla; Sans, Maria Dolors; Andrews, Philip C.; Williams, John A. (2010). "Molecular characterization of the endoplasmic reticulum: Insights from proteomic studies." PROTEOMICS 10(22): 4040-4052. <http://hdl.handle.net/2027.42/78298>en_US
dc.identifier.issn1615-9853en_US
dc.identifier.issn1615-9861en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/78298
dc.description.abstractThe endoplasmic reticulum (ER) is a multifunctional intracellular organelle responsible for the synthesis, processing and trafficking of a wide variety of proteins essential for cell growth and survival. Therefore, comprehensive characterization of the ER proteome is of great importance to the understanding of its functions and has been actively pursued in the past decade by scientists in the proteomics field. This review summarizes major proteomic studies published in the past decade that focused on the ER proteome. We evaluate the data sets obtained from two different organs, liver and pancreas each of which contains a primary cell type (hepatocyte and acinar cell) with specialized functions. We also discuss how the nature of the proteins uncovered is related to the methods of organelle purification, organelle purity and the techniques used for protein separation prior to MS. In addition, this review also puts emphasis on the biological insights gained from these studies regarding the molecular functions of the ER including protein synthesis and translocation, protein folding and quality control, ER-associated degradation and ER stress, ER export and membrane trafficking, calcium homeostasis and detoxification and drug metabolism.en_US
dc.format.extent318386 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherWILEY-VCH Verlagen_US
dc.subject.otherLife and Medical Sciencesen_US
dc.titleMolecular characterization of the endoplasmic reticulum: Insights from proteomic studiesen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Molecular and Integrative Physiology, The University of Michigan, Ann Arbor, MI, USA ; Department of Physiology, Wayne State University, 5215 Scott Hall, Detroit, MI 48201, USA Fax: +1-313-577-5494en_US
dc.contributor.affiliationumCenter for Computational Medicine and Biology, The University of Michigan, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumDepartment of Molecular and Integrative Physiology, The University of Michigan, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumCenter for Computational Medicine and Biology, The University of Michigan, Ann Arbor, MI, USA ; Department of Biological Chemistry, The University of Michigan, Ann Arbor, MI, USAen_US
dc.contributor.affiliationumDepartment of Molecular and Integrative Physiology, The University of Michigan, Ann Arbor, MI, USA ; Center for Computational Medicine and Biology, The University of Michigan, Ann Arbor, MI, USAen_US
dc.identifier.pmid21080494en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/78298/1/4040_ftp.pdf
dc.identifier.doi10.1002/pmic.201000234en_US
dc.identifier.sourcePROTEOMICSen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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