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The expression of GRP78/BIP and its interaction with recombinant human growth hormone in murine erythroleukemic and Chinese hamster ovary cellsDennett, Richard Albert January 1996 (has links)
No description available.
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Studies to characterize the requirements for the binding and release of ERdj3 a mammalian ER DnaJ homolog from substrates /Jin, Yi, January 2008 (has links) (PDF)
Thesis (Ph.D.)--University of Tennessee Health Science Center, 2008. / Title from title page screen (viewed on February 9, 2009). Research advisor: Linda M. Hendershot, Ph.D. Document formatted into pages (ix, 90 p. : ill.). Vita. Abstract. Includes bibliographical references (p. 67-82).
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Characterization of the beta-subunit of the mammalian SRP receptor and its role in assembly of the SRP receptor /Legate, Kyle R. Andrews, D. W. January 2003 (has links)
Thesis (Ph.D.)--McMaster University, 2003. / Advisor: David W. Andrews. Includes bibliographical references (leaves 122-141) Also available via World Wide Web.
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Membrane protein biosynthesis at the endoplasmic reticulumGuna, Alina-Ioana January 2018 (has links)
The biosynthesis of integral membrane proteins (IMPs) is an essential cellular process. IMPs comprise roughly 20-30% of the protein coding genes of all organisms, nearly all of which are inserted and assembled at the endoplasmic reticulum (ER). The defining structural feature of IMPs is one or more transmembrane domains (TMDs). TMDs are typically stretches of predominately hydrophobic amino acids that span the lipid bilayer of biological membranes as an alpha helix. TMDs are remarkably diverse in terms of their topological and biophysical properties. In order to accommodate this diversity, the cell has evolved different sets of machinery that cater to particular subsets of proteins. Our knowledge of how the TMDs of IMPs are selectively recognized, chaperoned into the lipid bilayer, and assembled remains incomplete. This thesis is broadly interested in investigating how TMDs are correctly inserted and assembled at the ER. To address this the biosynthesis of multi-pass IMPs was first considered. Multi-pass IMPs contain two to more than twenty TMDs, with TMDs that vary dramatically in terms of their biophysical properties such as hydrophobicity, length, and helical propensity. The beta-1 adrenergic receptor (β1-AR), a member of the G-protein-coupled receptor (GPCR) family was established as a model substrate in an in vitro system where the insertion and folding of its TMDs could be interrogated. Assembly of β1-AR is not a straightforward process, and current models of insertion fail to explain how the known translocation machinery correctly identifies, inserts, and assembles β1-AR TMDs. An in vivo screen in mammalian cells was therefore conducted to identify additional factors which may be important for multi-pass IMP assembly. The ER membrane protein complex (EMC), a well conserved ER-resident complex of unknown biochemical function, was identified as a promising hit potentially involved in this assembly process. The complexity of working with multi-pass IMPs in an in vitro system prompted the investigation of a simpler class of proteins. Tail-anchored proteins (TA) are characterized by a single C-terminal hydrophobic domain that anchors them into membranes. Though structurally simpler compared to multi-pass IMPs, the TMDs of TA proteins are similarly diverse. We found that known TA insertion pathways fail to engage low-to-moderately hydrophobic TMDs. Instead, these are chaperoned in the cytosol by calmodulin (CaM). Transient release from CaM allows substrates to sample the ER, where resident machinery mediates the insertion reaction. The EMC was shown to be necessary for the insertion of these substrates both in vivo and in vitro. Purified EMC in synthetic liposomes catalysed insertion of its TA substrates in a fully reconstituted system to near-native levels. Therefore, the EMC was rigorously established as a TMD insertase. This key functional insight may explain its critical role in the assembly of multi- pass IMPs – which is now amenable to biochemical dissection.
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Characterization of ERp29, a novel secretion factor of endoplasmic reticulum /Sargsyan, Ernest, January 2005 (has links)
Diss. (sammanfattning) Stockholm : Karolinska institutet, 2005. / Härtill 5 uppsatser.
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