NDLTD Global ETD Search
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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.

Search results

Showing 1 to 6 of 6 (0.076 seconds)

Spelling suggestions: "subject:"endoplasmic reticulum -- metabolism."" "subject:"endoplasmic reticulums -- metabolism.""

1

Characterization of p58 and rab1p, two proteins operating at the interface of the endoplasmic reticulum and the Golgi complex /

Lahtinen, Ulla, January 1900 (has links)
Diss. (sammanfattning) Stockholm : Karol. inst. / Härtill 4 uppsatser.
Endoplasmic reticulum: metabolism.
2

Folding and retention of rotavirus glycoproteins in the endoplasmic reticulum /

Mirazimi, Ali, January 1900 (has links)
Diss. (sammanfattning) Stockholm : Karol. inst. / Härtill 5 uppsatser.
Endoplasmic reticulum: metabolism.
3

Functional characterization of the yeast ER packaging chaperone Shr3p /

Gilstring, Fredrik, January 1900 (has links)
Diss. (sammanfattning) Stockholm : Karol. inst., 2001. / Härtill 4 uppsatser.
4

Unfolded Protein Response Inhibitors Identified by High Throughput Screening of a Combinatorial Chemistry Compound Library

Martel-Lorion, Chloe January 2004 (has links)
Note:
Endoplasmic Reticulum -- metabolism.
Protein Folding.
5

Nck1 is required for ER stress-induced insulin resistance and regulation of IRS1-dependent insulin signalling

Laberge, Marie-Kristine. January 2008 (has links)
Activation of the Unfolded Protein Response (UPR) following stress in the Endoplasmic Reticulum (ER) is an important mechanism by which obesity results in insulin resistance and type II diabetes. We uncovered a role for the adaptor protein Nck in modulating the UPR. In this study, we report that obese Nck1-/- mice, which show lower levels of UPR in liver and adipose tissue, present improved insulin signalling in these tissues. We established that the effect of Nck1 is cell autonomous by showing that HepG2 cells treated with Nck1 siRNA have reduced ER stress-induced UPR and Insulin Receptor Substrate-1 (IRS-1) serine phosphorylation. In these cells, we observed that the IRS-1 levels and activation of signalling components downstream of the insulin receptor were increased. This correlates with enhanced cell survival to stress and insulin stimulated glycogen synthesis. Overall, we demonstrated that Nck1 participates in ER-stress-induced insulin resistance and regulation of IRS-1-dependent signalling.
Insulin -- metabolism.
Insulin Resistance.
Insulin Receptor Substrate Proteins
Protein Folding.
Endoplasmic Reticulum -- metabolism.
6

Nck1 is required for ER stress-induced insulin resistance and regulation of IRS1-dependent insulin signalling

Laberge, Marie-Kristine. January 2008 (has links)
No description available.
Protein Folding.
Insulin -- metabolism.
Insulin Resistance.
Insulin Receptor Substrate Proteins
Endoplasmic Reticulum -- metabolism.

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